ID A0A010RWL5_9PEZI Unreviewed; 1103 AA.
AC A0A010RWL5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=SNF2 family domain-containing protein {ECO:0000313|EMBL:EXF76673.1};
GN ORFNames=CFIO01_03484 {ECO:0000313|EMBL:EXF76673.1};
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:EXF76673.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF76673.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF76673.1,
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:EXF76673.1}.
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DR EMBL; JARH01000803; EXF76673.1; -; Genomic_DNA.
DR RefSeq; XP_007599671.1; XM_007599609.1.
DR AlphaFoldDB; A0A010RWL5; -.
DR STRING; 1445577.A0A010RWL5; -.
DR KEGG; cfj:CFIO01_03484; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_8_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; 2.
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:SF14; ATP-DEPENDENT DNA HELICASE (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 299..484
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 880..1043
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 123191 MW; 1A9B9E7BF7DDFFFE CRC64;
MVNQRNPARG PLRPVNPNDD SQSSTSHELP KTGNPSKESR GAAHLLSRAE SRDSASFDPE
DLAAQVGSMR LSTTPKSKAP AAIPNSSARR NPPAYRQTSP DLVEISRNDF KPPPRPVSKE
SESSSQHEQS ILHSDALESF FSDVKRHDPF HSSSSQPVFG HPTKILSSLK QKATGIFNER
RSRPEHHRPQ QMSVPSVPLY QDRKPEPPTL YSSIGPDANP STFRPTTIFG ENEFWTDPAK
ASSDLKALLE GGMESEDEGE EKEKGEAVND GTVEGLKVKL LPHQVEGVEW MRGRELGPVK
KGKVPKGGIL ADDMGLGKTL QTISLILSNQ KPNKDEAGWK KHFSGIEKST LVVAPLALIR
QWEAEIKEKV TKSHGLKVCV HHGPQRTKNF KDLALYDVVV TTYQVLVSEW GHSSEDEKGV
KAGAFGLHWW RVVLDEAHTI KNRNAKSTKA CYALRSEYRW CLSGTPMQNN LEELQSLIKF
LRIKPYDNLK EWKEQIEKPL KNGQGHVAIG RLHSLLRCFM KRRTKEILKE DGALNPGGKP
TKEGEKSTTG FKVTERKVVT VATKFSPAER RFYTRLEARA DKSIEQMLQG KINYANALVL
LLRLRQACNH PKLLEGKLEK DREALSDAAP KTARGDIDSL AEMFGGMGIV SRQCDVCGRE
LPRDVANSGK DTCQECREDL AYFNEHETPK SKKQKKQKSS VKKVVRKSLG GDAEEETPYK
PKARRPRNRN VVVDSDDEEA DGSWLVPEDQ QGQLRMGKAG GEEDENAEGG GEWISANDSK
HDSEDEDDDS QLDSFVVKDD EDKNDQGVDQ SDVSDDSLLS IGAIASQVKE EKLRSSQSRV
SDSDTDSEED TGVDESELHS DKDTDYDPAG KASKVLASAK IREMMQILHK EARKHKFIVF
SQFTSMMDLV EPFFRKDGLK FTRYDGSMKN DEREASLDRL RNDKNTRILL CSLKCGSLGL
NLTAATRVII LEPFWNPFVE EQAIDRVHRL TQTVDVIVYK LTVENTVEER ILALQDKKRL
LAETAIEGGM KKDAFKLGFK EIMDLFRRDA SQAPAGLGDA YPDPSSSQVT SARTSRQGSP
ESSLVAGKKK AKKPEHEMFG RRW
//
