ID M1VWV4_CLAP2 Unreviewed; 1929 AA.
AC M1VWV4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000256|ARBA:ARBA00019805, ECO:0000256|RuleBase:RU368001};
DE EC=3.6.4.- {ECO:0000256|RuleBase:RU368001};
GN ORFNames=CPUR_05783 {ECO:0000313|EMBL:CCE31927.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE31927.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE31927.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE31927.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
CC -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair.
CC {ECO:0000256|RuleBase:RU368001}.
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;
CC Evidence={ECO:0000256|RuleBase:RU368001};
CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368001}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025, ECO:0000256|RuleBase:RU368001}.
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:CCE31927.1}.
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DR EMBL; CAGA01000035; CCE31927.1; -; Genomic_DNA.
DR STRING; 1111077.M1VWV4; -.
DR VEuPathDB; FungiDB:CPUR_05783; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_1_1; -.
DR OrthoDB; 5475375at2759; -.
DR PhylomeDB; M1VWV4; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd18002; DEXQc_INO80; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR031047; DEXQc_INO80.
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:SF2; CHROMATIN-REMODELING ATPASE INO80; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF13892; DBINO; 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; PS51413; DBINO; 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, ECO:0000256|RuleBase:RU368001};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU368001};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU368001};
KW DNA-binding {ECO:0000256|RuleBase:RU368001};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016801}.
FT DOMAIN 833..958
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 1082..1254
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1656..1815
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1846..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 903..944
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1016..1043
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1929 AA; 218844 MW; 990DADB7CA535E36 CRC64;
MDRHNSNRGV RRRDGRDDGP QREQLEVLEQ EQHEQLVAPS SSSTNAHAYF RLRSPTRSAR
TDLHREMQHP PFASPGSSDA NQSARGHHHH HHQNHHHHPS PASSILHSPP RPPLAAPLHH
ETPLHHHANH YHQEHRGLAR GPSASIVDLG PASIMAPSPP TPAGGAGAPT PSLLPPPSSS
SSSSTTANKH NHLQGPSSAS SGYYPPPTAS ESHLRTREQG VSGRVYDPTT DTTKERRVSD
AWHNAPQNST PKAREPYHYD RTPADHHQPS PYYPSNQTGK YTSPRQSYAR SRSPRSQSHQ
DLPARSHSPP SRSSHMASPP QRRAHGSAMN TTPSGISAVP AASNADPRVA SPSKPAALSA
TNTPSRPADP MSFSNILSSA EPAPKPVAER SAPIPTPPEA APEAAPKVDQ EKEQKQAQEQ
EQELKREKKQ TEQAPDVDTE VEAEHVEDLE PASLPIRKAE PIAKKKPARR AAKGRTMDII
REAEAPKSKR RSPIKRESPQ PRSATKRQAN GQPKVGTSWS NEMEKKIDVC EDDIDQDAAM
FDPAEFDEQE YKDRAQKRRR LMTNFDAEQG RLRREDYAKS ASKKLVLHSE LGKRRYDDVF
YDHALSEVRE QELFAEKERK KDMQRKRRRE KSMAVTIEQK EAALARALAA EDEAERQKHL
RDAERANKKA QQTKLILQKG IKGPARNLEL TLDGGAMSSF LASDADTPKK SKGKGTRLKK
TREQKKAEKE SAEAAQAALD AGKELPPKEE SKVRIKIKGR SKDKDKDKDK EKEKEKEKEK
DKGKDKGKEK EKDYKDGENV KVAKDVGKET KDDASDLDKR FSSKGYNQIY EQIWRDMARK
DVNKTFKLAM ESHGTKASNL KKTAILASKE AKRWQLRTNK GTKDLQARAK RVMRDMMGFW
KRNEREERDL RKAAEKQEIE NARREEADRE AARQKRKLNF LISQTELYSH FIGKKIKTDE
VERSTDNPDI QQPANAMSHN KLDVAEPAGP VGDRVTDFDK LDFDNADETQ LRAAAMANAQ
NAIAEAQKKA RQFNNEADLD MDEEGEMNFQ NPTGLGEMDV EQPKLINAQL KEYQLKGLNW
LVNLYEQGIN GILADEMGLG KTVQSISVMA YLAEKHDIWG PFLVVAPAST LHNWQQEIAK
FVPEFKILPY WGSAPDRKVL RKFWDRKHLT YRKDAAFHVC VTSYQLVVSD VAYFQKMRWQ
YMILDEAQAI KSSQSSRWKS LLGFHCRNRL LLTGTPIQNN MQELWALLHF IMPSLFDSHD
EFSEWFSKDI ESHAQSNTKL NEDQLKRLHM ILKPFMLRRV KKHVQKELGD KIELDIFCNL
TYRQRAYYSS LRNQINFMDL VEKATMGDEQ DSGHLMNLVM QFRKVCNHPD LFERAEVTSP
FSFGHFAETA SFVREGNMVS VGYSTRSLIK FELPSLVWAQ DGRLNRPSSS NATAGWRNKY
LDHMMNIWTP EHVQENVQGS KGFSWLRFAD VSPADVYRAT HEGLFTRACR ELQKKDRLGR
MSVIYDDEDQ SKAFTPTHAL FHVQARSNRR PLAEAMSEGI LNRLMNVARE TYDDSSMSRL
DIAGRPRASA PPIEVSCNSI SSVRERQETL FNNHIRQALY GPTSVEQTAL IEKRVPLELY
PQQSVLPRPD SERKRFTNVV VPSMRTFVTD SGKLAKLDEL LFKLKNEGHR VLLYFQMTKM
IDMMEEYLTY RNYKYCRLDG STKLEDRRDT VHDFQTRPEI FIFLLSTRAG GLGINLTSAD
TVIFYDSDWN PTIDSQAMDR AHRLGQTKQV TVYRLITRGT IEERIRMRAL QKEEVQRVVI
QGGGASVDFS GRRAPENRNR DIAMWLADDE QAEMIERREK ELLESGEYDK QKKKGGAKRR
QKTGDASASL DDMYHEGEGH FDDGSKGLPS GTATPGDGDV KGKRRGKTVG KRAKTAKQRL
AVADGIADE
//
