ID A0A2T3ZIE8_9HYPO Unreviewed; 1098 AA.
AC A0A2T3ZIE8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=M441DRAFT_24714 {ECO:0000313|EMBL:PTB44570.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB44570.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB44570.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB44570.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ679258; PTB44570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZIE8; -.
DR STRING; 1042311.A0A2T3ZIE8; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000240493; 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 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:UP000240493};
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 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 853..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 948..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 987..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1029..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1053..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..183
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 22..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 121721 MW; 459E932C5154BEA8 CRC64;
MPENIAPEPD EKEANDLRIT FNDVTHPSGR VGRTHTNDRE QGLPLSRKRS MSRGSVNSRR
DLPSSPYSGV QIEYRTLSIH VSESRQVDSD NLPDIKEKKD NKEEYFSNLT FHELEVDQLC
QQLNVSQEMG LSESAAALRI QRDGKNTLPH PKPNYLKKLL MYVFGGFCSV LWVGVVIFFI
CWRPLSNPPS PTNLALAILV LIVIVLQAGF SAFQDWSTSR TMNSIIDLLP SDALVCRDGQ
LMKLKATELV SGDIVHLQIG NKVPADMRII NHSGDLRFDR AILTGESDEI DASVDQTEEN
FLESRNIALM GTLVVNGSGV GVVVLTGPRS VMGRIAKATA SAEERPTLIQ KEITRFVYII
VGLTIVLALI ILFTWLGWLR KDHPDYMNVV AMLNNVMGCV VAFIPEGMPV AVALTLMMVA
RRMKASNVLP KGLSTVETLG CVNVICSDKT GTLTQNQMHV NSIAFLDEPI AIQDLYNSLS
SDKVDAGMKK LHQAASLCND ATFEPSTLHL PVASRTIQGN ATDGAVLRFS AGAPTSNEKA
ADQPTKVFQI PFNSKNKWML TMYKIPSESQ ATNEFQVFVK GAPDVLLPSC TAYWSRKSKC
VMPLDGPAKI AFKEYQDKLS KNAERVIVLC MKNMTVDEPI GTNHFGDEVT SRATEDLTVV
GILGITDPPR PETLSTVQEC RRAGTRFFMV TGDYGLTAAA IARNVGIITS ERDPDTIATI
KANNDADAVK KLNEARIAGE CRSLLLEGQS LGSLSDEDWS IVCEYQEIVF ARTTPEQKLR
IVEEFRKRDN VVAVTGDGVN DAPALRAADV GVAIVSGSDV AIEAADLVLL DRFDSIIDAI
RLGRLVFQNL QKVIAYLLPA GSWSEIWPVI LNVFFGVPLP LSSFLMIMIC VFTDLFLSLS
LIMEKEEFDL LSLPPRNHKK DHLINLKIYG QAYLFTGTAE TICAHSMFFF YMWKAAGIPV
HQLFFLFEGY TDGFHGYTQD QLNQFNYTGQ CVYFVTLVIL QWGNILSVRN RRLSIVQADP
FTKKRRNPWL LLGMLISLAI AIFVTEVPGL QTLFLTASVP IEFWLIPIPL ALGILVLDEF
RKLIVRLFPN GPVAKVAW
//
