ID A0A178ECV6_9PLEO Unreviewed; 1919 AA.
AC A0A178ECV6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=IQ07DRAFT_609080 {ECO:0000313|EMBL:OAL53840.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL53840.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL53840.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL53840.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; KV441639; OAL53840.1; -; Genomic_DNA.
DR STRING; 765867.A0A178ECV6; -.
DR InParanoid; A0A178ECV6; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
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:0015165; F:pyrimidine nucleotide-sugar transmembrane transporter activity; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR007271; Nuc_sug_transpt.
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 NCBIfam; TIGR00803; nst; 1.
DR PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04142; Nuc_sug_transp; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF103481; Multidrug resistance efflux transporter EmrE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 664..838
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 879..1067
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 425..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1847..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1919 AA; 213319 MW; 09141EBF8C4B23A5 CRC64;
MVTRTPSGTL GGVSLKHLSL ATLTFQNSAL ILIMHYSRVM PLVGGQRYHA STSVFLNEVI
KLGISLTVAL YEMSNTLPPN TTLWTICQTL TTAVFANESW KLAIPAVIYT VQNTLQYVAV
SNLDAATFQV TYQLKILTTA IFSVVMLGRS LSSRKWISLF LLVVGVSIIQ APQAMGKRSG
TDTAAHMNAK VGLTAVLVAC ALSGLAGVTF EKILKDSSSA KNTSLWVRNC QLSFWSLFPS
LFLGVLWKDG QVIAQTGFFA GYNWVVWTAI LFQAAGGVIV ALVINYADNI AKNFATSISI
LLSCIASVYF FDFKVTRSFF LGTCVVLFAT YLYTKPERSP LQIPLSEKPT IERTPSARFH
ASSRLMIRRV ATSSTTPSPS VNLSPLTPHF SFTRFHSLAA HHSRATAMSN EYVMPDGFGR
HQARHASRYE PSQPRYQESA RPMPPRQRYR ATQFNNPMYD VVEDDQYSQD EHFETFGALM
RSVDRELLQH GYRGSERPAA LPRPRLSIAP GPSRFAASRV EYQDCGVEKG EYEGKDRFAY
RPTQPSASSS DVQFNPSSPA LRASERRETH NNFTARGRMS KPSAPEMEHQ YDHDEEDESM
EPFQHVRPIK AKWPFRSKDE SKSSHSQGPI IQGIRLVPVT ALPDRLRGIF SFPAFNAVQS
KCFQKVFQGD DNFVLASPTG SGKTAILELG ICRAIATNAT GQYKVVYQAP TKALCSERQR
DWEIKFQPLG LKCAELTGDS DASDLRNVQS ANIIITTPEK WDSITRKWKD HDKLMKLVKL
FLIDEVHILK ENRGAVLEVV VSRMKSIGVD VRFIALSATV PNVHDVAAWL GKSPAEPFEP
AAVEKFGEEF RPVQLTKHVC GYTTSNPNDF AFDKMLDSKL PEVIAKFSER KPIMIFCATR
NSSVKTAKSI AEWWSSNSGR GRFWDEPSAT PAMVDRDLRS TIASGVAFHH AGLLPEDRLQ
VERGFLQGDI AVICCTSTLA VGVNLPCHLV IIKNTVTYTL AGLQEYSDLE MMQMLGRAGR
PQFDDSAVAV ILTRQAKVRR YEMMVTSQEL LESKLHLNLI DHLNAEVCLG TIWDLPSARK
WLTGTFLFVR LQQNPNHYKL EGATSRQSTT SQVDEICSRD ITLLQQTSLV SDQEHFRCTE
FGLAMARYYV HFETMKVFMG LHHKSSPSEI LSALAQASEF SNIRFRQGEK AVYKILNKSP
SIRWSIPVNL DLPAQKVSLI IQSVLGCADI SWEGEVAKHR SQFVTDTQVV FKSINSLARC
IIDCQISLGD SIGIHSALLL ERSLGSRAWD DSPLQMRQIE NIGVVAVRKL VNAGIRSMDD
LEACDATRIE TLVGRNPPFG LKILEQVRMF PKLRVSLHAN NSSIARRAEG VTIQVKADIG
FLNEKPPQRF VNKPVGQMLA SGQSLAFPAL LTSADQCINC YVMCEGIAGT MRMATLKPRV
TPSMFSATTK PELVPQHKPN VSRRRVESLK SNSKQSATSE DFGDDGIDDE ELMKVTCGGI
EFECIENYPD PAATFDRNKS TKAVSKKDKQ KPSKMRPSGP DDPEEPVQLP NGKWVCNHKC
KDKNACKHLC CKEGMDNRPK KKPATKRATL DDDPPSQVPP KRVKGTQTKL QLTPAPRKPI
RVVEQLDLTE PERGDSFGFA SANEPEYSGL LSKIGRTTFR HQNDAQHHVQ DLSEEPEAIT
QPYHMGNHDL LDLDFDDTFE YPEDETYPDF KPTAPVESSA SDVFGDDDSL LGDAMIGLAD
SQNLQTLNED YSDRTNFDIP EDGPNVPQEE DYLDDDFSAD LEVMIHDDGN IDFVPQSTNV
LTTAAVEVHD PVPKASVVVK SINTISPTDA IEAVNTGEDR TNRVRNSRPA LPMTTRDVNL
PQQSNELKTH GKVDEDNSEG SLMQENQTSS QLETGPEGLE GLEPWLLAEF GDIIEITDA
//
