ID A8N587_COPC7 Unreviewed; 1624 AA.
AC A8N587;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Helicase SWR1 {ECO:0000313|EMBL:EAU91697.2};
GN ORFNames=CC1G_04465 {ECO:0000313|EMBL:EAU91697.2};
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:EAU91697.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU91697.2, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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:EAU91697.2}.
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DR EMBL; AACS02000003; EAU91697.2; -; Genomic_DNA.
DR RefSeq; XP_001830032.2; XM_001829980.2.
DR STRING; 240176.A8N587; -.
DR GeneID; 6006470; -.
DR KEGG; cci:CC1G_04465; -.
DR VEuPathDB; FungiDB:CC1G_04465; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_3_1; -.
DR InParanoid; A8N587; -.
DR OMA; DAHVFKR; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000001861; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EAU91697.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT DOMAIN 832..997
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1348..1507
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..781
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1624 AA; 182920 MW; DFFE77DA57B0B035 CRC64;
MHPVGRDECL EVEPGSSNNM GGGQDVGRSL VPGDPIANET LTTSVANEKD LAEFSVTNEM
LEAEKALILS KKETERDQVF NRHDDLVREK FHMDNYRNML TYHPSAAKED DSRVFQEYKA
SFDLVGMIQP TAGPSRQTRR TINERKKLVN AFAPMPSSSS SAAPPRPTKR KLVPDVHVQN
REIFDILNDA LGKGKGKEVA PEPSQPTPKR MKTAPPSELV AQKSPSLSRS SSPLTDLDEE
LTIIIPRRKP PAGPKPVDKD KGPRLNGKEK KAKMKKAAIV IDENYDGVEA PLLESRAKTT
KGDKPNQVPI SPKPRPQPIS PVLGDPPGCS LVPDTTEGPS KSLPNKTIKR IKLVVRKPSR
TYTNPAQIPL PPKHGGSLSA LLATYRTNGL KEIVDEKAYQ RKIKKEAEIR NRELLFRRQQ
RFIPGKDVYF GTRLDEDDSN PAYEPPKRTT TDHWDDVVEA AVLNGKARLG KRIPVGRQVA
GQVAARIRAY WDAQEAKKER ARLQEEKRLR TLAKSTIKLV VAEWKKAVFH IREKRRLEEE
EEERRLGQEH LNAILEQSGH ILSTQQRHLI QGVTMLQGGQ GSDDEDGEGA LGEELSDTDD
YVSDGSLPAS QIADTDSEGS GDRLGTNLLL MDSDNPQRLR DGIQDGLEDE TLIDNILVPD
PDKSPVRQSS LAPLEDILLS GSMSSDPITL SPSPNKPIFN HESAPIFGDE YVASALERED
FGIYSPEPLS RPDTPVNGEG PASSRPTSPT STAMDVDAEP GMTLEEQEEE GIDEEGIVPE
NPEDSDYSRI PAYLRPYAVA PVDWDPSRTI QPPSLLRGVL RPYQQSGLEW LASLHTNHMN
GILADEMGLG KTIQTIALLA HLACDRGIWG PHLIVVPTSV LLNWEMEFKK FLPGFKVVSY
HGSPKRRKEL RQGWRDKYSF NVCITSYTLA SRDQLVFKRK NWYYLILDEA HMIKNFRSQR
WNVLLMFRSF RRLLLTGTPL QNNLTELWSL LQFLMSGSDF ANLKEFGDWF SNPLEKAIEH
GDVDEETMQR VSKLHTVLRP YLLRRLKRDV EKELPSKFEH LVLCPLSKRQ RFLYDEFMSR
AQTQKDLQSG VYLKIANILM QLRKVCNHPD LFEVRSIVTS FAMSRSAIAD YEIKELLVRR
RWCEDMEENV NLDVLGLQFI HRQNVSQYAA GRRQELDATS RLPFYGEGIG KAPPKDTRTI
AGFRNYARYL ERAKAIAHWS HISYLNRLRC SEHPIVSTEC ISQVHFAKPL LPLSLTDRRH
AYLDTVYSVH AAVLSHTDRE QQMAGLIDRF AFVTPSVVAL DMPRIALAGH CDRILQSPPE
FDNILHRAAV KLQIAFPEPS LLQYDCGKLQ RLAELLQEKK AGGHRVLIFT QMTRVLDILE
VFLNHHGYLY LRLDGATKIE DRQYITERFN ADSRIFCFIS SSRSGGIGIK TPQTDAKYSL
TGADTVIFYD SDFNPQMDRQ CEDRIGQIRD VHIYRFVSQY TVEEAMLRKA NQKRSLDDLV
IQKGEFDWRT LFNKEETALT KALGEYDDAE DAHAAELATR EAFELEGADA ADFEDGSGPR
GGNPGAAKPA GGDENNRAAS PPQFEGIVDA AGAGEEDEEE GGTTVDYMVA FVEYDYDFFS
DWRI
//
