ID A0A139HVX3_9PEZI Unreviewed; 878 AA.
AC A0A139HVX3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=SWI/SNF chromatin remodeling complex component {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC578_8501 {ECO:0000313|EMBL:KXT06631.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT06631.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT06631.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT06631.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT06631.1}.
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DR EMBL; LFZN01000005; KXT06631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HVX3; -.
DR STRING; 321146.A0A139HVX3; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000070133; 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; cd18009; DEXHc_HELLS_SMARCA6; 1.
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; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044753; HELLS_N.
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; PTHR47161; LYMPHOID-SPECIFIC HELICASE; 1.
DR PANTHER; PTHR47161:SF1; LYMPHOID-SPECIFIC HELICASE; 1.
DR Pfam; PF00271; Helicase_C; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 229..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 643..810
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 98669 MW; 272530BADAE1CDCE CRC64;
MSSEAAESAK STPPTSPETR DGGGTTEAME KEEARMVEAR RKEDEKREKK MAAERAKDIK
GGKEAVDSKY KALEYLLNQS KLYSAIMLEQ MTQQEQADEA KDEKSKKRAL KREDTAEKVA
QESQKRATRT AAANGGKVDE ESPKKQLPKR GRPAKNTKSE KISDYMKKED VAAKAGQTSI
SEALAEETKD ADVKPGDIGF QELRSAKQPD LVTGGLMRTY QLEGLDWLTS LYENGLNGIL
ADEMGLGKTI QTISFLAFLR EKGVNGPFLI AAPLSTTSNW VAEFKKWTPS IPVVLYHGSK
QEREDIRRKK LRNPGSETFP VVCTSYEICM NDRKFLAHYG WKFIIIDEGH RIKNLNCRLI
RELQSYQSAN RLLITGTPLQ NNLTELWSLL HFLMPSIFDK LESFEAWFDF SALKEKNGYE
QILSADRQKN VVASLHAILK PFLLRRVKAD VETSLPKKRE YVLYAPLTQT QRELYQEILE
GNSRAYLENK VVETLSRDST PASTRSGSLK RKAAGGTATP NKSAKSSRAS TPATNASTSA
RSRKAKKHQK YEEVSDAQYF KQLDEAPSSP AGEDSDSEEE ENTERAKTLA LAKREISQKK
LQNPVMQLRQ CCNSPHNFYY PFDLDDNTPV DETLVTESGK MLLLDRLLPD LLNKGHKVLI
FSQFKTQLDL LETYCSELRG WPVSRIDGSV AQTDRQQQIL DFNDQKSDTN IFLLSTRAGG
QGINLASADT VLLFDSDWNP QQDLQAQDRA HRIGQTRPVI VYRFATKGTV EQMLLEKADS
KRRLEKLVIQ KGRFRSRRGE GAGADFAELQ RLLGKDDGER IDLAEGKGLL SDDDLAILTD
RSPEAFERAE KGLDTVGEMF KAVQTRKDGD GLLESLQK
//
