ID R7YYL3_CONA1 Unreviewed; 1513 AA.
AC R7YYL3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=W97_06281 {ECO:0000313|EMBL:EON66879.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON66879.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
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DR EMBL; JH767583; EON66879.1; -; Genomic_DNA.
DR RefSeq; XP_007782196.1; XM_007784006.1.
DR STRING; 1168221.R7YYL3; -.
DR GeneID; 19903592; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_0_4_1; -.
DR OMA; VYGYQSH; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000016924; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
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:UP000016924}.
FT DOMAIN 211..385
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 425..613
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 169566 MW; 97712878762262B0 CRC64;
MEPEHYPREH YAFTEDDTAA GRELPLDAFD EEMLRRPYDD RQRQATQGRA RLTLAPRHTE
RSTQAREPSY PGQEYGSRGV MSQLDYATGE APNLSQFAYS PPSAPDVSSS PHILPSSPAI
RASQRRNDLR RSNSRPQRQY EDEPYDDRPR ASAAQDSQPS YYKAAPKQMV LQHAPPVAQG
IELVPTHELP DRFRSIFPFP LFNAIQSKSF QAVYRSNDNF VLSSPTGSGK TAILELAICR
IINGYSGGQY KIIYQAPTKS LCSERQRDWQ KKFGPLDLQC AELTGDTDGA QLHKVQNASI
IITTPEKWDS MTRKWKDHEK LMRMVKLFLV DEVHILKEDR GATLEAVVSR MKSVGSDVRF
VALSATVPNL EDVAAWLGRN PTNQGTPALH EKFGEEFRPV KLQKHVVGFQ SNGNDFVFDK
VMDAKLPDVI AKYSQRKPIM IFCCTRKATV NTAKLLANWW TTKGPGDRYW EAPRRHVKVL
DNDLRNCVSA GVSFHHAGIE QADRLAVEQG FLGGDINVIC CTSTLAVGVN LPCHFVIIKN
TVSWQGNVCK EYADLEVMQM LGRAGRPQFD DSAVAVIMTR TEKARHYEKM VSGEEILESC
LHLNLIEHLN AEIGLGTVRD LHSAKKWLAG TFLYIRLREN PNHYRLEGDS GSGSLDERLE
RICDRSVSLL REHELVEDGS TLRSTEFGDA MARYYLQFQT MKVFLSLQPK AKLSEILSAL
AQAAEFREVR FRSGEKPLYK ELNKSPFIKF SIPVDLAMPA HKVSLVIQSV LGGIDLPVDD
KTAKHRIQYN TDVSIIFQHV HRLIRCIIDC QLYLEDSIAS RNALMLARSL GARVWDDSPL
QLKQIEQIGI VAVRKLVNAG VKTIEELGNM EPHRIETVLS KHPPFGMKLQ DRLKAFPKLR
VSVQMMGKTI KPGEGVKVNL RVEIGFMNEK IPETYQKKPV YVCLLAETSD GHKVHFCRIS
AKKLNKGQDV LFSANMSSPS QSITCYVMCD EIAGTLRQAS LKPEIPVSAF PTPKAAKEAE
LSTRRSNDLH KPGPNTSKRR QDSVRLSHAA QNDDDFEDLD LDDSDFVKAA TTDLDFTHID
TLRSRTSAAT RKNTVSNAKS KKTPQHEPVQ EEEEREARRL DNGKWACNHI CRDKTSCNHL
CCREGMEKPP KRPKNKSTTG EKTSTQQAGG KNQKKPPGIQ GTQTKLNLNA TKSRPQPTLD
RASIECVDLS KREISDDYMA HAPRDYKALH RLHTSVQKAP PLPPSATRVM RNKPDYSYAE
GGIPSLSFLG DTRDTRDTEH RKSSEDYGGW PSPSVMAEDH MAEDHMADTM SPPHEPEEMD
MDQRSDSPRI SDDDSMLDAV MVGLADSEDL KPTQRTEDNS LPATQAYDDG DFSWSGPPKR
LSTPGLASPS PGKLVVPAPK EEKSLFVTDA SSSQAPESTP DGPPKSFLGF KRARELIEMP
QPMMPSLTKK SKKPLYDDKP KEKNAAEPVG EEEKWAPVAC EKSTPPAEIK QRPEFEGLEA
WIVAEFGDVA EFV
//
