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Database: UniProt
Entry: A0A1Y2A3D5_9FUNG
LinkDB: A0A1Y2A3D5_9FUNG
Original site: A0A1Y2A3D5_9FUNG 
ID   A0A1Y2A3D5_9FUNG        Unreviewed;      1235 AA.
AC   A0A1Y2A3D5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=BCR33DRAFT_731196 {ECO:0000313|EMBL:ORY16515.1};
OS   Rhizoclosmatium globosum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC   Chytriomycetaceae; Rhizoclosmatium.
OX   NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY16515.1, ECO:0000313|Proteomes:UP000193642};
RN   [1] {ECO:0000313|EMBL:ORY16515.1, ECO:0000313|Proteomes:UP000193642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL800 {ECO:0000313|EMBL:ORY16515.1,
RC   ECO:0000313|Proteomes:UP000193642};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY16515.1}.
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DR   EMBL; MCGO01000297; ORY16515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2A3D5; -.
DR   STRING; 329046.A0A1Y2A3D5; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000193642; 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; 2.
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; 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; 2.
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:UP000193642};
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        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        843..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1052..1070
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1144..1167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1179..1201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..182
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1235 AA;  136277 MW;  610B331517950EF8 CRC64;
     MSDKEAQNND QIGAPFPHPP KEKSHLHAAH VPSTRSRAAS ITPESRNPPT LVTPTATAAG
     ANQAPPTPVE EHHPLGEILQ KDDSKDAKDV GALKDASVTI DEHHLPIEAL VSRYKTSVNV
     KSPRDSTGLT HTLAKELLYQ HGKNILPRPK KESAFYRFFM CITNMFNLLL LFGGTGYLVL
     YSFDPVENFS NVYIGSVLLC VAFVNAFIEF YELTKVSKIV ESFTNMIPRE ARCIRASMLQ
     RINVAELVPG DVILLEAGDK IPADAIVFHS HELRVDNSSL TGESESVERS PVLVGVLAAD
     AGALEAKNVV FGGTVVSNGE AYVIIIRTGA HTVLGKIANL TNQSHGGKKS KKRSPLSSEI
     QRFCKLISLL ASGTAIFFFL ISLARGSEFN SSFQFAIGIL VAWIPQGLPV TVTMLLAVAG
     ERMAKRQVLI KDLHGVETLG AITMLATDKT GTLTMNQMKV SRVWTNMVNM YAGDGEAPVG
     ERLLKLDVSG VAQILHMAAT CTRARFDSTE GKISERKIIG DATDTGLLQF AASRLANVEK
     LFTQYPKIFE IPFSSETKTH LSIHRKGHPD GTLTMHVKGA PERVLASCAT ILMNGKAEPL
     TDFHRTQFKE TYEKMAKRGE RVIAFAQYWL PGRKFPDNYR FSLEKTNFPT TGLTFVGLVS
     VEDPPKHGVR EAIGSIRQAG IQVIMVTGDH PLTAAAIARR INLLTQPTLE EVAKECGKPP
     SKIPDSEVHA VVVNGELLAS FTDDDWDRVL SKQEVIFART SPKQKLEIVK RAQSLGHIVG
     VTGDGVNDAA ALRHADLGIA MNKTGSDVSK EAAGMILMDD NFASTVVGIL EGRLIFVNMK
     KSIQYFLTHI MSEVFPYLAN VVIPIPLALT AIQILVVDLG FELFITLSFA WEPPEDSEAL
     LRLGPRQPVT AESIQLMKNK RQAKKDVLEA QANAIHDAAE RRSSIGNQLD LEKQKTSITP
     KYQLTSADED DYQNLLENSN DEIYGDLNEA QKAALKLKGR WWRHISELKA MMTDIRYWKA
     QQKEWKALVA IKSGERLVDA EVLSWSYLEA GLMEASICIG TFFAVLYWGW DMTPTDAKRI
     QRSRGFKPHT ANHTLESGII ITGEDQLEAL EQAQSAFYLS ILIVQLWNLF ACKTRLRLPT
     QKIFVANVTT LIAVAVGVTF AMLIVYTPFM NAVFMTSNAL NPVFLLIPLS AGSLVFIYSI
     FRRALLRKWW PQTFAKDFGA KVRLNMAKSV DELNS
//
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