Protein : Qrob_P0107200.2 Q. robur
Protein Identifier  ? Qrob_P0107200.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=3) PTHR23012//PTHR23012:SF57 - MEMBRANE ASSOCIATED RING FINGER // SUBFAMILY NOT NAMED (PTHR23012:SF57) Code Enzyme  EC:6.3.2.19
Gene Prediction Quality  validated Protein length 

Sequence

Length: 103  
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0 Synonyms

1 GO Terms

Identifier Name Description
GO:0008270 zinc ion binding Interacting selectively and non-covalently with zinc (Zn) ions.

24 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|tcc:TCM_004794 1 97 + 97 Gaps:5 43.67 229 80.00 6e-49 RING/FYVE/PHD zinc finger-containing protein putative
blastp_kegg lcl|vvi:100260678 1 93 + 93 Gaps:1 42.73 220 78.72 1e-46 uncharacterized LOC100260678
blastp_kegg lcl|cit:102627127 1 97 + 97 Gaps:2 40.93 237 79.38 2e-46 uncharacterized LOC102627127
blastp_kegg lcl|cic:CICLE_v10021987mg 1 97 + 97 Gaps:2 40.76 238 79.38 4e-46 hypothetical protein
blastp_kegg lcl|cam:101504360 1 93 + 93 Gaps:1 39.15 235 80.43 2e-45 uncharacterized LOC101504360
blastp_kegg lcl|rcu:RCOM_1347380 1 97 + 97 Gaps:2 44.60 213 73.68 5e-45 protein binding protein putative
blastp_kegg lcl|pop:POPTR_0014s11700g 1 93 + 93 Gaps:2 54.82 166 75.82 2e-44 POPTRDRAFT_664363 hypothetical protein
blastp_kegg lcl|pop:POPTR_0002s19770g 1 93 + 93 Gaps:2 42.72 213 76.92 4e-44 POPTRDRAFT_644832 hypothetical protein
blastp_kegg lcl|mtr:MTR_1g087150 1 92 + 92 none 39.32 234 77.17 7e-44 E3 ubiquitin-protein ligase MARCH6
blastp_kegg lcl|mtr:MTR_7g109460 1 93 + 93 none 42.47 219 72.04 1e-43 E3 ubiquitin-protein ligase MARCH3
blastp_uniprot_sprot sp|F4JKK0|SUD1_ARATH 20 80 + 61 Gaps:5 5.78 1108 40.62 3e-09 Probable E3 ubiquitin ligase SUD1 OS Arabidopsis thaliana GN SUD1 PE 1 SV 1
blastp_uniprot_sprot sp|Q32L65|MARH2_BOVIN 19 87 + 69 Gaps:7 25.31 245 41.94 8e-09 E3 ubiquitin-protein ligase MARCH2 OS Bos taurus GN MARCH2 PE 2 SV 1
blastp_uniprot_sprot sp|Q9H992|MARH7_HUMAN 20 72 + 53 Gaps:8 8.66 704 36.07 5e-08 E3 ubiquitin-protein ligase MARCH7 OS Homo sapiens GN MARCH7 PE 1 SV 1
blastp_uniprot_sprot sp|Q5R9W2|MARH7_PONAB 20 72 + 53 Gaps:8 8.63 707 36.07 5e-08 E3 ubiquitin-protein ligase MARCH7 OS Pongo abelii GN MARCH7 PE 2 SV 1
blastp_uniprot_sprot sp|Q3TZ87|MARH9_MOUSE 20 72 + 53 Gaps:2 14.66 348 41.18 6e-08 E3 ubiquitin-protein ligase MARCH9 OS Mus musculus GN March9 PE 2 SV 1
blastp_uniprot_sprot sp|Q86YJ5|MARH9_HUMAN 20 72 + 53 Gaps:2 14.74 346 41.18 6e-08 E3 ubiquitin-protein ligase MARCH9 OS Homo sapiens GN MARCH9 PE 1 SV 2
blastp_uniprot_sprot sp|Q6ZQ89|MARH6_MOUSE 20 97 + 78 Gaps:11 9.57 909 33.33 2e-07 E3 ubiquitin-protein ligase MARCH6 OS Mus musculus GN March6 PE 2 SV 2
blastp_uniprot_sprot sp|Q5R9W1|MARH6_PONAB 20 97 + 78 Gaps:11 9.56 910 33.33 2e-07 E3 ubiquitin-protein ligase MARCH6 OS Pongo abelii GN MARCH6 PE 2 SV 1
blastp_uniprot_sprot sp|O60337|MARH6_HUMAN 20 97 + 78 Gaps:11 9.56 910 33.33 2e-07 E3 ubiquitin-protein ligase MARCH6 OS Homo sapiens GN MARCH6 PE 1 SV 2
blastp_uniprot_sprot sp|Q8CBH7|MARHB_MOUSE 20 71 + 52 Gaps:2 12.50 400 40.00 2e-07 E3 ubiquitin-protein ligase MARCH11 OS Mus musculus GN March11 PE 2 SV 2
rpsblast_cdd gnl|CDD|128983 19 67 + 49 Gaps:1 97.96 49 52.08 6e-12 smart00744 RINGv The RING-variant domain is a C4HC3 zinc-finger like motif found in a number of cellular and viral proteins. Some of these proteins have been shown both in vivo and in vitro to have ubiquitin E3 ligase activity. The RING-variant domain is reminiscent of both the RING and the PHD domains and may represent an evolutionary intermediate. To describe this domain the term PHD/LAP domain has been used in the past. Extended description: The RING-variant (RINGv) domain contains a C4HC3 zinc-finger-like motif similar to the PHD domain while some of the spacing between the Cys/His residues follow a pattern somewhat closer to that found in the RING domain. The RINGv domain similar to the RING PHD and LIM domains is thought to bind two zinc ions co-ordinated by the highly conserved Cys and His residues. RING variant domain: C-x (2) -C-x(10-45)-C-x (1) -C-x (7) -H-x(2)-C-x(11-25)-C-x(2)-C As opposed to a PHD: C-x(1-2) -C-x (7-13)-C-x(2-4)-C-x(4-5)-H-x(2)-C-x(10-21)-C-x(2)-C Classical RING domain: C-x (2) -C-x (9-39)-C-x(1-3)-H-x(2-3)-C-x(2)-C-x(4-48) -C-x(2)-C.
rpsblast_cdd gnl|CDD|193379 20 67 + 48 Gaps:1 100.00 47 51.06 4e-10 pfam12906 RINGv RING-variant domain.
rpsblast_cdd gnl|CDD|34782 20 72 + 53 Gaps:1 4.43 1175 40.38 2e-09 COG5183 SSM4 Protein involved in mRNA turnover and stability [RNA processing and modification].
rpsblast_kog gnl|CDD|36822 20 79 + 60 Gaps:1 18.89 323 42.62 2e-14 KOG1609 KOG1609 KOG1609 Protein involved in mRNA turnover and stability [RNA processing and modification].

