GRS - Genome Report System

Sclerotinia sclerotiorum GRS

Functional annotation

SS1G_01727.1

>SS1G_01727.1 | 3857 aa 
MASNNIDVLAQRLGSADTDLKLKVDVAVQLRDGLDHYITGPMYSTFLRKLIPIFINCLKGPPVFISTSLDQKLRCCVLEILHRLPMNPPEAFEPYAAEVVDLLISLVRIDNEENATLCVKTIMDLMRSQTKVLQDRVQTFLGLIQELFDQMDSVVHDQLDNSATGSNQTGVPSTPGSSQTFQNSPRPGSPIASVTDIGQDPQQQTRKLLKGMQSFKVLAECPIIVVSIFQVYRNSVPQNVKLFIPLIKSVLLLQAKPQEQAHAEAAKRGTIFTGISPDIKNRAAFGEFITAQVKTMSFLAYLLRVYSQQLTDFLPTLPDIVVRLLKDCPREKSGARKELLVAIRHIINFNFRKIFLRVIDQLLDERTLIGDGLTVYEGMRPLAYSMLADLIHHVRDALEPGQIRKTVEVYTRNLQDSFPGTSFQTMSAKLLLNMAECIAKMPSKTDARHYLIMILNAIGDKFAAMNRQYSNAVKLSKHYSQQTLDSAPENYLADKDNPPDWDEIDIFSAMPIKTSNPRDRGADPVADNKFLFKNLMNGLKNTFYQLKACNGGSPIELSNAPPHWAEVSHGFSAEEVQVIIKLFREGAYVFRYYEIEKPATESQYSSPVEFMANHYMVSSSKEEKDLLETFATVFHCIDPATFHEVFHEEIPKLYEMIFEHTALLHVPQFFLASEATSPSFAGMLLRFLMDRIDQVGTADVKKSSILLRLFKLAFMAVTLFSNQNEQVLLPHVVNIVTKSIELSTTAEEPLNYFLLLRSLFRSIGGGKFEHLYKQILPLLEMLLEVLNNLLMAARKPADRDLYVELCLTVPARLSNLLPHLSYLMRPLVVALRAGSDLVGQGLRTLELCVDNLTADYLDPIMAPVIDELMTALFDHLRPNPYSHFHAHTTMRILGKLGGRNRRFMTGAPNLNFQQFADDITTFDLKLVGSKRERPFPVEIGIDLAIGKLMEVPKGAAAKKSDPYYKKQALALVKSQLKLRLGADNLPDEFPRLVRLQAQDLLSKKADADLSLFETPVRDRSEAKKMQQDTMLKKLLKACIFAVSLPEFSSEATTLLSNVCKHITIIEVARSLGEMKVRMKPFDVNAGEGPPCIDSKVLADAIVESLASDLPAVRDAAKTAAQEVYDSTATIFGSNRFIYRLSFFSHLSSVFCHSCYQEEWFTKTGGSLGINLMLTKFDLSDSWMLEKQVEYTKALMHVIKDMPPDLPAKTRIAAQDTLELLLKRCAGKSSKADLQPSSQPGQPSRPSKLLQLCNLFNAEVYHMNGHVRETARKSLEIIAKEIDVEVYELLAHQQDRILAPIYNKPLRALPFATQIGYIDAVNYYMSLKNDFLAFDDTLNRLLMECLALADAPDESLAPKPTEHRTHEHIVTLRVSCIKTLTTAMGFDDFQKGPANPTRTRIVSVFFKCLYSNSKATIEAANDALRVVLSHSNKLPKDLLQNGLRPVLANLQDPKRLTTHGLDGLARLLQLLTTYFKVEIGSRLLEHIRVLADPNAFQRISFTLVEQNEQMKIIAAVFNIFHLLPPAAEQFKERLIDAVLELEEKLRRTRYSPFRDPLYKYINRYPKEVWAMLLSKIEDQKYGRFLAQVLSHPDSAPLRAVVVRSIDSLIKSCGDMGAENRETRYAAVINAINVMHSICSFKGTELWMDKKENLMWFRLVGKNLEQHLRTNTLPQNLRLAAEQAGQQLMIIFTKFLEYNPRDLDSFFNLIESITAEDFKPNQPIFDFIYKFIVCSESIDYRKAIVLRCLEIYVSKAATQKNKTFLLHNLVNPIIAMDIMRNFQQPSSAKSSRLIDRTIIESIHTKVWKVGLPDPSDDLTQPGIDHTRMELLQLTAMLVKYNHSILQEARKDIIKFGWGYIRLEDVINKHAAYVVIGYFIAHYETPAKIVQQVYFSLLKTNQNEGRALVTQALELIAPVLPKRCNAVPGDRNPVWAAAPRRILAEEGQNVQQMTSIFNFLVKHADLFYESRDKFINLIIGSLRKIAPPQTNPSNESKKLSLHLMSLIWHWEERRVEGKATSSERPLSESPNTKKRKLDSLNDPQTSSPSPSRPGTTSTNDKPEYQIPAVMRAKMIKYLVEFIASLNERYPLPSARGRDTTTSHGPAQPPPSVEVCKKSMSLLWNLLQPQYWGDLDIDLFPNVTEQVLASDKATAALLSERPDKDKPDDKFITNIINTLQIVRIVINVKPTKWILEKVPELQHILEKALKSDNPEVQDCMHAGDEKIDDGRKLSPLLKRILEAVPDDTPMEDADAECEPEASTSEIITYLSATATEMLSANNYISGLNILWTLAQRKASEMDQHIPQVMKALQQKLAREHVGHYTALTGQGAIPAAMRPGEVEPVGLMSQYDLEIQTGLMLKAIDVISLRMDTLGDSRRPFLSVLATLVEKSLSNPLCLKILEMVEAWVFKSEGSWPTLKEKTAVLHKMLSFEQRTDQTLLMKFLELVIRIYEDPKITRTELTVRMEHAFLIGTRAQDVDMRSRFMAIFDRSQSKTASTRLNYVIIGQNWDPLAESYWLAQASQLLLGAVDANHSIHLHSDDFKVMPASVLYETYAKDNRTPTLPQDNRFDSLMASHRRFVAELGDVKARDIIEPLSQLQHLDPNMAHEIWVALFPIYWNATPKDERSDLERGMVTLLTREYHSRQIDKRPNVVQSLLEGAAKAWPECKLPPHVVKFLAKTYDVWYTALVQLENAAIKPEINSDLVRESNLDALVELYSGLQEDDLFYGTWRRRCAYVETNAALSYEQNGMWDKAQTMYEHAQIKARTGALPFSQGEYMLWEDHWVLCAQKLQQWEVLQDFAKHENFQDLLLECAWRQFEIWQEPEHREQLDNIIKGVMDAPTPRRTFFQAFMSLLKLHKKTETQAEFSKVCDEAIQLSIRKWHQLPKRITNAHIPLLQNFQQLVELHDASVICQSLSQTTSANLDVKSGELKLLLGTWRDRLPNVWDDITAWQDLVTWRQHIFALINSTYLNLIPQQPPNANGASFAYRGYHETAWIINRFAHVARKHNLPEVCISQLSRIYTLPNIEIQEAFLKLREQAKCHYQNPNELNNGLDVINNTNLNYFGPNQKAEFYTLKGMFQEKLGLRDEASEAYGMALFFEIKLPKAWAEWGYFNDRLFKANPNDYTFARNALSCYLEAAGLFKNAKSRKLLTRILWLLSLDDAEGTLSAQFDEYKGETPVWYWITFIPQLLTGLGHKEAAKAHLILSKIAKSYPQALFFQLRTNREDMLAIKKQQDMKEAKKARAQTQAQGQALGGISNIKAENTNGTRPENASASRPGTAGAEGVPAIKTEPGETNGNITNTNGAPVNGAPTNGTANGSQDVAPSQGSQKKPPWEYTEELLGALKTAFPLLALSMEAMVDSIQKNFKCPPDEDAYRLIVALLNDGLSYVSRTPSSYAKDNKLPPATEANITRFAETILPPHIRTSFEQDFVKHKPTMFEYIHKLRTWRDKFEEKLDRRTLTVPLEGYNSYLIDFRFQKLDEIEVPGQYLLHKDKNQDFIRIERFMPDVDLVRTIGVCHRRIRIRGHDGSLHPFAIQHPAARHCRREERILQLFRHFNGTLSKRKESRRRNLNFHLPLMIPLAPHIRMVQDDPTYVSLQGVYDDHCRRNEIAKDAPIVFNMEKQKLLFENKQNKTPEQSATARLETFAAIQEKHVGPSIVLEYFTKTYPSFSEFWLFRRQFSYQYAALTFMTYILHMHNRYPHKISISRATGNIWGSELMSCMAAGKAIFHNPEPVPFRLTPNIQTLMGPLATEGIYSCAIMAIARCLSEPEFELEQQLCLFVRDEMIFWHTSSHKAIKDTELRQSVQTNSDMIVKRALSIAKSPEGALPANQTVIDLIAKAVNPMNLAQCDALWMPYL

