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Database: UniProt
Entry: A0A1G4BH50_9PEZI
LinkDB: A0A1G4BH50_9PEZI
Original site: A0A1G4BH50_9PEZI 
ID   A0A1G4BH50_9PEZI        Unreviewed;      1115 AA.
AC   A0A1G4BH50;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=DSHCT domain-containing protein {ECO:0000313|EMBL:OHF00724.1};
GN   ORFNames=CORC01_04041 {ECO:0000313|EMBL:OHF00724.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF00724.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHF00724.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF00724.1,
RC   ECO:0000313|Proteomes:UP000176998};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) 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:OHF00724.1}.
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DR   EMBL; MJBS01000025; OHF00724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4BH50; -.
DR   STRING; 1209926.A0A1G4BH50; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000176998; Unassembled WGS sequence.
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; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd13154; KOW_Mtr4; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 2.40.30.300; -; 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   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 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   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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176998}.
FT   DOMAIN          183..339
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          453..625
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1115 AA;  126064 MW;  E8DF2623918CE602 CRC64;
     MDELFDVFNA QPDAQSESHS EPEHETEVVD PPQKSRKKDK KSKKRKADGG IKNGVAEQPE
     DDDMPDADET SKDGKDAEEA EDAAASSDEQ QEPHKDKRRK KEDEAQPVLT DTFQTAQSRE
     VAGAAVFTPA QDESLVLSHN IQHQVALPPD LDYEYVPLSE HKPPAEPARQ YSFKLDPFQA
     LSVASIEREE SVLVSAHTSA GKTVVAEYAI AQCLKRNQRV IYTSPIKALS NQKYRDFEAL
     FGDVGLMTGD VTINPTASCL VMTTEILRSM LYRGSEIMRE VAWVVFDEIH YMRDKTRGVV
     WEETIILLPD KVRYVFLSAT IPNAFQFAEW IAKIHHQACH VVYTDFRPTP LQNYFFPAGG
     SGIFLVVDEK GVFREGNFQK TMALIEAGKG QDPNNANASW KGKGAKKQTQ KGGQASDMKS
     DISKIIRMIM QKSFHPVIVF NFSKKEVENL ALQISHFQFN NDSEQAMVKT VFNNAIQSLS
     EADRELPQIQ NLLPLLQKGI GVHHSGLLPI LKETIEILFQ ESLIKVLVAT ETFSIGLNMP
     AKTVVFTQTN KWDGVQRRPL TPSEYIQMSG RAGRRGLDTR GIVIMMIDDK MEPDTARGMV
     VGEQDRLNSA FYLGYNMILN LLRIEAISPE FMLERCFHQF QTGASVPALE RDLVALQQER
     DSMSIADEAT VKDYYNLRNQ LEQYTSDMRA VIQHPEHCTD FMQPGRLVRI HDPKKTNNTI
     GGTDFGWGVV ANLIRRDRNR KPGEPEYPPQ ESCLIDVMMV VDQKSAPIAE GSRHLTSDLP
     SGLVPYSNPE QPDNGARFEI IPCLLTCVKT ISQIRVFMPK DCKSQSALNE VGNSLREVHR
     RFPDGLPILD PVENMGITDE SFRALMRKIE MLEARLLTNP LHGSPLLPEL YLQYRAKEKL
     GEQIKSKKKE IARLHSIAQM DELKARKRVL RRLGFLNESE VVELKARVAC EISSTEGHEL
     VLAELLFDRF FNELSPELIA ATLSCFVLDE KLETAQLREE LAKPYREVQA KAKQVAKVSR
     ESKLELNEEE YLAGFKWQLM ETVYSWAQGK PFADICKMTN AYEGSLIRLF RRLEELLRQM
     GQGAKVMGSD ELTQKFEDSL AKIRRDIVAA QSLYL
//
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