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Database: UniProt
Entry: F4RM90_MELLP
LinkDB: F4RM90_MELLP
Original site: F4RM90_MELLP 
ID   F4RM90_MELLP            Unreviewed;      1117 AA.
AC   F4RM90;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=MELLADRAFT_48408 {ECO:0000313|EMBL:EGG06378.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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DR   EMBL; GL883108; EGG06378.1; -; Genomic_DNA.
DR   RefSeq; XP_007410212.1; XM_007410150.1.
DR   AlphaFoldDB; F4RM90; -.
DR   EnsemblFungi; EGG06378; EGG06378; MELLADRAFT_48408.
DR   GeneID; 18928521; -.
DR   KEGG; mlr:MELLADRAFT_48408; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_48408; -.
DR   eggNOG; KOG0203; Eukaryota.
DR   HOGENOM; CLU_002360_4_1_1; -.
DR   InParanoid; F4RM90; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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   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; 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; PR00121; NAKATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000001072};
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        155..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        350..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        387..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        875..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        905..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        946..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1009..1026
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1047..1066
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1078..1096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          106..179
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  122333 MW;  7C1FF97435C69D4E CRC64;
     MDEKDSLKDA VNVGASHASK SVEDEEKQIG FATSSRTPRV DALNRQLRIE RTNSICLATA
     PPRTSPGTTF PALYKTMSIQ VENVEKSKAT DSKMEGKQAT DLANLEFHAI SVDDLLSRLA
     TSTIHGLDQN QVTRRMTQYG PNVISPPPKN LAKKIFFYIF GGFGSLLFVA SLICFLAWKP
     IGEPDPQSAN LVLAIVLLLV IVIQAIFNAW QDNVTSRVMA SISNLVGAEA LVLRDGKLAT
     VAASELVPGD LIKVTLGCKL PADLRLIEIS SDLKFDRSIL TGESDAIAAT IDSTDCNFLE
     TRNVALQGTL CTSGSGMGIV VQTGDNTVFG RIAKLSSQSS GRRTTLEAEI LRFVTIIASL
     AIVVASFIII LWAAWLRVKH PNFISVSGLL INVVSVMVAF IPEGLPVCVT LSLTVIANAM
     RKKKVLCKSL ATVETLGAVD VLLSDKTGTL TTGKMTVTNL AFGTTYMSAS VAKEAIRSDD
     KIKGDDSNSS HALKDLACLR DLAAIAAICN DAMFEDEEPV NQMDIETTKV NGDATDSGLL
     KFSQSIQSVS KSRESWKEIS KIAFNSKNKF AMKLMKAEAR DSYPGGVITS VASCANSMVI
     FVKGAPDVLL PKCSSLVDSD GIEVELTEHL TRSLIKAQER FASQGERVLL LSRKVIPLDS
     LDMDLINDAG YLSGLVSDLT IVGLLALTDP PKHDTAETVR ICRRAGMRFF IVTGDFALTA
     AAIGKKVGVI TTDNPHFLVD LPRNQDLDTI PSYSAEDPEG NMPHAVVLTG SDLFQMTDSQ
     WKQTLCYREI VFARTSPQQK LQITKRFQDA GHTVAVTGDG VNDAPALKAA DIGIAMGGGS
     EVAMEAADLV LLEDFSAIVT AIEYGRMCFE NLKKVCLYLL PAGSFSELMP ILLNVLFGLP
     QALSSFQMII ICVGTDVLPA LSLIYEKPES DLLLRKPRDR KKERLVNWQL LFHAYFFIGL
     LETLCAMATA FYFGFVRHGI PFSAIWLSYG EVKGVSTDRL NEATYRCQSI YFFCLVFMQW
     GNLLATRTRR LSIFHQSPIF KKATNNYYLF PAMIFALLVT IFFSYVSWFQ KVMFTRGVAF
     ENYLMPLAFA VGILMCDEVR KYFVRRYPRG PIAKMAW
//
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