ID A0A0W0G2N9_9AGAR Unreviewed; 1491 AA.
AC A0A0W0G2N9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WG66_4625 {ECO:0000313|EMBL:KTB42826.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB42826.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB42826.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB42826.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB42826.1}.
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DR EMBL; LATX01001295; KTB42826.1; -; Genomic_DNA.
DR eggNOG; KOG0920; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 664..842
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 951..1127
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1491 AA; 167109 MW; C3FFF7BAA8DAE917 CRC64;
MAKKKKSQLK PVPRGFATTS VPKKVAPAEE EEPQAAVEIS QILQSEAGGV EKEAVPLNAE
RAPVEDEFDP EKAEEQSLQN LVDKLQEKTE KEITRRVVIA VSARIQAIEQ DRRFAKSLPI
LELNSTLATR ILELSFEFDK PDRKPIEEPE DKVIGKLAIT YGALRRLGFS EERVQECLKA
INGVELEEAY DWLYMNCSES ELLGPGASEE SLPRTPRTPG SLSEFSTLPP STPRTPRTPA
DFLAPPSLTH NRPRKVASRL DANAPAFVPS KLYNLVQSPA IFSTPEDTDS PTPSMTPIES
ELSSDSDGSG LTHNYVRTRM KIADLTRRLP GNKAPADHLE ELQSKLLAIQ QNYMFDEEEA
ETEYQKAREV ADANSLRDRL RGSAPAVEQP PQPKKRPPAM QLDPPPEPET APAPDVFDQE
QDEGGMFGLL EELPASETAN DGRTITFRDM ALPKHWSGRT PKILLADAVT KADKYAIVTY
SIISGESRAK RSSVRIRWDG KKTDEWTMDD IACHDEGQAE QYIATVALHA LTYPTTDGFA
AGNPRAAGGQ TFFRLLPPVF RDLWDELSDA LKNKNDEINR KVWSTLRSII EIKSEFERRT
TPAESKPSER TSSTKHNRTR PYANNSGDEQ IIAAFQARQS SPAYQEMLQH RNKLPVAHYR
EEIIETLESN QVLVLSGETG CGKSTQVPTF ILEDQLSRGQ PCKVYCTEPR RISAISLAQR
VSRELGEPPN VVGTSGSLVG YSIRLESNTT KNTRLAFVTN GIALRMLEGG SGQGGQGTGF
DEITHIVIDE VHERTIESDF LLIVLKSMLV QRPDLKIILM SATVDAQKIA DYFGGCPTFH
VPGRTFPVEV RYLEDAVEYT KWTISESSPY ARRSPFLLLQ HFTITDKSAA HDKFYKGKNK
VDWSEELMAG DDDDSDPAPS AVKLEKRYSQ STADAINLFD ERLVPYELIV RLLDYIYFKD
NTYREFSDAI LIFMPGIAEI RRLNDMLIEH KQFGSDAFRV YPLHSVLSSE NQSAVFDIPP
PGIRKIVIAT NIAETGITIP DITCVIDPGK HREMRFDEKR QISRLVETFV AKSNAMQRRG
RAGRVRSGLC FHLFTKLRFD TQMAENPLPE MMRLSLSDLA LRIKIMKINL GSSIEDVLSR
ALDPPVSINV QRAISMLVEV RALTPSEDIT PMGRLLSKLP TDVHLGKFLL IATLMRCLDP
ALTIAASLNS KSPFVTPFGL EQEADRAKAS FRVENSDFLT LHNAFASWRR ASQNSGFVRD
FCRRNFLSHQ NLQQIEELRQ QFLGYLVDSS FIQVDKSVIR ELNYARHSRN RNRFVTVPHE
YNTNSANSSL VHAALVAGLY PKVLAVDAQS KQMRTISNNQ VASFHPSSVN FGRKPKDLGV
NHLVYFTLMH SKKLYAWETG PVDDMALLLL CGEAEFKLIS NTVTIDRKIR FQLSPKDIVA
VKALRSQLAS LFAYQFRSKI LTESHILWND LAFTILGKSK AEGEKSVDLS L
//
