UniProt: A0A0D2JLM6

Database: UniProt
Entry: A0A0D2JLM6_9EURO

LinkDB:  A0A0D2JLM6_9EURO 
Original site:  A0A0D2JLM6_9EURO

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Ontology (6)   
   GO (6)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (14)   
   Pfam (5)   
   PROSITE (2)   
All databases (30)   

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ID   A0A0D2JLM6_9EURO        Unreviewed;      1645 AA.
AC   A0A0D2JLM6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE            EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN   ORFNames=Z518_01452 {ECO:0000313|EMBL:KIX10370.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX10370.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX10370.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX10370.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362082}.
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DR   EMBL; KN847475; KIX10370.1; -; Genomic_DNA.
DR   RefSeq; XP_013277506.1; XM_013422052.1.
DR   STRING; 1442369.A0A0D2JLM6; -.
DR   GeneID; 25289523; -.
DR   HOGENOM; CLU_001828_3_1_1; -.
DR   OrthoDB; 6047at2759; -.
DR   Proteomes; UP000053617; 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; cd02440; AdoMet_MTases; 1.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; 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   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
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; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF02353; CMAS; 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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053617};
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        142..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        537..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1077..1096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1117..1136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1193..1211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   TRANSMEM        1231..1249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362082"
FT   DOMAIN          126..245
FT                   /note="P5B-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12409"
FT   DOMAIN          268..319
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
FT   DOMAIN          1077..1248
FT                   /note="Cation-transporting P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00689"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1645 AA;  186070 MW;  6C297801B6454F12 CRC64;
     MATDEPFSGP VSESVPSSVT GFAYQRPRQR QGSISSFTYF QEQEETPEYS DEEAVVDVSD
     EEDGHILGED RDLEAGDDSS LRRKSSSRYR TSSDRPLLRR HESARSDTQE HDHGGNFSQK
     LYIETEDLTM VIAGFFTSPV GYLIYVAICV LTAGIGYLVF RWIPRWRISL VGTPAALQKC
     SWVVVENQWG EFTVHHVSVE EYGHPMSTVF TRSGKEKLNG YRYDEDQELP FLRYLDYRYM
     RLLYHPIEDK FVLNNDWWDP QWTEVKALRR GLDSEERDPR DQVFGKNMIE IQQKTIPELL
     LDEAFHPFYI FQIASLILWS MDEYYYYAAA IFLISVFSIT TTVIETRSTM RRLREISRFE
     CDVRVLRNGF WRSALSGDLV PGDVYEVSDP SLSQLPCDSL LLAGDCIINE SMLTGESIPV
     SKVPITDEAL RYVDLGATSI HPSVARHFLF CGTKIIRARR PQDVDDDEAV ALAMVVRTGF
     NTTKGALVRS MLFPKPSGFK FYRDSFRYIS VMGVIAAVGF IASFINFVKL GLAWHLIIVR
     ALDLITIVVP PALPATLTIG TNFALSRLRK QQIFCISPQR VNVAGKLDVI CFDKTGTLTE
     DGLDVLGVRL VQHPEIRFGD ILEEAHELLP PSPYDRDPTV DYRVNKTMLY TMATCHSLRS
     VDDELIGDPL DLKMFQYTDW SFEEGSRHTS HFIEHGTNQT APSVARPPPG LEYDLEDSQG
     NSNPIRVEMG VLRSFEFVSH LRRASVIVRQ QGDPGASIYV KGAPEVMKDI CISSSIPDDF
     EDLLSYYTHK GFRVIACASK YISRLSWDEI ENMDRSEAES RLQLIGFIIF ENKLKAITTE
     IIEELNGARI RNVMCTGDNI LTAISVAREC GIIDRNEHCF VPHFAEGDKM NAKARLTWES
     VDNPIYQLDE NTLLPLPLLP EDDTAAPYDA IAMGDYTLAV TGDAFRWIID FGSTEVLQRM
     LVKGTVFARM SPDEKHELVE KMQSIDYCCG FCGDGANDCG ALKAADVGVS LSEAEASVAA
     PFTSHVFDIS CVPTLIKEGR AALVTSFCCF KYMSLYSAIQ FTSVSFLYAS ASNLGDFQFL
     FIDLALILPI AIFMGWTGAY PVLSKKHPTA NLVSRKVLTP LLGQIVLSIL VQLIAFETVQ
     DQPWYQPPQL DKDKSNVDNS QNTALFLVSC YQYTLSGVVL SSGPPFRQSM TTNAPFCVTI
     VVALLISLYM LLDPAKWLAD FMDLTEMSLD YELFLLALAA TGFAVAYLSE QYAFPSLAKF
     IGRLKLRLRP DRPKKRKRGL QLGRSSYHII YLTWAKLEHP PMDPTEYLID NGWLPSSVIR
     IGIRRQLAQR VRLIKSESLT KAYERKMSYI SALRGRPIAI DTDKANEQHY EVGTSVLRAY
     LGPRMKYSSC LYPTGRETLA QAEVAMLESY VRKADLRDGQ YILDLGCGWG SACLYLAELF
     PGSKVTAFSN SRTQRAYIEG QAKLKGLTNL TVITGDVVTY EFAGDSFDRV VSIELFEHMK
     NYKSLMAKIA RALRPGGKLF VHIFAHKESP YDFEEGWMST HFFTGGTMLS ADLLHFFQDD
     LTLREQWWVS GKHYAKTCED WLTMINGNKK EIWPGLEETY GKDKAAMWYY RWQVFYMACA
     ELFAFEGGDT WGVCHYLFEK DQSSK
//

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