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Database: UniProt
Entry: W5LLD7_ASTMX
LinkDB: W5LLD7_ASTMX
Original site: W5LLD7_ASTMX 
ID   W5LLD7_ASTMX            Unreviewed;      2539 AA.
AC   W5LLD7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Ubiquitin protein ligase E3 component n-recognin 5 {ECO:0000313|Ensembl:ENSAMXP00000020649.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000020649.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000020649.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   STRING; 7994.ENSAMXP00000020649; -.
DR   Ensembl; ENSAMXT00000020649.2; ENSAMXP00000020649.2; ENSAMXG00000020014.2.
DR   eggNOG; KOG0943; Eukaryota.
DR   GeneTree; ENSGT00940000156357; -.
DR   HOGENOM; CLU_000257_0_0_1; -.
DR   InParanoid; W5LLD7; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000020014; Expressed in olfactory epithelium and 14 other cell types or tissues.
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   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   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          925..993
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   DOMAIN          2118..2195
FT                   /note="PABC"
FT                   /evidence="ECO:0000259|PROSITE:PS51309"
FT   DOMAIN          2255..2539
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ZN_FING         925..993
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          75..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1263..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1605..1637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1733..1770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1862..1891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2073..2133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2213..2233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..781
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1311..1325
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1370..1399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1408..1433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1447..1487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1623..1637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1745..1764
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1862..1883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2078..2111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2213..2231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2508
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   2539 AA;  280500 MW;  7494435A2A29B208 CRC64;
     MSLLDADIHS AHPSVIIDAD AMFSEDISYF GYPSFRRSSL SRLGSSRERD SELLRERESV
     LRLRERRWLD GASFDAERGS TSREGEPSVD KKSVPLQSPV SLGEELQWWP DKDGTRFVSI
     AAMFSELVAI SSKGELYQWK WSEPEPYRNA QNPSIHHPRV SFLGLANEKI TLLSANSIRA
