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Database: UniProt
Entry: M2N9U8_BAUPA
LinkDB: M2N9U8_BAUPA
Original site: M2N9U8_BAUPA 
ID   M2N9U8_BAUPA            Unreviewed;      1067 AA.
AC   M2N9U8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=BAUCODRAFT_34659 {ECO:0000313|EMBL:EMC95899.1};
OS   Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS   (Baudoinia compniacensis (strain UAMH 10762)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX   NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC95899.1, ECO:0000313|Proteomes:UP000011761};
RN   [1] {ECO:0000313|EMBL:EMC95899.1, ECO:0000313|Proteomes:UP000011761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC95899.1,
RC   ECO:0000313|Proteomes:UP000011761};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KB445556; EMC95899.1; -; Genomic_DNA.
DR   RefSeq; XP_007676823.1; XM_007678633.1.
DR   AlphaFoldDB; M2N9U8; -.
DR   STRING; 717646.M2N9U8; -.
DR   GeneID; 19112474; -.
DR   KEGG; bcom:BAUCODRAFT_34659; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   HOGENOM; CLU_002360_3_3_1; -.
DR   OMA; KMHACET; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000011761; Unassembled WGS sequence.
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   GO; GO:0030001; P:metal ion transport; IEA:UniProt.
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; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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; PR00121; NAKATPASE.
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   Reference proteome {ECO:0000313|Proteomes:UP000011761};
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        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        369..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        836..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        994..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1025..1043
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..127
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1067 AA;  114169 MW;  452F4DE743C4FFA7 CRC64;
     MSRDALPLYH PSNNAPSRAT SQSLQPPADA PKRGHSRAKS RVKIPGQQSV TSIHAQLSAE
     QVAERHSTSL SHGLHPSDAN TRLHVQGPNE LPREEPEALW LRFVKQFQET LILLLLASAA
     ISAIMGNFED AVSIAVAVTI VVTVAFVQEY RSEKSLEALN QLVPHSAHVI RSTASSRPNG
     SAQANGTPHG PGTADLGTAE KASTTISASQ LVTGDLVLFH TGDRIPADIR ITHSADLSID
     ESNLTGENEP VGKTAETLSP GQHGVNGSIS TPFSAPSMGG ELRLNEQHNI AFMGTLVRTG
     YGQGIVIGTG GETEFGAISA SLQEIESPRT PLQLSMDRLG KDLSYMSFGV IGLIMLVGLW
     RGLRFLELFQ IGVSLAVAAI PEGLPIIVTV TLALGVLRMS KRNAIVRRLP SVETLGSVNV
     VCSDKTGTLT INHMTVTKLW GFGSDAPEEV GKVHKTAPNG PITQAILRTA NIVNNARLNT
     HVQTQGHVSS AAAQAVLAST RSGEELAAAK SRWAGQPTDV ALLDLLDAFG EDDIREKLGA
     RKHEIPFSSE RKWMGVAIQG QDGEERAYIK GALERVLGRC DRYLDAQGQE VVLDDKARRR
     VEEAADTMAE EGLRVLSFAS GPVRTPERTP TAPSRSSTRS GASTPASVNG DRSASSTHDD
     TYTSLTFTGL VGMSDPPRPG VDRSIRRLMA SGVKVIMITG DAEVTALAIA KKLGMPLNFS
     SALGSPVLRG DQLDAMSEAE LAEQIPRVTV FARTSPDHKL KIIRALQSRG DVVAMTGDGV
     NDAPALKKAD IGISMGRLGT DVAKEAADMI LTDDDFSTIL SAIEEGKGIF WNIQNFLTFQ
     LSTSVAALGL VMMSTLGGWR NPLNAMQILW INILMDGPPA QSLGVEPVDP ALLTSLPPRP
     RHARVLSPRL IKRVLQSAAV ILLGTLFTYV RNLTPEDLAA HSVSARDTTL TFTQFVIFDM
     FNALTCRSST KSVVLGEVPL GWWWGSSKSG RGNVMFNYAV LGSLVGQGMV VYFPPLQRVF
     QTEALGVGDL CGLVAMGSLV LWVDEGRKWW ERRRGGGGGL AGYSRRV
//
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