ID A0A0H2RTQ0_9AGAM Unreviewed; 1197 AA.
AC A0A0H2RTQ0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=SNF2 family DNA-dependent ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCHPADRAFT_849585 {ECO:0000313|EMBL:KLO15390.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO15390.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO15390.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO15390.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ085930; KLO15390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2RTQ0; -.
DR STRING; 27342.A0A0H2RTQ0; -.
DR InParanoid; A0A0H2RTQ0; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000053477; Unassembled WGS sequence.
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; cd17998; DEXHc_SMARCAD1; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
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 SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000053477}.
FT DOMAIN 570..744
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 957..1135
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1197 AA; 132153 MW; B2633716799E0B3B CRC64;
MGSEANRTSG LNTLQASWNQ RQMYQQHPQM ASSSSIASSS SSSSNGPPAQ SRDATVSSRY
FTPQQPAGRI LVPSSSPMGP QSGYRPYQTF STPSEMMQIP GLMNYQNHSF GGRAYADPLS
QPSGFILPTN ANNASGSRQQ SSSLRRPFDE AGLHDGMRPP KRQNVGPSSP MPTMAVSPGS
PPSPDVARPG QRRKRPLNEE THIPSSPNSS EEFPTDPRAM LGGSSRPRIV RGQRSDPDAI
DESALTSFVF CYPGDDRRAT AAFRKCNGDK NAAAKLMQPG SGFTGDPPPS PPKPSPTEGP
KVTGKNKDVV EKREAEKALL KELGAKSAIY KQRRNLEHAS ESPSATASTS QVIDIPSSPL
APVRSARTKV RKIVVDSDSE GDAEIVSPVK SVSNGTKVLE GNYFERKALE SLNTFGMEAL
RQLTGCSEEQ ASRIISLRPF ASEEDLVKRL NLGKKKAGLA GISPRVFQDC VSIYEGFGAV
DEILLGCEEI GSELKTAISA WSGKTKGKQR EGSVSAASLF DDEADDGAID LVSLPFENGT
LGSGLISAPS SLSKDVQLKD YQIIGINWLN LLHSRRLSCI LADEMGLGKT VQVISFFAHL
KEKGIRGPHL IVVPSSTLEN WLREFQRFAP KIAVQPYYAD KNDRPQLREN LLETRVGGLD
QDPWEVLITT YNLAVGDEKD RKFFRRIDWN TCVFDEGHVL KNFQSQRYQA LMRFDAKWKL
LLTGTPLQNN LQELVSLMNF ILPNQFAEHL ESLRAIFKVK GDSKVSLLAE ERVSRAKRMM
TPFVLRRRKD QVLKDLPRKS ERIEWCEMTA TQKAIYRDVR LRSRKTVLEA TDTLNTDAND
KQSKGAAKGQ KKGRPNARGK EKVYLENSAN VLMDLRKAAA HPMLFRTQFT DNTLTSITRL
LLKEPDFKKR GAIFEYVKED MEVMTDAELQ HFCKLYKSTQ KFLLDGESFL DAGKVKAMLM
LLEKYQSEGR RCLIFSQFTQ VLDILQVVLK AKDIKYLVLT GSTAVDARQG LVDEFTKDTS
IPVFLLSTRA GGMGINLTAA SVVILFDQDF NPHNDRQAAD RAYRIGQKRD VDIVKLITKG
SIEEDMLRLG ETKLALDEAV AGDTEESDGK AESAPEKMMK TSLLETLRKQ FEEEDKRGEA
SDPDPAVTGG ETRPPSPSPL SSSRSSPPRS TPKAQVKSTK AKTMILDSDS DLTDLDS
//
