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Database: UniProt
Entry: K2T109_MACPH
LinkDB: K2T109_MACPH
Original site: K2T109_MACPH 
ID   K2T109_MACPH            Unreviewed;       831 AA.
AC   K2T109;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=SNF2-related protein {ECO:0000313|EMBL:EKG22600.1};
GN   ORFNames=MPH_00068 {ECO:0000313|EMBL:EKG22600.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG22600.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG22600.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG22600.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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:EKG22600.1}.
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DR   EMBL; AHHD01000006; EKG22600.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2T109; -.
DR   STRING; 1126212.K2T109; -.
DR   VEuPathDB; FungiDB:MPH_00068; -.
DR   eggNOG; KOG0390; Eukaryota.
DR   HOGENOM; CLU_000315_10_2_1; -.
DR   InParanoid; K2T109; -.
DR   OrthoDB; 5480555at2759; -.
DR   Proteomes; UP000007129; 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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013967; Rad54_N.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08658; Rad54_N; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT   DOMAIN          255..433
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          588..741
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  94118 MW;  482C47523B1056CA CRC64;
     MYDEPSNESR QHADIRRYRS RPATLSDDKE NVTPAKKIAT LYGGTPQSVD RLIRPFKCPG
     SATPTRASEK PARKRRKINY SGADGDAEDG DKAYTNEDRL ALATRDVNKY PVFKVKDKDT
     AFRQRFSVPL LKKDVDAYNP NRPAPLLGMR QGAVFVARPL HDPTGEFAIV LYDPTVDDKP
     TPVEEDKDKD KKEDEQEKPK LDEPIVHKSL ADILGLKKKV EGRPRVPVVI DPRLAKVLRP
     HQVEGVKFLY RCTTGLVDPK ANGCIMADEM GLGKTLQCIA LMWTLLRQSP DAGKPTIQKC
     VIACPSSLVK NWANELVKWL GKDAINPFAV DGKASKEELI QQLRQWSIAS GRAVVRPVLI
     VSYETLRLYV DELKSTPIGL LLCDEGHRLK NDESLTFTAL NNLNVQKRVI LSGTPIQNDL
     SEYFALLNFA NPNYLGTKND FRKRYELPIL RGRDADGTDE DRKLGDERLS ELLTLVNKFI
     IRRTNDILSK YLPRKYEHVV FCNLAPFQRD LYNLFIKSPE IQQLLRGKGS QPLKAINILK
     KLCNHPDLLD LPGDLPGSES CFPDDFVPKD ARGRDRDVKS WYSGKMAVLD RMLARIRQDT
     NDKIVLISNY TQTLDVFEKL CRSRSYGCLR LDGTMNVNKR QKLVDKFNDP EGPEFVFLLS
     SKAGGCGINL IGANRLVLFD PDWNPAADQQ ALARVWRDGQ KKDCFVYRFI GTGTIEEKIF
     QRQSHKQSLS SCVVDSAEDV ERHFSLDSLR ELFQYQPNTT SDTHDTFKCK RCRSDGNQHI
     KAPAMLYGDT STWNHFVNDG EKGALAKIQD LLLRQETSEE AVSAVFQYIS H
//
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