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Database: UniProt
Entry: A0A167LGV8_PHYB8
LinkDB: A0A167LGV8_PHYB8
Original site: A0A167LGV8_PHYB8 
ID   A0A167LGV8_PHYB8        Unreviewed;      1051 AA.
AC   A0A167LGV8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=PHYBLDRAFT_115367 {ECO:0000313|EMBL:OAD70429.1};
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD70429.1, ECO:0000313|Proteomes:UP000077315};
RN   [1] {ECO:0000313|Proteomes:UP000077315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV440988; OAD70429.1; -; Genomic_DNA.
DR   RefSeq; XP_018288469.1; XM_018428456.1.
DR   AlphaFoldDB; A0A167LGV8; -.
DR   STRING; 763407.A0A167LGV8; -.
DR   GeneID; 28989362; -.
DR   VEuPathDB; FungiDB:PHYBL_115367; -.
DR   InParanoid; A0A167LGV8; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000077315; 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; 2.
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:UP000077315};
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        70..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        876..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        938..960
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        981..1000
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1012..1030
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..94
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1051 AA;  116633 MW;  C85F8F1364D4D570 CRC64;
     MTNCLIFNFT NLIVLDLTNV NYHNLSILEL SQQYSTSIER GLDKEQATKR SAQYGKNAIS
     PPPSNWGKKL FNYFFGGFCS LLWFASIICW ISWKPLGNPN PAPLNLALAV ILMFVVFLQA
     FFNAWQDWST NRVMHSINNM LPTQTLVQRE NNVITIDAVG LVPGDIVHVK MGNKIPADLR
     LIEVSDDLKF DRSVLTGESE AIPGTVDATD SNVLESHNVA MMGTHCLNGS AVGVVVAIGD
     NTLMGRIARL SLADNGARTL LQIEILRFVI IIAVLSITVG AACIITWAAW LRVSYPDFLT
     VSNALIAVIS VIVAFVPEGM PVAVTLCLTL IANRMKRNNV LCKVLTTVET LGSVNVLCSD
     KTGTLTENKM FVSDACIYNE YLASHVCRDV LVQRDIEVVN KYALSHQVGH LQAVSALCNG
     SRFDPETMHE QVRLRKTFGD ATDSAILRFA EQTNPSSTVA DCREKSEKIF EIPFNSKNKW
     MLTIHRPFHP DMANALSSNT THVSTDDWVL ICKGAPDVLM NRCTHVILPD GVEEPLTDKR
     RELLEEVQTR WANDGKRVLL LARRVIKASD TPNNIQAGTS SFGAWATQMN QNLVVIGLLA
     IVDPPRADSA ETVKICRRAG IRFYMVTGDF PTTAAAIARQ IGIFTTAHPK TIKDLDPSRP
     IDQIPRYIQT EFNNSSSIEL TQKGSSETTL EDSTSLLLSG TDLITLNDNQ WEQVCQFEEI
     VFARTSPDQK LRIIKEFQKR DNVVAMTGDG VNDAPSLKAA DVGVAMGGGS DVAIEAADMV
     LLDQFSSIIA AIENGRLVFD NLKKVILYLL PAGSWSELWP VVVNIFFGSP QTLSSFQMIV
     ICVLTDLMPS MALMMEKPEA GLLTRLPRRP KQDRLVNARL LMQAYGFIGI MEMASSMFMF
     YLYLGMNGLP PNKVFFSFSN FNSPDGYMGY TASEISSLLY TAQSIYFVNL VICQWGNVLS
     TRTRRLSLFQ TNPLWGPSQN LYLFAAMIGS LIIALIILYV PVFNTYLQTS PIPVKFWFIP
     FGWAGMIMAA DETRKFLART YPKGFFGKLA W
//
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