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Database: UniProt
Entry: A0A162W1V6_DIDRA
LinkDB: A0A162W1V6_DIDRA
Original site: A0A162W1V6_DIDRA 
ID   A0A162W1V6_DIDRA        Unreviewed;      1255 AA.
AC   A0A162W1V6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=ATP binding {ECO:0000313|EMBL:KZM18738.1};
GN   ORFNames=ST47_g10111 {ECO:0000313|EMBL:KZM18738.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM18738.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM18738.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM18738.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KZM18738.1}.
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DR   EMBL; JYNV01000322; KZM18738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162W1V6; -.
DR   STRING; 5454.A0A162W1V6; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45626:SF52; SNF2-RELATED DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000076837}.
FT   DOMAIN          1007..1157
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          22..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1255 AA;  139773 MW;  356872167525C152 CRC64;
     MSGSLLVERG MNGRMHHSSL NAIGCSTASG PKNTTRDDDA ASNATATAAS TPQASVSSST
     EENKLEDLKH YIALGCLHLD QHIPAQGGQA PILDLAWDEL LHSRFPGEVR LIIGNEASQL
     LDAQWIRLFL HRSQRETLGS VARVYLLPED WSRRSISRSS ITLKKALRQL LSRIDTSPDT
     WAGNVSDKQI QPFDPWAGQL NTSLYYLFNK LPSPAPSPAN IKSRYARRAA NDLIGSAEAS
     DWEEDGQQPL KGLRTRLYPY QARSASLMIE REFAPQLQLD PRLETRKSPN GDRFLYCARD
     GSFLQDPRFY ESNRGGILAE TMGLGKTIIC LAVILASQGN HPQIPALYQR PLPVRTRVGT
     LKEMASHVPG RYAIPGKVCL EEMADHADVN LPRLKDVLDE NIPFYEIPPE MPRMNRNTRM
     PPARQYVMCS GTILVVPKNL LHQWQSEIRK HLLPQALKIL IVDTVSKHNK VKAVPLHQED
     FAYAHELPAP TELMKYDVVL FTRNRFEQEI QDGVDNQGRR YVAGVSRACM CPYIGATRIP
     DCNCFGSGTV YESPLLKLHW LRIIIDEGHN FSSATSNAVL VAKQIQVERR WVVSGTPAKD
     LVGVEVDMST LETNDEDPTS LRASAIEQRK SFNLTDESKA VKALGSLASN YLMVRPWCAS
     SAEGGLEWDE YVYRHEHSHR KTYSGFSTCF QRILEGLVVK TRPEDVEKDI VLPPLRHNVV
     YLQPCWYDKM TANLFIQVLR ANAITSERID VDYLFHPNSV KDKHNLIRNL RQSNFTWTSF
     SVETVVSTLE TSAKYLSKDD KKCSVEDAQS LLESSHSVAG LPATSDWAAL STAHEVGVAV
     EKWPAESEES FAFAYPDEPT MIGMTQLLEG QLHVDSNIRS DDPSNNLVLV GEAGKAKIRA
     MNEAEHKIKQ PIDDASADAE ATSRKTGIPP VLIEGSQPLN SRRASILASK VSPIKPGRTE
     PTDTPEPSTP LPARPKKRKL THDDETATLP AGSPLLETRI IGTTSAKLTY VVDKVVEHQA
     SKKIIIFYDG DNAAFYIAQS LEALYVNHRI YARQLDNTKR SEYVRLFNED DSVRVLLIDV
     ACGALGLNLN AASVILIVNP INRPALEAQA IKRAHRIGQT KEVIVETLVL ENTIEHAIFE
     RAKNMSRAQH MEAKELEDDA GIVEIIQNAQ ILPVLDEELG LAKYALLKRP QQLFGRPDRD
     RYHRIPVKDT PEKSRKKRKI SNTTTPSRGS GVDTPIVIGG LSSMSSRAGP LVSEL
//
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