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Database: UniProt
Entry: A0A0B4HNP2_METMF
LinkDB: A0A0B4HNP2_METMF
Original site: A0A0B4HNP2_METMF 
ID   A0A0B4HNP2_METMF        Unreviewed;      1085 AA.
AC   A0A0B4HNP2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:KID94027.1};
DE   Flags: Fragment;
GN   ORFNames=MAJ_10021 {ECO:0000313|EMBL:KID94027.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID94027.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KID94027.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID94027.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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:KID94027.1}.
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DR   EMBL; AZNE01000139; KID94027.1; -; Genomic_DNA.
DR   RefSeq; XP_014573021.1; XM_014717535.1.
DR   AlphaFoldDB; A0A0B4HNP2; -.
DR   HOGENOM; CLU_001771_0_0_1; -.
DR   OrthoDB; 5480493at2759; -.
DR   Proteomes; UP000031176; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.30.70.100; -; 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; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR46594:SF4; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031176};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        433..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        463..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        493..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        529..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        679..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        721..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1024..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1051..1072
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          281..348
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          21..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KID94027.1"
SQ   SEQUENCE   1085 AA;  116149 MW;  B5638A45DBC0F3A1 CRC64;
     MGTECCSGHG SHDAVPAAVS EHNQDSLHHE EHGHHHGGHN HEQVQDHGHI HDHDHGPDPC
     KGEEHCTQEG ECCDDEFCCD NPSLSETLAC CSSNEEHCDE KCILAAAALE CEKTCETDNL
     DQKTAAGHEH QHDANGRHPS GACSSHLEKA FKQYSAYLDS ARCICRSVLE RGWSTTCCAN
     QPKKTIPSAV PNALDDKAEI YASGRKVHRH DGPHHHHEIR RRGKMAKHQG EDDSCCEPAN
     HDCCSDHDHA PGHDAIQPLD SSKSDGHRSI ERDVEKVEGL EHVALVVDGM TCSGCGNKMT
     NTLNKIAGVS SVKVNFVMSH AEFEVDTSVN TAAEVIRAAE RATNFRCNRM ASDDQVLDVL
     ASGKSAKTLL DCNIKGVAGT TILSKTTVRL SYVPTTIGAR DLFEKLQGQV EGLAPPGDDP
     SVSSGRKRLY DQLFKTILAA VFTIPVLVLA WGSTPVNEKT RGIISLVLAT LVQIIAIPDF
     YRPAIGALIH SCTIEMDMLV VISITAAYVY SVVAFGFRMA GKPLETSEFF ETSTLLITLV
     ILGRLVAAFA RIRAVEAVSL RSLQTTTAVI VENNKDRTID ARLLQYGDKL KIGPDSGVPT
     DGLVLSGQSD VDESMLTGES VPVSKGPGDA VIAGTVNKNG TLIAQLTRLP GKNTVTDIAQ
     LVEEAQNSKP KLQDYADRVA SWFVPVVTAV AIIVVIVWLV VGFKVRKYKA GQSISNAITY
     AVATLAVSCP CALGLAVPMV LVIAGGIAAR SGVIIKSAEC TERGRKVTDV VFDKTGTITE
     EKLDVKKQVL LINEALAISI AKALVAGNKH PVSLAVANYL KDRSIPAETL NDVQVIPGAG
     VEAKLNGSIL RAGNPKWTKT ASHDQVSRLQ NEGMTLLVVT QDGAPIAVFG LRTHLRKEAA
     GVVSQLARRN ITTHLVSGDQ KHAVEMVGSE VGIPNIVSQC TPVEKRDYVA KLMQEGKCVM
     FVGDGTNDAV AVSQADVGVQ LGSVLSSSDV TGKAADVVLL NGLEGIPFLL EISRVSFRRM
     VFNFAWSAVY NVLAILLASG AFVNIRIPPA YAGLGEVVSV VPVIVAAMTM LLKKPKVSAP
     TVERR
//
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