ID A0A162LDV8_CORDF Unreviewed; 1690 AA.
AC A0A162LDV8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=ATPase, P-type, transmembrane domain protein {ECO:0000313|EMBL:OAA69234.1};
GN ORFNames=LEL_10110 {ECO:0000313|EMBL:OAA69234.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA69234.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA69234.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA69234.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA69234.1}.
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DR EMBL; AZHF01000011; OAA69234.1; -; Genomic_DNA.
DR STRING; 1081108.A0A162LDV8; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_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 InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
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; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
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 729..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 890..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1387..1420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1510..1532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1613..1633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1645..1665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 503..532
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 1690 AA; 186959 MW; 75BF5149F16E0066 CRC64;
MQAKLAEFHI PVFGKRAFLK NFTFLNISPP NNSQMPKAII IVGGGSAGIA TATRLRRLDE
SAIITVFEKG PHVSYANCGI PYALGDVIKD DALLVLKDDA LLLTYEAQYF KQRFNIDVYV
NTEVTEIDRR NEQICVRAGG HVKCHRIDYD KLVLCQGAEP IWPSIDHQSH CHVFHLRTSA
HLQAIKTFMI NCGVSSVCII GGGLLGIEAA ENLRKLSLKV SIVEKTSHII PGIDGGMAEM
LHAEVERNGV ILHLNSEVKD MSKSHVVLST GAEVPAEFVL LAMGTVPRKE LAEKAGLEVG
IHGVRVEENL QTSDEDIYAI GDMADTRHRF TKHSIPVAFA GPASRQGRMV ANDIAGRSTV
YRGNIGTVVC RVFNLTLGFA GLSVFALREL GQDPLWVTVH PADHESYYPN AYLITIKLAF
ERTSGRILGF QVVGRAGVDK RLDVLATAMQ ADMIVLDLEH LELGYAPPYG SAKDPVNIVG
FVAANVMRGD CRIVHVEDLD LEGLANWQVV DVRSPEEFAS SHLLPAINVP IEMTEINIVT
RWNFSIAQSK AYSAFSALMD DENDPSHCQV LRSTNTSEQD ADSAHDARNT ATMQAIQMTP
DARFASNEKT DNGTDGGNRL GFALTSRRHS VAFIPQVMSA KEKKRHRRQK EHEKEHVDID
EHLMSPQAVA ARYRTNIRMD RPETSLGLSS QEAEERLREH GLFNLLLILA GVLEYILLGI
NFTENLQNTY LGAILIAVAL LNAFIEFYQQ QKSQAILESF LDMIPAKCVC LRDGKLAQIE
ASALVPGDVV TVCMGGKNPA DILVFFASGC SVDNSSLTGE SEPQERTRDN DKQRLLEATN
IMFNSTLVVS GEAYGIVIRT GDGTVLGQIA HLASGEEKTK SPLAHEIDSF VRLIAAIAII
TAVIFFGIAF PVSHNNAPLA INVAIGIFVA WVPEGLPATV NILLTIAAKR MATQNVLVKG
LQGVETFGAI TLLATDKTGT LTRNQMTVAN IWTCDKLYSA SSAYGTEGDA TDLGSPGLMD
MLYIFALCSR AKFDRVDVPI EDRKVLGDAT ESALTRYAAK RLDNFDALDS KYEKVFEQPF
NSDTKWQMSI HKKAHAHGSL TLYIKGAPER IWLLCNRVLT GSNGASEYLN EKHRMAYDET
YEYMAGRGHR VLGFAQLLLP GDQYPDSSAF DKKAKGFPTC DFTFLGLCSL EDPPKHGVRE
AIGHCRAAGI KVIMVTGDHP LTAEAIGRKT NLILSETKEM VAKRMGRQLE DIKEHEYNAI
VVHGEQIERL TDLEWDMVLW KEEIIFARTS PKHKLEIVRR AQSMGHIVGV TGDGVNDSPA
LKKADVGIAM NISGSDVSKD AASMILLDDN FSSIVSGIRE GRLIFVNLKK SIQYTISHSI
PEVIPSLLYV IVPIPLPLSA ILILVIDLGF ELIAAISFAW EPPEMEDSLM KLPPRKLVTP
KTSNTFRRRK LRQTRSHFDE ESGTIVSPEH QTILQIWAHK VRQVFIREYW VDKFEDTGAE
VLVDGPLLSW AYLEIGVIES VGALTSFFVV LYRRGLTPMD TRIMQKGAGS PTNYWTKGAE
PYKGIDGPTQ VDILAEAQSM YYWAIMTMQI FNLFACKTRL TLPFGKYMFA NRATFYFIFV
GVALATFIIY TPGVEYVFKT SRNLLPLYWL IPMAFGFFII GYASVRMIVG RLIKPVKWNP
VIQGLQMSPD
//
