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Database: UniProt
Entry: A0A553P4L1_TIGCA
LinkDB: A0A553P4L1_TIGCA
Original site: A0A553P4L1_TIGCA 
ID   A0A553P4L1_TIGCA        Unreviewed;      1039 AA.
AC   A0A553P4L1;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   02-APR-2025, entry version 18.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=TCAL_09958 {ECO:0000313|EMBL:TRY72627.1};
OS   Tigriopus californicus (Marine copepod).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Hexanauplia; Copepoda; Harpacticoida; Harpacticidae; Tigriopus.
OX   NCBI_TaxID=6832 {ECO:0000313|EMBL:TRY72627.1, ECO:0000313|Proteomes:UP000318571};
RN   [1] {ECO:0000313|EMBL:TRY72627.1, ECO:0000313|Proteomes:UP000318571}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=San Diego {ECO:0000313|EMBL:TRY72627.1,
RC   ECO:0000313|Proteomes:UP000318571};
RX   PubMed=29988158; DOI=.1038/s41559-018-0588-1;
RA   Barreto F.S., Watson E.T., Lima T.G., Willett C.S., Edmands S., Li W.,
RA   Burton R.S.;
RT   "Genomic signatures of mitonuclear coevolution across populations of
RT   Tigriopus californicus.";
RL   Nat. Ecol. Evol. 2:1250-1257(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TRY72627.1}.
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DR   EMBL; VCGU01000008; TRY72627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A553P4L1; -.
DR   STRING; 6832.A0A553P4L1; -.
DR   EnsemblMetazoa; TCAL_09958-PA_mrna; TRY72627.1; TCAL_09958.
DR   Proteomes; UP000318571; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd20338; BRcat_RBR_RNF19; 1.
DR   CDD; cd20355; Rcat_RBR_RNF19; 1.
DR   FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000318571};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
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:PRU00175}.
FT   TRANSMEM        553..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        604..637
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          308..543
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          312..359
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..96
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..160
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..182
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..216
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..287
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..725
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..840
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..956
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1028
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1039 AA;  111001 MW;  30027F64790E8773 CRC64;
     MARPHPGQIE AGPRGHVAPD CGPTVSLAPS SSAPPSPPSL SGFSIARLTR GLSRDWARIS
     IPPVATPPTT QMKFGWPKSS PSTAPPRQPS PAPRPTSAPV DWAGTATPTH PRRAKFEADR
     RKEEQPRRKK ALPPFRTRLD LARAHSGLAG SSRPSASPGA DGLLPMPDSP PVRGRRPARF
     SLRRLFDGHP LLPPPWGQPL TSAWPSRSRR PAHPHRNGAG LEEGGSRTNA TTPSSTRSRP
     FFPPDSTSER SVTHPSSASS AGMNGRDWRG DSHAPYPSSS CASSLAGGSA GPSSAHYPAS
     FVGADGRAMR ECSLCLVSLP LTEFPSLRNC HHLFCFDCLQ IYVKIELQEG RVNVRCPQCV
     EPLHPNDIEL FIGDRNSNLQ HLYEFLMLRR ILATDPDTRW CPGPNCTFAV IAAGCASCPK
     ITCERPGCGF SFCYHCKAEW HPNQTCDMAR AQRQGGHAQP GSLMMSMMNA STVSFSGQAD
     SRGPQNPSEV KVCPRCDVLI VKMDDGSCNH MTCSVCGVEF CWLCMKEISD LHYLSPSGCT
     FWGKKPWSRK KKLLWQLGTL VGAPVGIALL AGISIPAMII GIPVWVGRKL YAQYNKAPIH
     KRNLIIASGV SASVIVSPVI AALAVSIGVP ILLAYVYGVV PISLCRSEGC GVSTSSNGVS
     IDVDEELNPD TDLSHMPFRP MVMDNYSTAT GPSANWNPSI GEMSLGRSMS MGSTSHLDHE
     ADRESASNTA VAGTSRTVSL ASSSVLMGGV TSIRGVSTEG LSETASLTDP NQDGASTRAL
     AGSILAYKTD TQSVNSFRTG GDPSDILPAS GDEISLRSLP LGSVPSQLPR SLSPTASCRS
     SGHEDIVRRS GRRRTNSNVP HLERQLSEDA EDTEAAALAL TGNDRVRFDD NVSFIDETGS
     CTLMVNAPPT CIEEGLSAGV KTGNNKGLKS DKPCPSNSSS TPSTTTSVSI VSGSSNLNGP
     TPIPLREETP EELAGMISPE IQRHYPASWS TRVNPSPCPD LIVSSSLNMS SNLEEKELEE
     RQSADRNVTR LQIGEETDQ
//
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