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
//