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Database: UniProt
Entry: A0A067T9L6_GALM3
LinkDB: A0A067T9L6_GALM3
Original site: A0A067T9L6_GALM3 
ID   A0A067T9L6_GALM3        Unreviewed;      2164 AA.
AC   A0A067T9L6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Sec63-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GALMADRAFT_139507 {ECO:0000313|EMBL:KDR76589.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR76589.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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DR   EMBL; KL142378; KDR76589.1; -; Genomic_DNA.
DR   STRING; 685588.A0A067T9L6; -.
DR   HOGENOM; CLU_000335_1_0_1; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000027222; 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; 4.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027222}.
FT   DOMAIN          504..688
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          723..917
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1353..1529
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          25..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..260
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2164 AA;  244519 MW;  D6FC57F096F9AFB2 CRC64;
     MSGRGKPDLS GYNYGAISSL VLTTDRSALP RRDKEPDGAP VSLAGRIDPK DMGSRVIRQA
     PKDLDKKKKK AVEGADPSEK AAVKRKAEAA GFGYADIIEA TQDVEGLTYR PRTAETRQVY
     ELILSAVHTS LGDQAQDIVR SAADAVLETL KNENMKDFDK KKEVEEVVGL ISGEQFSQLV
     SLSKKITDYN ADDETMADPD QERKDAEIDE EGGVAVVFDE EEQEEEDEEG FEIREDSDED
     EDEGEKEDEN DVEAEGNDED IVIGGESSGK NKVKAEKDIV SPHSIDGFWV QRQISEVYPD
     PVTAADKAAS VLSILGSESS ARDAENQLME LFEYQSFHIT AKFLKNREVV VWCTKLMRSD
     AEERVNVEVA MREKGLGWIL RDLAGDRQTK ASRSDAMDVD ESKPAQVPKT ATLAPGSTVQ
     PKRTVDLESM AFSQGGHLMS NKKCKLPDGS FKRAKKGYEE IHVPAPKQKA VAEGELVPIS
     SLPEWARQAF TVPKLNRVQS KLYPIAFGTD EPILLCAPTG AGKTNVALLT ILNEMSKHRN
     AETGEFDLDA FKIVYIAPMK ALVQEMVGNF TQRLKVFGIK VGELTGDSQM TKQQIAETQI
     IVTTPEKWDV ITRKQTDTSY TNLVRLVIID EIHLLHDDRG PVLESVVART IRRMEQTHEY
     VRLVGLSATL PNYQDVATFL RVDEKKGLFY FDASYRPCGL QQQFIGVSEK KAIKRYQITN
     EVCYEKVLDQ VSNKNQVLVF VHSRKETAKT AKFLKDMAIE KETITQFVRP DAASREILQE
     EAGSAKDRNL KELLPFGFAI HHAGMSREDR VVVEELFADN QVQVLVCTAT LAWGVNLPAH
     AVIIKGTQIY NPEKGKWVEL SSQDVLQMLG RAGRPQYDTY GEGVIITNHS ELQYYLSLLN
     QQLPIESQFV AKLADNLNAE IVLGTVRNRD EAVQWMGYTY LYVRMLRSPA LYGVGADYQD
     DDTGLIQKRA DIAHSAAVLL EKCQLIKYER SSGRFTSTEL GKIASHYYVT YNSMMVYNQH
     LRPTMSALEL FRVFALSNEF RLLPVRQEEK LELAKLLERV PIPVKETVEE PAAKINVLLQ
     AYISQLKLDG FVLVADMVFV QQSAGRILRA MFEICLKRGW AVPAKAALDM CKMVDKRMWG
     AMTPLRQFKG VPPEVVRKAE GKQFPWYRYF DLTPPEIGEL IGVPNAGRLV HRLVHNFPKL
     QLQAQVQPIT RSLLHIDLSI VPDFRWDEKI HGSAETFLII VEDVDGEVIL FHDTFVLRQR
     YAEDEHTVTL TVPMFEPVPP NYYISVISDR WLHAETRLPI SFKHLILPKK FPKPTPLLDL
     QALPLSALHN EEFEALYANT IQTFNKIQTQ VFQALYTSDE NVFIGAPTGS GKTICAEFAL
     LRLWSKRERS RAVCIEPYQE MVDLRVKEWK KKFQNLQDGK QIVSLTGETS SDLRMLEVGD
     VIVCTPTQWD MISRRWRQRK AVQTLGLLIA DEVQMVGGEV GPVYEVVISR TRYVERQTGN
     KTRIVACGVS LANAEDLGKW MGASEHTIFN FSPSARPLDM SIHIQSFSIP HFPSLMIAMS
     KPTYLAIKEY SPSKPVIVFV PSRRQCRLTV DDLLTHCSAD DQPDMFLNIE LEDLQPHLDH
     INDKALVETL KHGIGYYHEA LDKRDKIIVQ RLFESGAIQV LVASKDTAWS LPVASYMVII
     MGVQFYEGKE HRYVDYPVMD VLQMMGKACR PLEDENSRCV LMCQQTRKDF YKKFISEGLP
     IESHLPTHYL HDYFLAEIAV KTIENKQDAM DVLTWTYFYK RMLENPNYYN LHNTSHQHVS
     DHLSELVETT LNDLVNSKCI SIEDEMDVAP LNLGMIAAYY NISYVTVEVY TLSLKERTKL
     KGLLEVVSSS AEFESIPIRR HEDTLLRRIY DRVPVKLDRA DFEAPHFKTF LLLQAHFSRI
     QLPPDLAADQ TLVLEKVLNL LSACVDVMSS NAWLNALGAM DLSQMCVQAM WETDSPLKQI
     PHFEPDVIKR CKGANIESVY DVMEMEDDQR NELLQMSPAQ MRDVATFVNS YPTLDVSHEL
     VKGEYTAGSS IFLKVTLARD IDEDDQSDQT VVAPFYPLKK LANWWLVVGD PATRQLLVIK
     RVTVTKSLAA KLEFSLPKGK HSLKLYVICD SYVGADHDIA LDPIDVAEGE DSDSDEDMDS
     DENE
//
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