ID A0A135THN1_9PEZI Unreviewed; 1281 AA.
AC A0A135THN1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DSHCT domain-containing protein {ECO:0000313|EMBL:KXH47615.1};
GN ORFNames=CSAL01_10020 {ECO:0000313|EMBL:KXH47615.1};
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:KXH47615.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH47615.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH47615.1,
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 -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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:KXH47615.1}.
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DR EMBL; JFFI01001969; KXH47615.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135THN1; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 1.20.1500.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR InterPro; IPR040801; Ski2_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF8; HELICASE SKI2W; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR Pfam; PF17911; Ski2_N; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 321..477
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 605..806
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 217..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 142825 MW; 0D9E1C3958FF2AD4 CRC64;
MASDLAAAIQ GLYLEDLPDS NIDDILFQQR PSKRVKQDVS ELKTSLETDF LMPCMKFSPE
WLNGLQQRWD CPVDYTELFK IGNPQTRTVT RFERHGLEGR VSGYRNVTVP ANSATAKNST
SFLRKPANRA DFVRGAAGFF PFAPGGLDGI EATAALEDQV HRSGGGEAAA LSNNKLERVI
KLGVEGGLLE VAPGLSRGLN IGQKKADEDE ARAIEQELDQ EPEQPPGVDE ADGEAQTNDD
KVDEADSEVE EDSEDIDAIL PVEFPALEPH GALAASSARK AGREWAHMVD IDRDITNFRE
LVPDMARDWP FELDTFQKEA IYHLESGDSV FVAAHTSAGK TVVAEYAIAL ATKHMTKAIY
TSPIKALSNQ KFRDFRQTFD EVGILTGDVQ INPEASCLIM TTEILRSMLY RGADLIRDVE
FVIFDEVHYV NDFERGVVWE EVIIMLPEHV TLILLSATVP NTYEFASWVG RTKQKDIYVI
STPKRPIPLE HYLWAGKNIH KIVDSDKKFI EKGWKEANSA IQGKEKTRAP EPVNAPRGGG
GQRGGQRGGG GAQRGGQRGG QRGGGPQQRG RGGAPRTSHN PGHMGRTGRQ GGFASAAQDK
NLWVHLVQFL KKSSLLPSCI FVFSKKRCEE NADALSNQDF CTATEKSAIH MTIEKSIARL
KPEDRALPQI IRLRELLSRG IAVHHGGLLP IVKEIVEILF AQTLVKVLFA TETFAMGLNL
PTRTVVFSGY RKHDGHSFRN LLPGEYTQMA GRAGRRGLDT VGSVIIVPPG GDEAPPVADL
QKMILGEPSK LRSQFRLTYN MILNLLRVEA LKIEEMIKRS FSEHATQQLL PEHEKAVKIS
EADLAKIKRD SCSVCDVSMD ECHQASEDYK QLTGEVYKSL IGITIGRKMF SQARLIVYNR
DGIRTPGILL SDGASDKGQG GPTLHVCEIR LMRETRDSTD LLPFIPAFRK YFTPLPQAKK
HVRIKTLQVP LSDVECLTRY VTKGIVPEIF QGGEKYAKAK DRLHALCRSW DDLWDEMDLS
KIKNLSFQEM MKKRKDTEVV ASSSPALSCP QFLKHFAMCH DQWLIKEHIS QLRQSLSDQN
LQLLPDYEQR IQVLKQLQFI DDSARILLKG KVACEIHSGD ELVLTELILD NVLADYEPAE
IAALLSAFVF QEKTDTQPNL TGNLERGKGT IIAISEKVNE VQTLHQVIQS ADDSNDFISR
PRFGLMEVVY EWARGMSFKN ITDLTDVLEG TVVRTITRLD ETCREVKNAA RIIGDPELYQ
KMQTAQEMIK RDITAVASLY M
//
