ID A0A1S3RWZ3_SALSA Unreviewed; 2850 AA.
AC A0A1S3RWZ3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=E3 ubiquitin-protein ligase UBR5 isoform X20 {ECO:0000313|RefSeq:XP_014056770.1};
GN Name=LOC106605530 {ECO:0000313|RefSeq:XP_014056770.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014056770.1};
RN [1] {ECO:0000313|RefSeq:XP_014056770.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014056770.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014056770.1; XM_014201295.1.
DR GeneID; 106605530; -.
DR OrthoDB; 2911162at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd14423; CUE_UBR5; 1.
DR CDD; cd19675; UBR-box_UBR5; 1.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 2.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR047503; UBR-box_UBR5.
DR InterPro; IPR024725; UBR5_UBA.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR46276; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR PANTHER; PTHR46276:SF1; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR Pfam; PF11547; E3_UbLigase_EDD; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00658; PABP; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1229..1297
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 2428..2505
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT DOMAIN 2566..2850
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ZN_FING 1229..1297
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 79..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1909..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2037..2073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2383..2443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1629
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2049..2067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2388..2421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2819
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2850 AA; 312858 MW; 07F073E066CB3C3F CRC64;
MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNFNSHPHL NLLEQATLKQ CVVGPNHAGF
LLEDGRVCRI SFAVQPDRLE LTKPDGNDGS KLSGSGSGTG RSSRPGRTSD PPWFLSGSDT
LGRLAGNTLG SRWSSGVNGG SGGGGGGGGG GGGGSSSVGG AGGGGVGGAV SGGGGGGGSS
GRSSTAARDS RRQTRVIRTG RDRGSGLLGS QPQPVIPASV IPEELISQAQ VVLQGKSRSV
IIRELQRTNL DVNLAVNNLL SRDDEDGDDG DDTASESYLP GEDLMSLLDA DIHSAHPSVI
IDADAMFSED ISYFGYPSFR RSSLSRLGSS RVLLLPLERD SELLRERESV LRLRERRWLD
GASFDTERGS TSREGEPSLD KKNIPVQSPV SLGEELQWWP DKDGVKFVSI GSLFSELVAV
SSKGELYQWK WSEPEPYRNT QNPSIRHPRV SFLGLTNEKI TLLSANSIRA TVATETNKVA
TWMDDTLSSV ASKLEHSAQV YPELQGERIV SLHCCALYTC AQLESSLYWW GVVPFSQRKK
