ID E3Q5Q2_COLGM Unreviewed; 1037 AA.
AC E3Q5Q2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=SNF2 family domain-containing protein {ECO:0000313|EMBL:EFQ26543.1};
GN ORFNames=GLRG_01687 {ECO:0000313|EMBL:EFQ26543.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG697334; EFQ26543.1; -; Genomic_DNA.
DR RefSeq; XP_008090563.1; XM_008092372.1.
DR AlphaFoldDB; E3Q5Q2; -.
DR STRING; 645133.E3Q5Q2; -.
DR EnsemblFungi; EFQ26543; EFQ26543; GLRG_01687.
DR GeneID; 24407052; -.
DR VEuPathDB; FungiDB:GLRG_01687; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000008782; 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; cd17919; DEXHc_Snf; 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; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 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:UP000008782}.
FT DOMAIN 500..674
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 863..1030
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1037 AA; 117151 MW; 1D5287C508F04881 CRC64;
MVINLSLSSS PPVGSSAIGT SPIRGTRRSD DTDELADETI PCSPFQTQAT QIVNRTSLAS
PSKPHSDLSS SPSSRSVIEV PASSPFQPDK TSTISSYFSR LVPPGSRFQP PPKSQPTPRS
LKRPSEEPII VDSSDDENNR SSRENIARTS FKRHVTNFEY IPVDKLQKKI EQVSQALGST
MPVQFCKEAL TACHNNVEDA INYLLEARHL KPKANPLLSC KKPAITVGNE RPVSLERKIS
RYDEPSKPKL LGRHTPSLPT PSRSTTPSPS KPKRRRLIQG RRPDRSPIAS QHIQEIEPTL
DELADERLDE PIVIPDDNED EDFDNEDEVN EAVKESLHDK ALQAINSSSI EDLSAMTNIK
LDELRVIETK RPFDTIDEVQ AVTVLKKSGA RGRKPRVAIG ETLVDAIMEF TRSVNAIDEV
VADCEKKANK VKQEISLWDL DVKGQKRSSQ SSQAKNDMPL TPTSFQGQKL SEPPIPCQPK
MMEGHCTMRP FQVFGLNWMS LLYNSGYGCI LADEMGLGKT CQVISLICHL VENYEETGRG
DRPWPNLVVV PPSTFSNWMV EFQRFAPGLS VLAYQGPQAE RRDIAYEMLD NPGDYHVVLT
TYTQVGSEDD LEALRELQPA AAIFDEGHKM KNPKTKIYKD LIRIKARWRM LLTGTPVQNN
LMEMLSLLNF IDPKQFSGRM DQLQYMFSQK VTIRDVNNGA FLYGERVSRA RTILEPFILQ
RRKQQVLSDM PSKTCNVAYC DLAPVQKELY EEYERLFKAG PAKKTNTGRQ SDQNNSWMQL
RKAAIHPQLF RRYFDNKKVE QMAKILMRDV PQSELQQPRL DHLIGELKNS SDFELHLWCR
DYACIRHLDV PEGSWMDSGK VTKLLQLIHQ YRDNGDRVLV FSKFAKVIEI LREVLHTDGI
KHCVLYGQTS VGERQDLIDD FNKDIDITAF LLTTGAGGTG INLTSANKII IFDQSDNPQD
DIQAENRAHR LGQTRDVEVI RLLTAHTIEE LIYKACQKKI ELAEKVTGAV EDVEDKNAEE
NLEKEVRKMM ADQMTPS
//
