Protein : Qrob_P0761160.2 Q. robur
Protein Identifier  ? Qrob_P0761160.2 Organism . Name  Quercus robur
Score  71.3 Score Type  egn
Protein Description  (M=1) KOG1046//KOG1932 - Puromycin-sensitive aminopeptidase and related aminopeptidases [Amino acid transport and metabolism Posttranslational modification protein turnover chaperones]. // TATA binding protein associated factor [Transcription]. Gene Prediction Quality  validated
Protein length 

Sequence

Length: 222  
Kegg Orthology  K03128
Paste the following link
Lists
This Protein isn't in any lists. Upload a list.

Sequence Feature Displayer

Protein Sequence Displayer

J Browse Displayer

0 Synonyms

2 GO Terms

Identifier Name Description
GO:0008270 zinc ion binding Interacting selectively and non-covalently with zinc (Zn) ions.
GO:0008237 metallopeptidase activity Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

27 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa000205mg 12 219 + 208 none 14.15 1470 79.33 4e-109 hypothetical protein
blastp_kegg lcl|pvu:PHAVU_003G177400g 12 219 + 208 none 15.05 1382 78.37 5e-109 hypothetical protein
blastp_kegg lcl|pmum:103342208 12 219 + 208 none 13.96 1490 78.85 1e-108 transcription initiation factor TFIID subunit 2
blastp_kegg lcl|gmx:100792795 5 219 + 215 Gaps:2 15.63 1388 75.12 1e-107 transcription initiation factor TFIID subunit 2-like
blastp_kegg lcl|gmx:100803129 12 219 + 208 none 14.99 1388 76.92 3e-107 transcription initiation factor TFIID subunit 2-like
blastp_kegg lcl|cam:101506465 12 219 + 208 none 14.91 1395 76.44 4e-107 transcription initiation factor TFIID subunit 2-like
blastp_kegg lcl|fve:101293784 12 219 + 208 none 14.15 1470 78.85 4e-103 transcription initiation factor TFIID subunit 2-like
blastp_kegg lcl|cmo:103496328 12 219 + 208 none 15.28 1361 73.56 3e-101 transcription initiation factor TFIID subunit 2
blastp_kegg lcl|mdm:103437964 12 219 + 208 Gaps:4 14.34 1464 77.14 6e-101 transcription initiation factor TFIID subunit 2
blastp_kegg lcl|csv:101210662 12 219 + 208 none 15.27 1362 73.08 1e-100 transcription initiation factor TFIID subunit 2-like
blastp_pdb 3mdj_C 89 177 + 89 Gaps:3 9.77 921 32.22 8e-06 mol:protein length:921 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 3mdj_B 89 177 + 89 Gaps:3 9.77 921 32.22 8e-06 mol:protein length:921 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 3mdj_A 89 177 + 89 Gaps:3 9.77 921 32.22 8e-06 mol:protein length:921 Endoplasmic reticulum aminopeptidase 1
blastp_uniprot_sprot sp|Q8LPF0|TAF2_ARATH 9 219 + 211 none 15.18 1390 61.14 3e-84 Transcription initiation factor TFIID subunit 2 OS Arabidopsis thaliana GN TAF2 PE 2 SV 1
blastp_uniprot_sprot sp|Q32PW3|TAF2_DANRE 18 193 + 176 Gaps:2 14.61 1191 40.23 1e-32 Transcription initiation factor TFIID subunit 2 OS Danio rerio GN taf2 PE 2 SV 2
blastp_uniprot_sprot sp|Q5ZIT8|TAF2_CHICK 18 193 + 176 Gaps:2 14.90 1168 39.08 4e-32 Transcription initiation factor TFIID subunit 2 OS Gallus gallus GN TAF2 PE 2 SV 1
blastp_uniprot_sprot sp|Q6P1X5|TAF2_HUMAN 18 193 + 176 Gaps:2 14.51 1199 38.51 5e-32 Transcription initiation factor TFIID subunit 2 OS Homo sapiens GN TAF2 PE 1 SV 3
blastp_uniprot_sprot sp|Q8C176|TAF2_MOUSE 18 190 + 173 Gaps:2 15.49 1104 39.18 1e-31 Transcription initiation factor TFIID subunit 2 OS Mus musculus GN Taf2 PE 2 SV 2
blastp_uniprot_sprot sp|Q24325|TAF2_DROME 18 192 + 175 Gaps:2 14.17 1221 40.46 3e-31 Transcription initiation factor TFIID subunit 2 OS Drosophila melanogaster GN Taf2 PE 1 SV 2
blastp_uniprot_sprot sp|P87121|TAF2_SCHPO 17 202 + 186 Gaps:18 16.72 1172 31.63 2e-18 Transcription initiation factor TFIID subunit 2 OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN taf2 PE 3 SV 3
blastp_uniprot_sprot sp|P23255|TAF2_YEAST 79 194 + 116 Gaps:10 7.53 1407 37.74 2e-10 Transcription initiation factor TFIID subunit 2 OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN TAF2 PE 1 SV 3
blastp_uniprot_sprot sp|Q8C129|LCAP_MOUSE 62 184 + 123 Gaps:5 12.10 1025 25.81 1e-05 Leucyl-cystinyl aminopeptidase OS Mus musculus GN Lnpep PE 1 SV 1
rpsblast_cdd gnl|CDD|189018 17 205 + 189 Gaps:2 36.88 507 54.55 5e-74 cd09839 M1_TAF2 TATA binding protein (TBP) associated factor 2. This family includes TATA binding protein (TBP) associated factor 2 (TAF2 TBP-associated factor TAFII150 transcription initiation factor TFIID subunit 2 RNA polymerase II TBP-associated factor subunit B) and has homology to the aminopeptidase N (APN) subfamily belonging to the M1 gluzincin family. TAF2 is part of the TFIID multidomain subunit complex essential for transcription of most protein-encoded genes by RNA polymerase II. TAF2 is known to interact with the initiator element (Inr) found at the transcription start site of many genes thus possibly playing a key role in promoter binding as well as start-site selection. Image analysis has shown TAF2 to form a complex with TAF1 and TBP inferring its role in promoter recognition. Peptidases in the M1 family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TAF2 however does not seem to contain any of the active site residues.
rpsblast_cdd gnl|CDD|189002 28 196 + 169 Gaps:3 40.79 407 25.30 4e-15 cd09595 M1 Peptidase M1 family contains aminopeptidase N and leukotriene A4 hydrolase. M1 Peptidase family includes aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. APN consists of a small N-terminal cytoplasmic domain a single transmembrane domain and a large extracellular ectodomain that contains the active site. It preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. APN expression is dysregulated in many inflammatory diseases and is enhanced in numerous tumor cells making it a lead target in the development of anti-cancer and anti-inflammatory drugs. LTA4H is a bifunctional enzyme possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different but overlapping sites. The activity and physiological relevance of the aminopeptidase in LTA4H is as yet unknown while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4) a potent chemotaxin that is fundamental to the inflammatory response of mammals.
rpsblast_cdd gnl|CDD|189010 19 196 + 178 Gaps:40 42.89 415 24.72 1e-11 cd09603 M1_APN_4 Peptidase M1 family Aminopeptidase N. This family contains mostly bacterial and some archaeal aminopeptidase N (APN CD13 Alanyl aminopeptidase EC 3.4.11.2) a Type II integral membrane protease belonging to the M1 gluzincin family. APN consists of a small N-terminal cytoplasmic domain a single transmembrane domain and a large extracellular ectodomain that contains the active site. It preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and in higher eukaryotes is present in a variety of human tissues and cell types (leukocyte fibroblast endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain rheumatoid arthritis multiple sclerosis systemic sclerosis systemic lupus erythematosus polymyositis/dermatomyosytis and pulmonary sarcoidosis and is enhanced in tumor cells such as melanoma renal prostate pancreas colon gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation thus considered a marker of differentiation. Thus APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets Some APNs have been used commercially such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae causing extensive damage. Several different toxins including Cry1Aa Cry1Ab Cry1Ac Cry1Ba Cry1Ca and Cry1Fa have been shown to bind to APNs however a direct role of APN in cytotoxicity has been yet to be firmly established.
rpsblast_kog gnl|CDD|37143 18 205 + 188 Gaps:2 15.76 1180 44.09 1e-50 KOG1932 KOG1932 KOG1932 TATA binding protein associated factor [Transcription].
rpsblast_kog gnl|CDD|36264 86 206 + 121 Gaps:5 13.61 882 20.83 3e-09 KOG1046 KOG1046 KOG1046 Puromycin-sensitive aminopeptidase and related aminopeptidases [Amino acid transport and metabolism Posttranslational modification protein turnover chaperones].

