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Database: UniProt
Entry: A0A310TPM0_XENLA
LinkDB: A0A310TPM0_XENLA
Original site: A0A310TPM0_XENLA 
ID   A0A310TPM0_XENLA        Unreviewed;       522 AA.
AC   A0A310TPM0; A0A974BRZ7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC108704994 {ECO:0000313|RefSeq:XP_018097227.1};
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|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018097227.1};
RN   [1] {ECO:0000313|RefSeq:XP_018097227.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018097227.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018097227.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_018097227.1; XM_018241738.2.
DR   AlphaFoldDB; A0A310TPM0; -.
DR   PaxDb; 8355-A0A310TPM0; -.
DR   GeneID; 108704994; -.
DR   KEGG; xla:108704994; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 108704994; Expressed in oocyte and 4 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; 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   4: Predicted;
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
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   REGION          198..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  59295 MW;  529C1F94E3444542 CRC64;
     MAAADLRAEL SCSICTSIYT DPVSLPCGHN FCQVCIGTTW DTQEETFQEN PSCPECRNRF
     SRRPELTTDW KLRGLVEKFC LTETEPGETG IFCTYCVLSP VPAAKSCLLC EASLCETHLR
     GHSKSAEHVL TQPTDSFMGR KCSVHHKVLE YYCCEESVCI CVSCCLAGEH RGHRVELLSE
     ASEKKKETLR KVLEKLRPER EETERGAQRL QERRREVAEK AAGEKERVTA LFRDIREQLE
     ALEKRLLSNI SSQKEKLTLT DLMEQLEIKK DELSRKIRHI EELCNMADPL TVLQERESHG
     AADNEGGRER HDIKVPAVGD LDVDLISETL LTGLAAIVTG VKGRIYGQEA TDLLLDINTA
     HNPVSVSGDR KSASYSLTDQ RHPQTPERFH VPQTLSSRSF PSGRHYWEVE VSESGNWRVG
     VAYPSIERRG GQSLIGINNK SWCLWRWNNK YTVRHDSKDT QLPHVPSSRR IRISLDYEAG
     RLSFYELSEP IRHLHTFTAT FTEPLHAAFC VWGDNVWVRI IS
//
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