ID T0LJG7_COLGC Unreviewed; 2564 AA.
AC T0LJG7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=SNF2 family domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_12440 {ECO:0000313|EMBL:EQB48330.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB48330.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB48330.1}.
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DR EMBL; AMYD01002642; EQB48330.1; -; Genomic_DNA.
DR STRING; 1237896.T0LJG7; -.
DR eggNOG; KOG0392; Eukaryota.
DR HOGENOM; CLU_000315_1_0_1; -.
DR OMA; WYSDIAC; -.
DR OrthoDB; 180798at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.58.610; Cdc37, Hsp90 binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR InterPro; IPR013855; Cdc37_N_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR Pfam; PF03234; CDC37_N; 1.
DR Pfam; PF12054; DUF3535; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SMART; SM01071; CDC37_N; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000015530};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1294..1467
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1639..1790
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 73..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2183..2208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2273..2326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2283..2300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2564 AA; 284563 MW; 27C3DBD6127DD0AF CRC64;
MASRLDRLVT ILETGSTRLI RDTAVNQLAD WQKQHPDELF NLLSRVVPYL RHKEWETRST
AAKAIGKIIE NAPLYDPNED EGDSAPIKKD EPEENGHVKK EEEKDVPSFA TDELLKLGTL
NVEHIIKHGR QLLRGGNIDF ALASLDPSAR LAHQKKTLNG RLGLLGRAFE DAEMPVLVEK
DHSPMTPQES ANGHNGSKEN ASQGQSQPAE EAGLSSRQLN VLKRKRKREL QKAAQGKGGF
GDLSIRRTTT AGSEGFDDTP MPDADSKQKN GKVNDYFNLD RPADVDEESK VVSEFKGPVI
PIKSEIEADE TMEGAEWPYD RLCDFLKVDL FDPSWETRHG AAMGIREVIR VHGAGAGRIR
SKSRAENNRL NQAWLDDLAC RLCCVLMLDR FTDYSSDTSV APIRETIGQS LGSVLRHVPA
DSVHGIYKIL YRMVMQDDLH LEMLQCLLLE DNEMIDGVVR LVMKGLEEHD DDVRSVSAAT
LLPMAKEFVT MRPGSIDGLI NIMWGSLADL GDDLSASTGK IMDLLATLCS YPEVLQAMET
SAAQDEERSF TLLVPRLYPF LRHTITSVRL AVLKALMTFA NLGAQNSRGW LNGRILRLIF
QNILVERDRE TLNMSIDVWT ALVRSLSQTP DVLADEFAAH VDPLMTLTLH PVGVSRHPLP
MPAHLFQRPS GGTYTAVTAT PARKASSPEG PERATKRRRK SAKTDDAPVA THTHDVDGHM
IQGDVDLVGM DTLIRSRVSA AKAMGLIMSF IPNSHMAEYD QLITSGLADR NASTQLAACM
VIDEYAKNNT AAEGPQRFVA PLQKIIEAER PSHYGDLVSY MHRVRSQCQQ LLNMFRDHGK
VSSGRLPTLA VLVQGDEQAG PGAFSIAVAD KVVGEDFDKL KKAMSPGQRL VASQQLGEAR
DVAASAITDA RTAKEARDVR IKAAAACALV AIKVLPKKPS PLIKGIMDSI KTEENQELQC
RSSATIASLV QLFNEKGRRG PADKVVSNLI KFSCVEVAET PEFPVHATKT DCVLSMQKEE
DRVDHADAAK WAREAKAARI TRRGAKEALE ILSRTYGAEL LTAVPTVRTF MEEPLVKAFS
GDLPAEARDP ENTFGQEIVD ALSLIRTLMP TLDRAIHPFV MEKVPLVIKA LHSELSVFRY
MAAKCMATIC SVITVEGMTA LVEKVLPSIS NPVDLNFRQG AIEAIYHLIA VMGDAILPYV
IFLIVPVLGR MSDSDNEIRL IATTSFATLV KLVPLEAGIP DPPGLSEELL KGRDRERTFI
SQLLDPKKVE SFQIPVAIKA ELRSYQQDGV NWLHFLNKYH LHGILCDDMG LGKTLQTICM
VASDHHNRAE EFAKTGAPDV RRLPSLVVCP PTLSGHWQQE IKTYAPFLSV TAYVGVPAER
KTMKDNLDKT DIVITSYDVC RNDAEVLAKY NWNYVILDEG HLIKNPKAKI TIAVKKLASN
HRLILTGTPI QNNVLELWSL FDFLMPGFLG AEKVFLDRFA KPIAASRFSK ASSKEQEAGA
LAIEALHKQV LPFLLRRLKE EVLDDLPPKI LQNYYCDLSD LQKKLFDDFT RKQGKKLQEE
AGREDKDAKS HIFQALQYMR KLCNSPAMVM KPTHSMYDET QRILNKQGTS LEDPVHAPKL
TALRDLLVDC GIGVEEAESN DPLYQPIKPH RALIFCQMKE MLDMVQNTVL KNMLPGVSHL
RLDGSVEANK RQDIVNKFNS DPSYDVLLLT TSVGGLGLNL TGADTVIFVE HDWNPQKDMQ
AMDRAHRIGQ KKVVNVYRLI TRGTLEEKIL SLQRFKIDVA STVVNQQNAG LSTMDTDQIL
DLFNLGDTGP SLISDKPKNA MEGREEDMVD IETGDVVTGK QPGKKAWLDD LGDLWDNSQT
NMANMGVAQK GLIQYMSDLH LEVGNQYSTF DFPAMSPYLL IAGDVGSLAD YEEYLGFIRR
QTNRFEGVVL VLGNHEFHGL DHDSAIERAR RLEMEPSLEG KLHILHRDRF DIPGSLVTIL
GCTLWSLVPD EATAAVTAKV KDFEHIEAWT VDDHNEAHLE DVAWLRRALG NVPEERSVNV
VTHHAPSMEG TSEPRHSGSV WSSAFATDVL EAGEALLATY TASPNTAKMP VDYSKWDALE
LSDDSDVEVH PNVDKRSFIR AKQNQIHQER LQRKHQIETL KYERVINDGL MKRISGLLEA
LKSHASEAET RNPGEVAFQA VMESAGKPED DQPPPRPEGV HTESEPLPTF SKMMAVLLDQ
VNKELDEKKP ENRYQGMLEG VEGHLKKVQG LQKELLAKLA ELEKEEVRKI TSEGIHTGFD
SSHVNKSKSE GKEPERKPEL LNPNFDMSQT LPPKDSKTSY DDDEEIEASP AAKKFAQIKA
ADYSSSLAYL SSNPQILTEK ETDGLLVLAF DAALEGKDDY CRQCVHQALL LQYCRALGKD
GVGMFFKRIT TKGHQAQDVF YKDVQDTYGK IRNRAREIVK ERANEPEGVE QIQLHAVEPG
TEIKITIPPE GSEDPAVKEG RAIFEGFSAE FRKALESGSL DEVNKVLGNM KVDEAEDIVG
KLSEAGILSL EEQIIDATTE EGQKALKDME AAAGSESGFA PDPE
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