ID A0A177DLX1_ALTAL Unreviewed; 704 AA.
AC A0A177DLX1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Golgi apyrase {ECO:0000313|EMBL:RYN75135.1};
GN ORFNames=AA0117_g6620 {ECO:0000313|EMBL:RYN75135.1}, CC77DRAFT_1020560
GN {ECO:0000313|EMBL:OAG20012.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG20012.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG20012.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG20012.1,
RC ECO:0000313|Proteomes:UP000077248};
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.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN75135.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN75135.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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; KV441479; OAG20012.1; -; Genomic_DNA.
DR EMBL; PDXD01000015; RYN75135.1; -; Genomic_DNA.
DR RefSeq; XP_018385433.1; XM_018525068.1.
DR STRING; 5599.A0A177DLX1; -.
DR GeneID; 29110662; -.
DR KEGG; aalt:CC77DRAFT_1020560; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1020560; -.
DR OMA; WHDALFD; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF121; NUCLEOSIDE-DIPHOSPHATASE MIG-23; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 523..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 612..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 182..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 704 AA; 78615 MW; 0774AE480294A111 CRC64;
MGKWRYGVVL DAGSSGTRVH VYRWLNSDAA RKKASDAQLH SLPVIETDKK WTKKIHPGIS
TFGEHPHDVG SEHLDKLLSH ALKHVPLEEV PNTPLFLLAT AGMRILPERQ RKEVLKEVCE
FARATTQFQL PDCDVHVQVI PGETEGLYGW IAANYLLGGF DQPKEHDHGK GHNTYGFLDM
GGASAQIAFA PNATEAEKHA NDLTLMRLRT IDGTPLEYKV FVTTWLGFGV NQARERYIKA
LLESSAETEL PDPCLPADLE VEVTKDGKII DLDDDDDDDD KPKQKTAAKL IGTGQFAECL
HRTFPLLEKE KECKDSPCLF NGQHVPAIDF NVNHFVGVSE YWHTTHEIFE HGHKDKAYDL
KTYQERVDEF CSQDWKSIEK GIKKEKWGHK VDEEKARDVC FKASWVINML HDGIGVPRVG
IEDMKGGQNT TKAVIDNAKT KGFLDPFQAV NKINDVEVSW TLGKMVLYAS SEVPLPSEKA
LAVGFGSNVP GIPSDFQYPG GVPREYESDS DWHRLFVEHP QRIPGFFIMI FIFIFIFCLI
LGKEKRNTAK QYIGRLFKSK QGKDPLHRRR GRGFPAKLFG LGGASSHTQQ PYERVDLEDG
DAANEFELEE TYLDSSDNEL SDSSEGSKVG RTSGWATPQI KTEPVPGGPS YFGTTTAGDV
VREGTGLGLG PPSAFELSRT YSRERIKSRA SSPKRGKGMS KLDE
//
