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Database: UniProt
Entry: A0A197JZ15_9FUNG
LinkDB: A0A197JZ15_9FUNG
Original site: A0A197JZ15_9FUNG 
ID   A0A197JZ15_9FUNG        Unreviewed;       782 AA.
AC   A0A197JZ15;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=K457DRAFT_481743 {ECO:0000313|EMBL:OAQ29681.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ29681.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ29681.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ29681.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial 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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
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DR   EMBL; KV442039; OAQ29681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197JZ15; -.
DR   STRING; 1314771.A0A197JZ15; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000078512; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049621; S1_DHX8_helicase.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078512}.
FT   DOMAIN          199..269
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          503..666
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          137..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..165
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  87463 MW;  6712635B0BFF5E77 CRC64;
     MDLEQFEVLE LVNKIRNEVL NHLGMDDKSV AEFIIHVHEK SADYTAFKDT LQDAGDFSPS
     FIGNLDRLIR TMHPKYRKAE EPTVADKAAI ADEKAHKFPG LAIPDRLGWM ADDDKPKEKK
     ATGGDDFMSE FESMIENAKQ ETRNKSRSRS RSRSPRRKRA RSRSRDGYGR SRSRSPRRRD
     DRGRSESSRS SLDDAPVLYK IYTGKVTNTK PFGAFVALDG VKGKVEGMVH IGMLAAGRVN
     EVSDVVKRND SVKVKVMSVT STRVSLSMRD VDQKTGKDLS PNLRIRTKEE MAQDAARNPD
     RPSSSTVPIV DDVEPRSSKL KRLSSPERFE LKQLRASGVH IPMGQDDLDE DFGTIDNMEA
     EEELDIELCD DEPLFLKGQA RHALDLSPIK VVKAPDGTMN RAALSGAALA KERKELRQSE
     VNAEYDSVPK DINKPWLDPM PEPGERNFAQ DLRGSAASGK AGQVPEWKAS TFGKATTYGR
     ITNLSMQQQR ESLPIFKLRT QLVNAVKNNQ ILIVVGETGS GKTTQMAQYL AEEGFTANGR
     IGCTQPRRVA AMSVAKRVAE EVGCRLGQEV GYTIRFEDCT SPETKIKYMT DGMLMRECLI
     DMTMSQYSVI ILDEAHERTV STDVLFGLLK QVCKKRKDLK IIITSATMDA EKFSTYFYGC
     PIFTIPGRAF PVEILYTRDP ESDYLDASLY TVMQIHLSEP AGDILLFLTG QEEIDTAAEI
     LYERMKALGP MVPELIILPV PERSSLPPTL LRQVSLSMES TTSSTLDSSS RTPMMPSWVW
     IL
//
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