GenomeNet

Database: UniProt
Entry: A0A091NMW8_APAVI
LinkDB: A0A091NMW8_APAVI
Original site: A0A091NMW8_APAVI 
ID   A0A091NMW8_APAVI        Unreviewed;       649 AA.
AC   A0A091NMW8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   Flags: Fragment;
GN   ORFNames=N311_03324 {ECO:0000313|EMBL:KFP90259.1};
OS   Apaloderma vittatum (Bar-tailed trogon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX   NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP90259.1, ECO:0000313|Proteomes:UP000054244};
RN   [1] {ECO:0000313|EMBL:KFP90259.1, ECO:0000313|Proteomes:UP000054244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP90259.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC       {ECO:0000256|ARBA:ARBA00008518}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL386982; KFP90259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091NMW8; -.
DR   Proteomes; UP000054244; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19806; Bbox1_TRIM32_C-VII; 1.
DR   CDD; cd14961; NHL_TRIM32_like; 1.
DR   CDD; cd16587; RING-HC_TRIM32_C-VII; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR047051; TRIM32_Bbox1_Znf.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR25464:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM32; 1.
DR   PANTHER; PTHR25464; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR   Pfam; PF01436; NHL; 3.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51125; NHL; 5.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          20..65
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          95..138
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          354..397
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          411..454
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          460..495
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          558..601
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          612..642
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          318..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          139..173
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP90259.1"
FT   NON_TER         649
FT                   /evidence="ECO:0000313|EMBL:KFP90259.1"
SQ   SEQUENCE   649 AA;  72127 MW;  9AC0D5E4C51D72B6 CRC64;
     KAMAAAPHLN SDALREVLEC PICMESFTEE HLRPKLLHCG HTICKQCLEK LLANSINGIR
     CPFCSKITRI TSLAQLTDNL TVLKIIDTAG LGEVVGLLMC KVCGRRLPRH FCKNCSLVLC
     EPCKEASHMP QGHRVIAIKE AAEERRREFG TRLARLRELM GDLQKRKAAL EGVSRDLQSR
     YKAVLQDYSK EERKIQEELA RSRKFFTTSL SEVEKVNNQV MEEQAYLLNL AEVQIMSRCD
     YFLAKIKQGD IALLEEAADE EEPELTNNLP KELTLEEVEL LKVSHVGPLQ IGQVVKKPRT
     VNMEESFMET AASSSASFRE PDLVQEEGGC TPNSSPAKPR MPEAATSIQQ CHFIRKMGSK
     GSLPGMFNLP VSLHVTLQGE VLVADRGNFR IQVFTRKGFL KEIRRSPSGI DSFVLSFLGA
     DLPNLTPLSV TMNCHGLIGV TDSYDNSVKV YTMDGHCVAC HRSQLSKPWG IAALPSGQFV
     VTDVEGGKLW CFTVDRGVGV VKYSCLCSAV RPKFVTCDAE GTIYFTQGLG LNLENRQYEH
     HLEGGFSIGS VGPDGQLGRQ ISHFFSENED FRCIAGMCVD ARGDLIVADS SRKEILHFPK
     GGGYNILIRE GLTCPVGIAI TPKGQLLVLD CWDHCIKIYS YHLRRYSTP
//
DBGET integrated database retrieval system