ID A0A0L6U7J0_9BASI Unreviewed; 1150 AA.
AC A0A0L6U7J0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=VP01_911g1 {ECO:0000313|EMBL:KNZ44478.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ44478.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ44478.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ44478.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KNZ44478.1}.
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DR EMBL; LAVV01014738; KNZ44478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6U7J0; -.
DR STRING; 27349.A0A0L6U7J0; -.
DR VEuPathDB; FungiDB:VP01_911g1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000037035; 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; 2.
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; 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; 2.
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:UP000037035};
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 141..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1059..1079
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1091..1116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..165
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 126045 MW; BCAD7F30402A8D56 CRC64;
MSFDPNLEKM NESDDRNTNQ ATAPPTGGIS FADPKRLANN AGGRDLGLRR ELTQDEKQLA
NAGYEELESK MKAKALEGAT ADISEHKLSP QQVAEAVGTS INIGNPSSSA GLSNEESQSR
LVRDGPNQLT PPKKKSALRK YFDALLSLFN VLLILAGILE YVLLAIDFEN NKANEYLGAI
LILVAFLNAF IEWYQGQKAD AILASFLSMM PPSCKVVRGG QISSLPAQEL VKGDIVFIKM
GDKVPADMVL FSSSDVKVDN SSLTGESEPQ ERAVLLEGDP VRPVEARNLL FNSTLVVSGE
GFGIVVRTGD HTFIGQIAGL TGGESDNKSV QSLFHTSIIT AIIFFGVGIG TTYKGKIAAT
VTFAVSVLVA WVPEGLPATV TLLLSIAAKR MAKAKVLVKD LQGVETLGAL TMLATDKTGT
LTRNQMTVTA MWTNLTMRSA FESHNDEAEV QHFKTEDLGV REILEICTLC SKVKFDKMDI
PFEKREILGD ATESGLTRFA GKNLEFDHVR EKHPEAYSIP FNSTAKWALV VVQKPHANGD
LTLYLKGAPE RVLDRCSHAL VNGESIPITE QFKTQYGEAY QYMASRGHRV IACAQLLLPA
AQFPRDFQFS KKHDNCPTEN LCFVGLISLE DPPKHGVREA IGQLRSAGIK VVMVTGDHPL
TAEAIARKIN LVIGHTKESL AKATGRQVDE IHEDEVDAVV VHGDAIDALQ GWEWDTILSK
TEIVFARTSP KHKLEIVRRA QALGHIVGVT GDGVNDSPAL KKADLDAHNP GIAMNLSGSD
VSKEAANMIL LDDNFASVVD GVREGRLIFT NLKRSIQYTV THSVPEVIPQ LLYVIVPIPL
PLSAILILVI DLGFELFAAL SFAWDCPESS EALMTTMPRK PVTDRSIMQL KKKALRRTRT
NQMDVEAGND KPQSHLGETL RNAVENVKKP FSKWWWDDLL EKSDGEALVD GSLLSYSYLQ
AGMIETVGCM MAYFVIFNYN HFTPRDLQIA QKAGIYFTDN SPPYTNLSGR VIDSTAQTEA
LAQAQGMFYM SIFLMQCFNM FAVKAKLKFP FGKAAVGNKW NFVGALAGAI LAAFIIYVPP
LRVVFGASHR ILPLFWLIPI GFGFVILLWA SIRVLFLRKK LLSSSVQPPK GLNMHPTKRT
MSIRSTSAKH
//
