ID A0A161W8Y8_9PEZI Unreviewed; 1337 AA.
AC A0A161W8Y8;
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=Dshct domain-containing protein {ECO:0000313|EMBL:KZL83695.1};
GN ORFNames=CI238_07686 {ECO:0000313|EMBL:KZL83695.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83695.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL83695.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83695.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL83695.1}.
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DR EMBL; LFIW01001087; KZL83695.1; -; Genomic_DNA.
DR STRING; 1573173.A0A161W8Y8; -.
DR Proteomes; UP000076584; 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:UP000076584};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 378..534
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 660..861
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 252..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1337 AA; 149658 MW; D7BBC98BAC14FB35 CRC64;
MLTCCERRTF QVKISFHRCC RYPRLTSTQP LPYLTHNPSL ERPSVAYHHI VKMAADLATA
IQGLHLEDCP NENIDDILLQ QRPRKRVKQD ASHLKAHLEA DFLTPSTQFS PVWLNRLQQR
WDCPVDYTEL FKISTPQTRT VTRFERHGLE GRVTGYKNVT VPANSATAKN STSFLRKPAS
RADFVRGAAG FFPFAPGGLD GIEATAALED QVHRAGGGDS AAASSNKLER VIKLGSEGGL
LEVAPGLSRG IDVNKKKTNE DEARAVEQEL DQEPEHAPGA EEAEGEARTN EEIEAGANTG
AEAESEEEDG EDIDAILPVE FPALEPHGAL ATSSARKAGR EWAHMVDINR DVTNFRELVP
DMARDWPFEL DTFQKEAIYH LESGDSVFVA AHTSAGKTVV AEYAIALASK HMTKAIYTSP
IKALSNQKFR DFRQTFDEVG ILTGDVQINP EASCLIMTTE ILRSMLYRGA DLIRDVEFVI
FDEVHYVNDF ERGVVWEEVI IMLPEHVTLI LLSATVPNTY EFASWVGRTK QKDIYVISTP
KRPIPLEHYL WAGKNIHKIV DSEKKFIEKG WKEANQAIQG KDKPKAPELS TAPRGGGGQR
GAQRGGAQRG GQRGGQRGGG SQQRGRGGAP RASHNPGHMG RTGRQGGFTS AAQDKNLWVH
LVQFLKKSNL LPACIFVFSK KRCEENADAL SNQDFCTANE KSAIHMTIEK SIARLKPEDR
ALPQIIRLRE LLSRGIAVHH GGLLPIVKEI VEILFAQTLV KVLFATETFA MGLNLPTRTV
VFSGYRKHDG HSFRNLLPGE YTQMAGRAGR RGLDTVGSVI IVPPGGDEAP PVADLQKMIL
GEPSKLRSQF RLTYNMILNL LRVEALKIEE MIKRSFSEHA TQQLLPEHEK AVKLSEADLA
KIKRDSCGIC DVYMDECHQA SEDYKQLTGE VYKSLIGIPI GRKMFSQARL IVYNRDGIRT
PGILLSDGAS NKGPQGSPTL HVCEIRLMRE TRDSTDLLPF IPAFRKYLTP LPQAKKHMRI
KTLHVPLSDV ECLTRYVTKG IVPEIFQSGE KYLKAKDRLH SICRSWDDLW DEMDLSKIKN
LQFQEMMKRR KEAEVTASSS SALSCPQFLK HFAMCHDQWL IKEHISQLRQ SLSDQNLQLL
PDYEQRIQVL KQLQFIDESA RIQLKGKVAC EIHSGDELVL TELILDNVLA DYEPAEIAAL
LSAFVFQEKT DTQPNLTGSL ERGKDTIIAI SEKVNEVQTL HQVIQSADDS NDFISRPRFG
LMEVVYEWAR GMSFKNITDL TDVLEGTIVR TITRLDETCR EVKNAARIIG DPELYQKMQT
AQEMIKRDIT AVASLYM
//
