ID A0A162VSU7_DIDRA Unreviewed; 1286 AA.
AC A0A162VSU7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=ATP binding {ECO:0000313|EMBL:KZM18603.1};
GN ORFNames=ST47_g10228 {ECO:0000313|EMBL:KZM18603.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM18603.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM18603.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM18603.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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:KZM18603.1}.
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DR EMBL; JYNV01000324; KZM18603.1; -; Genomic_DNA.
DR STRING; 5454.A0A162VSU7; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07543; P-type_ATPase_cation; 1.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT COILED 1252..1279
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1286 AA; 142679 MW; 1B44551C85BC7A8C CRC64;
MAPLVNQPQI RQASLHNPLP LQLHLYVWPF LIVWPAFSSI YLSSARYEQY IQSQEWTFVW
VASIVTLQSL VWLLTQWNIN LRTLFTTTKA ADIRSARLIK VQPVENAGAA EICELRRDNA
GGKPNLSFLF QKRRFLYDAA AGSFAPLAYA LDSEPKPQLK TLQQTQGLVS PAEMERIQQH
YGDNAFDIPV PTFTELFKEH AVAPFFVFQI FCVGLWMLDD YWYYSLFTLF MLVMFESTVV
WQRQRTLTEF RGMSIKPYEL LAYRQKKWQD VMSDKLLPGD VVSVGRTKED SGVACDMVLL
EGAAIVNEAM LSGESTPVLK ESVQLRPGDA RIEPEGLDKN AFLWGGTKVL QVSHGNTADD
DANTVSRLSS GVPPPPDRGA VAVVIKTGFE TNQGSLVRTM IYATERVSAN NVEALLFILF
LTVFAIAASW YVWQEGVRLD RQRNKLLLDC VLIVTSVVPP ELPMELSLAV NTSLAALSKY
AIFCTEPFRI PFAGRVDIAC FDKTGTLTGE DLIVEGIAGL TLGQTNAKTS PDGAHTDLTK
VTDVGTHTTL VLATAHALVK LDEGDIVGEP MEKATIEALG WKVGAKDTLN ASTTTAKSHA
ELVQIRRRFQ FSSALKRQSS VATVLVTNNS GKKVRSTFVG VKGAPETIRK MLVNAPANYE
ETFKHFTRNG GRVLALAYKF LAEEGEWGQN RINDLKRETV ESDLHFAGFL VLQCPLKPDA
IEACRALNES SHRVVMITGD NPLTAVHVAK LCEIVDRECY ILDAPEHDES GNALVWKSVD
DKVNIPVDPT QPLAADIISS KDICITGYAL AKFAGQPGWK QILRHAWVYA RVSPKQKEEI
LLGLKEGGYT TLMAGDGTND VGALKQAHIG VALLNGTRED LDKIGEHYRN TKMKEIYEKQ
CQMMTRFNQP QPPVPVLIAH LYPPGPTNPH YEKAMLQQAQ RKGLAASANG AVNGSTDVAA
PQEKKPLGIG EQLTAKMMES ELEELNSEPP TIKLGDASVA APFTSKLANV VAIPNIIRQG
RCTLVATIQM YKILALNCLI SAYSLSVLYL DGIKFGDGQV TISGMMMSVC FLSISRAKTV
EALSKERPQH NIFNIYIIGS VLGQFAVHIV TLIYVSQFVQ RVEPKDPNPD LEKDFEPSLL
NSAIYLLQLI QQISTFAINY QGRPFRESIR ENKAMYWGLV SVSAVAFSCA TEFIPEINEK
LKLVPFTTEF KIMITTVMAG DFIACYVIEK GLKFLFSDNK PKDIAVRRPD QLEREKERKK
LEEVEAQKKK NELIEEKARA AGIVPA
//
