ID E3Q6D9_COLGM Unreviewed; 1602 AA.
AC E3Q6D9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=GLRG_01531 {ECO:0000313|EMBL:EFQ26387.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; GG697334; EFQ26387.1; -; Genomic_DNA.
DR RefSeq; XP_008090407.1; XM_008092216.1.
DR STRING; 645133.E3Q6D9; -.
DR EnsemblFungi; EFQ26387; EFQ26387; GLRG_01531.
DR GeneID; 24406896; -.
DR VEuPathDB; FungiDB:GLRG_01531; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_16_0_1; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EFQ26387.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT DOMAIN 722..903
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 913..1077
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1361..1444
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1602 AA; 178189 MW; 6F86E22520F76253 CRC64;
MAKLTSSTRP RRPSLAVKHQ QLLTPSSTTS GGRFQQAYMA KLQQEDAQHE RASMNPPLSS
QDAMRKPSPA GTPDFLDDDD DEILDLTGND TVLSSGSAAL DDEVALWAAE SASRTELPEK
RGHKRKSTEM SKAGDLGSES DEFPDIYKTL GTPAPQGSRS AKGPKTIPSS IRRTNIESGV
FEERTITQTI SRTQRTYKMT DEDNGNGTPD RIPMALGAPK VLGRTPSKAL QISSSPESSS
RIKPLNIQAS TNKQRIRPRV VQDSDDEYDE DIDEELLATP SRHKSTHLPA TNPRSRPASI
PLDDGELSDG LVAPDTPSRP HPSVLPIVRH CTPVDTDHVQ SSSRPDSGKP LSQPNCSSQG
QNSSSILKFV LSNSDSLKVK EKMIQEQLEQ NSKEYGRALL EGNREDRARL KSAKELLLKQ
QAGLNEVSEL LKSHAKLEGE RESLAIQIAD AYDKGRDTEE DENRLDELAD KVKDLEQSIG
PLLPGVGIDG ESFVEEYRRS KSIVMSTQPS HKAPSRVERN VQSVMEMDNQ VIHQTQFPGS
SRLTDPRDCS PPPFPRGRLQ VPKSARPLAS DVKPPRRDDF DDDFFDDIED DFGPLHAPVP
PISRQAPNRK SPLKKTRPRA QDMSSDYGDD ADADMLALAQ DFELRQSSSA DTARGRSVLS
TTSGNATQSS KAAEPLKKRE PAKAKLSIPP ELMKHPWSAD VRKALKDRFR MRGFRSNQLE
AINATLAGKD AFVLMPTGGG KSLCYQLPAI ISSGKTRGIT IVVSPLLSLM QDQVDHMSAL
NIQAVSLNGE TNAQKRNQIF SSFKERSPEL YIQLLYVTPE MLNNSQNFMR ALTNLYSNKR
LARIVIDEAH CVSQWGHDFR PDYKALGKLR HQFPTVPIIA LTATATQNVI VDIKHNLGMD
SCQVFSQSFN RPNLTYEVRR KEKELIHKIA DLIMSKYNGQ CGIIYTLSRK TSEQVAEKLR
SQYNIKASHY HAQMTPEDRI RVQREWQADK IHVVVATIAF GMGIDKPDVR FVIHHSVPKS
LEGYYQETGR AGRDGNPSDC ILFFGYQDVA TLKKMIADGE GSETQKERQR IMLNRVTAFC
DNRENCRRVE ILRYFGEVFN ADDCEKTCDN CRAGAVFEQQ DFSELAQAAI QTIELHDRLT
INQCSDILMG KKYQRTINPH PDDPHGIAKG MKKHEIERIL DRLTAEEALE EENVVNKRAG
IAIQYLIVGR NAHLFLNGRR KLLLSVQVSD RVRESSAPKP KKRVKKSKRD DEQNSDEESL
RRLPPSTNVS SPAQARRTQD KRKKDKSLAT IIDSDEEDEM MRQEEQNLPM HANGYIKDGF
VMSDNDSDDG FEPLPKAQKR GNVSREVGPR IEGDIRLASL DELHQDVVHN FVGEAKQLEE
SLRNAQGLRK PLFSEKSFQE MAIRWTTTLP QMRQIAGIEP EKVDKFGSKF IPLIKRFHSN
YKAMISIADE DDMDEGEQDV VDLISSDEDE DEAMEDDEEE ECSKYFSNGP PPLVPAVQEW
NERMKELETA PPSRAPSSSS TRGRGVGGRG GRRSGSRKGS STWAGFKKQG GGVTKRKAVG
GARRSSGGTT AAGSKNGSVT SFLTKGGKRG GRGGGGIGLM PH
//