Domain/Motif (Interproscan results)

Localization / Targeting

Blast based analysis

Analysis	Hit	start	end	length	Note	Hit coverage	Hit length	Hit pident	Hit pcons	eValue	Hit description
blastp_kegg	ssl:SS1G_01727	1	3857	3857	n/a	100.00	3857	97.67	0.00	0.0	hypothetical protein K08874 transformation/transcription domain-associated protein
	bfu:BC1G_13732	1	3857	3857	Gaps:23	100.00	3876	91.28	2.99	0.0	hypothetical protein K08874 transformation/transcription domain-associated protein
	fgr:FG06089.1	1	3857	3857	Gaps:73	100.00	3880	67.60	12.22	0.0	hypothetical protein K08874 transformation/transcription domain-associated protein
	ncr:NCU01379	3	3857	3855	Gaps:130	99.97	3842	66.62	13.54	0.0	similar to histone acetylase complex subunit Paf400 K08874 transformation/transcription domain-associated protein
	mgr:MGG_09523	1	3857	3857	Gaps:89	100.00	3888	65.43	13.43	0.0	MG09523.4 hypothetical protein K08874 transformation/transcription domain-associated protein
	pan:PODANSg8711	1	3857	3857	Gaps:86	100.00	3875	65.14	13.60	0.0	hypothetical protein K08874 transformation/transcription domain-associated protein
	act:ACLA_002590	5	3857	3853	Gaps:124	99.92	3906	60.65	14.27	0.0	histone acetylase complex subunit Paf400 putative K08874 transformation/transcription domain-associated protein
	aor:AO090102000372	5	3857	3853	Gaps:126	99.92	3898	60.64	14.45	0.0	histone acetyltransferase SAGA TRRAP/TRA1 component PI-3 kinase superfamily K08874 transformation/transcription domain-associated protein
	afv:AFLA_004770	71	3857	3787	Gaps:116	98.68	3868	61.17	14.41	0.0	histone acetylase complex subunit Paf400 putative K08874 transformation/transcription domain-associated protein
	pcs:Pc21g15390	5	3857	3853	Gaps:112	99.92	3852	60.69	14.81	0.0	Pc21g15390 K08874 transformation/transcription domain-associated protein
blastp_uniprot_sprot	sp\|Q9HFE8\|TRA1_SCHPO	12	3857	3846	Gaps:344	98.68	3699	37.37	20.16	0.0	Transcription-associated protein 1 OS Schizosaccharomyces pombe GN tra1 PE 2 SV 1
	sp\|P38811\|TRA1_YEAST	6	3857	3852	Gaps:252	99.41	3744	39.04	19.75	0.0	Transcription-associated protein 1 OS Saccharomyces cerevisiae GN TRA1 PE 1 SV 1
	sp\|Q10064\|YAMB_SCHPO	49	3857	3809	Gaps:322	93.79	3655	36.79	20.83	0.0	Uncharacterized PI3/PI4-kinase family protein C1F5.11c OS Schizosaccharomyces pombe GN SPAC1F5.11c PE 2 SV 1
	sp\|Q9Y4A5\|TRRAP_HUMAN	13	3857	3845	Gaps:408	94.87	3859	29.09	20.65	0.0	Transformation/transcription domain-associated protein OS Homo sapiens GN TRRAP PE 1 SV 3
	sp\|Q8I8U7\|TRA1_DROME	316	3857	3542	Gaps:359	87.72	3803	28.51	20.80	0.0	Transcription-associated protein 1 OS Drosophila melanogaster GN Nipped-A PE 1 SV 3
	sp\|Q80YV3\|TRRAP_MOUSE	1300	3857	2558	Gaps:263	94.97	2565	27.34	20.65	1e-179	Transformation/transcription domain-associated protein OS Mus musculus GN Trrap PE 1 SV 2
	sp\|Q54T85\|TRA1_DICDI	26	3857	3832	Gaps:371	58.80	4582	28.10	20.53	2e-73	Probable transcription-associated protein 1 OS Dictyostelium discoideum GN tra1 PE 3 SV 2
	sp\|O14356\|TOR1_SCHPO	3480	3856	377	Gaps:62	17.09	2335	25.31	16.29	4e-17	Phosphatidylinositol 3-kinase tor1 OS Schizosaccharomyces pombe GN tor1 PE 1 SV 1
	sp\|Q02099\|RAD3_SCHPO	3502	3857	356	Gaps:22	14.08	2386	25.00	19.94	7e-17	Protein kinase rad3 OS Schizosaccharomyces pombe GN rad3 PE 1 SV 2
	sp\|Q95Q95\|TOR_CAEEL	3480	3856	377	Gaps:39	14.24	2697	26.56	17.97	7e-17	Target of rapamycin homolog OS Caenorhabditis elegans GN let-363 PE 2 SV 3
blastp_pdb	no results
