ID A0A165QZ54_EXIGL Unreviewed; 1427 AA.
AC A0A165QZ54;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Sec63-domain-containing protein {ECO:0000313|EMBL:KZW04271.1};
GN ORFNames=EXIGLDRAFT_709628 {ECO:0000313|EMBL:KZW04271.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW04271.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW04271.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW04271.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV425882; KZW04271.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165QZ54; -.
DR InParanoid; A0A165QZ54; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000077266; 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 GO; GO:0010467; P:gene expression; IEA:UniProt.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
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:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 1.
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; 1.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 110..302
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 338..536
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 972..1138
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1427 AA; 158081 MW; 1CB88EE18F616B79 CRC64;
MNASLEAAAN RPLFSSDAKA FVPEILPNIY TSTSLGYGGV LSATGHKYML PADTTRVEHE
EFIEVTIPPA KTVPPRGNER LIPISSLDPL CKGSFPGYTS LNRIQSIIYD TVYKTNENML
ICAPTGAGKT DVAMLSVLRI LSQHLSTDVS NTASLSSSIR KHEFKIIYVA PMKALAAEIV
RKLGKRLQWL GINVRELTGD MQLTQAEIAA TQIIVTTPEK WDVVTRKPTG EGELASKVKL
LIIDEVHLLN EERGAVIETI VARTLRQVES TQSLIRIVGL SATLPNYRDV AEFLGVSPYA
GLFFFDSSFR PVPLEQHFLG IKGKPGSAQS KKNLDAVTFE KIAELVRAGH QAMVFVHARK
ETVKTALALK DSAIEDGSID DFSCQDLPNW QLLRRDVGSS RNREMRELFD HGFGIHHAGM
LRADRNITER LFASKAIKVL VCTATLAWGV NLPAHAVVIK GTQVYDTARG KFVDLSVLDV
LQIFGRAGRP GLESSGEGYI LTTEDKLTHY LDAVTSQHPI ESKFEGGLID ALNAEIALGT
VSSVTEGMTW LSYTYLFVRM RRNPFVYGMP HDEPANDPTL SAKRALLIGA AARRLAAAKM
ITFDEATGRF AITDLGRIAA RYYIRHASIE IFNKELRPVM SEADVLAVIS QSTEFDQIQL
RENEVKELKT IMEEIIPCEV KGGTETSQGK VNILLQGYIS QAYVEDFALV SDMAYCAQNG
GRILRAVLEI SLSRKWATAS ATMMSLSKAV EKRMWPFEHP LKQAELSLSR DVLYNVERFI
DELAVSDLAA KTPAELGDLI HMNERHGTAL HRAATQFPSL ELHYDLRPLS FDLLRIVVHA
RPAFEWSSKV HGSIEPWWIW LEDEKGVDIL QASNVLLRQT TQSLDFNFVI PIRAAKPPAF
VRLRAVSDRW LGAEHEVDIS LQELIMPPAS ADRTALLDLP FLPVTALRDQ PLQGHYSRLF
GSFNALQTQA FWTIYNAKSN ALLCAPGSCG KSTLAYAAVC KTVASGSPDK WALVVVPSRS
AAKEATFNLR RICQLKGITL DLAVTPDVLL DRVNGRTIRV VTSACLVEAL PLRPAVFTGV
SLVLCDDLHL LDDKYELAVS MLMHTLQNQP VRYLGLSESL DDPSGLAQWL RVDEQSLYCF
RPSDRDQPLA IGTKTFSIPH SAALFKAMLK PAHSLIISRP AEEAALVFVP SRFHCKVVAA
DLITQCAVQL NTNGFLGHNT LSESLEPYTT RLVDRSLVDL LHNGIGVYHD GVHKADQKLI
MQLFLEGIVR VLIAPRETCW SIPVRAATVI VLGTQYSRTT DGGDDRRVVD YTPQEVMRML
GRAIRHGRAG HFHLFCQADA LDTFMRFINH GLTLESQLAD GELLRNWVTA RRRDGTIAGK
QDAMDALAFS YLGRRLRTNP VYYNATDSAR DESLSRVLDS VWTAQLS
//
