ID A0A1S3FYN4_DIPOR Unreviewed; 1091 AA.
AC A0A1S3FYN4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=Ankib1 {ECO:0000313|RefSeq:XP_012881490.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012881490.1};
RN [1] {ECO:0000313|RefSeq:XP_012881490.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012881490.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_012881490.1; XM_013026036.1.
DR AlphaFoldDB; A0A1S3FYN4; -.
DR GeneID; 105992935; -.
DR KEGG; dord:105992935; -.
DR CTD; 54467; -.
DR InParanoid; A0A1S3FYN4; -.
DR OrthoDB; 3084186at2759; -.
DR Proteomes; UP000081671; Unplaced.
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:SF437; ANKYRIN REPEAT AND IBR DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00248; ANK; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
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 145..177
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 330..570
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 334..380
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 293..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 613..640
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 301..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1091 AA; 122602 MW; 31CB36A0FA14D2A3 CRC64;
MGNTTTKFRK ALINGDENLA CQIYENNPQL KESLDPNTSY GEPYQHNTPL HYAARHGMNR
ILGTFLFGRD GNPNKRNVHN ETSMHLLCMG PQIMISEGAL HPRLARPVED DFRRADCLQM
ILRWKGAKLD QGEYERAAID AVDNKKNTPL HYAAASGMKA CVELLVKHGG DLFAENENKD
TPCDCAEKQH HKDLALNLES QMVFSRDPDA EEIEAEYAAL DKREPYEGLR PQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMCNPEN CCQRSGVQMP TPPPSGYNAW
DTLPSPRTPR TTRSSVTSPD EISLSPGDLD TSLCDICMCS ISVFEDPVDM PCGHDFCRGC
WESFLNLKIQ EGEAHNIFCP AYDCFQLVPV DIIESVVSKE MDKRYLQFDI KAFVENNPAI
KWCPTAGCER AVRLTKQGSN TSGSDTLSFP LLRAPAVDCG KGHLFCWECL GEAHEPCDCQ
TWKNWLQKIT EMKPEELVGV SEAYEDAANC LWLLTNSKPC ANCKSPIQKN EGCNHMQCAK
CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQHVEEQSK EMTVEAEKKH KRFQELDRFM
HYYTRFKNHE HSYQLEQRLL KTAKEKMEQL SRALKETEGG CPDTTFIEDA VHVLLKTRRI
LKCSYPYGFF LEPKSTKKEI FELMQTDLEM VTEDLAQKVN RPYLRTPRHK IIKAACLVQQ
KRQEFLASVA RGVAPADSPE APRRSFAGGT WDWEYLGFAS PEEYAEFQYR RRHRQQRRRG
DVHSLLSNPP EADEPSESTL ADIPESGSGR RPGASVVSSA SMSVLHSSSL RDYTPASRSE
NQDSLQALSS LDEDDPNILL AIQLSLQESG LTIDEETRDF LNNEASLGAI GTSLPSRLDS
VSRNTDSPRA ALSSSELLEF GDSLMRLGAE SDPFSTDTLS SHPLSEARSD FCPSSSDPDS
AGQDSNINDN LLGNIMAWFH DMNPQSIALI PPATTEISAD SQYPRDKDES EGVRNMELVP
PEEDSVFDAA VSESGGIQIE ENPLEENILA VETLAQAAES NIEAANKGNG SDASSQTPQT
SRDWLDQVHL V
//