rpsblast_cdd	gnl\|CDD\|119423	3500	3790	291	Gaps:38	100.00	253	58.50	19.76	1e-104	cd05163 TRRAP TRansformation/tRanscription domain-Associated Protein (TRRAP) pseudokinase domain The TRRAP catalytic domain is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs) aminoglycoside phosphotransferase choline kinase and RIO kinases. TRRAP shows some similarity to members of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily in that it contains a FATC (FRAP ATM and TRRAP C-terminal) domain and has a large molecular weight. Unlike PIKK proteins however it contains an inactive PI3K-like pseudokinase domain which lacks the conserved residues necessary for ATP binding and catalytic activity. TRRAP also contains many motifs that may be critical for protein-protein interactions. TRRAP is a common component of many histone acetyltransferase (HAT) complexes and is responsible for the recruitment of these complexes to chromatin during transcription replication and DNA repair. TRRAP also exists in non-HAT complexes such as the p400 and MRN complexes which are implicated in ATP-dependent remodeling and DNA repair respectively..
	gnl\|CDD\|34637	1261	3857	2597	Gaps:226	70.97	2105	31.19	15.93	6e-95	COG5032 TEL1 Phosphatidylinositol kinase and protein kinases of the PI-3 kinase family [Signal transduction mechanisms / Cell division and chromosome partitioning / Chromatin structure and dynamics / DNA replication recombination and repair / Intracellular trafficking and secretion].
	gnl\|CDD\|145423	2804	3154	351	Gaps:80	100.00	351	33.90	14.25	2e-81	pfam02259 FAT FAT domain. The FAT domain is named after FRAP ATM and TRRAP.
	gnl\|CDD\|128451	3533	3789	257	Gaps:59	98.02	202	28.28	20.71	5e-28	smart00146 PI3Kc Phosphoinositide 3-kinase catalytic domain. Phosphoinositide 3-kinase isoforms participate in a variety of processes including cell motility the Ras pathway vesicle trafficking and secretion and apoptosis. These homologues may be either lipid kinases and/or protein kinases: the former phosphorylate the 3-position in the inositol ring of inositol phospholipids. The ataxia telangiectesia-mutated gene produced the targets of rapamycin (TOR) and the DNA-dependent kinase have not been found to possess lipid kinase activity. Some of this family possess PI-4 kinase activities.
	gnl\|CDD\|144156	3530	3788	259	Gaps:35	98.71	233	27.83	15.65	8e-26	pfam00454 PI3_PI4_kinase Phosphatidylinositol 3- and 4-kinase. Some members of this family probably do not have lipid kinase activity and are protein kinases.
	gnl\|CDD\|119432	3500	3788	289	Gaps:66	99.15	235	28.33	18.45	3e-14	cd05172 PIKKc_DNA-PK DNA-dependent protein kinase (DNA-PK) catalytic domain The DNA-PK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs) aminoglycoside phosphotransferase choline kinase and RIO kinases. DNA-PK is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain similar to that of lipid PI3K and their large molecular weight (240-470 kDa). DNA-PK is comprised of a regulatory subunit containing the Ku70/80 subunit and a catalytic subunit which contains a NUC194 domain of unknown function a FAT (FRAP ATM and TRRAP) domain a catalytic domain and a FATC domain at the C-terminus. It is part of a multi-component system involved in non-homologous end joining (NHEJ) a process of repairing double strand breaks (DSBs) by joining together two free DNA ends of little homology. DNA-PK functions as a molecular sensor for DNA damage that enhances the signal via phosphorylation of downstream targets. It may also act as a protein scaffold that aids the localization of DNA repair proteins to the site of DNA damage. DNA-PK also plays a role in the maintenance of telomeric stability and the prevention of chromosomal end fusion..