     TVATETNKVA TWVDETLSSV ACKLEHGAQT FPELQGERIV SLHCCSLYTC AQLDSSLYWW
     GVVPFSQRKK MLEKARAKNK KPKSSAGIAS IPNITVGTQV CLRNNPLYHA GAVAFSVSAG
     VPKVGVLLES VWNMNDSCRF QLRSPESLKS MEKSTKAQEI KTESKPELVK TEMGPPPSPA
     STCSDTSSIA SSASLPYKRR RSTPAPKEEE KVNEEQWPLR EVVFVEDVKN VPVGKVLKVD
     GAYVAVKFPG TSSSVSSQSA APTDSDPSSL LQDCRLLRID ELQVVKTGGT PKVPDCFQRT
     PKKLCIPEKA EILAVNVDSK GVHAVLKTGS WVRYCIFDLA TGKAEQENHF PTSNLAFLGQ
     SERNVAIFTA GQESPIILRD GNGTIYPMAK DCMGGIRDPD WLDLPPIASL GMGVHSLANL
     PSNSTIKKKA AIIIMAVEKQ TLMQHVLRCD YEACRQYLVS LEQAVLLEQN PHALDALLGH
     RCDGNRNLLH ACVSVCFPVS NKETKEEEEA ERSERNTFAE RLSAVEAIAN AISVVSSNSS
     GNRTGSSSSR GLRLREMMRR SLRAAGLGRH ESGPSSADHQ DPVSPPIAPP SWVPDPPPMD
     PDGDIDFILA PAVGSLTTAS TGPSQGPSTS TIPGPSSEPS VVESKDRKAN AHLILKLMCD
     SVVLRPHLRE LLSAKDARGM TPFMLAVSGR AYPAAITVLE AAQKIAKGEP GIGEKEDVNS
     VFMEMICPAG TNPDDSPLYV LCCNDTCSFT WTGAEHINQD IFECRTCGLL ESLCCCTECA
     RVCHKGHDCK LKRTSPTAYC DCWEKCKCKT LIAGQKAARL DLLYRLLTTT NLVTSPNSRG
     EHILLFLVQT VARQSVEHCQ YRPPRIREDR NRKAANAEDS DMPDHDLEPP RFAQLALERV
     LQDWNALKCM IMFGSQENKD PLSASSRIAH LLPEEQMYLN QQSGTIRLDC FTHCLIVKCA
     PDITFIDTLL GTLVKELQNK YTPGRREEAI CVTRRFLRSV ARVFVILSVE MASSKKKNNF
     IPQPIGKCRR VFQALLPYAV EELCNVAESL IVPVRMGIAR PTAPFTLAST SIDAVQGSEE
     LFSVEPLPPR PSPDQSSNSG QSASSYIIRN PQPRRSSQSQ TARGRDEEQD DIVSADVEEV
     EVVEGVAGEE DHHDDQEEQG EETAEAEGQH DEHDEDGSDM ELDLLAAAET ESDSESNHSN
     QDNASGRRSV VTAATAGSEA GASSVPAFFS EDDSQSNDSS DSDSSSSQSD DADQETYLLD
     EPLERTTGSA HANSAAQAPR SMQWAVRTTP SQRSAGGAPA SSSTPAASST GLIYIDPSNL
     RRSSAISTSA AAAAAALEAS NSSSYLTSAS SLARAYSIVI RQISDLMSLI PKYNHLVYSQ
     YPAAVKLTYQ DAVNLQNFVE EKLIPTWNWM VSIMDSTEAQ LRYGSALSSA GDPGHPSHPL
     HASQHAGRRE RMTAREEASL RTLEGRRRAA TLLTARQGMM SARGDFLNYA LSLMRSHNDE
     HSDVLPVLDV CSLKHVAYVF QALIYWIKAM NLQTTLDTTQ IDRKRNRELL ELGLDNEDSE
     HENDEDTNQS STLQDKEEES VSSETGQHHP FFRRSDSMTF LGCIPPNPFE VPVAEAIPLA
     DQPHLLQPNA RKEDLFGRPS QGLYSSSYMA SKGLSDLTVD MNCLQILPTK MSYSANMKNV
     MSMESRQRGS EDQPTSAQEM DTSKPGPSPH DLAAQLKSSL LAEIGLTESD GPPLPTFIPH
     CSFMGMVISH DMLLGRWRLS LELFGRVFME DVGAEPGSIL TELGGFEVKE SKFRREMEKL
     RNLQSRDLAL EVDRDRDQLI QQTMRQLNTH FGRRCATTPM AVHRVKVTFK DEPGEGSGVA
     RSFYTAIAQA FLSNDKLPNL DCVQSVSKGM QASNLMQRLR NRDRERERRS GGLRAGSRRD
     RDRDSRRQLS IDTRPFRPAS EGNPSDEPDP LPAHRQALGE RLYPRVHAMQ PAFASKITGM
     LLELSPAQLL LLLASEDSLR ARVEEAMELL ITHGRENGAD SILDLGLLDT PEKAQENRKR
     HGSTRSVVDM ELDDPDDGDD NAPLFYQPGK RGFYSPRPGK NTEARLNCFR NIGRILGLCL
     LQNELCPITL NRHVIKVLLG RKVNWHDFAF FDPVMYESLR QLIRHSQTGE AEAVFAAMDL
     AFAIDLCKEE GSGQVELLTG GANMPVTPQN VYEYVRKYAE HRMLVVAEQP LHAMRKGLLD
     VLPKNALEDL TAEDFRLLVN GCGEVNVQML ISFTSFNDES GENAEKLLQF KRWFWSIVEK
     MSMTERQDLV YFWTSSPSLP ASEEGFQPMP SITIRPPDDQ HLPTANTCIS RLYVPLYSSK
     QILKQKLLLA IKTKNFGFV
//
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