ID A0A093Q6F0_PHACA Unreviewed; 1031 AA.
AC A0A093Q6F0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE Flags: Fragment;
GN ORFNames=N336_00672 {ECO:0000313|EMBL:KFW82020.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW82020.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW82020.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW82020.1};
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=[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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL416352; KFW82020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Q6F0; -.
DR Proteomes; UP000053238; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd20361; Rcat_RBR_ANKIB1; 1.
DR CDD; cd16774; RING-HC_RBR_ANKIB1; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047564; Rcat_RBR_ANKIB1.
DR InterPro; IPR047563; RING-HC_RBR_ANKIB1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685:SF465; ANKYRIN REPEAT AND IBR DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00248; ANK; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:PRU00175}.
FT REPEAT 82..114
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 267..507
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 271..317
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 219..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW82020.1"
FT NON_TER 1031
FT /evidence="ECO:0000313|EMBL:KFW82020.1"
SQ SEQUENCE 1031 AA; 115927 MW; 5811007BB57C12C0 CRC64;
TFLFVRDGNP NKRNVHNETS MHLLCMGPQI MISEGALHPR LTRPSEDDCR RADCLQMILK
WKGAKLDEGQ YERAAIDAVD NKKNTPLHYA AASGMKTCVE LLVKHGGDLF AENENKDTPC
DCAEKQHHKE LALNLESRMV FSRDPEAESI EAEYAALDKK EPYEGLRLQD LRRLKDMLIV
ESADMLQAPL FTAEALLRAH DWDREKLLEA WMSNPENCCQ RSGVQMPTPP PSGYNAWDTL
PSPRTPRTTR SSVTSPDEIS PSPGDIETAV CDICMCNISV FEDPVDMPCG HDFCRACWEA
FLNLKIQEGE AHNIFCPAYD CFQLVPVDII ESVVSKEMDK RYLQFDIKAF VENNPAIKWC
PIPGCERAVR LTRQGSNSTG SDTLSFPMLK APAVDCGKGH LFCWECLGEA HEPCDCQTWK
DWLQKISEMK PEELVGVSEA YEDAANCLWL LTNSKPCANC KSPIQKNEGC NHMQCAKCKY
DFCWICLEEW KKHSSSTGGY YRCTRYEVIQ HVEEQSKEMT VEAEKKHRRF QELDRFMHYY
TRFKNHELSY QLEQRLLKTA KEKMEQLSRA LSGTEGGCPD TTFIEDAVQE LLKTRRILKC
SYPYGFFLEP KSTKKEIFEL MQTDLEMVTE DLAQKVNRPY LRTPRHKIIR AACLVQQKRQ
EFLASVARGV APADSPEAPR RSFAGGTWDW EYLGFASPEE YAEFQYRRRH RQRRRGDMHS
LLSNTPDPDD PSESTLDTQE GGSSRRHGTS MVSSASMGIL HSSSLHDYTP VSHSENQDSL
QALSSLDEDD PNILLAIQLS LQESGLAIDE ETRDFLNNEA SLGAIGTSLP TRLDSAPISI
DNPRGALSSS ELLELGDSLM RLGAGDDPFS ADRLHSHPCS DTRSGLYSTS SDADSSSQDP
NTNENLLGNI MAWFHDMNPQ SIALIPSTST ETDEDSRQPS TEDRSAGQPN LIDTGPEPQE
EHALFEDALK NEGRGTQTEE STSEENIIPG ETVSQSSDNN REVASTLDAS GDTSSQTPQT
SSEWIEHVHL V
//