	gnl\|CDD\|119416	3659	3783	125	Gaps:1	56.62	219	25.00	15.32	6e-11	cd00142 PI3Kc_like Phosphoinositide 3-kinase (PI3K)-like family catalytic domain The PI3K-like catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs) aminoglycoside phosphotransferase choline kinase and RIO kinases. Members of the family include PI3K phosphoinositide 4-kinase (PI4K) PI3K-related protein kinases (PIKKs) and TRansformation/tRanscription domain-Associated Protein (TRRAP). PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives while PI4K catalyze the phosphorylation of the 4-hydroxyl of PtdIns. PIKKs are protein kinases that catalyze the phosphorylation of serine/threonine residues especially those that are followed by a glutamine. PI3Ks play an important role in a variety of fundamental cellular processes including cell motility the Ras pathway vesicle trafficking and secretion immune cell activation and apoptosis. PI4Ks produce PtdIns(4)P the major precursor to important signaling phosphoinositides. PIKKs have diverse functions including cell-cycle checkpoints genome surveillance mRNA surveillance and translation control..
	gnl\|CDD\|119430	3524	3790	267	Gaps:41	92.51	307	22.18	17.61	4e-10	cd05170 PIKKc_SMG1 Suppressor of morphogenetic effect on genitalia-1 (SMG-1) catalytic domain The SMG-1 catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs) aminoglycoside phosphotransferase choline kinase and RIO kinases. SMG-1 is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain similar to that of lipid PI3K and their large molecular weight (240-470 kDa). In addition to its catalytic domain SMG-1 contains a FATC (FRAP ATM and TRRAP C-terminal) domain at the C-terminus. SMG-1 plays a critical role in the mRNA surveillance mechanism known as non-sense mediated mRNA decay (NMD). NMD protects the cells from the accumulation of aberrant mRNAs with premature termination codons (PTCs) generated by genome mutations and by errors during transcription and splicing. SMG-1 phosphorylates Upf1 another central component of NMD at the C-terminus upon recognition of PTCs. The phosphorylation/dephosphorylation cycle of Upf1 is essential for promoting NMD..
	gnl\|CDD\|119424	3660	3768	109	Gaps:1	48.65	222	26.85	18.52	1e-09	cd05164 PIKKc Phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily catalytic domain The PIKK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs) aminoglycoside phosphotransferase choline kinase and RIO kinases. Members include ATM (Ataxia telangiectasia mutated) ATR (Ataxia telangiectasia and Rad3-related) TOR (Target of rapamycin) SMG-1 (Suppressor of morphogenetic effect on genitalia-1) and DNA-PK (DNA-dependent protein kinase). PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain similar to that of lipid PI3K and their large molecular weight (240-470 kDa). They show strong preference for phosphorylating serine/threonine residues followed by a glutamine and are also referred to as (S/T)-Q-directed kinases. They all contain a FATC (FRAP ATM and TRRAP C-terminal) domain. PIKKs have diverse functions including cell-cycle checkpoints genome surveillance mRNA surveillance and translation control..
rpsblast_kog	gnl\|CDD\|36107	10	3857	3848	Gaps:362	99.72	3550	39.41	19.52	0.0	KOG0889 KOG0889 KOG0889 Histone acetyltransferase SAGA TRRAP/TRA1 component PI-3 kinase superfamily [Signal transduction mechanisms Chromatin structure and dynamics Replication recombination and repair Cell cycle control cell division chromosome partitioning].
	gnl\|CDD\|36108	3518	3857	340	Gaps:27	13.56	2382	25.08	17.96	4e-18	KOG0890 KOG0890 KOG0890 Protein kinase of the PI-3 kinase family involved in mitotic growth DNA repair and meiotic recombination [Signal transduction mechanisms Chromatin structure and dynamics Replication recombination and repair Cell cycle control cell division chromosome partitioning].
	gnl\|CDD\|36109	3328	3856	529	Gaps:93	24.35	2341	22.11	14.04	9e-17	KOG0891 KOG0891 KOG0891 DNA-dependent protein kinase [Replication recombination and repair].
	gnl\|CDD\|36110	3550	3857	308	Gaps:34	11.26	2806	24.37	17.72	4e-08	KOG0892 KOG0892 KOG0892 Protein kinase ATM/Tel1 involved in telomere length regulation and DNA repair [Signal transduction mechanisms Chromatin structure and dynamics Replication recombination and repair Cell cycle control cell division chromosome partitioning].

Other analysis

Functional Gbrowse

Ortholog