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Database: UniProt
Entry: A0A178BD92_9PLEO
LinkDB: A0A178BD92_9PLEO
Original site: A0A178BD92_9PLEO 
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
//
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