MLEKARAKNK KPKSSAGISS VPNITVGTQV FVSSLQVCLR NNPLYHAGAV AFSVNAGIPK
VGLLLESVWN MNDSCRFQLR SPESLKNMDK TTKTQEIKTE SKPELVKTEM GPPPSPASTC
SDTSSIASSA SLPYKRRRST PAPKEEEKVN EEQWPLREVV FVEDVKNVPV GKVLKVDGAY
VAVKFPGTSS SVSTQPSLPS APAPITDSDP SSLLQDCRLL RIDELQVVKT GGTPKVPDCF
QRTPKKLCIP EKAEILAVNV DSKGVHAVLK TGNWVRYCIF DLATGKAEQE NNFPTSNLAF
LGQSERNVAI FTAGQDSPVI LRDGNGTIYP MAKDCMGGIR DPEWLDLPPI ASLGMGVHSL
ANLPTNSTIK KKAAIIILAV EKQTLMQHVL RCDFEACRQY LVNLEQAVLL EQSPHVLHSF
LGHRCDGNRN ILHACVSVCF PVSNKETKEE EEAERSERNT FAERLSAVEA IANAISVVSS
NSSGNRTGSS SSRGLRLREM MRRSLRAAGL GRHESGPSSS DHQDPVSPPI APPSWVPDPP
PMDPDGDIDF ILAPAVGSLT TASTGTSQGP STSTIPGPSS EPSVVESKDR KANAHLILKL
MCDSMVLRPH LRELLSAKDA RGMTPFMLAV SGRAYPAAIT VLEAAQKMAK VGEPGMTEKV
DADSAFMEMI CPSGTNPDDS PLYVLCCNDT CSFTWTGAEH INQDIFECRT CGLLESLCCC
TECARVCHKG HDCKLKRTSP TAYCDCWEKC KCKTLIAGQK AARLDLLYRL LTTTNLVTSP
NSRGEHILLF LVQTVARQSV EHCQYRPPRI REDRNRKAAN AEDSDMPDHD LEPPRFAQLA
LERVLQDWNA LKSMIMFGSQ ENKDPLSASS RIAHLLPEEQ VYLNQQSGTI RLDCFTHCLI
VKCAPDITFI DTLLGTLVKE LQNKYTPGRR EEAIVVTRRF LRSVARVFVI LSVEMASSKK
KNNFIPQPIG KCRRVFQALL PYAVEELCNV AESLIVPVRM GIARPTAPFT LASTSIDAVQ
GSEELFSVEP LPPRPSPDQS SNSSQTASSY IIRNPQPRRS SQSQPVRGRD EEQDDIVSAD
VEEVEVVEGV AGEEDHHEDQ EEQGEENAEA EGQHDEHDED GSDMELDLLA AAETESDSES
NHSNQDNASG RRSVVTAATA GSEAGASSVP AFFSEDDSQS NDSSDSDSSS SQSDDVDQET
FLLDEPLERT TTASHVNSAA QAPRSMQWAV RNTPSQRATG SAPSSSSTPA ASSTGLIYID
PSNLRRSSAI STSAAAAAAA LEASNSSSYL TSASSLARAY SIVIRQISDL MSLIPKYNHL
VYSQYPAAVK LTYQDAVNLQ NFVEEKLIPT WNWMVSIMDS TEAQLRYGSA LSSAGDPGHP
SHPLHASQHS ARRERMTARE EASLRTLEGR RRAATLLTVR QGMMSARGDF LNYALSLMRS
HNDEHSDVLP VLDVCSLKHV AYVFQALIYW IKAMNQQTTL DTTQMDRKRS REILELGLDN
EDSEHENDED TNQSSTLQDK EDDSVPAEMG QNHPFFRRSD SMTFLGCIPP NPFEVPLAEA
IPLADQPHLL QPNARKEDLF GRPSQGLYSS SYTASKGLAE ATLDRSCLEV NMGSSQILPT
KMSYSANLKN VMSMETSQRG REDQPMDQEL VAPKPGPSPH DLAAQLKSSL LAEIGLTESD
GPPLPSFRPH CSFMGMVISH DMLLGRWRLS LELFGRVFME DVGAEPGSIL TELGGFEVKE
SKFRREMEKL RNLQSRDLAL EVDRDRDQLI QQTMRQLNTH FGRRCTTTPM AVHRVKVTFK
DEPGEGSGVA RSFYTAIALA FLSNDKLPNL DCVQSVSKGM QASNLMQRLR NRDRERERRS
GGLRAGSRRD RDRDSRRQLS IDTRPFRPAS EGNPSDEPDP LPAHRQALGE RLYPRVHAMQ
PAFASKITGM LLELSPAQLL LLLASEDSLR ARVEEAMELL IAHGRENGAD SILDLGLLEA
PEKAQQENRK RHGSTRSVVD MELDDPEDGD DNAPLFYQPG KRGFYSPRPG KNTEARLNCF
RNIGRILGLC LLQNELCPIT LNRHVIKVLL GRKVNWHDFA FFDPVMYESL RQLIRHSQAG
EAEAVFAAMD VAFAIDLCKE EGAGQVELLS GGVNMPVTPL NVYEYVRKYA EHRMLVVAEQ
PLHAMRKGLL DVLPKNALED LTAEDFRLLV NGCGEVNVQM LISFTSFNDE SGENADKLLQ
FKRWFWSIVE KMSMTERQDL VYFWTSSPSL PASEEGFQPM PSITIRPPDD QHLPTANTCI
SRLYVPLYSS KQILKQKLLL AIKTKNFGFV
//
