ID S3CWB3_GLAL2 Unreviewed; 2223 AA.
AC S3CWB3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:EPE29219.1};
GN ORFNames=GLAREA_00379 {ECO:0000313|EMBL:EPE29219.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE29219.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE29219.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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DR EMBL; KE145367; EPE29219.1; -; Genomic_DNA.
DR RefSeq; XP_008083328.1; XM_008085137.1.
DR STRING; 1116229.S3CWB3; -.
DR GeneID; 19459437; -.
DR KEGG; glz:GLAREA_00379; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EPE29219.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT DOMAIN 553..737
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 772..984
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1404..1580
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 49..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2223 AA; 250696 MW; D3FA35C9EC6574B9 CRC64;
MTDQQRDVSQ YKYSAMSNLV LQADRRFVTR RNDEVTGDPE SLAGRLSIRD MGSRNARDNA
PKQKKKALGL PDVERGGLQE GQDVLEREQR KRKRGEPAQL RGTGILSASD ALVEGIVYRP
RTSATRATYD LILTTVANNL GDVSHEIVRS AADAVLEFLK DDDMKDFDKK KEIDDLLGAT
MTPKAFNELV NLGKKITDYD AQDEDEVMAD GENRGEDGAD IDDRQGVAVV FDDNSEDEDG
AEMINEIRDE SSEDEEDRED RPGEEETATA GGAGKDRAEE SDESEADAMI LEAGPREKTD
TKDKKKNIVP ARDIDAYWLQ RQIGTIYSDA HIQQVKTQQA LHILSGAPEE EGGEEKPLRE
IENDLAELFD YENHELVHKL ITNRDKVVWL TRLARAEDAE DRGVVERKIA SEGLRWILDE
LRGVISSGDG SKKRKLEIKM DIDVPSALTN GGAKKENTGD EGLVGGLQPG KLINLENLVF
DQGNHLMTNP KVKLPEGSTK RTFKGYEEIH VPPPKKRNDP SDRDIPVSEM PEWSRVPFSS
ATKLNKIQSA CFPQAFQDDG NMLICAPTGS GKTNVGMLAI LREIGKNRNP DTGDINLDAF
KIVYIAPLKA LVQEQVGNFG ARLKPYGITV SELTGDRQLT KQQIADTQII VTTPEKWDVI
TRKATDLSYT NLVRLIIIDE IHLLHDDRGP VLESIVSRTI RKMEQTGDPV RLVGLSATLP
NYRDVASFLR VDPLKGMFHF DGSFRPCPLR QEFVGITEKK AIKQLKTMND VTYTKVLEHV
GKNNHQMLIF VHSRKETSKT ARYIRDKALE METIGQILRS DAGSREALNS EAEAVNDREL
KDLLPYGIGI HHAGMSRPDR TSVEDLFNDG MIQVLVCTAT LAWGVNLPAH TVIIKGTQVY
SPEKGSWVEL SPQDVLQMLG RAGRPQYDTY GEGIIITTQS EMQYYLSLLN QQLPIESQFV
SKLVDNLNAE VVLGNVRSRD EGVEWLGYTY LFVRMLRSPG LYSVGADYEG DSALEQKRVD
LIHSAAVVLE KSNLIKYDKK TGKLQSTELG RIASHYYITH SSMLTYNHHI QPSITPIELF
RVFALSDEFK YIPVRQDEKL ELAKLLGRVP IPVKEGIEEP HAKINVLLQA YISRLKLEGL
ALMADLVYVT QSAGRILRAI FEITLKKGWS SVAKTALELC KMAEKRMWPT MTPLRQFQSC
PRDIVQKAER IDVPWANYFD LDPPRMGELL GLPKAGKTVC NLVSKFPRLD VQAQVQPMTR
SMLRVELTIT PRFEWDEDIH GSAESFWIIA EDCDGEDILF HDQFILRKDF AQSEENQHVV
EFTVPITEPM PPNYFVSVIS DRWMHSETKL AVSFQKLILP EKFPPHTPLL DLQPLPVAAL
KSNDFKSLYP NWERFNKIQT QAFNSLFSTD DNVFIGAPTG SGKTVCAEFA LLRHWNKQTA
GRVVYIAPFQ ELVDARLVDW QLRFAELRGG KEIVKLTGET TADLKLLERG DLVLATPSQW
DVLSRQWQRR KNIQNVELFI ADELHMLGGH SGFVYEIIVS RMNYIRSQTE LPLRIIGLSV
SLANARDIGE WIDAKKHNIY NFSPHVRSVP LELHVQSFTI PHFPSLMLAM AKPTYLSILQ
MSADKPALVF VPSRKQARAT TRDLLAACVA SDDEDRFLHA DVDQMRPLLE RIGEEALAEA
VSHGVGYYHE ALSASDKRIV KHLYNNGAIQ VLVASRDVCW ELDCVAHLVV VMGTQYYEGR
EHRYVDYPLS EVLQMFGKAS RPLEDKLGRG VLMVPAVKRE YYKKFLNEAL PIESHLQAYL
HDAFVSEIST KMIESADDAI NWTTFTYFYR RLLANPSYYS LLDVSHEGLS AHLSELVETT
LKELAEFKII DLDEEDDSVT PLNAAMIAAY YNISYVTMQT FLLSLSGKTK LKGILEIITS
ATEFESIQIR RHEDNLLRRV YDRVPVKMGQ PSYDSPHFKA FVLLQAHFSR MQLPIDLAKD
QEIILTKVIS LLSATVDILS SDGHINAMNA MEMSQMVVQG MWDRDSPLKQ IPHFTPEVIA
AANKSGVKDI FEFMEAMDPS ENPDYEALVK RLSLSQTQLA QAAAFTNNKY PNIELDFQVE
DPENITAGDP AYLKVKIARE VDEDDEAGDV DMTVHAPFYP QKKMENWWLV VGEESSKTLL
AIKRITIGKS LNVRLEYTVP TPGKHELKLY LMSDSYVGVD QDPEFTVDVA EGMDEDDDEE
DEE
//