ID A0A135V1X7_9PEZI Unreviewed; 1328 AA.
AC A0A135V1X7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXH66582.1};
GN ORFNames=CSAL01_12007 {ECO:0000313|EMBL:KXH66582.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH66582.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH66582.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH66582.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000256|ARBA:ARBA00008593}.
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:KXH66582.1}.
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DR EMBL; JFFI01000640; KXH66582.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135V1X7; -.
DR OrthoDB; 170176at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR CDD; cd05402; NT_PAP_TUTase; 1.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF113; POLY(A) RNA POLYMERASE CID11-RELATED; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 299..353
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 493..547
FT /note="PAP-associated"
FT /evidence="ECO:0000259|Pfam:PF03828"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1328 AA; 144247 MW; D39604AC9611C83E CRC64;
MESRAATTES KHTYPTSPWI QAPTISSSTS GSYFGDASSR VPAQLDFWPL LFPQQASVYQ
AQLLHYTNLV SPGRGGGLHQ PQALPQATVA TPQIQAAPRS RSSSKVSNKE ISSTKGSQGG
HGNRAVQNKD KGDRAVITGK DAPPKMQQSS QQQPELSHPL PARPAARTGN GQSHSNSMPS
TPQQHARNFS FESREPSPTA TNNHSPRSAY SETNSNLPSL RPLPPRLGGC KYETSQINSK
RRMPYSIGSD KLDKTSLDTI KSKLSEDVET KLTTDMRELY DRLRPTEKVE ENRQKLVVKL
EKLFNEEWPG NDIRVHLFGS SGNLLCSDDS DVDICITTPW KDLEYVCMIA ALLAKKGMEK
VVCISGAKVP IVKIWDPELG LACDMNVNNT LALENTRMVR TYVEIDPRVR PLAMVIKYWT
RQRIVNDAAF GGTLSSYTWI CLIIGFLQLR DPPVLPSLHQ RQHQRLPKNG GPESAFADDM
DKLSGFGAKN QASLGELLFA FFRFYAYEFD YDKYVISIRL GRKATRMEKK WHIGINNYLC
VEEPFNTARN LGNTADEYSF RGLHLELRRA FDLISEGKLG ECCEQYVYPK EETPVFQRPP
NTSRPVMIRS SSQQHSGRGR GNFRGGRHSN NFQRNTNSNR RASSSVAYDT NTMYMPQVAM
TPQDLAWYAQ QAQSHQQYPA LVGAAMAAQV QQENNIRFQL YTQSQVYQQV QAQMAAQMHA
AQRMQGSSSA TPQGPERSRT NSFDNPPLSA PIAGPQDWYS MYGVPMAAYY GQSSFAYPSS
PATVATTTPE FRRGLQRSSA TTESGASTSG SSLRSQSQPA SRSASTAQHN QAYPGTSTPM
NTISNPTRQV NGIPVSNGAP GDAEYDEASQ APASNSPASD EGAYLGYYVS DASSPAHSQV
APNAIAFADT TQPAQGRRRL STEVPQTILD RRMRRTSRSP SPLGHARAFS GGNSTALAPV
VASGSTNGPR AASRPLVVNG TGSSLRTSST PSQRHNPAVI ATGPTPADDQ GRSSQENTLQ
VQGLGISGYA SEQLDGQAFL RSEPVQTPVS ERTPVIVNGT TTPSSTTNAT ASASPASVSA
PQQSASQSID DASFRDRIAL MSMNQYAWSP QAQVQTQPYP DVANGTQTSL RQRALSRQQS
GVIAPLDLAT RENRMNGHQL SIDAQHLSPI NETRSPSPTV VRKNDFASRA DQLPSASQSS
TPKAHAEPSD SGHRSNDNKG SVGKEPRQGH ASTHSPKRSS TAAQRSSQAT AQSQLQPHTS
GQAQAQSSRV NGVRENGHTR GAKSESHGAE SSWQKATKGR KKGADTKNHG GSASSEQPPK
HDADRKGG
//
