GenomeNet

Database: UniProt
Entry: K9FR72_PEND2
LinkDB: K9FR72_PEND2
Original site: K9FR72_PEND2 
ID   K9FR72_PEND2            Unreviewed;      1094 AA.
AC   K9FR72;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Na/K ATPase alpha 1 subunit, putative {ECO:0000313|EMBL:EKV11679.1};
GN   ORFNames=PDIG_49050 {ECO:0000313|EMBL:EKV11679.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV11679.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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:EKV11679.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AKCT01000198; EKV11679.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9FR72; -.
DR   STRING; 1170229.K9FR72; -.
DR   eggNOG; KOG0203; Eukaryota.
DR   HOGENOM; CLU_002360_4_1_1; -.
DR   InParanoid; K9FR72; -.
DR   OMA; FQDWSTK; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000009882; 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; 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; 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:UP000009882};
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        162..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        356..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        849..871
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        877..898
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        929..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        987..1004
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1025..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1057..1076
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..186
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1094 AA;  121049 MW;  62CC3FAA4189E316 CRC64;
     MTPENSNKDI DIESESNAFK DDERTGRSTQ ITFEGSTPAE GFRSIYQTQS NRPRSISRDT
     IHSTRSSIQG MPELPIEFRT ISIQISESQN APKQAIVNAT EKQPHQDYFE SLDFHIISPD
     SLCREFNVDQ RTGLSSSSAA TRLQRDGKNV IAHHGENYLK KIFFYVFGGF CSVLWVGVVI
     FFICWKPLSN PPSSQNLSLA VLILIVIALQ AGFSAFQDWS TKRVMNSILD LLPAEAMVLR
     DGKLIHIPAT DLVAGDIVHI GIGNKVPADM RLLSSSGDVR FDRAILTGES DEVEGAIDCT
     ETNFLETRNI ALMGTGVTNG NAIGIVILTG SRSVMGRIAS MTAGVKQKTT LIQREINRFV
     TIIVILTVVL ALLILLTWLG WLRKDHHSYM SVVAMLNNVM GCVVAFIPEG MPVAVALTLM
     MIAKRMKQTN ILPKGLSTVE TLGCVNVLCS DKTGTLTQNR MFVKSLGMVD WEYSLEDLAP
     GGFGTVDLPE GLKRMLQASV LCNDATFDPT TLHLPVHERD VNGNATDAAV LRFGDSFGLI
     SPTALALYER VHQIPFNSKN KWMLTLHRDP KSTKEFILYV KGAPDVLLGR CTTYWSAVHN
     AVRPLDVESR EKFSNFQAKL SRRAERVIVI CQRRYIPHSA PGSNDFSNEM LDDGVQDLTV
     LGIFGIIDPP RPETASTVAA CRKAGIRFFM VTGDFGLTAA AIAREIGIYD GQAEPDTIEE
     LRDGLDQSME VKVPKSRHSL LLEGPNLSAL TSEHWEIVCG YDEIVFARTT PEQKLRIVTE
     LQARSCVVAV TGDGVNDAPA LRAADVGIAV GSGSDVAIEA ADLVLLDKFD SIIEAIRLGR
     LVFQNLQKVI AYLLPAGSWS EIWPVIMNVF FGCPSPLSTF LMIIVCVFTD LFLSLSLIME
     KEEFDLLSLP PRRPTKDHLI NLRIYGQSYL FVGVMEAFSA HAMFFLYMWR HAGISFSDLI
     FAFEGYSEGF HGYTADELNH FVSVGQSVYF VTLVIMQWGN VLSVRSKRMS ILQADPIRPA
     RRNPWLPLAI LISFIIAIFV TEVPGIQNLF STASVPIEFW CIPLGLALGV LCMDELRKVL
     VRLFPKGPVA WASW
//
DBGET integrated database retrieval system