8 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 28 188 161 PF01433 none Peptidase family M1 IPR014782
Phobius 23 197 175 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
PANTHER 17 197 181 PTHR15137 none none none
Phobius 198 218 21 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 6 22 17 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 1 5 5 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
SUPERFAMILY 64 198 135 SSF55486 none none none
Phobius 219 221 3 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none

3 Localization

Analysis Start End Length
TMHMM 5 22 17
SignalP_EUK 1 23 22
TMHMM 198 220 22

5 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2004_QTL5_peak_Bud_burst_A4 Qrob_Chr10 10 s_1C8OKQ_688 v_12844_707 25,6 13,9 39,9 lod 2,7 6,1
Bourran2_2002_QTL13_peak_Bud_burst_3P Qrob_Chr10 10 s_1B1AG7_637 s_1A3A1N_709 19,44 0 49,44 lod 3 5,6
Bourran2_2002_QTL15_peak_Bud_burst_A4 Qrob_Chr10 10 v_7579_71 s_1ATZMJ_189 23,94 0 43,64 lod 3,7 5,4
Bourran2_2014_vSeqBC_A4 Qrob_Chr10 10 s_1BAM4E_1326 s_1C0HD0_1012 36,88 7,71 46,03 lod 2,6164 7,3
Champenoux_2015_nPriLBD_3P Qrob_Chr10 10 v_15000_157 v_15000_310 15,68 15,9 15,91 lod 2.4 5.5

0 Targeting