(data stored in ACNUC7421 zone)

HOGENOM: NEUCR_197_PE159

ID   NEUCR_197_PE159                      STANDARD;      PRT;   920 AA.
AC   NEUCR_197_PE159; P07038; Q7RV59;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Plasma membrane ATPase; EC=3.6.3 6;AltName: Full=Proton
DE   pump; (NEUCR_197.PE159).
GN   Name=pma-1; ORFNames=B1D1.210, NCU01680;
OS   NEUROSPORA CRASSA.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5141;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEUCR_197.PE159.
CC       Neurospora crassa supercontig 7.5 EF1 full sequence 1..1121413 annotate
CC       Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:PMA1_NEUCR
CC   -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a
CC       hydrogen ion pump. The proton gradient it generates drives the
CC       active transport of nutrients by H(+)-symport. The resulting
CC       external acidification and/or internal alkinization may mediate
CC       growth responses.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIIA subfamily.
CC   -!- GENE_FAMILY: HOG000160005 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Neurospora_crassa;EFNCRG00000001832;EFNCRT00000001834;EFNCRP00000001834.
DR   UniProtKB/Swiss-Prot; P07038; Q7RV59; -.
DR   EMBL; M14085; AAA33561.1; -; Genomic_DNA.
DR   EMBL; J02602; AAA33563.1; -; Genomic_DNA.
DR   EMBL; AL355927; CAB91270.1; -; Genomic_DNA.
DR   EMBL; AABX02000005; EAA27650.1; -; Genomic_DNA.
DR   PIR; A26497; PXNCP.
DR   RefSeq; XP_956886.1; XM_951793.2.
DR   UniGene; Ncr.15464; -.
DR   PDB; 1MHS; EM; 8.00 A; A/B=1-920.
DR   PDBsum; 1MHS; -.
DR   ProteinModelPortal; P07038; -.
DR   SMR; P07038; 1-920.
DR   STRING; P07038; -.
DR   TCDB; 3.A.3.3.1; P-type ATPase (P-ATPase) superfamily.
DR   EnsemblFungi; EFNCRT00000001834; EFNCRP00000001834; EFNCRG00000001832.
DR   GeneID; 3873048; -.
DR   KEGG; ncr:NCU01680; -.
DR   NMPDR; fig|5141.1.peg.6052; -.
DR   eggNOG; fuNOG06156; -.
DR   GeneTree; EFGT00050000000742; -.
DR   OrthoDB; EOG4M68RQ; -.
DR   PhylomeDB; P07038; -.
DR   BioCyc; NCRA-XX3-01:NCRA-XX3-01-005390-MON; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR000695; ATPase_P-typ_H-transp.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006534; ATPase_P-typ_PM_proton-efflux.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 2.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; NEUCR_197.PE159; -.
KW   EFNCRG00000001832g.scaffold_90100000011;
KW   P07038;
KW   3D-structure; ATP-binding; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Hydrogen ion transport; Hydrolase;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   920 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADHSASGAP ALSTNIESGK FDEKAAEAAA YQPKPKVEDD EDEDIDALIE DLESHDGHDA
     EEEEEEATPG GGRVVPEDML QTDTRVGLTS EEVVQRRRKY GLNQMKEEKE NHFLKFLGFF
     VGPIQFVMEG AAVLAAGLED WVDFGVICGL LLLNAVVGFV QEFQAGSIVD ELKKTLALKA
     VVLRDGTLKE IEAPEVVPGD ILQVEEGTII PADGRIVTDD AFLQVDQSAL TGESLAVDKH
     KGDQVFASSA VKRGEAFVVI TATGDNTFVG RAAALVNAAS GGSGHFTEVL NGIGTILLIL
     VIFTLLIVWV SSFYRSNPIV QILEFTLAIT IIGVPVGLPA VVTTTMAVGA AYLAKKKAIV
     QKLSAIESLA GVEILCSDKT GTLTKNKLSL HDPYTVAGVD PEDLMLTACL AASRKKKGID
     AIDKAFLKSL KYYPRAKSVL SKYKVLQFHP FDPVSKKVVA VVESPQGERI TCVKGAPLFV
     LKTVEEDHPI PEEVDQAYKN KVAEFATRGF RSLGVARKRG EGSWEILGIM PCMDPPRHDT
     YKTVCEAKTL GLSIKMLTGD AVGIARETSR QLGLGTNIYN AERLGLGGGG DMPGSEVYDF
     VEAADGFAEV FPQHKYNVVE ILQQRGYLVA MTGDGVNDAP SLKKADTGIA VEGSSDAARS
     AADIVFLAPG LGAIIDALKT SRQIFHRMYA YVVYRIALSI HLEIFLGLWI AILNRSLNIE
     LVVFIAIFAD VATLAIAYDN APYSQTPVKW NLPKLWGMSV LLGVVLAVGT WITVTTMYAQ
     GENGGIVQNF GNMDEVLFLQ ISLTENWLIF ITRANGPFWS SIPSWQLSGA IFLVDILATC
     FTIWGWFEHS DTSIVAVVRI WIFSFGIFCI MGGVYYILQD SVGFDNLMHG KSPKGNQKQR
     SLEDFVVSLQ RVSTQHEKSQ
//

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