ID G0UTC7_TRYCI Unreviewed; 2431 AA.
AC G0UTC7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Uncharacterized protein TCIL3000_9_350 {ECO:0000313|EMBL:CCC92641.1};
GN ORFNames=TCIL3000_9_350 {ECO:0000313|EMBL:CCC92641.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC92641.1};
RN [1] {ECO:0000313|EMBL:CCC92641.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC92641.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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DR EMBL; HE575322; CCC92641.1; -; Genomic_DNA.
DR VEuPathDB; TriTrypDB:TcIL3000_9_350; -.
DR OrthoDB; 120727at2759; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd11709; SPRY; 1.
DR Gene3D; 2.60.120.920; -; 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 Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR042469; HECTD3.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR PANTHER; PTHR46654; E3 UBIQUITIN-PROTEIN LIGASE HECTD3; 1.
DR PANTHER; PTHR46654:SF1; E3 UBIQUITIN-PROTEIN LIGASE HECTD3; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 4: Predicted;
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};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 1307..1337
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1689..1882
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 2282..2431
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 2398
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2431 AA; 269211 MW; FE78D27B3E4FADCA CRC64;
MFSNGISPCI GTKAPHPLVR ELTEMSDAAL CKLVPCRQSD VCGVREALCI IGSFLARRDP
DQVMWGSWVW QDAVKRVGLA SSALRWRSDV TDLVTFALGN AAPCEPSPVQ IVEGTIALLT
SDITVSQLRE YLATQSNRAK TCVRALLLLL RAKENFLPSD LFCVVRLLRD LMACQGDHYL
LRFRGCGEVL LHQIRDLVHR LLTAMFKALQ CVMSPLEGER RGLGPHRFLW DTDEFGPFAL
VTLSLLATPL DERDLNFIWH KIVSQVEELL PRFTDFSRTA SFKVDEVEED SVLRSMQALV
SDSEFDGNGG SVIGSAEVGN GEEYDSFVGL TMNGANEFSM GVWIPTGEGR VCSTSTPLYS
PSVQFSSLSP VETLSSPPLL ASAVSSPRPA PSVSSPAHAA SLPCVADISL VCSPSRALFI
ALASERHGKL TKSVIDDDPL GFYFNPQSGQ LHHGNRVYSM PPITHGDTLT ICFLFLPKMT
TRVLCFLVNG VRFASFPTPP QSLYLVVGVM DSSPLSRNTV RISFRLHKEL DTLLSTRAVP
TTACSGVGEA IFSGDGLPTR SFISMFATFM FAYLVSLCTR RLAQVRRTVS GSSTATTTPL
RVIAGSTTSF QSEEAWGSFI DGCCDRLRHN VESLIESTRH LSLLDGISDA TERVKRCAAF
FVYHRFLMDY ITIMRTAIYC SSRPVDILST LAKVVCCEEA GERAQCAALT SIYTVLLEPS
ANFDAYVFNP MQLWDCCCSL SRHTTAPGYK ALFTPESTAR ELRVVSGGSH ILSAAPGGCN
SRATQNTVSF ASQGIPLDGS LGDVISFSVR IKRGFDFDSL GRFYYIGVAC PNPSSTKTTL
ERIPKSREEM KYVYAITDYF TDMEPSSACV ELPRHSKHWM NSQEKIIFGS GDIITVTIYT
KLRCVSFQRN GLTLGTLYTS IPQDVKVVFP FVEMYNKDAC ATWMYAPREL GIRARLVMRA
MLVHWGPILI TRLARMLEEK EVVALQVLGA DGDELSFIYS GPPCSERKGL YKVRLIKQMG
TAAEVVVEGE RAGGSNDSGG AFTVPSVALE PNYSSVISNN LPLKLVVEEI ARIISRCISF
TTDEIDGEVV HIRSTKVFMC AVRLLSELEV DDVVLASIEA HRTLLNDFLR ILAVSDVVPL
DGPRVVLDAW NELMLLPDDD ELRMTLSPEA VSLGNICDEN YWGVTSSGVE SNDEGEEIIC
LRCPACDKEW SSCTETDHAA PYSLCSTLHN VMQRLSLPSP FVGFACGWVL EEKSFRLNLR
AVSRDEIEGD GSDSRGVFSF TGTYVSSHCV RGRCVYKFVE NPNTAKRCDE EWTCSVCTFI
NLSDSTRCAM CTTARPGATW SCLLCSYAFN SINSKICTTC GHLRLGSGAA EAAADGSSKQ
TFCTDCGNIR EYTKFSTFEA HHFCDKCQRE VLWLPEDRHV GVVEARLAGA GDRMTWLLTF
GSEKCFYSNI KSTDYSFEEM LGAVSAVSAS ESNLSRYVPP LVHPRLSSEE GHSDFSVEGA
GSAQDSQKLV REYRAVIPAV LLFCSRVVCR WAPVLAPQEL TKSSILCRLR VLEDSWLTQF
EKVPIGVARR ILSSCLRILL DGQRNGRVVW SLSSVARAII NCNPLLQQQR HYLLYALSLN
VARRGADREF RELCYAALNM LLEDSCGQSL KVQCLQEVIA VTPFVAKQQQ LMVHASLRGI
NTEISAEVTL TSWLIDVVER MERGQSLPTT FNNTSPDTFP HIVELPDTRM GSGGELVVGQ
VRGSVGVFGN KGGHYYYEVV LPPNFDDRSK TIVMGWGTIQ HEVVSSGQHV GSDFHSWGFN
CQDRLRILSG EQALVTPRPI VGGDVVGTLL DLDTMMMCWS VNGEELMWIP VSTDGKGEAI
YPYVSASMEP YGVLVRLSYT QFKPEGYKDF SPVWSGDLIP EDKVKPQSLD FYRQLCCLVN
NVVNTGFTVD SLSETTTWME EALASLHNYP LLSSEIHDGS LQQLQPYLQH LRSINALAVS
VAKSHSIFRT SPLLMRSYEK ARQLLFFAAR WAIVERQIDR GLLRNNVKRN CQVSISLSAA
KNVPTRGGSF DFVTLFNSSI TGQLFRQTHE VDIYRDAVMF VTRLTDEVAD DAGGVTRSVV
SMMCDELSYR DDDGGSRVDP LLPFFKLSNH STIVNLVPNI DFYRNNPDHR KLFIQFFTWF
GKLIGNVTLS GYVLFSITLP RLVWMFLTFG EPTVDDYYFD IDDTVRGAVS DDEFLLNDEF
YNSIPVINSR PEANSDAVSG ACSGCHWDSA VLRSNADGTT TAFGRPPDFD ESAEAGRRRV
EVERRLVHQY DELLLAMRSG VSSVIPPHCL QLIRWDDLQQ RVCGSPCASA EDVMSSLDVS
LLSQGILDML TEVVRGLSNK QRAQFLLFCS GQRRVPLPER VKVLCGDDPS AFPTAHTCSP
ISLHLQPYSS AAIMREKLEV SIHHMYEFGF V
//