ID A0A484G6J3_COLOR Unreviewed; 1430 AA.
AC A0A484G6J3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=ATP-dependent DNA helicase hus2/rqh1 {ECO:0000313|EMBL:TDZ25853.1};
GN Name=rqh1 {ECO:0000313|EMBL:TDZ25853.1};
GN ORFNames=Cob_v000960 {ECO:0000313|EMBL:TDZ25853.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ25853.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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}.
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:TDZ25853.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMCV02000001; TDZ25853.1; -; Genomic_DNA.
DR STRING; 1213857.A0A484G6J3; -.
DR Proteomes; UP000014480; 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; 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; IPR002121; HRDC_dom.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:TDZ25853.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014480}.
FT DOMAIN 540..721
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 746..895
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1181..1264
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 249..293
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1430 AA; 159074 MW; F12AE812F350ACA4 CRC64;
MARLTSSTRP KKPSLAVKQQ QLLTPSSTTS GGRFQQAYTA KLQQEEAKNG RGRNIPPSSS
QERKYKPAPR PTPDFIDDDD DDEILDLTGN DTILSSDSVA FGEGVTIWNE EHASRPEPLP
RRGQKRKSTE MSKAGGLDSE SDEFPDIYES LATPVPQTGR STKNQKVIPS SIRRKTADDV
FEETITQTIS RTQLRDSIIK EKLERNSREY AKSLREGCRE DRPRLKSEKE LLVKQQSQLE
EVTGLLKSHA RLEAEREGLA QRIADAYDEG RDTEEDENSL DELTDQARAL EQSISRLLPS
VGIEDDGFIE EYRTSKPMVM GTQPSSKAPS RASRAPQPIA ENDNQVIHQT QFPGSSRLTD
PRDLSPPPFP RTKTPAPRST KKSTASAVKA VNRQDDFEDT FFDDIEDDFG TYHPPASNVR
AVSSRRSPLK TSRPRAMDFS SDYGDDADAA DMLALAQDFE LRQSSSAETA AKRRNVLSAT
SGNASQPPRG GESSRKRDAS KAKLAMPPEL MKHPWSADVK RCLKDRFRMR GFRQNQLEAI
NATLAGKDAF VLMPTGGGKS LCYQLPAIIS SGKTKGITIV VSPLLSLMQD QVDHMSAINI
QAVSLNGETP TQKRNQIFAS FHECSPELFI QLLYVTPEML NNSPMFLKAL ATLYSNRRLA
RIVIDEAHCV SQWGHDFRPD YKALGKLRHQ FPTVPIIALT ATATQNVIVD IKHNLGMDNC
EVFSQSFNRP NLTYEVRRKE KDLVTKIADL ITSKYSRQCG IIYTLSRKTA EQVAEKLRTK
YDILAHHYHA QMSAEDRIQV QRDWQKDRIH VVVATIAFGM GIDKPDVRFV IHHSIPKSLE
GYYQETGRAG RDGNPSDCIL YFGYQDVVTL KKMIADGDGN EVQKERQRVM LNRVTAFCDE
RENCRRVEIL RYFGEVFNGD DCNKTCDNCR AGAVFEQKDF SGMAMAAIRT VDNHSKLTIN
QCSEILMGKK YQANIVQHPD DPHGIAKGLK KHEVERIIDR LTAEDALEEE NVVNKRAGIA
IQYLVVGRNA NLFLSGRRKL LLSVQVSDKT REPSASKPKR RAKASRANED DDGMAERPSR
HLPPSTNVSS PAQARIPNKR RKGKLLATLF DTDEDEEMLQ QGAEAQDLSI HANGYAKDGF
VMSDDDLDDG FEPLPRTLGR DNSSRDVGPR IQEDSRLGDL DELHQDIVHS FVREAKQLEE
NIRNAQSLRK PLFSEKIFRE MAIRWTTTLP QMRLIPGIDL EKVDKFGTKF TPLVKRYQQS
YKEMLSMVDE DDDMGANQDV VDLISSDDDR DEEMEDDEDE AEESSKYFGG GPPPLAPAVQ
EWNARMRELE TTAPAARSSP STATRGRGGG RGGKKSGFRR GSAGGSSFKR GGVTKRRSTG
GTSRRSSGGG ASASGSGSKT PSAANYFSRG GKRGGGRGGG SAGGIGLMPH
//
