ID A0A091QQV4_MERNU Unreviewed; 1579 AA.
AC A0A091QQV4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=E3 ubiquitin-protein ligase UBR5 {ECO:0000313|EMBL:KFQ29925.1};
DE Flags: Fragment;
GN ORFNames=N331_03944 {ECO:0000313|EMBL:KFQ29925.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ29925.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ29925.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ29925.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK705353; KFQ29925.1; -; Genomic_DNA.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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 InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
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 SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51309; PABC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1158..1235
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT DOMAIN 1284..1579
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 75..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1548
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ29925.1"
FT NON_TER 1579
FT /evidence="ECO:0000313|EMBL:KFQ29925.1"
SQ SEQUENCE 1579 AA; 176551 MW; 483C8F02805A0EDD CRC64;
CRLKRTSPTA YCDCWEKCKC KTLIAGQKSA RLDLLYRLLT TTNLVTMPNS RQGEHLLLFL
VQTVARQTVE HCQYRPPRIR EDRNRKTANP EDSDMPDHDL EPPRFAQLAL ERVLQDWNAL
KSMIMFGSQE NKDPLSASSR IGHLLPEEQV YLNQQSGTIR LDCFTHCLIV KCTADILLLD
TLLGTLVKEL QNKYTPGRRE EAIAVTMRFL RSVARVFVIL SVEMASSKKK NNFIPQPIGK
CKRVFQALLP YAVEELCNVA ESLIIPVRMG IARPTAPFTL ASTSIDAMQG SEELFSVEPL
PPRPSSDQSS SSSQSQSSYI IRNPQQRRIS QSQPVRGRDE EQDDIVSADV EEVEVVEGVA
GEEDHHDEQE EHGEENAEAE GQHDEHDEDG SDMELDLLAA AETESDSESN HSNQDNASGR
RSVVTAATAG SEAGASSVPA FFSEDDSQSN DSSDSDSSSS QSDDIEQETF MLDEPLERTT
NSSHANGAAQ APRSMQWAVR NTQNQRTAST APSSTSTPAG NSAGLIYIDP SNLRRSGTIS
TSAAAAAAAL EASNASSYLT SASSLARAYS IVIRQISDLM GLIPKYNHLV YSQIPAAVKL
TYQDAVNLQN YVEEKLIPTW NWMVSIMDST EAQLRYGSAL ASAGDPGHPN HPLHASQNSA
RRERMTAREE ASLRTLEGRR RATLLSARQG MMSARGDFLN YALSLMRSHN DEHSDVLPVL
DVCSLKHVAY VFQALIYWIK AMNQQTTLDT PQLERKRTRE LLELGLDNED SEHENDDDTN
QSATLNDKDD DSLPAETGQN HPFFRRSDSM TFLGCIPPNP FEVPLAEAIP LADQPHLLQP
NARKEDLFGR PSQGLYSSSA NSGKCLMEVT VDRNCLEVLP TKMSYAANLK NVMSMQNRQK
KEGEEQNVPT EESESSKPGP SAHDLAAQLK SSLLAEIGLT ESEGPPLTSF RPQCSFMGMV
ISHDMLLGRW RLSLELFGRV FMEDVGAEPG SILTELGGFE VKESKFRREM EKLRNQQSRD
LTLEVDRDRD LLIQQTMRQL NNHFGRRCAT TPMTVHRVKV TFKDEPGEGS GVARSFYTAI
AQAFLSNEKL PNLDCIQNAN KGTHTSLMQR LRNRGERDRE REREREMRRS SGLRAGSRRD
RDRDFRRQLS IDTRPFRPAS EGNPSDDPDP LPAHRQALGE RLYPRVQAMQ PAFASKITGM
LLELSPAQLL LLLASEDSLR ARVDEAMELI IAHGRENGAD SILDLGLLDS SEKVQENRKR
HGSSRSVVDM ELDDTDDGDD NAPLFYQPGK RGFYTPRPGK NTEARLNCFR NIGRILGLCL
LQNELCPITL NRHVIKVLLG RKVNWHDFAF FDPVMYESLR QLILASQSTD ADAVFAAMDL
AFAIDLCKEE GGGQVELISN GVNIPVTPQN VYEYVRKYAE HRMLVVTEQP LHAMRKGLLD
VLPKISLEDL TAEDFRLLVN GCGEVNVQML ISFTSFNDES GENAEKLLQF KRWFWSIVEK
MSMTERQDLV YFWTSSPSLP ASEEGFQPMP SITIRPPDDQ HLPTANTCIS RLYVPLYSSK
QILKQKLLLA IKTKNFGFV
//
