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Database: UniProt
Entry: A8N501_COPC7
LinkDB: A8N501_COPC7
Original site: A8N501_COPC7 
ID   A8N501_COPC7            Unreviewed;       740 AA.
AC   A8N501;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=CC1G_04579 {ECO:0000313|EMBL:EAU91812.2};
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:EAU91812.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU91812.2, 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|RuleBase:RU363044};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU363044};
CC   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|RuleBase:RU363044}.
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:EAU91812.2}.
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DR   EMBL; AACS02000003; EAU91812.2; -; Genomic_DNA.
DR   RefSeq; XP_001829890.2; XM_001829838.2.
DR   AlphaFoldDB; A8N501; -.
DR   STRING; 240176.A8N501; -.
DR   GeneID; 6006327; -.
DR   KEGG; cci:CC1G_04579; -.
DR   VEuPathDB; FungiDB:CC1G_04579; -.
DR   eggNOG; KOG0987; Eukaryota.
DR   HOGENOM; CLU_375056_0_0_1; -.
DR   InParanoid; A8N501; -.
DR   OMA; RRTINIE; -.
DR   OrthoDB; 1654409at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363044};
KW   DNA damage {ECO:0000256|RuleBase:RU363044};
KW   DNA recombination {ECO:0000256|RuleBase:RU363044};
KW   DNA repair {ECO:0000256|RuleBase:RU363044};
KW   Helicase {ECO:0000256|RuleBase:RU363044};
KW   Hydrolase {ECO:0000256|RuleBase:RU363044};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT   REGION          20..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  82323 MW;  DF9B2CB555BD0FFD CRC64;
     MEQVQATLSP QDKQRLENMS LLAEGRESRA SFPRQTKTDD LRDWDGLPEG VDDTESTPVS
     RNVFDCVVND ASEFDNQYNE PLEPLLNVDV INAFARCYYS DSQGMKLTKS DSVVPKTELL
     LANARTAYVK LTAPHTDHYQ ESVDTDFNGD LIAITQATQQ ELPSVSTERL ANGITNFTVD
     DSVSETTIAN GRRSIPHHVI EEMNMGNNRE QRRAFSIIAD HILDGGPQLL MYVGGMGGTG
     KSHVIRAVVM LLERLGRRHE LLIGAPTGIA ATLIGGTTLH SLILANPGRK GEGTANERLT
     RIWANIRYLI VDEVSMVGAQ FLAEMSSKIR IAKGNDPQAR TRPFGGVSVI FTGDFCQLTP
     PRQTSLFSHS LVRDPSFLQS RDNDGIDSLA GAYLWRLVGT VVILTSNQRQ KTDPTFARAL
     ELIRMRRCYD SLGHSEIINE TPIYEYLRNR ELVRVARENP ESLRAFLDAP VIVGSKLLQD
     ALNAKLVKFN ADRQKEEVCL YHSLDSSHRQ PIAHEPLRTQ LWNLSSRKNS ESLGKLPLFV
     GMKVMITENV SITHKAVNGA EGTVVQIVYS ENKEGLRFAE VVYVQIPGSG IQLHTLPPET
     LPLFPTSTTI KHHIKSATLA ARSFTRKQVP LVPAYSYTDY KSQGRSLSRA IVDISTARGQ
     GVYVMLSRVK WLEGLLILRS FPASKIFESM SGELRSELNR LTILDVATEA AYQSRQNPGN
     CYEVLSHSPD DLIMLPDHSK
//
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