ID A0A1X0P726_9TRYP Unreviewed; 1941 AA.
AC A0A1X0P726;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative ubiquitin-protein ligase {ECO:0000313|EMBL:ORC92230.1};
GN ORFNames=TM35_000044440 {ECO:0000313|EMBL:ORC92230.1};
OS Trypanosoma theileri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC92230.1, ECO:0000313|Proteomes:UP000192257};
RN [1] {ECO:0000313|EMBL:ORC92230.1, ECO:0000313|Proteomes:UP000192257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC92230.1};
RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA Matthews J., Matthews K., Carrington M.;
RT "An alternative strategy for trypanosome survival in the mammalian
RT bloodstream revealed through genome and transcriptome analysis of the
RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORC92230.1}.
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DR EMBL; NBCO01000004; ORC92230.1; -; Genomic_DNA.
DR STRING; 67003.A0A1X0P726; -.
DR VEuPathDB; TriTrypDB:TM35_000044440; -.
DR OrthoDB; 147918at2759; -.
DR Proteomes; UP000192257; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ORC92230.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192257};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1665..1941
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1874..1891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1908
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1941 AA; 216075 MW; 588F955C005CDD8D CRC64;
MQGHVIVEDS KQQVKEVHRQ KNDPDKVLGP LDRMCLSLVM GVERYLREFD AAAAIPMLVR
MSEKEAFAFR GDALTMLFRA ISLIMEHVPT SYESMGPYQK QLMKSVCQTL SRTLAGRMKY
NNTDNVMLME ECLRLIRFIS RDESNISALR FGMTDIIQIA ASENSLLARQ AFDVLLILCS
KVILPSEAEK PHMLGLPISF MGWKKKKKQK TKDDSPPFSQ DPVVVAVEQI IAPFLHTSIQ
QYAATLESFP EAWTFLEMAL QCLGMLMQRA LLCHRPSTAQ KMVTEDLCKI LFHLILFNDN
NVALEQGVRS ERLLLCETML DAAISASWRV ASESLLTEEA QSFYKLMFEE SDSEVTTLLD
DPFPVAGSSL RGAQRRDKNH IASIAAVRLF ILACPRLPSE AFGPKPKVLL PVHEWKWEDE
MRHKNLIDEE RCIALETSFV RLSKESVIKI QTKSMVVDLH TMKMCGGFGG IDRNIYRKFV
PFVFHVVDEE NLRLVKSAKE VMVSSNLFVQ SKHETKTAMT VTTANMPPHL KNLMRFYVIN
KDAPVLLGNV KMAELYLERL CNFVVWVPGQ MTMQLGTCAC ASLLHSVIRS GEDKRFVSLI
RSVLRPLCEM LRVALASSDK ATKSICLTMM VWLLCHPRAA EWQFCGIAQR CGILRELEEL
SRGGSKGNGN SGGSISSGNH TNTAKSTHAA SEERQTRTKY LATTASAIHA AITEEMKRLQ
APGNPAGLST VDVTVVRQAV QDLKTSAKLP GVHRKVVEHV LYVMEMSLRT ITAFEISMLG
IADAVLTYLL EDNENNADAT SVNGSTTTNT NTTNTGEGKT SALGNFVFTS SVDLAPFDGR
SVADRLFQRC RRERLECFLM CAAEKPRGVE ALIENLVSAL PMHSTFPLVE TVLSAKSVSC
RTPLKAAMIC SHISPCVTLC SKANGNSKRN NNNNNNNNNN NNNNNNNNNS NNKPPAVLSV
HSSKDTNSRG VSGGGGGGEE EETPSQLRGF IEREVVVPNP RDFCPQGHRL QIIVTPRDII
SPCDLCEEEV RSGFRCAQCR FHVCMECYAN PDVHYEGGSP LLSSRSNPED DNVSNSVERT
PVNRIKKVNV RAHLFASVGD IERHFRTGSS AIKNTDVAPA PVSALQNIDN FIGHVQSVLI
RRKKQLAPGS LRKSIQEALK TFISPGSIPD NTTTTNKSSE DQSIQNQETQ EMMQLIRDAM
EERYVLYTSP GGRCTYQETF IGNLLQRALL EGSVSLVEQI ENCLLSMEGV AENASPSDYL
QTGEVNFEKH ADSALQSSRE LPDRVDSTQT FVFHHFENDE ETHCCCGEKS RQELNTMHSS
NIVRNPTRLS QNQDTILLIL LHKILNPLIK QHVVDINPAA FVSAPFTTLI VKSLAASALR
VAILPPKIAV PRWVDFILTQ AKFLLPLNVR ERIARFFAYG ARRALHAHMK GSCVSRSYRS
IRIYPAEWAR VSNHKYRVRR MELLHDAYIV LRKSADSRSP ISIEFEGDVG VGQGPTAHFY
TLIADKMKKE QVHLWRGVRT IRKENDLGKS GNSKDKSNSS SNTNINMNSK SDCDEVEVIL
PLEGIYPCKD VLVRTSWKGS AVSPQTLPDG GRILTDYRIC MDDFAEFDCE RAQCYYLVGA
ALARAFTDEV VFPLDISPAL AIFLSHGAPP SRVILHNVPC ADKNIERPVD FMGLSLNDVE
LMDKSLASSL HSLLSLDTAT LEAMDLPFTL PGDDNFEMTS GGTKLRVTTK NLSRYFHRAA
AGLLYESAVF PIRFLVYGFH DVVPCGALTA LDPEDMMELL CGSKQCDSQP LWTLSEIKSI
LVPDHGYQND SPQITMLQNV LAKRLTPREQ RLFLLFCTGC PRLPAGGIGS LGAITVVRRS
DVAFFTQFFN SGYGSADRGS HSASTSRDNE LTGSLTEKDW PLPSVNTCFR YLKLPPYPTE
EIMYRKLQLS ITQGGETFQL S
//
