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Database: UniProt
Entry: A0A1S3RWY8_SALSA
LinkDB: A0A1S3RWY8_SALSA
Original site: A0A1S3RWY8_SALSA 
ID   A0A1S3RWY8_SALSA        Unreviewed;      2877 AA.
AC   A0A1S3RWY8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=E3 ubiquitin-protein ligase UBR5 isoform X14 {ECO:0000313|RefSeq:XP_014056763.1};
GN   Name=LOC106605530 {ECO:0000313|RefSeq:XP_014056763.1};
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_014056763.1};
RN   [1] {ECO:0000313|RefSeq:XP_014056763.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014056763.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_014056763.1; XM_014201288.1.
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          2441..2518
FT                   /note="PABC"
FT                   /evidence="ECO:0000259|PROSITE:PS51309"
FT   DOMAIN          2580..2877
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          2403..2456
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        2403..2434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2846
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   2877 AA;  316014 MW;  A672C9FA8EA6A578 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 QASSTCHHDY NSSMTLNLMQ
     RLRNRDRERE RRSGGLRAGS RRDRDRDSRR QLSIDTRPFR PASEGNPSDE PDPLPAHRQA
     LGERLYPRVH AMQPAFASKI TGMLLELSPA QLLLLLASED SLRARVEEAM ELLIAHGREN
     GADSILDLGL LEAPEKAQQQ ENRKRHGSTR SVVDMELDDP EDGDDNAPLF YQPGKRGFYS
     PRPGKNTEAR LNCFRNIGRI LGLCLLQNEL CPITLNRHVI KVLLGRKVNW HDFAFFDPVM
     YESLRQLIRH SQAGEAEAVF AAMDVAFAID LCKEEGAGQV ELLSGGVNMP VTPLNVYEYV
     RKYAEHRMLV VAEQPLHAMR KGLLDVLPKN ALEDLTAEDF RLLVNGCGEV NVQMLISFTS
     FNDESGTKTL ARIHKESQRE NADKLLQFKR WFWSIVEKMS MTERQDLVYF WTSSPSLPAS
     EEGFQPMPSI TIRPPDDQHL PTANTCISRL YVPLYSSKQI LKQKLLLAIK TKNFGFV
//
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