ID A0A135S7D4_9PEZI Unreviewed; 1120 AA.
AC A0A135S7D4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=SNF2 family domain-containing protein {ECO:0000313|EMBL:KXH31828.1};
GN ORFNames=CNYM01_13750 {ECO:0000313|EMBL:KXH31828.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH31828.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH31828.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH31828.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:KXH31828.1}.
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DR EMBL; JEMN01001604; KXH31828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135S7D4; -.
DR Proteomes; UP000070054; 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 GO; GO:0046872; F:metal ion binding; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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 SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 463..669
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 833..896
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 943..1101
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 34..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 124518 MW; B4797D7BA7CF4BDE CRC64;
MASPNGPNGR ANYINAQPQT QSWNAQALLN PRSYAVSNAA SRRNSPKPQH LSNRSTPGNQ
NITNNPSVFQ FASPNDTTSE SLTPSITSGA STPVHDGGIS PYGMANMIER MNDVQDRAAA
PLPKRRKVDT PDPESDADNK KKMGPAGSGM LGAYVKEKQD EGKKENSKVS TQTVDLTEEG
DDVVMVEDPA TEEVCYGMLT GFLDCHKVPS AKPGTQSIFG ADFMPPVKIV LKRIIGDSTK
KIQAYDYTRD IIGNVDANTA NALVPLLDSN VRLRTDCKIP ARRKQADEHP GQAISRSYPV
EMTLYGQYRF VKAVGKHFER FKIVLRHPNR VDKGVRYENV HADNKPNPAP GARNLAGALA
QYNNHSSSTY YTNPTPRTVE EIRSDVMGVF DSMGKTDELP EMDPAPIITT ELLKHQKQGL
YFMTAREKES TAEERVKGSM WQLKIGPTGQ KFYYNVITGH QERTLPADTH GGLLADMMGL
GKTLSILSLI GSSLDQAKEW AGRTPVQPEM PPQKAGGKAT ASSSLPLTGI AMNAKATLLV
CPLSTVTNWE EQIKQHIAPG ELSYYIYHGS NRIKDVEKLA EFDLVITTYG SVSSELGSRS
KRKSGKYPLE EIGWFRIVLD EAHMIREVAT LQFKAIVRLQ AARRWAVTGT PVQNRLEDLA
ALLQFVRLKP FDDRNKFNRF IVDPFKACDT EIVPKLRVLV DSVTLRRLKD KINLPPRSDH
IVKLDFTEEE REVYNLFEKN AQDRVKVLSG NGVQKALGGH TYIHILRSIL RLRLLCAHGK
DLLNQEDLEA LQGMTADMAI DLDSDDEDKK PGLSDRKAYE MFELMQETNT DACSACSKKI
GTNDDASIES EGQEDILGYM TPCFHIICGS CIKGVKEQAR RLLPPGQAMG PCPICSTVIK
PAYVDIRRSR VKVEHEGPAK EKTATNGRKS FGKYTGPHTK TRALVEDLLK SKADTDANPD
EPPYKSVVFS TWTSHLDLIQ MALDNVGVKY VRLDGSMTRI ARTQAMDSFR EDHSVHVILV
SITAGGLGLN LTAGSNVYVM EPQYNPAAEA QAIDRVHRLG QKRPVRTVRY IMRNSFEEKM
LELQEKKNKL ASLSMDRKER VFDKSEAARQ RLLDLRSLFK
//
