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Database: UniProt
Entry: H2TND1_TAKRU
LinkDB: H2TND1_TAKRU
Original site: H2TND1_TAKRU 
ID   H2TND1_TAKRU            Unreviewed;      2791 AA.
AC   H2TND1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Ubiquitin protein ligase E3 component n-recognin 5 {ECO:0000313|Ensembl:ENSTRUP00000026187.3};
GN   Name=ubr5 {ECO:0000313|Ensembl:ENSTRUP00000026187.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000026187.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000026187.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000026187.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   Ensembl; ENSTRUT00000026294.3; ENSTRUP00000026187.3; ENSTRUG00000010399.3.
DR   eggNOG; KOG0943; Eukaryota.
DR   GeneTree; ENSGT00940000156357; -.
DR   HOGENOM; CLU_237999_0_0_1; -.
DR   TreeFam; TF314406; -.
DR   Proteomes; UP000005226; Chromosome 7.
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:UP000005226};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1163..1231
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   DOMAIN          2368..2445
FT                   /note="PABC"
FT                   /evidence="ECO:0000259|PROSITE:PS51309"
FT   DOMAIN          2507..2791
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ZN_FING         1163..1231
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          79..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1501..1548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1565..1728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1843..1870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1971..2011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2323..2383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1018
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1608..1637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1646..1671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1679..1728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1983..2001
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2328..2361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2760
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   2791 AA;  306770 MW;  624BE168CBE68735 CRC64;
     MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYSYNSHPHL GLLEQATLKQ CVVGPNHAGF
     LLEDGRVCRI SFAVQPDRLE LSKPDGSDGS RWSSGVNGGN GGGGSGGGAG GGGAGGGSSG
     GSGSGGGGGG TSGRSSTAAR DSRRQTRVIR TGRDRGSGLL GSQPQPVIPA SVIPEELITQ
     AQVVLQGKSR SVIIRELQRT NLDVNLAVNN LLSRDDEDGD DGDDTASESY LPGEDLMSLL
     DADIHSAHPS VIIDADAMFS EDISYFGYPS FRRSSLSRLG PSRERDSELL RERESVLRLR
     ERRWLDGASF DTERGSTSRE GEANLDKKSI PVQSPVSLGE ELQWWPDKDG VKFVSIGAMF
     SELVAVSSKG ELYQWKWTEP EPFRNAQNPS IHHPRVSFLG LANEKITLLS ANSIRATVAT
     ETNKVATWVD ETLSSMASKL EHSAQAFPEL QGERMVSLNC CALYTCAQLE NGLYWWGVVP
