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Database: UniProt
Entry: A0A093BB60_CHAPE
LinkDB: A0A093BB60_CHAPE
Original site: A0A093BB60_CHAPE 
ID   A0A093BB60_CHAPE        Unreviewed;       353 AA.
AC   A0A093BB60;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   03-MAY-2023, entry version 26.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369081};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU369081};
DE   AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|RuleBase:RU369081};
DE   Flags: Fragment;
GN   ORFNames=M959_02397 {ECO:0000313|EMBL:KFU85721.1};
OS   Chaetura pelagica (Chimney swift) (Hirundo pelagica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes; Apodidae;
OC   Apodinae; Chaetura.
OX   NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU85721.1, ECO:0000313|Proteomes:UP000031515};
RN   [1] {ECO:0000313|EMBL:KFU85721.1, ECO:0000313|Proteomes:UP000031515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M959 {ECO:0000313|EMBL:KFU85721.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000031515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25504712; DOI=10.1126/science.1251385;
RG   Avian Genome Consortium;
RA   Zhang G., Li C., Li Q., Li B., Larkin D.M., Lee C., Storz J.F., Antunes A.,
RA   Greenwold M.J., Meredith R.W., Odeen A., Cui J., Zhou Q., Xu L., Pan H.,
RA   Wang Z., Jin L., Zhang P., Hu H., Yang W., Hu J., Xiao J., Yang Z., Liu Y.,
RA   Xie Q., Yu H., Lian J., Wen P., Zhang F., Li H., Zeng Y., Xiong Z., Liu S.,
RA   Zhou L., Huang Z., An N., Wang J., Zheng Q., Xiong Y., Wang G., Wang B.,
RA   Wang J., Fan Y., da Fonseca R.R., Alfaro-Nunez A., Schubert M., Orlando L.,
RA   Mourier T., Howard J.T., Ganapathy G., Pfenning A., Whitney O., Rivas M.V.,
RA   Hara E., Smith J., Farre M., Narayan J., Slavov G., Romanov M.N.,
RA   Borges R., Machado J.P., Khan I., Springer M.S., Gatesy J., Hoffmann F.G.,
RA   Opazo J.C., Hastad O., Sawyer R.H., Kim H., Kim K.W., Kim H.J., Cho S.,
RA   Li N., Huang Y., Bruford M.W., Zhan X., Dixon A., Bertelsen M.F.,
RA   Derryberry E., Warren W., Wilson R.K., Li S., Ray D.A., Green R.E.,
RA   O'Brien S.J., Griffin D., Johnson W.E., Haussler D., Ryder O.A.,
RA   Willerslev E., Graves G.R., Alstrom P., Fjeldsa J., Mindell D.P.,
RA   Edwards S.V., Braun E.L., Rahbek C., Burt D.W., Houde P., Zhang Y.,
RA   Yang H., Wang J., Jarvis E.D., Gilbert M.T., Wang J.;
RT   "Comparative genomics reveals insights into avian genome evolution and
RT   adaptation.";
RL   Science 346:1311-1320(2014).
CC   -!- FUNCTION: E3 ubiquitin ligase. {ECO:0000256|RuleBase:RU369081}.
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         ECO:0000256|RuleBase:RU369081};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369081}.
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DR   EMBL; KN126004; KFU85721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093BB60; -.
DR   Proteomes; UP000031515; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd16817; mRING-HC-C3HC5_RNF157; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22996:SF1; E3 UBIQUITIN LIGASE RNF157; 1.
DR   PANTHER; PTHR22996; MAHOGUNIN; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031515};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369081};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU369081};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369081};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          248..287
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFU85721.1"
FT   NON_TER         353
FT                   /evidence="ECO:0000313|EMBL:KFU85721.1"
SQ   SEQUENCE   353 AA;  39422 MW;  A13BC51C4EF3F91E CRC64;
     GSYFANHFIM GGEKFDSTQP EGYLFGENSD LNFLGNRPVV FPYAAPPPQE PVKTLRSLIN
     IRKDTLRLVR CSEEVKTPGE EVSKAKVHYN VEFTFDTDAR VAITIYYQAS EEFHNGVASY
     IPRDNSLQSE TVHYKQGVCQ QFCVPSHTVD PSEWSEEELG FDLDREVYPM VVHAVVDEGE
     EHIGHCHVLL ATFEKHSDGT FCVKPLKQKQ VVDGVSYLLQ EIYGIENKYN TQDSKVAEDE
     VSDNSAECVV CLSDVRDTLI LPCRHLCLCN TCADTLRYQA NNCPICRLPF RALLQIRAMR
     KKLGPLSPTS FNPIIASQAS DSEEPSSSEH VPPGYEVVSL LEALNGPLTP SPA
//
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