ID H9F9T1_MACMU Unreviewed; 2497 AA.
AC H9F9T1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=E3 ubiquitin-protein ligase UBR5 {ECO:0000313|EMBL:AFE71390.1};
DE Flags: Fragment;
GN Name=UBR5 {ECO:0000313|EMBL:AFE71390.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE71390.1};
RN [1] {ECO:0000313|EMBL:AFE71390.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE71390.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; JU327634; AFE71390.1; -; mRNA.
DR UniPathway; UPA00143; -.
DR GO; GO:0003723; F:RNA 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 GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd19675; UBR-box_UBR5; 1.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 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; IPR003126; Znf_UBR.
DR PANTHER; PTHR46276; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR PANTHER; PTHR46276:SF1; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 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 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 875..943
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 2075..2152
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT DOMAIN 2202..2497
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ZN_FING 875..943
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 25..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1682..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2171..2191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2027..2068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2171..2189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2466
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFE71390.1"
SQ SEQUENCE 2497 AA; 276812 MW; 224CC96CB2169014 CRC64;
RDSELLRERE SVLRLRERRW LDGASFDNER GSTSKEGEPN LDKKNTPVQS PVSLGEDLQW
WPDKDGTKFI CIGALYSELL AVSSKGELYQ WKWSESEPYR NAQNPSLHHP RATFLGLTNE
KIVLLSANSI RATVATENNK VATWVDETLS SVASKLEHTA QTYSELQGER IVSLHCCALY
TCAQLENNLY WWGVVPFSQR KKMLEKARAK NKKPKSSAGI SSMPNITVGT QVCLRNNPLY
HAGAVAFSIS AGIPKVGVLM ESVWNMNDSC RFQLRSPESL KNMEKASKTT EAKPESKQEP
VKTEMGPPPS PASTCSDASS IASSASMPYK RRRSTPAPKE EEKVNEEQWS LREVVFVEDV
KNVPVGKVLK VDGAYVAVKF PGTSSNTNCQ SSSGPDADPS SLLQDCRLLR IDELQVVKTG
GTPKVPDCFQ RTPKKLCIPE KTEILAVNVD SKGVHAVLKT GNWVRYCIFD LATGKAEQEN
NFPTSSIAFL GQNERNVAIF TAGQESPIIL RDGNGTIYPM AKDCMGGIRD PDWLDLPPIS
SLGMGVHSLI NLPANSTIKK KAAIIIMAVE KQTLMQHILR CDYEACRQYL MNLEQAVVLE
QNLQMLQTFI SHRCDGNRNI LHACVSVCFP TSNKETKEEE EAERSERNTF AERLSAVEAI
ANAISVVSSN GPGNRAGSSS SRSLRLREMM RRSLRAAGLG RHEAGASSSD HQDPVSPPIA
PPSWVPDPPA MDPDGDIDFI LAPAVGSLTT AATGTGQGPS TSTIPGPSTE PSVVESKDRK
ANAHFILKLL CDSVVLQPYL RELLSAKDAR GMTPFMSAVS GRAYPAAITI LETAQKIAKA
EVSSSEKEED VFMGMVCPSG TNPDDSPLYV LCCNDTCSFT WTGAEHINQD IFECRTCGLL
ESLCCCTECA RVCHKGHDCK LKRTSPTAYC DCWEKCKCKT LIAGQKSARL DLLYRLLTAT
NLVTLPNSRG EHLLLFLVQT VARQTVEHCQ YRPPRIREDR NRKTASPEDS DMPDHDLEPP
RFAQLALERV LQDWNALKSM IMFGSQENKD PLSASSRIGH LLPEEQVYLN QQSGTIRLDC
FTHCLIVKCT ADILLLDTLL GTLVKELQNK YTPGRREEAI AVTMRFLRSV ARVFVILSVE
MASSKKKNNF IPQPIGKCKR VFQALLPYAV EELCNVAESL IVPVRMGIAR PTAPFTLAST
SIDAMQGSEE LFSVEPLPPR PSSDQSSSSS QSQSSYIIRN PQQRRISQSQ PVRGRDEEQD
DIVSADVEEV EVVEGVAGEE DHHDEQEEHG EENAEAEGQH DEHDEDGSDM ELDLLAAAET
ESDSESNHSN QDNASGRRSV VTAATAGSEA GASSVPAFFS EDDSQSNDSS DSDSSSSQSD
DIEQETFMLD EPLERTTNSS HANGAAQAPR SMQWAVRNTQ HQRAASTAPS STSTPAASSA
GLIYIDPSNL RRSGTISTSA AAAAAALEAS NASSYLTSAS SLARAYSIVI RQISDLMGLI
PKYNHLVYSQ IPAAVKLTYQ DAVNLQNYVE EKLIPTWNWM VSIMDSTEAQ LRYGSALASA
GDPGHPNHPL HASQNSARRE RMTAREEASL RTLEGRRRAT LLSARQGMMS ARGDFLNYAL
SLMRSHNDEH SDVLPVLDVC SLKHVAYVFQ ALIYWIKAMN QQTTLDTPQL ERKRTRELLE
LGIDNEDSEH ENDDDTNQSA TLNDKDDDSL PAETGQNHPF FRRSDSMTFL GCIPPNPFEV
PLAEAIPLAD QPHLLQPNAR KEDLFGRPSQ GLYSSSASSG KCLMEVTVDR NCLEVLPTKM
SYAANLKNVM NMQNRQKKEG EEQPVLPEEA ESSKPGPSAH DLAAQLKSSL LAEIGLTESE
GPPLTSFRPQ CSFMGMVISH DMLLGRWRLS LELFGRVFME DVGAEPGSIL TELGGFEVKE
SKFRREMEKL RNQQSRDLSL EVDRDRDLLI QQTMRQLNNH FGRRCATTPM AVHRVKVTFK
DEPGEGSGVA RSFYTAIAQA FLSNEKLPNL ECIQNANKGT HTSLMQRLRN RGERDRERER
EREMRRSSGL RAGSRRDRDR DFRRQLSIDT RPFRPASEGN PSDDPDPLPA HRQALGERLY
PRVQAMQPAF ASKITGMLLE LSPAQLLLLL ASEDSLRARV DEAMELIIAH GRENGADSIL
DLGLVDSSEK VQQENRKRHG SSRSVVDMDL DDTDDGDDNA PLFYQPGKRG FYTPRPGKNT
EARLNCFRNI GRILGLCLLQ NELCPITLNR HVIKVLLGRK VNWHDFAFFD PVMYESLRQL
ILASQSSDAD AVFSAMDLAF AIDLCKEEGG GQVELIPNGV NIPVTPQNVY EYVRKYAEHR
MLVVAEQPLH AMRKGLLDVL PKNSLEDLTA EDFRLLVNGC GEVNVQMLIS FTSFNDESGE
NAEKLLQFKR WFWSIVEKMS MTERQDLVYF WTSSPSLPAS EEGFQPMPSI TIRPPDDQHL
PTANTCISRL YVPLYSSKQI LKQKLLLAIK TKNFGFV
//