ID A0A135RS65_9PEZI Unreviewed; 1096 AA.
AC A0A135RS65;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=CSIM01_02865 {ECO:0000313|EMBL:KXH26564.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH26564.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH26564.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH26564.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) 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:KXH26564.1}.
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DR EMBL; JFBX01000863; KXH26564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135RS65; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000070328; 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 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 160..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..900
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1027..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1051..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..184
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 121024 MW; 8ACB5E1E8CD37EE3 CRC64;
MEDSRKSAEI IRPNGNHNAH ISFRGDEEMG NDIRGRPNIN NKSANRPRSA RSAASSISRR
RRQSTSENFG IQIGYRTLSI HVSESQHATA NAETDLKATK EGDDEYFAEL NFHTVPGVQV
CQQLGVSPDQ GLSEQEASTR LQKNGPNTLP EPQANYLKKL LVYVFGGFCS VLWIGAIIFF
ICWKPLSDPP SAQNLAMAVL ILIVIFLQAG FSAFQDWSTQ KTMKSITSLL PSETLIMRNG
DVKRMTASEL VEGDIVHLRT GSKVPADLRL LSHSGDIRFD RGVLTGESEE VEGAIDSTDP
NFLESRNIAL MGTTVVNGHG VGIVILTGAR SVMGRVARAT TDVGEKATLI QKEIWRFVRI
IVVLTVFLAL LIFVAWIAWL KRDHPSYMNV VQMLNNVMGC VVAFIPEGMP VAVALTLMMV
ARRMKAVNIL PKGLSTVETL GCVNVICSDK TGTLTQNQMT VNSVAFVDKP LSSPDDVHKG
LNEEKPDAIF SVLQKAALIC NDASFGADTM HLPPQERTAE GNATDVAVLR FAASARDSDA
IMSNSARVFS IPFNSKNKWM LTLVHEDTVE KSNRFRVFVK GAPDVLLPAC ASFWSGRTQS
IEALDGNAKM LFKDIQDKLS RNAERVVVIC EKTLETILSP GTNAFSDEVA MKALENLTVV
GILGIIDPPR PEAAWTVANC RRAGARFFMV TGDYGVTAAA IAHNIGIFTT SEPDTFDTIR
RGMTPTAEEL RHERLVGNGR SLLLEGTSIA RLLAQDWDVV CEYEEIVFSR TTPEQKLRIV
NEFRDRDNVV AVTGDGVNDA PALRAADVGV AVVTGSDVAI EAADLVLMDQ FDSIVEAIRL
GRLVFQNLQK VIAYLLPAGS WSEIWPVLVN VFFGVPLPLS VFLMIVICVF TDLFLSLSLI
MEKQEFDLLS LPPRNAKRDH LINLKIYAQA YLFTGFMETI CAHSMFFFYM WKYAGFPIHE
LFFLFEGYAE GYHGYTLDEL TSFNATGQCV YFVTLVFLQW GNILAVRNRR LSIAQADPIT
KKRRNPWLIA SAIISLAIAV FVTEVPGIQK LFGTASVPIE FWLLPVPLAL GILFADEIRK
LLLRLFPQGP ISKVAW
//
