ID A8NB77_COPC7 Unreviewed; 1129 AA.
AC A8NB77;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=DNA helicase {ECO:0000313|EMBL:EAU89723.2};
GN ORFNames=CC1G_07448 {ECO:0000313|EMBL:EAU89723.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU89723.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU89723.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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 -!- 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:EAU89723.2}.
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DR EMBL; AACS02000009; EAU89723.2; -; Genomic_DNA.
DR RefSeq; XP_001832077.2; XM_001832025.2.
DR AlphaFoldDB; A8NB77; -.
DR STRING; 240176.A8NB77; -.
DR GeneID; 6008561; -.
DR KEGG; cci:CC1G_07448; -.
DR VEuPathDB; FungiDB:CC1G_07448; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_22_3_1; -.
DR InParanoid; A8NB77; -.
DR OMA; DVENSCH; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000001861; 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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EAU89723.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT DOMAIN 379..555
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 580..741
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 124161 MW; DFDC4943E05DA9FD CRC64;
MSKLRAKPTE VFNVEDDGYE ASSSFGDTGT TSISAAAPGR GHLKKPKPLQ PFSTKGWSKE
TSSTKTTNPV VYLSDSSATS PHGAGVKRTS SDISLGLDPS PTLQKRVKQG AVASTVRSST
NGKENLNVPN RTSKDTKGKG KPTYQEAIMD VDDDTRRRQK ERTPLEALRQ SASRHGCESR
RLENVIPDSL ATLPREHLGQ AKSSCDQLLH HINDLIIQHY RGAKLIDLEI HEEIKQLLEK
RISSIDAYMS GVPTEATLPI SMPPPPPPLQ QIPSDTSTTS TLVENSVSAV LQPQSEPIVV
DDDDEDADLW DQMPDVDFAE ISEVPSPAPP PIPAQTVDSA PTSAPDPKLL QSPYYPEVMQ
QLKNVFGLDS FRKNQLEAVL SAMDGKDTFV LMPTGGGKSL CYQLPAVCTS GPRRGVSIVV
TPLVALMNDQ VGQLTKKYRV NAVLWNADNQ ASSEHITALN QGQIALLYVT PEKLVESNRA
KDIFKRLYES GLLARFVIDE AHCISTWGQD FREAYTTLGS LRKEYPNVPI IALTATANKR
TVGDIISQLQ MRSPLMLIQS FNRQNLSYKV VQKSPRFKFE ISNEIKDHYP GKSGIVYCRA
KQTCENIAQF LKTQGIIAAY YHAGMEKDDR HRVATDWQEN RIQVVVATIA FGMGIDKPDD
YNFGDLNTSL RMIRSDDKTT PEAKARQEAD VRQMFDFAAN QSECRRVQLL QHFDERFDRR
LCQKTCDTCA DERETVKADV TSVARAAVTL VRSARKAGMS LTPSLLMNGL RGSTNQDIKS
KRVDTLDGYG KANDSPQDLV DLVIKHLLHE EYLATDSIKN AHNAFHTDVI VLGPKANEVN
HRKEITVAWR PKLKGGRKGP ERSNSTPSTS GKPASRAPNQ RRGRKVGTEL ADDPIEDDIY
DFQDNVQPAP SISAPPSAAA SKPASRRDKP SSKVVPVTPA SLLEKSSDDP AAAFHSKMEA
LRQQVARERK MNPQDLIDNA VLEMLTLMCP MDYRSFKEVV NDAWPESDRR GIDHAEELWR
LCGQRFLDLC IANKTGGPAK KPVSTRTVSQ LRDNYAYQSS VTSTTGRSDS AGSSTSRTTG
KTGTPVAKPP VSSGTVVTPP VPKPPPTVAS PALGTVPNGS RAKRFVFRH
//
