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Database: UniProt
Entry: A0A0G2H2L7_9PEZI
LinkDB: A0A0G2H2L7_9PEZI
Original site: A0A0G2H2L7_9PEZI 
ID   A0A0G2H2L7_9PEZI        Unreviewed;      1092 AA.
AC   A0A0G2H2L7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative h k atpase alpha subunit {ECO:0000313|EMBL:KKY29553.1};
GN   ORFNames=UCDDA912_g10537 {ECO:0000313|EMBL:KKY29553.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY29553.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY29553.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY29553.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY29553.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY29553.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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:KKY29553.1}.
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DR   EMBL; LCUC01000694; KKY29553.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2H2L7; -.
DR   STRING; 1214573.A0A0G2H2L7; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        852..873
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        879..901
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        930..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        981..1001
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1022..1041
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1047..1071
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          118..191
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          17..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1092 AA;  119059 MW;  352150A4382BA5D4 CRC64;
     MSSPVAQSYK TYLSMAENEE AEAATTERLR FKDEEEAAGG GGHGHHHGRR ASMAASRRPQ
     LARSSTALSE DSISIRPSSR REPTVALPIQ YRTLSIDLED AKAKNKNNAA VEDLADLDWH
     TIPTHELSQR LNVSDRHGLS EEQVRRRLSR YGRNAPSPPQ KHRLRAMAGY LFRGFGPVLL
     VASVLVFVAW RPLGDPPAQA NLALAIVLLA VFFIQAGLNM WQDWSSSRVM ASIKTMLPGE
     CRVTRGGALA ALPASELVPG DVLLVGAGSK LPADVRFIRV SSDTKFDRSV LTGESVPLAA
     TVDPTDTNYL ETKNIGLQGT HCVSGSCTGI VVSTGDRTVF GKIAKLTNEP KAGLSTLEKE
     ILSFVWIICS IMILMIIIVI VLWAAWLRTT YPDWINVPTL IVNCVSVAVA FIPEGLPVAL
     TASLTISANM MRKNKILCKS LKTVETLGAN KMVVTDCFVG LEKMTADNVR DTLIAERNID
     GNFAGNAIDQ LRTVGGLCNA AVFDAQTRKL PLDERKIHGD ATDTAILRFS ESLGPISGIK
     RCWRTKFDLA FNSKNKFMVR VLSMSHPDGK IDAMPLDVAS VFEPSDLAKI EAAQAEYSAR
     GRRVLLLAHK TLSRPSIKST PPSPAFEKEM ADSARSGLTL VGLVAIQDPP RPEIPEVVRA
     LRGAGIRIFM VTGDFGLTAR AIAAECGIIT NDPGSVRAAA DLDDNNSNNN NSNNNNNNND
     GEGQAAARAV RFSDQARPRS IVVTGPELTA MGGTQWDELI GSYAEVVFAR TTPEQKLRIV
     RELQARGVVV GMTGDGVNDA PALRAADVGI AVGSGSEVAA EAADMVLLDS VGSVVEAVRC
     GRTMLDNLKK TMAYLLPAGS FSEFWPVFTS VALGLPQVLG SFLMIVICCF TDCLAATALA
     YEKPEADVLL RPPRVVGVDR LVDWRLVVQS YGFVGVAETA ASFAMSYWYL ERSGIPFSRL
     WLGFGSPEGI DADYYAGKLR VASSIYFVTL VVMQWFNLMC VRTRRLSLFQ HPPLFNRRTQ
     NAWLFPAVLF ALAMAFFWLY TPRLQEVLST AAVPAEYWFL PMAFGLAILL MDEGRKFLVR
     RWPTGLMAKW AW
//
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