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Database: UniProt
Entry: A0A1S3FYN4_DIPOR
LinkDB: A0A1S3FYN4_DIPOR
Original site: A0A1S3FYN4_DIPOR 
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};
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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
//
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