ID   A0A091LRK5_CARIC        Unreviewed;      1191 AA.
AC   A0A091LRK5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=N322_13694 {ECO:0000313|EMBL:KFP60994.1};
OS   Cariama cristata (Red-legged seriema).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX   NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP60994.1, ECO:0000313|Proteomes:UP000054116};
RN   [1] {ECO:0000313|EMBL:KFP60994.1, ECO:0000313|Proteomes:UP000054116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP60994.1};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
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DR   EMBL; KK504827; KFP60994.1; -; Genomic_DNA.
DR   RefSeq; XP_009699636.1; XM_009701334.1.
DR   AlphaFoldDB; A0A091LRK5; -.
DR   GeneID; 104162565; -.
DR   CTD; 54542; -.
DR   OrthoDB; 2909513at2759; -.
DR   Proteomes; UP000054116; Unassembled WGS sequence.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd16782; mRING-HC-C3HC3D_Roquin2; 1.
DR   Gene3D; 1.20.120.1790; -; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR041523; ROQ_II.
DR   InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13139; RING FINGER AND CCCH-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13139:SF2; ROQUIN-2; 1.
DR   Pfam; PF18386; ROQ_II; 1.
DR   Pfam; PF21206; Roquin_1_2-like_ROQ; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          14..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          410..438
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         410..438
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          519..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..683
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1191 AA;  131568 MW;  0E65735C3D8956E1 CRC64;
     MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC PFDQTAINTD
     IDVLPVNFAL LQLVGAQVPD HQTVKLSNVG ENKHYEVAKK CVEDLALYLK PLSGGKGVAS
     LNQSALSRPM QRKLVTLVNC QLVEEEGRVR AMRAARSLGE RTVTELILQH QNPQQLSANL
     WAAVRARGCQ FLGPAMQEEA LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG
     HVVQLLYRAS CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW
     SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL RPHLELLANI
     DPNPDAASPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH ETPQPQPNSK YKTSMCRDLR
     QQGGCPRGTN CTFAHSQEEL EKYRLRNKKI SATVRTFPLL NKVGVNSTVS TTTGNVISVI
     GSPEATGKMV PSTNGIANLE SGVPQLIPRC ADTSLRTLEN TKKGGKTGAN GQNVSASPTE
     SLPENKIGSP PKTPVSQAAA TSAGPPNIGT EVNSVPPKSS PFVPRVPVYP PHSDNVQYFQ
     DPRTQLSYEV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSN NVPESSLPPA SVPYADHYST
     FPPRDRLNSP YQPPPPQPYG PVPPVPSGMY APVYDSRRIW RPQMYPRDDI IRSNSLPPMD
     VMHSSVYQTS LRERYNSLDG YYSVACQPPN EQRTVPLPRE PCGHLKTGYD EQLRRKPEQW
     AQYHTQKTPL VSSTLPMATP SPTPPSPLFS VDFSTEFSEG VSDLSGTKFE EDHLSHYSPW
     SCGTIGSCIN AIDSEPKDVI ANSNAVLMDL DSGDVKRRVH LFETQRRAKE EDPIIPFSDG
     PIISKWGAIS RSSRTGYHTT DPIQATASQG SATKPISVSD YVPYVNAVDS RWSAYGSDST
     SSARYAERDR FIVTDLSGHR KHSSTGDLLS IELQQAKSNS LLLQREANAL AMQQKWNSLD
     EGSRLTLNLL SKEIDLRNGE TDYTEDCADT KPDRDIELEL STLDTDEPDG QGEQIEEILD
     IQLGISSQDD QLLNGTTVEN GHLLKQHQKE SMEQKRQSLG EDLVILEEQK TILPVTSCFS
     QPITTSVSNA SCLPISTSVS VGSLILKTAH IMSEDKNDFL KPVANGRMVN S
//