GenomeNet

Database: UniProt
Entry: Q6NRB1_XENLA
LinkDB: Q6NRB1_XENLA
Original site: Q6NRB1_XENLA 
ID   Q6NRB1_XENLA            Unreviewed;       540 AA.
AC   Q6NRB1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 119.
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   Name=trim25l.L {ECO:0000313|Xenbase:XB-GENE-6251559};
GN   Synonyms=LOC431932 {ECO:0000313|EMBL:AAH70851.1}, trim25l100490741
GN   {ECO:0000313|Xenbase:XB-GENE-6251559}, trim25l100490741.L
GN   {ECO:0000313|Xenbase:XB-GENE-6251559};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH70851.1};
RN   [1] {ECO:0000313|EMBL:AAH70851.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocytes {ECO:0000313|EMBL:AAH70851.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) 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};
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DR   EMBL; BC070851; AAH70851.1; -; mRNA.
DR   RefSeq; NP_001084882.2; NM_001091413.2.
DR   AlphaFoldDB; Q6NRB1; -.
DR   DNASU; 431932; -.
DR   GeneID; 431932; -.
DR   KEGG; xla:431932; -.
DR   AGR; Xenbase:XB-GENE-6251559; -.
DR   CTD; 431932; -.
DR   Xenbase; XB-GENE-6251559; trim25l.L.
DR   OrthoDB; 2939962at2759; -.
DR   Bgee; 431932; Expressed in egg cell and 18 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   CDD; cd19769; Bbox2_TRIM16-like; 1.
DR   CDD; cd16597; RING-HC_TRIM25_C-IV; 1.
DR   CDD; cd12891; SPRY_PRY_C-I_2; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
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; PTHR25465:SF39; B BOX AND SPRY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          25..69
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          149..190
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          347..540
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          248..297
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAH70851.1"
SQ   SEQUENCE   540 AA;  60591 MW;  54D39898C67E6D5C CRC64;
     GALCDSQTQK SVMAAAADLR DELNCSVCLT IYSDPVMLPC GHNFCQGCIV QVLDTQEATG
     GVYTCPECRA QYMERPALQR NRTLGNIAER FFCAQPEPDG TGIFCTYCIH SPVPAAKSCL
     LCEASLCESH VRVHSRSAEH VLTTPTAALE MRKCSVHREP LKYYCYVDSS CICASCCLAG
     QHKRHRVELL SDASEKKKEK LRKVLLNLPL MIEEAERGGW RLQERRREVQ EQAAAETERV
     VALFVDIRER LEALEQRVLR EVARQEEELS LQVSELIQQL EVKKEELSRK ILQTEELCNM
     ADPLAVLQAG ESDRAEDDGG REGSDPKVLT VGDLDKDLIS ETLHSGLDSI VTVAKGWGVY
     GKGATHIRLD IDTASNNVAV SEDRRTASWT SANQLRPQTP SRFIGYQVLS NNSFTSGQYF
     WDMEVSESGS WRVGVAYPSI GRKGNQFWIG NNIKSWCLWR WNNGYSVRHD SHGTDLPQVP
     SCTRIRISLD YQAGRLSFYE LGEPITHLHT FTASFTEPLH AAFWVWKDTL RGHSLVKVIS
//
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