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Database: UniProt
Entry: C9Z4E5_STRSW
LinkDB: C9Z4E5_STRSW
Original site: C9Z4E5_STRSW 
ID   C9Z4E5_STRSW            Unreviewed;       949 AA.
AC   C9Z4E5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Putative helicase {ECO:0000313|EMBL:CBG74347.1};
GN   Name=helY {ECO:0000313|EMBL:CBG74347.1};
GN   OrderedLocusNames=SCAB_73621 {ECO:0000313|EMBL:CBG74347.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74347.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG74347.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG74347.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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DR   EMBL; FN554889; CBG74347.1; -; Genomic_DNA.
DR   RefSeq; WP_013004887.1; NC_013929.1.
DR   AlphaFoldDB; C9Z4E5; -.
DR   STRING; 680198.SCAB_73621; -.
DR   GeneID; 24310299; -.
DR   KEGG; scb:SCAB_73621; -.
DR   eggNOG; COG4581; Bacteria.
DR   HOGENOM; CLU_002902_4_1_11; -.
DR   Proteomes; UP000001444; Chromosome.
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; 1.10.3380.30; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012961; Ski2/MTR4_C.
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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CBG74347.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          59..217
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          297..501
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          263..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  105657 MW;  94662BD19FFDA682 CRC64;
     MIVLLSVGPG TLESTMTEDL SPAERYAAAR RRAAEQATAL ASFREMYEFG LDPFQIEACQ
     ALESGKGVLV AAPTGSGKTI VGEFAVHLAL EQGKKCFYTT PIKALSNQKY SDLCRRYGAD
     KVGLLTGDNS VNSDAPVVVM TTEVLRNMLY AGSRTLLGLG YVVMDEVHYL SDRFRGAVWE
     EVIIHLPESV TLVSLSATVS NAEEFGDWLD TVRGDTDVIV SEHRPVPLFQ HVLAGRRMYD
     LFEEGEGNRK AVNPDLTRMA RMEASRPSYQ DRRRGRAMRE ADRERERRQR SRIWIPSRPE
     VIERLDSEGL LPAITFIFSR AACEAAVQQC LYAGLRLNDD ENRLKVRALV EERTASIPHE
     DLHVLGYYEW LEGLERGIAA HHAGMLPTFK EVVEELFVRG LVKAVFATET LALGINMPAR
     SVVLEKLVKW NGEQHADITP GEYTQLTGRA GRRGIDVEGH AVVLWQRGLS PDHLAGLAGT
     RTYPLRSSFK PSYNMAVNLV EQFGRHRSRE LLETSFAQFQ ADKSVVGISR QVQRNEEGLE
     GYQESMTCHL GDFEEYARLR RELKDRETDL AKQGAAQRRV EAAVALERLK PGDVIHVPTG
     KYAGLALVLD PGLPAGRSNG HRGFEQHDGP RPLVLTAERQ VKRLASMDFP VPVEALERMR
     IPKSFNPRSP QSRRDLASAL RTKAGHLVPD RHRKRRAAAA DDREIARLRA ELRAHPCHGC
     SDREDHARWA ERYYRLKRDT AQLERRIEGR TNTIARTFDR IVALLTELDY LRADEVTEHG
     KRLARLYGEL DLLASECLRA GVWEGLGPAE LAACVSALVY EARAADDAMA PKLPSGNAKA
     ALGEMVRIWG RLDALEEEFR ITQSEGVGQR EPDLGFAWAA YMWASGSGLD EVLREVEMPA
     GDFVRWCKQV IDVLGQISAA APAGSSVGKN ARKAVDELLR GVVAYSSVG
//
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