ID Q8PYG1_METMA Unreviewed; 945 AA.
AC Q8PYG1;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=Cation-transporting ATPase {ECO:0000313|EMBL:AAM30597.1};
GN OrderedLocusNames=MM_0901 {ECO:0000313|EMBL:AAM30597.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30597.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM30597.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30597.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PYG1; -.
DR KEGG; mma:MM_0901; -.
DR PATRIC; fig|192952.21.peg.1061; -.
DR eggNOG; arCOG01578; Archaea.
DR HOGENOM; CLU_002360_3_0_2; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
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 PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
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.
DR PROSITE; PS00154; ATPASE_E1_E2; 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 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 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 811..835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..900
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..121
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 103332 MW; 7555AF82C4714389 CRC64;
MTSVFLSDPD VSEGKENKQG PEEKGKNNPS QEKHSETEIL ESHSKTTSWY SLENEVIFKK
LATSSRGLDP EEVAIRLKEY GRNTLPSKKP PGIAEIVIHQ FKSPLIYILL IAGVISLLLD
DIKDAAFIFL VVIINAVIGT IQEWKAEQSA SQLQTILKIM SRVRRGGTES QISAEELVPG
DIVLLESGNR VPADIRIFRA TNLTIDESLL TGESEAVQKT ADIMREDIPV SDRRNMAYAG
STVITGRGCG VVTATGSRTE VGMIARAVTE TVSAKPPLLI RMEEFAQKIG IIVIAASAVM
SAVALSQGTA PIEVFFLAVA LVVSAIPEGL PVGVTVALSI ASTRMAKRNV IVRRLSAVES
LGSCTTIATD KTGTLTVNQQ TAKKVLLPPE NYFEVSGEGY VPSGEIKEEK GSTPETKDME
RLQKFARAAV ICNEGTLYQE EGKWVHHGDA IDVAFLSLAS KISINPKEAK KEVKIVAEVP
FESERMYAAV YYKEDKSDHI RVAVKGAMEA VLPYCRKMYT AGGEVPIDPD SLNRELNSLM
EKGYRALVVA EGPVQGEIGK EAELEYVKPE LTFLGIAAFI DPLRPDVNEA VRTCKKAGID
VIMITGDHPK TALAIAGELG ITDSREEMLT GREIEDLGDP ELPTFMTTLE KIRVFARVTP
VQKMQIVDAL VRRGHFVAVT GDGVNDAPAL RRANIGVAMG SGTDVAKDTS SMIVTDDTFS
SIVAGVEEGR VAYDNIRKVT LLLISTGLSE VILFILALLV GLPIPLLAVQ LLWLNLVTNG
IQGVALAFEA GEPGVMYRKP REPEEGIFNN LMIKETLVSG ATIGLIAFAV WMWLLGEGYE
ENWARNLLLL LMVLFENFHV FNCRSEYRSA FRVPIRNNYF LVIGVVMMQA LHILAMQVPF
MQGLLSISPV TFQSWFSFFV IAATIIVVME IFKKIRAARD KDIVT
//