     FSQRKKMLEK ARAKNKKPKS SAGMSSIPNI TVGTQVCLRN NPLYHAGAVA FSVSAGIPKV
     GVLLESVWNM NDSCRFQLRS PESLKTMEKT AKTQEIKTES KPELVKTEMG PPPSPASTCS
     DTSSIASSAS LPYKRRRSTP APKEEEKVNE EQWPLREVVF VEDVKNVPVG KVLKVDGAYV
     AVKFPGTSSS VSNQSSAAPA DSDPSSLLQD CRLLRIDELQ VVKTGGTPKV PDCFQRTPKK
     LCIPEKAEIL AVNVDSKGVH AVLKTGNWVR YCIFDLATGK AEQENNFPTS NLAFLGQSER
     NVAIFTAGQE SPIILRDGNG TIYPMVKDCV GGIRDPDWLD LPPINSLGMG VHSLANLPSN
     STIKKKAAII IMAVEKQTLM QHVLRCDYEA CRQYLVNLEQ AFMLDQGSQA LGALLDHRCD
     GNRNILHAAV SVCFPVSNKE TKEEEEAERS ERNTFAERLS AVEAIANAIS VVSSNSSGNR
     TGSSSSRGLR LREMMRRSLR AAGVGRHESG PSSSDHQDPV SPPIAPPSWV PDPPPMDPDG
     DIDFILAPAV GSLTTASTGT SQGPSTSTIP GPSNESPVVE SKDRKANAHL ILKLMCDSVV
     LRPHLRELLS AKDARGMTPF MLAVSGRAYP AAITVLEAAQ KMAKVGDPGI TEKEDADSVF
     MEMICPSGTN PDDSPLYVLC CNDTCSFTWT GAEHINQDIF ECRTCGLLES LCCCTECARV
     CHKGHDCKLK RTSPTAYCDC WEKCKCKTLI AGQKAARLDL LYRLLTTTNL VTTPNSRGEH
     ILLFLVQTVA RQSVEHCQYR PPRIREDRNR KATNAEDSDM PDHDLEPPRF AQLALERVLQ
     DWNALKSMIM FGSEENKDPL SASSRIAHLL SEEQVYLNQQ SGTIRLDCFT HCLIVKCAPD
     ITFIDTLLST LVRELQNKYT PGRREEAVNV TRRFLRSVAR VFVILSVEMA SSKKKNNFIP
     QPIGKCRRVF QALLPYAVEE LCNVAESLIV PVRMGIARPT APFTLASTSI DAVQGSEELF
     SVEPLPPRPS PDQSSSSSQT AASYIIRNPQ PRHSSQSQPV RGRDEEQDDI VSADVEEVEV
     VEGVAGEEDH HDDQEEQGEE NPETEGQHDE HDEDGSDMEL DLLAAAETES DSESNHSNQD
     NASGRRSVVT AATAGSEAGA SSVPAFFSED DSQSNDSSDS DSSSSQSDDV DQETFLLDEP
     LERTTSSSHA NSAAQAPRSM QWAVRNTPSQ RASGSAPSNS STPSASSTGL IYIDPTNLRR
     SSAISSSAAA AAAALEASNS SSYLTSASSL ARAYSIVIRQ ISDLMSLIPK YNHLVYSQYP
     AAVKLTYHDA VNLQNYVEEK LIPTWNWMVS IMDSTEAQLR YGSALSSAGD PGHPSHPLHA
     SQHSARRERI NAREEASLRT LEGRRRAATL LTARQGMMSA RGDFLNYALS LMRSHNDEHS
     DVLPVLDVCS LKHVAYVFQA LIYWIKAMNQ QTTLDTPQMD RKRNREILEL GLDNEDSEHE
     NDEDTNQSST LQDKDEDPVP AETGQNHPFF RRSDSMTFLG CIPPNPFDVP LPEAIPLADQ
     PHLLQPNARK EDLFGRPSQG LYSSSFMANK GLAEASVDRN CLEVNMGSSL PSPSQILPTK
     MSYSANLKNV MSMESGQRNT GTQSIADHEM DTSKPGPSPQ DLAAQLKSSL LAEIGLTESD
     GPPLPSFRPH CSFMGMMISH DMLLGRWRLS LELFGRVFME DVGAEPGSIL TELGGFEVKE
     SKFRREMEKL RNLQSRDLAL EVDRDRDQLI QQTMRQLNAH FGRRCTTTPM AVHRVKVTFK
     DEPGEGSGVA RSFYTAIALA LLSNDKLPNL DCVQSVSKGM QASNLMQRLR NRDRERERRS
     GGLRAGSRRD RDRDSRRQLS IDTRPFRPSS EGNPSDEPDP LPAHRQALGE RLYPRVHAMQ
     PAFASKITGM LLELSPAQLL LLLASEDSLR ARVEEAMELL IAHGRENGAD SILDLGLLEA
     PEKAQQQENR KRHGSTRSVV DMELDDPDDG EDNAPLFYQP GKRGFYSPRP GKNTEARLNC
     FRNIGRILGL CLLQNELCPI TLNRHVIKVL LGRKVNWHDF AFFDPVMYES LRQLIRHSQA
     GEADAVFAAM DLAFAIDLCK EEGAGQVELL SGGVNMPVTP LNVYEYVRKY AEHRMLVVAE
     QPLHAMRKGL LDVLPKNALE DLTAEDFRLL VNGCGEVNVQ MLISFTSFND ESGENADKLL
     QFKRWFWSIV EKMSMTERQD LVYFWTSSPS LPASEEGFQP MPSITIRPPD DQHLPTANTC
     ISRLYVPLYS SKQILKQKLL LAIKTKNFGF V
//
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