ID A0A5N5P9W9_9PEZI Unreviewed; 1339 AA.
AC A0A5N5P9W9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=GE09DRAFT_608894 {ECO:0000313|EMBL:KAB5575903.1};
OS Coniochaeta sp. 2T2.1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5575903.1, ECO:0000313|Proteomes:UP000325492};
RN [1] {ECO:0000313|EMBL:KAB5575903.1, ECO:0000313|Proteomes:UP000325492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5575903.1,
RC ECO:0000313|Proteomes:UP000325492};
RX PubMed=31572496;
RA Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K.,
RA Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.;
RT "Genome expansion by allopolyploidization in the fungal strain Coniochaeta
RT 2T2.1 and its exceptional lignocellulolytic machinery.";
RL Biotechnol. Biofuels 12:229-229(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
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:KAB5575903.1}.
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DR EMBL; VSMA01000005; KAB5575903.1; -; Genomic_DNA.
DR Proteomes; UP000325492; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; P-type_ATPase_cation; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000325492};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 585..616
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1105..1123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1129..1148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1169..1191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1216..1234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1246..1265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1285..1306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 177..296
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 150582 MW; 506F66C8C2B9E22B CRC64;
MEGDTESVFS EATGRQTPRR GLYRLGSNQS RTSVFEDVEM ATDELYSGPM AESMPTSVSA
FTHRRARADS TASFAFYPDE EPDESPIIHD EYEESRGRLD VDDMRFGQEI PDEDDSTDLS
ADLERQAPEN DYVLHRRAST QSRGSVRSRL LRRDSGLSGG SEFGKARFSQ KTYMVNEDLY
IVIAGFKTSV VGMAVYVLLC IMTFGLAWLL FRWIPKWHVK LVGLASTLRD SEWVVIENSW
NEMAILDVRS KPYGRPMSTV FGAPDKITSY LFDDDPDPIL EDLRTLDYRY VRFFYHPAKD
KFQLCHGWKD PAWTDIRAVR SGVDSDEKSH RELVFGDNLI DIEQKSTFRI LVDEVFHPFY
VFQIASLILW SMDQYYYYAL AIFIMSVGSI VTTLVETKST MKRLKEISRF ECDVRVMRNG
FWRYVTSGDL VPGDIYEISD PNLGQFPADS LLLAGDCIVN ESMLTGESVP VSKTPATDES
IHYLDLTAST MMPEIAKHFL FCGTKIIRVR RPQEDPNQEA VALAMVVRTG FNTTKGSLVR
SMLFPKPSGF KFYRDSFRYI SVMGCVALLG FVASFVNFIR LRLAWHLIIV RALDLITIVV
PPALPATLTI GTNFALSRLK KKQIFCISPQ RVNVGGKIDI MCFDKTGTLT EEGLDVLGVR
VVSRENNRFS ETIEDPHMLV PHHSHGQNTP DDISTRKAAL YTMATCHSLR SVDGELMGDP
LDVKMFEFTR WSYEEGNAGG GNTNDEDQGT LQPSVARPPA DAKGDYEAGS PATGNDRPLE
LGVIKSFEFV SQLRRASVIV RAFDQRSGDI YVKGAPECMR DICRAESFPT DYDDLLAEYT
HKGYRVIGCA TRHIKKLSWV KAQKMSRPEV ESDLEFVGFI IFENKLKPTT TPVIEELLRS
NIPCVMVTGD NILTAISVAR ECGLMNKTAH CFIPHFAEGD SRDSNARLHW ESIDNGLYQL
DEHTLLPRAP PPEADASLPY DIANLRNYSV AVSGDVFRWV IDYASPEVVR RMLVTGRVFA
RMSPDEKHEL VEKLQSIDYC AGFCGDGAND CGALKAADVG ISLSEAEASV AAPFTSRVFD
IRCVPEVIRE GRAALVTSFS CFKYMSLYSA IQFTSVSFLY ASASNLGDFQ FLFIDLALIL
PIAIFMSWAG PFPELSHKRP TANLVARKVL TPLLGQMLIC IIIQAAAFIL VREQPWFIPP
KLKHDHSNIK NSENTALFLT SCFEYILSGV VLNAGRPFRQ KAIDNWPFVA MIGVALLVTL
DLVLAPAKWV SHLMQLTYIS WDFKLVIIGL GGLYFVLAYI GEHYIFQPVA RVIGRVVTAV
TKKTKKRKEY KLIQEKMLF
//
