ID A0A340XSZ7_LIPVE Unreviewed; 2798 AA.
AC A0A340XSZ7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=E3 ubiquitin-protein ligase UBR5 {ECO:0000313|RefSeq:XP_007463317.1};
GN Name=UBR5 {ECO:0000313|RefSeq:XP_007463317.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007463317.1};
RN [1] {ECO:0000313|RefSeq:XP_007463317.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR RefSeq; XP_007463317.1; XM_007463255.1.
DR STRING; 118797.A0A340XSZ7; -.
DR GeneID; 103085633; -.
DR KEGG; lve:103085633; -.
DR CTD; 51366; -.
DR InParanoid; A0A340XSZ7; -.
DR OrthoDB; 2911162at2759; -.
DR Proteomes; UP000265300; Unplaced.
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 Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
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:UP000265300};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1177..1245
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 2377..2454
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT DOMAIN 2503..2798
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ZN_FING 1177..1245
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 77..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1859..1890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1984..2021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2323..2393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2473..2500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2116..2130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2329..2370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2473..2490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2767
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2798 AA; 309224 MW; 2F811AEB8222F816 CRC64;
MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF
LLEDGRVCRI GFSVQPDRLE LGKPDNNDGS KLNSNSGAGR TSRPGRTSDS PWFLSGSETL
GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI
PASVIPEELI SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE
SYLPGEDLMS LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP
LERDSELLRE RESVLRLRER RWLDGASFDN ERGSTSKEGE PNLDKKNTPV QSPVSLGEDL
QWWPDKDGTK FICIGALYSE LLAVSSKGEL YQWKWSESEP YRNAQNPSLH HPRATFLGLT
NEKIVLLSAN SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA
LYTCAQLENN LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GISSMPNITV GTQVCLRNNP
LYHAGAVAFS ISAGIPKVGV LMESVWNMND SCRFQLRSPE SLKSMDKASK TTETKPESKQ
EPVKTEMGPP PSPASTCSDA SSIASSASMP YKRRRSTPAP KEEEKVNEEQ WSLREVVFVE
DVKNVPVGKV LKVDGAYVAV KFPGTSSNTN CQNNSGSDAD PSSLLQDCRL LRIDELQVVK
TGGTPKVPDC FQRTPKKLCI PEKTEILAVN VDSKGVHAVL KTGNWVRYCI FDLATGKAEQ
ENNFPTSSIA FLGQDERNVA IFTAGQESPI ILRDGNGTIY PMAKDCMGGI RDPDWLDLPP
ISSLGMGVHS LINLPANSTI KKKAAIIIMA VEKQTLMQHI LRCDYEACRQ YLMNLEQAVV
LEQNLQMLQT FISHRCDGNR NILHACVSVC FPTSNKETKE EEEAERSERN TFAERLSAVE
AIANAISVVS SNGPGNRAGS SSSRSLRLRE MMRRSLRAAG LGRHEAGASS SDHQDPVSPP
IAPPSWVPDP PAMDPDGDID FILAPAVGSL TTAATGTGQG PSTSTIPGPS TEPSVVESKD
RKANAHFILK LLCDSVVLQP YLRELLSAKD ARGMTPFMSA VSGRAYPAAI TILETAQKIA
KAEVSSSEKE EDVFMGMVCP PGTNPDDSPL YVLCCNDTCS FTWTGAEHIN QDIFECRTCG
LLESLCCCTE CARVCHKGHD CKLKRTSPTA YCDCWEKCKC KTLIAGQKSA RLDLLYRLLT
ATNLVTLPNS RGEHLLLFLV QTVARQTVEH CQYRPPRIRE DRNRKTANPE DSDMPDHDLE
PPRFAQLALE RVLQDWNALK SMIMFGSQEN KDPLSASSRI GHLLPEEQVY LNQQSGTIRL
DCFTHCLIVK CTADILLLDT LLGTLVKELQ NKYTPGRREE AIAVTMRFLR SVARVFVILS
VEMASSKKKN NFIPQPIGKC KRVFQALLPY AVEELCNVAE SLIVPVRMGI ARPTAPFTLA
STSIDAMQGS EELFSVEPLP PRPSSDQSSS SSQSQSSYII RNPQQRRISQ SQPVRGRDEE
QDDIVSADVE EVEVVEGVAG EEDHHDEQEE HGEENAEAEG QHDEHDEDGS DMELDLLAAA
ETESDSESNH SNQDNASGRR SVVTAATAGS EAGASSVPAF FSEDDSQSND SSDSDSSSSQ
SDDIEQETFM LDEPLERTTN SSHANGAAQA PRSMQWAVRN TQHQRAASTA PSSTSTPAAS
SAGLIYIDPS NLRRSGTIST SAAAAAAALE ASNASSYLTS ASSLARAYSI VIRQISDLMG
LIPKYNHLVY SQIPAAVKLT YQDAVNLQNY VEEKLIPTWN WMVSIMDSTE AQLRYGSALA
SAGDPGHPNH PLHASQNSAR RERMTAREEA SLRTLEGRRR ATLLSARQGM MSARGDFLNY
ALSLMRSHND EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL
LELGIDNEDS EHENDDDTNQ SATLNDKDDD SLPAETGQNH PFFRRSDSMT FLGCIPPNPF
EVPLAEAIPL ADQPHLLQPN ARKEDLFGRP SQGLYSSSAS SGKCLMEVTV DRNCLEVLPT
KMSYAANLKN VTNMQNRQKK EGEEQNVVPE EAESSKPGPS AHDLAAQLKS SLLAEIGLTE
SEGPPLTSFR PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV
KESKFRREME KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT
FKDEPGEGSG VARSFYTAIA QAFLSNEKLP NLDCIQNANK GTHTSLMQRL RNRGERDRER
EREREMRRSS GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPDPL PAHRQALGER
LYPRVQAMQP AFASKITGML LELSPAQLLL LLASEDSLRA RVDEAMELII AHGRENGADS
ILDLGLLDSS EKVQENRKRH GSSRSVVDMD LDDTDDGDDN APLFYQPGKR GFYTPRPGKN
TEARLNCFRN IGRILGLCLL QNELCPITLN RHVIKVLLGR KVNWHDFAFF DPVMYESLRQ
LILASQSSDA DAVFSAMDLA FAIDLCKEEG GGQVELIPNG VNIPVTPQNV YEYVRKYAEH
RMLVVAEQPL HAMRKGLLDV LPKNSLEDLT AEDFRLLVNG CGEVNVQMLI SFTSFNDESG
ENAEKLLQFK RWFWSIVEKM SMTERQDLVY FWTSSPSLPA SEEGFQPMPS ITIRPPDDQH
LPTANTCISR LYVPLYSSKQ ILKQKLLLAI KTKNFGFV
//
