ID A0A369HF63_9HYPO Unreviewed; 1531 AA.
AC A0A369HF63;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RDA93872.1};
GN ORFNames=CP533_4538 {ECO:0000313|EMBL:RDA93872.1};
OS Ophiocordyceps camponoti-saundersi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA93872.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA93872.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA93872.1,
RC ECO:0000313|Proteomes:UP000253071};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) 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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- SIMILARITY: Belongs to the neutral ceramidase family.
CC {ECO:0000256|ARBA:ARBA00009835}.
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:RDA93872.1}.
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DR EMBL; PDHQ01000020; RDA93872.1; -; Genomic_DNA.
DR STRING; 2039874.A0A369HF63; -.
DR Proteomes; UP000253071; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046514; P:ceramide catabolic process; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 2.60.40.2300; Neutral/alkaline non-lysosomal ceramidase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006823; Ceramidase_alk.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR038445; NCDase_C_sf.
DR InterPro; IPR031331; NEUT/ALK_ceramidase_C.
DR InterPro; IPR031329; NEUT/ALK_ceramidase_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR12670; CERAMIDASE; 1.
DR PANTHER; PTHR12670:SF1; NEUTRAL CERAMIDASE; 1.
DR Pfam; PF04734; Ceramidase_alk; 1.
DR Pfam; PF17048; Ceramidse_alk_C; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Helicase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000253071}.
FT DOMAIN 6..280
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 281..590
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 711..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1531 AA; 169993 MW; 171AB5CD27284D93 CRC64;
MSTVLESLND AQRRAVTSNA PTVAILAGPG SGKTHTLTAR VAWLVQQAGY KPCDIIIATF
TVKAAREMKT RIENALGQEL SSRIILGTFH SIARRYLAKY GRLIGVDPRF GIADAGDSKA
IIERICKRFK LNVEPSVARS WISKRKSAGA SSATSAPPTK QGCETSALLT CFEEYQAHLS
RVDLLDYDDL LVRCVHLLQE YKSCVSNIQA VLVDEYQDTN GVQYDLMKLF AQERQRITIV
GDPDQSIYGW RSADSRNLGR LLRDFQGTKE VALEENYRSS ELILSLSLNV IRQEAHRYNK
NLVAVHREGL KPVLRKLKTS VAEGEWIVSE IRRITMLSGN MLKLQDIAIL LRSASLSRHI
ESALGKANIL YRMVGGTKFF DRKEIKVLLD YLRVIHKPDC NDALARIIGS RRGIGGATVK
SLLEEAEQER RSLWCLLWRH CREGRRAKTN IRAQMEQSLN EVLRIMHNLR VKAAQVDQAS
PLMLVETIQG LVDQLHFKKY LESEYAEDHE GRWASVQELI NMAGDMARGF LEAVDEEALP
EIVGVEQTRD DDVLGRFLAN VALASDAGRD DEGGDETALV TISTIHAAKG LEWPVVFIPS
VYTGSIPHAR SEDLDEERRL LYVAMTRAQA CLYLSWPLYG PGNFGGMELS PFVSSVARMF
APKGPSMDKK VVQKIAKVLG REAPKDKDIY DQLPVNFMPE DDLFPIDPTA RDNPNDFKGH
NSKAARRPLT ACSAQKEQQP WKPDYVTTMG NASQFTMSVG TDSWWTRKAD CYPATGHLSA
STRSAESVGG KQSAVSHSAF LLVSLAMMIR MMLLAIFTLL FRFVAGVYEA GDKHLIGVGK
ADITGPVVEL GLSGYANLKQ VGTGLRQRLY SRAFIIGSVS EPSQRFVYVV LDLQSGDTAV
RNGVIERLAD LGGGYKDYGH NNVALVGTHS HAGPGGWCNY LLPQIPNLGF DRQSYEAIVN
GTVLSIQRAH ESMQEGYLEV NDDRLEDGAI NRSLHSWLAN PKAERDSYPD ETDKTLTLLR
FQRASDLATI GVLTWFSVHG TSLLGNNTLV AGDNKGVAAW LLEEDYKKQF GGASDAVSVP
NFVAGFSQSS VGDTTPNVLG AYCDDGSGQL CDFETSTCAD GKSQSCHGRG PEFRALDLGV
KSCFEMGQRQ FNLAKRLMRE RIGQGTHIAA TDVKSFHFFH DMRFWEFTTL NGTKAMTCPA
ALGYSFAAGT SDWPGALDFT QGDGGEPGAS PLWRIVSRFI KNPSERQKNC QGVKPILLDV
GEMENPYAWA PNIVDIQMFR VGQLFFIISP SEVTTMSGRR WKAAVADYAK NELGVKKPMV
VLGGPANTYA HYCATPEEYQ VQRYEGASTL YGPHQLDAYI NLTVSNMMYL RGGSRDSPAR
GGAPPDNRHK SISLVPPVIF DEPGFGTYFG KTLQEARRVY RPGSTVNVTF QAANPRNNLR
LEETHVAVEK WIIDSQKWVR YRDDSDWFLT FQWRRTNAIL GWSEVDVAWD TSGNAETGRY
RIRYYGTQKS LISGKKDFEG LSRAFIVEYL G
//
