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Database: UniProt
Entry: C9ZY44_TRYB9
LinkDB: C9ZY44_TRYB9
Original site: C9ZY44_TRYB9 
ID   C9ZY44_TRYB9            Unreviewed;      1857 AA.
AC   C9ZY44;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Polymerase nucleotidyl transferase domain-containing protein {ECO:0000259|Pfam:PF01909};
GN   ORFNames=TbgDal_IX4190 {ECO:0000313|EMBL:CBH14343.1};
OS   Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH14343.1, ECO:0000313|Proteomes:UP000002316};
RN   [1] {ECO:0000313|Proteomes:UP000002316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX   PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA   Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA   Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA   Barry J.D., Berriman M., Hertz-Fowler C.;
RT   "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT   chronic human african trypanosomiasis.";
RL   PLoS Negl. Trop. Dis. 4:E658-E658(2010).
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DR   EMBL; FN554972; CBH14343.1; -; Genomic_DNA.
DR   RefSeq; XP_011776609.1; XM_011778307.1.
DR   GeneID; 23860430; -.
DR   KEGG; tbg:TbgDal_IX4190; -.
DR   VEuPathDB; TriTrypDB:Tbg972.9.4190; -.
DR   OrthoDB; 170343at2759; -.
DR   Proteomes; UP000002316; Chromosome 9.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; IEA:UniProt.
DR   GO; GO:0071076; P:RNA 3' uridylation; IEA:UniProt.
DR   Gene3D; 1.10.1410.10; -; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   InterPro; IPR045862; Trf4-like.
DR   PANTHER; PTHR23092; POLY(A) RNA POLYMERASE; 1.
DR   PANTHER; PTHR23092:SF47; POLYMERASE SIGMA, PUTATIVE-RELATED; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          491..537
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          999..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1494..1571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1636..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1764..1783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1809..1857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1042
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1266..1287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1494..1544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1641..1679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1722..1742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1766..1780
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1857 AA;  199549 MW;  6ECE219DC14FBEAF CRC64;
     MSFDSKPGCN ELEGELHDSP IDPQDSSGAC VSLHERQIQH WSPLETPSSP SDHLEGAESV
     RAHGDLFFPL DEYLSSEVVL VPSRHVSQCG SSSADVVASA AACVSVAHED LSESTEHINI
     AQTDNACENS SGSDVCTQLK DEEMAQANSP PQLCATVLPV ACVLDEISAD SPCTLNSVPI
     TRGGFIEDNT TAGVGTGVSE DTESSNTVER RDLDHGIEEP TAKSSKRSVG PAKDSESSLN
     GIRPPRKVAR GRAAETTKTQ QVPQRARTAA PPTSSTLPHE RILDDPQHGR WPSASGISSI
     DHAVTSETSC RTNKGKSNDG SRKQSSRVGP KSNNNNNGSA SELGKGSNSL DGGVSGDKSG
     PARPATPHRS RRHKARQQQQ VEETFGPFGF PFQRNMMLDS MPDGAQRVAE HTAMMLAQKQ
     QLLYPVPLQG DTSKMIDVSG GTPHWSMLPS YYFVSSLQIY VDTCLGLRGG DRQERHEFVS
     RIQRITTKVL GPRARLRMHG SITTDLALAS SDIDILVVGY EPLAPLQAIQ QLSKAIQSIS
     GEELEGLSLE PAEGCSLETE VMHQPGNSSS LRESTGVVSV DNNVVDTTGS GVEENLLAMA
     VEPPESDCIL RVEEEEAEYR LQIERDYALS TRVGPNAAAV ALHSCIPSFT SAPLPPLPPL
     GRRRLYVPTV DGPLYQVQTI ISTRVPVIKV TEKMTGLRCD ISFAGGEHWR SMQLTNRLLK
     RYPTSRGLIL FLKHCVRQMG IGDSQPGDMT SFAIYLLVHH FFNEISKHLE ETLREQIRRQ
     QQVGDGAQPC VQNPCELDPR NPTGGRSSPC VPSLRVQVSP SAHHGSGTTS PADQKPSSPD
     DRFPVVTGML LGQFLSRQQQ HSNQQGGNSR LSTEGILKSF ILSMESEEVR GGAKGVDEAQ
     LPTKSGSPPN QIAEALDEWQ QQQQQHTDVT EAPVVTVPGS VVSQSLDESA VDTAAVDDFD
     GRDIVCCDDV VDESAAGGPT CPNPMVECGS FSVSGAVEDG DVNAKHPSEE VEDGEPVGEG
     ERNAETPDED AERKVGTESQ AESVEEDDLV RCTVHRLLTT SPLGHLFNDF CYYYGFVFNY
     DTQGLRFGPD GSSLVVPKPQ QCQQRGQHLY MTSPFDVQYD ITAHMMHTRA FQELCCMFVP
     LTNPLPLLTG DGSNVCTLRQ VLEWISPDTA HKELIEVHNA VQMQQLHHGE VQQVPQVNPQ
     LALENDRCTL FPSSRGRLSS GIEERSTSPS QLNFPDDGNE LSSGGRSLRP RDQSHGRKGG
     KNANASSGLR DVNDGSAGST GSSRGGKGLP ANGTYVSDAT KGRSGQPVGW RQGKRSEGDS
     EDVGAETRTA AVSATSPASE VSSAMDAEVS VVSPSPFPNA PLASGSKMVK GAPAMGDVNA
     GNCDPTYVPT NPTHANVLPG QQPMNFVADP SLSMFMFPPG GVNSPYPGMP QYYHPMPYTT
     EAQLHFRPDA YQQHPMAPFV YQGYDMNQMF PHRVMGDTTN DSVVNATNTV VTGKRQSSAY
     GSSTHSNTQS SARSGVSGNF LSRGRGRSSH RGSGSNNNGG EKASQYKAGH SDALEEQAPT
     PVVSSPSLTA EPLGTATFGG LTSSGINRDS MTTIAVGTVP GKEHQQQPLQ SYVGDPKEWL
     KPETPTQGIE FHHYSHQTHR QASYPHHQQS SAPQHYHHHI QSSPKMRSNT QQQAQGHWRH
     QRCTMMMVPS PMYSIMSGME GTATTSLCSP AQAGSPFQKQ AAGGGSVFSS ASQGATSPSG
     FSMSSALGMP DCGKVGNVVT DNHQQHSYHH HHHHFIHHNV HIQQRWPQPL GQQQRAEGTT
     TNTNTAAATV TSVGSGNGGK GAGGAPRPVA TQSLDGRPEE FSLEKIHQQG AGDTNSM
//
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