ID V5G1I9_BYSSN Unreviewed; 1133 AA.
AC V5G1I9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Na/K ATPase alpha 1 subunit, putative {ECO:0000313|EMBL:GAD98228.1};
GN ORFNames=PVAR5_6919 {ECO:0000313|EMBL:GAD98228.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD98228.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD98228.1}.
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DR EMBL; BAUL01000236; GAD98228.1; -; Genomic_DNA.
DR AlphaFoldDB; V5G1I9; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; V5G1I9; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000018001; 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:UP000018001};
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 196..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 916..937
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 968..988
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1022..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1064..1086
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1098..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..220
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 125902 MW; 7E26676BDFCB1C09 CRC64;
MPSSPSSQEP ASEENPHDSE ADVEANARSD VPNGGDYELE TQEQRGSQRV IFESPADDPR
SETRRSRNNA SKRLRSISRS KSIDTIRSSR SNKDNRESSV APGIPIEFRT LSIQISESHN
TSEELLKGKK DKGDKNLVNQ DYFEQLDFHI LSQDRLCQQL NVDSEKGLSA SAAATRLQRD
GKNTVAQRRE NYLKKIFFYV FGGFCSVLWV GVIIFFICWR PLSNPPSATN LALAILVMIV
IALQACFSAF QDWSTKQVMN SILGLLPSDT MVLRDGRLVK MPATDLVAGD IVHISIGNKV
PADMRILKTS GDVRFDRAVL TGESEEVEGA TDATEKNFLE TRNIALMGTS VTNGNAVGVV
VLTGSRSVMG RIASLTADVK EKPTLIQKEI NRFVRIIICL TIVLACSILF TWAGWLRVDH
SGFMNVVSML NDVMGCVVAF IPEGMPVGVA LTLMMVARRM KSANILPKGL STVETLGCVN
VICSDKTGTL TQNKMLVRSV GFIDKRYSVD SFTEDVQKDQ APLPVQTLLQ GSVLCNDAFF
DPETTHLPLG EREVNGNATD EAVLRFAETV NPGSTTKFEQ YERLYQVPFN SKNKWMLTLH
KTMAKPESVK LNDSKEIYLV YLKGAPDVLL PKCTSYWSGI DNEVKQLDYS AKQMFSAFQE
EMSKKAERVI VLCQRYYSPR ATLGSNDFAD EIQAEGAQNL TIIGLFGIVD PPRPETARTV
ASCRKAGIRF FMVTGDFGLT AAAIARDIGI FTGTAEPDTV ADLADLTVDK DVISSRQSLL
VDGSQISSLK EEDWDLICQY QEIVFGRTTP EQKLRIVNEF RNRDNVVAVT GDGVNDAPAL
RAADVGIAVV SGSDVAIEAA DLVLMDKFDS IVQAIRLGRL VFQNLQKVIA YLLPAGSWSE
IWPVIMNVFF GVPLPLSSFL MIIICVFTDL FLSLSLIMEK EEYDLLDGPP RNHKKDHLIN
LKIYGQSYLF IGVLEALCAH SMFFLYMYKA AGIPFHALVF AFEKYSDGFY GHTEDQLTHY
NNVGQCVYFV SLVIMQWGNI LSVRNKRMSI LQADPVRKER RNPWLPLAML ISLIIAIFVT
EVPGIQSLFN TASVPLEFWF IPIGLAFGIL LMDEVRKVVV RLFPKGPIAR IAW
//