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 19 72 54 G3DSA:3.30.40.10 none none IPR013083
ProSiteProfiles 12 74 63 PS51292 "UniPathway:UPA00143" Zinc finger RING-CH-type profile. IPR011016
Pfam 20 67 48 PF12906 "UniPathway:UPA00143" RING-variant domain IPR011016
PANTHER 20 81 62 PTHR23012 none none none
SUPERFAMILY 15 72 58 SSF57850 none none none
SMART 19 68 50 SM00744 "UniPathway:UPA00143" The RING-variant domain is a C4HC3 zinc-finger like motif found in a number of cellular and viral proteins. Some of these proteins have been shown both in vivo and in vitro to have ubiquitin E3 ligase activity. IPR011016
PANTHER 20 81 62 PTHR23012:SF57 none none none

0 Localization

4 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2015_nP_3P Qrob_Chr12 12 v_10140_295 v_838_303 16 14,69 18,01 lod 5.1 13.7
Bourran2_2015_nSecLBD_3P Qrob_Chr12 12 s_A4YYC_633 s_2F1IZB_703 18,64 18,01 21,53 lod 6.5 17.2
Bourran2_2014_nSeqBC_3P Qrob_Chr12 12 s_1EO8V5_710 s_1A2VMU_355 11,04 0 32,58 lod 1,7196 4,7

0 Targeting