ID A0A317VQ94_9EURO Unreviewed; 1901 AA.
AC A0A317VQ94;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:PWY75451.1};
GN ORFNames=BO70DRAFT_411756 {ECO:0000313|EMBL:PWY75451.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY75451.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY75451.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY75451.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY75451.1}.
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; MSFL01000021; PWY75451.1; -; Genomic_DNA.
DR STRING; 1448321.A0A317VQ94; -.
DR VEuPathDB; FungiDB:BO70DRAFT_411756; -.
DR OrthoDB; 2971338at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd17936; EEXXEc_NFX1; 1.
DR CDD; cd06008; NF-X1-zinc-finger; 2.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR046439; ZF_RZ_dom.
DR InterPro; IPR000967; Znf_NFX1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF445; FINGER AND HELICASE DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF20173; ZnF_RZ-type; 1.
DR SMART; SM00438; ZnF_NFX; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51981; ZF_RZ; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:PWY75451.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1822..1898
FT /note="RZ-type"
FT /evidence="ECO:0000259|PROSITE:PS51981"
SQ SEQUENCE 1901 AA; 212541 MW; EEDFD8B295B457F4 CRC64;
MITSSLETRR AFVEDLATES GLQNIRLIVE TDFATSYSVL KPTFDPHCLL FLRMISHQEI
LSSLVLEKAV GTIYNVIYGP GGRRGMDFLT NVTRYLVETN GGSVSEENTK VKGDAATNGS
TKASAPWAEA LLLTTKVLLS TLNLNQEAAA HPDLKHIIES LCSCCQKESA TADANIDLAR
ANIINIGDSL SIGDSLYISK VTEKVKKTNP KKIEEMPVDF PGELSERGPR HDNDHAAIPR
IRILPTISEI LSDARAEFLP SQGSLDPSSH HERGVCRLID THFRLLREDT SGVVRDALRL
IIHNWDFLAH SSDWKLKHKF LRQYSPTPLR IFSGVQMRQI NADQKKGIEI DLEFDQLHRL
KNMSALRRKQ WWLDTRTLRG GPLLALLDAE DLDNAYAMFF LVSKREVNHI EKKRNASPTP
ISDVVSDAER AMITLRLADS AYESDANRLL SMMREKPARP LILIEFPAVP YNSFEGILRC
LQSLHKSPWR VPFATWLAPS GVSDELIEAL TTSCTKNINV PPPVYLQGRV VNLSSLPRRN
LDNGDPAIPI LMSPFEDNHS ITARLSQETI LDEGQAAAMV SALRCKLALI QGPPGTGKSY
VGLQIARCLL DNQESLQLGP ILCVCYTAHA LDQFLDGLVK SGISNIVRIG PPSASSHIEA
LSLDARKREP GPRVGGVNRI KDESRGALLT LTSKIKCLLE TAGRDINSLI MGFLRKKFPS
QASMINLGPC EKDGEAMQEW ASGDVPRWNE DGTAERSIEE LLKSDMDLWT LHNAERARIL
QYWQDTAWTE LSVGLSRLLK FHHEEKRKHT SAFGLLDLQR LNSSQVVGIT TTQLANNADL
LRNINSKVLI CEEAGEVLES HVITALLPSV QHAILIGDHL QLRPRISNIR LSKACDETNF
NLDESLFERL ATYRFGDLNA EEQGFGFPVA QLSHQRRMHS VVSDLVRDTF YPNLKDHPVT
AAYPPISGLK RRLFWLDHRN IEDPTDPADP MQSKTNAWEA GMVVALVRHL TRQGKYGPGE
IAVLTPYVGQ LRMLEDILGR EMALIISETD KDDLDEEDVE APVSIPTGPS RSRNLQGNVH
KGSLLDVIRL STVDNFQGEE ATVVVVSLVR SNRYRNCGFL DLPNRINVLL SRAKHGMYII
GDANTASTAP MWSSVIGILE RDANIGPKLE LHCSRHPGIQ SYISQPDDFA VYAPEGGCAD
KCELRLACGH RCPVKCHSEK LHKAVKCMEP CTRVKGCGHA CPKKCHERCG DCQETVLNVL
LPCGHRAQRV ECRMMGNLKN IRCVEQLVRT ISGCSHRLKV RCFENASSMK CFHLCGNVLP
CGHNCRKPCW QCRSTMAGKS TIDHGVCHNP CGRPFTTCAH VCNQPCHQGT ACAPCDRTCE
VRCKHSRCAK NCSEPCAPCA EPCGWGCDHR KKCALPCAVP CSKVPCNLRC KKKLWRCGHR
CPGMCGEPCP DSAYCRLCCN QGVLTRNVDL LEFKAYKDIN IDQDPLIFLS CGHFYTSTSL
DGVMSMSEYY DMDQLTGIII RPKVSYRAMS SGDVKGCPEC RMPLRNINRY NRIIKKGLLD
EATKRFVSHT NSIYAGLMEA IRKRETDIEK ERVQFMSNWP LDDLGSKGPD QVQRSIEAYR
AKGNRLQRQI KEFTKSVGRE EQPFGRVNNM LAAAAARDQS IVTTSFPFDE SIIQTGFESR
GEILGLRLTW ALFWDLDAIY TRKDTDPRIR ATLVQVVASQ LERILKRCHE LAEASQTARF
PQQEVESRIY HVLFTMLSLS NSDAQGKVVD IPTQTAIRDK AREELKACEE ICLRHRRILS
SLHEDIEKAK TLVNGGMFYS FVSTDEKRQV YRAMEQQFAG TGHWYYCENN HPFTVGECGM
PMEQARCPQC EAPVGGLNHE LAPGMRRADD IDVEFGGTSR N
//
