ID A0A135UVM0_9PEZI Unreviewed; 1376 AA.
AC A0A135UVM0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=SNF2 family domain-containing protein {ECO:0000313|EMBL:KXH64392.1};
GN ORFNames=CSAL01_04000 {ECO:0000313|EMBL:KXH64392.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH64392.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH64392.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH64392.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
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:KXH64392.1}.
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DR EMBL; JFFI01000972; KXH64392.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135UVM0; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000070121; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT DOMAIN 75..110
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 311..383
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 494..659
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 805..956
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1224..1294
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1376 AA; 155334 MW; 13398763689A35C1 CRC64;
MASVQAAPAV QLPGAGMAAT TPQQAQEIFN STQPPTSSAP SASALPAANS NNAAAAATAG
SPSTAAPPSG PGAGQFNPQQ LSLLRQQIHA FKLLTKNAGV PLQMQQAIFA QRERRKAIAA
EAAALAASST PATTGRDSAQ PGINGSEAKS ESPPEVQGPT FKTVKSPYGD NNLIRKSISH
FDHTQRKSRK LIPGLFPTGV DFDQLRYERE LIVFNRMRDR FAELRNTPAN IAHWDTTKDD
VELDDSAKVK AIIEMKSLGL YAKQKALRDK IGRSMMFYDN LAMTTNRSGY RRTKKMTVRE
ARITEKLEKQ QRDIRENREK KRHIDFLAAI TQHRNEIQQT ASSQRNKSTK LNKLMFAQHY
NIEKEEQKRI ERTAKQRLQA LKANDEEAYL KLLDEAKDTR ITHLLRQTDG FLRQLAASVK
SQQRKALLEQ TGEEELPEEE EESEPEQDDD DTSGRKIDYY AVAHRIKEEV TEQAGILVGG
KLKEYQVKGL QWMISLYNNN LNGILADEMG LGKTIQTISL ITYLIERKKQ DGPYLVIVPL
STLTNWTLEF EKWAPSVSKI VYKGPPLARK VHQDKIRQGR FQVLLTTYEY IIKDRPILSK
IKWFHMIIDE GHRMKNQNSK LTTTIQQYYN TRFRLILTGT PLQNNLTELW AMLNFTLPTI
FKSATTFDEW FNTPFANTGG QDKMELTEEE QILVIRRLHK VLRPFLLRRL KKDVEKDLPD
KTEKVIKCKF SALQSKLYKQ MVTHNRILVS DGQGGKAGAR GLSNMIMQLR KLCNHPFVFD
EVENLMNPMS ISNDLLWRTA GKFELLDRIL PKYKATGHRV LMFFQMTAIM DIMEDYLRYR
NLKYLRLDGT TKSDERSDLL REFNAPDSDY FMFLLSTRAG GLGLNLQTAD TVIIYDSDWN
PHQDLQAQDR AHRIGQKNEV RILRLISSNS VEEKILERAR FKLDMDGKVI QAGRFDNKST
ETDRDAMLRT LLETADMAET GDQDEMDDEE LNLLLARSDD EVGVFQKLDE VRKQDKTYGE
AAGANAKPRL LAEDELPDIY LGDGNPIEEE IETSLGRGAR ERTKVRYDDG LTEEQWLMAV
DDDDDSPEAA AARKQARKDK RETNRLKRSG MSNAADDSPS ASRASTEEVE ETPKKRGRGK
GAAKNQEKRK AEEGDDEPPA KKRRGPQGRA KAVSVSVGSE TPRVSAQQRQ HLQANTRALF
DGLMNLEVDD PEPPEEDDDE SVAGKRIIIG PFLALPPKRD YADYYLIIQA PISMKQIETK
IKKQQYHSLG DMRKDVDLMF RNCQTYNEEA SLLYQDSLTL QKFFHEELQK ALDKHPELQE
LESDGGKEGS VAPSASASAG TPQPATSTTR IKLISSASNG DKEANGASNG AQSDKE
//
