ID A0A178BD92_9PLEO Unreviewed; 1159 AA.
AC A0A178BD92;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=SNF2 family helicase/ATPase-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ06DRAFT_289196 {ECO:0000313|EMBL:OAL07473.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL07473.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL07473.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL07473.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV441705; OAL07473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178BD92; -.
DR STRING; 765868.A0A178BD92; -.
DR InParanoid; A0A178BD92; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD/H BOX 1; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 584..755
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 947..1110
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 130644 MW; A2C9497C4B766E7D CRC64;
MYRDDPIVSS SPPRARSNSP YVTQPTQPFE ARSPLYAVPT QPTLPLTPRA NRQYQSPTPQ
LQVPRSSPGA ERYSSPVMSQ PHSQSQRPMA YNLMAPPGTS FLPPQPVRKQ VFDLTSDDPP
VERDPFEEES GYRSNIPLSK VEMGSRMTRV EETPPQKPSW NLSGYAYTGN AENTNQRKRP
SAGLAASTPP KKQKMAPLRQ GGPSRAMPVD LTEDEPMTLD DIADADLKRK TVRLLAIYPN
RSIQKLYDAL LRKKGHMDDA CDLLGEEESE DEELKSPQIG VARTNTEMAA KKSTAQRMAK
APVKSILDKY TKLHATQITP TGPITSPAHD DEQPKPKRRL IRGRRNPLPS SPDASPVRPQ
PTIQNRPHVI ESDDEDMNDG VVEISDDDSA QGASSEHEVG ASSLLGFFND CTVEAMVDLS
GHKEEEVKEL LDQRPFNSLD DVRKIHVDLQ QQSQEKGKKK ARKPRITFGA RLVESAEDMW
DAYSTIDSVV KKCENLGKPM IAGMERWGIN IFGASTEDGV EITSLDDNSD SSSNRDSGYH
TPHSDVGVSE IRKNKRAKLL KQPAIMNEGF ELKDYQVVGL NWLNLLWENK ISGILADDMG
LGKTCQIIAF LSHLKEQGNS DGKPTLIVVP GSTLENWCRE FERFSSTIHF TPYYGTQAER
YEHQETILDN INQGECDVII TTYDLTFRKP DNAFLRKCRP KICIFDEGHV LKNANTIRYK
SLMRIHTQCR ILLTGTPLQN SLQELMSILG FLMPDVFYGE DSDVPDMLQI LFKHKAKVTE
TNSHSTLLSA QRIHRARTML TPFILRRKKA QVLKHLPAKT SRVEYCDLTE TQKQLYTEQL
EKQRRILQDR AAGILVKDHA NVMMKLRQAA LHPLLFRHRY TDDKIRKMSK ACLREDMFAE
SSADLIFEDL TVYQDYQCHQ LALKYPGALK KYQLQDREWM DSGKVLKLLE LLKQYKENGD
RALVFSQFTS VMDILSWVFD EHDIAFMRMD GSTPIGERQS MMDDFYNDES IGVFMISTKS
GGAGINLACA NKVIIFDSSF NPQDDIQAEN RAHRVGQTRE VEVVRLVTRD TVEEQIYALG
ISKLELDKMV QGEEADDGAA SKKKGKKEEG EKISKAEEAG IEAVEKMMLQ QLASGGEKKE
DVKDLFKDGL KKAGVNIAE
//