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Database: UniProt
Entry: A0A010QRH9_9PEZI
LinkDB: A0A010QRH9_9PEZI
Original site: A0A010QRH9_9PEZI 
ID   A0A010QRH9_9PEZI        Unreviewed;      1060 AA.
AC   A0A010QRH9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=SNF2 family domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CFIO01_13659 {ECO:0000313|EMBL:EXF79270.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF79270.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF79270.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF79270.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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:EXF79270.1}.
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DR   EMBL; JARH01000560; EXF79270.1; -; Genomic_DNA.
DR   RefSeq; XP_007597086.1; XM_007597024.1.
DR   AlphaFoldDB; A0A010QRH9; -.
DR   STRING; 1445577.A0A010QRH9; -.
DR   KEGG; cfj:CFIO01_13659; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_7_1; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000020467; 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; cd18008; DEXDc_SHPRH-like; 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; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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:UP000020467}.
FT   DOMAIN          421..625
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          865..1017
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          187..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  118459 MW;  4AF44D70F890998F CRC64;
     MDPNQEFRYP PAKRIRLNQA LELGPDLTAG RYVGIQQPQA DWTLPSASGP RPPFMPQYRP
     EGHPLSISPS SSHRYQPPLA PAAIENRPPD YGAFGSTNSW EGLQEDQPWH LANNYVSNPQ
     NTLLQCDPYN AHAHMISHQR WPSACPSLAH SLMPQPHSLQ SYPAPLSQLQ VVCPEFTVSL
     DCTSALPMGD KTEPSNPDQM QSSTHPEPPY EQDQVVCFGM ITSITGKVDR RSLPETIVPF
     LVQLESGYGF TKAENPTING ILTSEHGHNQ MIQEMLDDDT LRLYAVCNVS EPPDVRLSGN
     KFDQASCNLN ITVYGPAEDF EEIGNWFQEY EVYLQDPLMC HVDTRYCNPH KLASNGIGTC
     PMLSDVVVQG SEQNTFQDIT EPMDMLDMLN SRCDLKESNQ PAAITAELKR FVNMISESHQ
     HEEPPQFYGG IIADPMGLGK TLTMIALVAT DLEKQAHESE VRTSSDEYGG PHTGATLIVI
     PPPLIGSWEE QLSDHVLEGG LKYRRHHGKS RLVVNEVNRD DVNVVLTTYH TVSTEWRTGD
     GMQTSPLFAV RWRRIILDEG KRSHAETRHN PWTLTRLAHY IRNENSRMAR AVCALDSISR
     WAVTGTPIQN RLSDLATIVK FIRAHPYTDT RQFDADLSQL WKSGEDKKAV QRLKNLSACL
     ILRRAKGTIS LPPRHDKLCH VDFTQGERSV YDEMRQRAIA KIEEALLQDS GLETSNVSMY
     HNALQQIESL RLFCNLGLGY HSRHEKVTHY STENYQDWTL HAQQLFNLQW QKGPIVCLWC
     SSTLDTDETM TNHSDAAQAG PRYSRCLQFS CSDCVKRSSR AGRTLACGHQ PPCPVAPVST
     SHSALEEIPT STPPDAMSGA GLPSKVKALI ADLNRQPPGV KSIVFSTWKM TLDVVERALN
     EAGKTSVRFD GNVPQKDRQP LIEKFRNNRG VSVMLLTLSC GAVGLTLTVA SRVYLMEPHW
     NPNLEEQALA RVHRIGQTRE VTTVRLYVRD SFEEQVMEVQ KSKKQLAGLL LSPHDGGQSD
     DSLSGLQVSD SGKSIRLDLT LRTDQPAVEI EVSSLRSAIL
//
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