ID Q8X0V7_NEUCS Unreviewed; 1391 AA.
AC Q8X0V7; Q7RV11;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KHE88230.1};
GN Name=123A4.350 {ECO:0000313|EMBL:CAD21386.1};
GN ORFNames=GE21DRAFT_7558 {ECO:0000313|EMBL:KHE88230.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAD21386.1};
RN [1] {ECO:0000313|EMBL:CAD21386.1}
RP NUCLEOTIDE SEQUENCE.
RA German Neurospora genome project;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAD21386.1}
RP NUCLEOTIDE SEQUENCE.
RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA Nyakatura G., Mewes H.W., Mannhaupt G.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KHE88230.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73 {ECO:0000313|EMBL:KHE88230.1};
RG DOE Joint Genome Institute;
RA Baker S.E., Grigoriev I., Haridas S., LaButti K., McCluskey K.;
RT "Draft genome sequence of Neurospora crassa strain FGSC 73.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AL670009; CAD21386.1; -; Genomic_DNA.
DR EMBL; KN389636; KHE88230.1; -; Genomic_DNA.
DR PIR; T48753; T48753.
DR SMR; Q8X0V7; -.
DR VEuPathDB; FungiDB:NCU01143; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_4_0_1; -.
DR OMA; LFRVCNM; -.
DR OrthoDB; 53793at2759; -.
DR Proteomes; UP000053122; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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; 3.30.160.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 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 Pfam; PF05773; RWD; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KHE88230.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 306..347
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 623..798
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 866..1038
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 153798 MW; 6747478FEC36AC2A CRC64;
MAKKGTKSSA PAPAAASSSA ASQPTSKSKK DSKKAAGPSE GDFIVFSNSD KEPKGKRGGA
KAGPSKPAEE LDAGPPKPTV KQLIGGHSWT GKLPVNLLSE HCQKQKWERP DYNTIKTKDG
FSVFVTLSAK NPKTQEVTTL PPFKLPPSHV HLAYKPTALE AKHFAATYAL YRVCSMKNMH
MTLPPDYRSL WKEFEALKKQ DVKEGKAWMY EADPFQAQRE REEAKAAAEK KRAQLQAAKE
KAANEPGVSL AFRGSGSGGA GGGGAHNVMR GWANVPKIEM GNKTRSQLED LLRRETVWNP
NGVVMSASQK AAIVKEFKDL GFRQSHIEEA VEECKDREEA LEWLLVHIPE DDLPRWALPE
KYSAGVTVAA TDLKREGAIT RLAQSGYSID LCRKLLALHN GDEAKAAEDL QKLLLASGSE
SIDDSSQDAD GLDTWRDADE CWEEEMATLE ACFGEKFSKI SPEICEIKLE GVKNGSQTNV
DACVQFRKSE QYPTQVILAM VAALPSYIKL SVIKQALAYA LTLEGEEMKI FYVASWVQEN
INDIIEKPGR IREVAAVASA ASEEPKKAVK RARRAPRCPK PINWSPDPRS TEEWRARTES
PSYKKMLYAR QNLPAWQVQD YLIQTVSENQ VTIISGETGS GKSTQSVQFI LDDLYSKGLG
KSANIIVTQP RRISALGLAD RVSDERCSQV GQEVGYSIRG ESKTSPNTRI TFVTTGVLLR
RLQTSGGRVE DVVASLADVS HVVVDEVHER SLDTDFLLAI IRDVLYKRRD LKLILMSATL
DAASFKDYFT VDGKNVSVGL VEISGRTYPV QDYYLDDVIH MTGFSIGNNR EYYYDDNAGS
KSKEDPNDDP INKIIQRMGS RINYDLLVET VCAIDSELAE TQKAGGILIF LPGVAEINRA
CNALRAVPSL HVLPLHASLE TKEQKRVFAS APPGKRKVVI ATNVAETSIT IDDIVAVIDS
GRVKETSFDP QNNMRKLEET WASRAACKQR RGRAGRVQAG KCYKLFTRNL EMQMAERPDP
EIRRVPLEQL CLAVRAMGIK DVSHFLSRAP TPPEATAVEA SITMLRRMGA LDGEELTALG
QQLAMIPADL RCGKLMVYGS IFGCLDDCVT IAAILSTKSP FVSPQEKREE AKEARKRFSQ
GDGDLLTDLR AFQEWNDQMQ ERMGQSRVRA WCGDNFLNYQ TLSDIASTRS QYYSALKEMG
IIPHNYSESN NSQQTKSMAL LRALTASAFS PQIARIQFPD KKFAASMTGA VELDPEAKTI
KFFSQENGRV FIHPSSTLFD SQGFTGNASF MSYFTKIATS KIFIRDLTPF NAYTLLLFSG
AIDLDTQGRG LVVDGWLRLR GWARIGVLVS RLRGLIDKLI TMKVENPSLD VEKNDIIKTV
VKLVELDGLD A
//
