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Database: UniProt
Entry: M1VZ65_CLAP2
LinkDB: M1VZ65_CLAP2
Original site: M1VZ65_CLAP2 
ID   M1VZ65_CLAP2            Unreviewed;      1756 AA.
AC   M1VZ65;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Related to antiviral protein and putative helicase {ECO:0000313|EMBL:CCE34662.1};
GN   ORFNames=CPUR_08597 {ECO:0000313|EMBL:CCE34662.1};
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:CCE34662.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE34662.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE34662.1,
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   -!- 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:CCE34662.1}.
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DR   EMBL; CAGA01000101; CCE34662.1; -; Genomic_DNA.
DR   STRING; 1111077.M1VZ65; -.
DR   VEuPathDB; FungiDB:CPUR_08597; -.
DR   eggNOG; KOG0949; Eukaryota.
DR   HOGENOM; CLU_002305_2_0_1; -.
DR   OrthoDB; 33910at2759; -.
DR   PhylomeDB; M1VZ65; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd18025; DEXHc_DDX60; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR44533; DEAD/H RNA HELICASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR44533:SF4; HELICASE ATP-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:CCE34662.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801}.
FT   DOMAIN          730..903
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1174..1347
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          491..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1151..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1661..1728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1066
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1676..1692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1756 AA;  197916 MW;  D6044626752D9DDF CRC64;
     MAFNRQDEDM QLRCLSLIKV DIVGDFAGKE LFAIHGDSLL LHCIRKAKVD IEIGFQLLHA
     VFAVEAFIET LNKRGCNFNI VWFSDHEKLC MPEDVSPTAK WNYCLTRAII VKHLERRNSD
     CAAGSTSSLS MHSSSFQRYL DENAIYFFLS LGGQDDEDLS HNGVQYMQLL RWLSSKGYSI
     AALDSLEISS SKVYARVRSP AMMKEAIELP EVQQIPRSKS VNELKSSCDM LLFDSSPWGD
     GLPCSERDRV SLVGLTNTLL LDDRQRMKHC ALAYIIHLSL LRHLDLSQRS CTEITLPTLE
     QKSMDEFLSS FNNICTSFVE NMIPSRNWDL FDLVDGRILR QIYVNLANIS LPKLIIDEVL
     RYANVLRQST QVDLSRSIPQ YDMVRTSNPA VALIDNSTSC SVLDFTHPVL DAFLSEMSLS
     TQRSITSQST LKIFQELSHW HNARISIDKK QIPKQKTLLA MKRHQRLMNN ILSYSASLTN
     ASGKTINPET IVSEVQMKPP SKKSNKVNRG VDGKAPKLPT SHEPKHKKPA ASGGRQAAMK
     EANLIQARKS NELLKKALSY WDRLCGQFEH ETDLDSRYRK TVKYLAELVD QDMGVIRAEA
     SLYLCNCLAL IIHNARKKSK KIDEMGLMAI IWSKLLDINS LSLSNEGADL FKLFAAAVKF
     PASVAPDASL KGRKLPFRHI MAYLGNKLSI PLSSLHFQLL HCGPYLERGF DSAPDPRVLF
     NPDAWQRKVL DAIDANQSLF VVAPTSAGKT FLSFYAMKKV LQSNDDDVLV YVAPTKALVN
     QIAAEVQARF SKSYKNAGSS VWAIHTRDYR INSPKGCQIL ITVPHILQIL LLHPSNSSES
     KAWSLRIKRI IFDEVHCIGQ ADDGVIWEQL LLIAPCPIIA LSATVGNPED FRAWLETSEK
     AKGHELTMIA HSSRYSDLRK FVYHLPIEQN FQGLKSAEGI HIPGLDEGQH AALSFSHVHP
     VATLVNRNRG KLNDINLEPR DCFVLWKYMS KHQTKDFCIS DNLNPEHSFS GIIKKSDVTK
     WEAALKRVME GWIQAADSPF PSLRADLQSL TAQNAPVNSK TPRVKEPTSA KSVDPGTEAS
     DLRNAALPLL TDLHRHESLP AILFNYDRTY CERVLCFVND QLKVAEDKWK ADSPAWQRKI
     AKFEEWKRSG VKSKQKVNRT GPNQRRQDEG EHSKLDSMQD EADKDISRWE SFDPEAPLEM
     FSFADRTKML DSEFEIQIER LKWQNLKPEI LGALRRGLGV HHAGMNREYR QIVEMLFRKG
     YLRVVIATGT LALGINMPCK SIVFFGDSVF LTALNYNQCA GRAGRRGFDV LGNVVFVGLR
     PERVFEIMSS RLPDLRGQFP LSTTLVLRLM GLLHHTNNSP YAVRIMKSLQ VQSRLFLGGP
     SDQMSIKHHL RFSIEYLRRQ DLLSEHGAPL NFAGLVGHLY FTENAVFAFH SLLRGGYFHR
     ICRNINRTKY GVSQQLMLIL SHLFGRIPLR MADAKAITDK EHRSPSIVVL PALPKAAEDI
     LTEHNKETLH IFRNYVGSFV EQHLYDQPDN QLPLTNCAIL KKTGADTIEA SSFLDIVPPT
     KLRSAFAALS GFTDEFESIH DLCTTVRAGV FLEESAVPYI PLYPNDDANM HWNAYLYDFF
     KHGSLEALVR YNGIKAGDVW FHLKDFSLVL AAIVTTLQNS HGSAVQQQST GPPKPDDLEE
     SWDSEMKPEI SSQDENTSRA QDNEGGGPAD ALTESEAEEE GKEAEKYDAE ESLANILLAF
     MELQSQFNEA FYKVGA
//
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