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Database: UniProt
Entry: A0A1X2I6A0_9FUNG
LinkDB: A0A1X2I6A0_9FUNG
Original site: A0A1X2I6A0_9FUNG 
ID   A0A1X2I6A0_9FUNG        Unreviewed;      1128 AA.
AC   A0A1X2I6A0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=BCR42DRAFT_359172 {ECO:0000313|EMBL:ORZ09281.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ09281.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ09281.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ09281.1,
RC   ECO:0000313|Proteomes:UP000193560};
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:ORZ09281.1}.
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DR   EMBL; MCGE01000028; ORZ09281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2I6A0; -.
DR   STRING; 90262.A0A1X2I6A0; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000193560; 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   Pfam; PF08282; Hydrolase_3; 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:UP000193560};
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        131..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        370..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        882..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        910..932
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        953..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1014..1037
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1058..1077
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1089..1107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..155
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1128 AA;  124639 MW;  83549731759D3131 CRC64;
     MTLYSQDDGK PQIEFSTPPH PDVLPSTNKK QPSRRRSSKI QGIIAFRTLS LTVSETQVDK
     KSKQLGKKKK DYNLAEDLSN ATYHKLGVAE VLQQYNTCME KGLDQEQALK RVELYGKNAI
     SPPPNNWPRK IFGYFFGGFC GLLWFASIIC WISWQPLGNP NPSPVNLALA VILMMVVFLQ
     AFFNAWQDWS TSQVMHSINN MLPSKCQVVR QDGKTLTLDA IQLVPGDIVH IKMGDKIPAD
     IRLLQVSDDL KFDRSVLTGE SDAIPGSIDA TNDNVLESHN MAMMGTHCLN GNGSGVVISI
     GDKTMMGRIA RLSLDDPAKR TILQTEILRF VLIIASLSIS VGSICLITWA AWLRVDYPDY
     LSVSNALIDV ISVIVAFVPE GMPVAVTLCL TLIARRMQKA NVLCKVLTTV ETLGSVNVLC
     SDKTGTLTEN KMYVSDISIS DHQITTPISR DIVVKADSQQ QLLRCQVLQM QLSSALCNGA
     QYDMSDVDKK DVAARAIIGD ATDCAILRYA AAVNPDLTVE SIRSQADPIF EIPFNSKNKW
     MLTIHRSTTT GLAKQFSTPS QEVAPSDWIL LCKGAPDVLI DRCDSIMQPD GSLEPLTEKR
     REALVNVQTQ WANDGKRVLM VARRILSASL LPSESSASSS KFAGWATQMN QGLTIVGLIA
     IVDPPRPESA ETVRVCRNAG IRFYMVTGDF PLTAAAIARQ IGIFTTTHLH DINNLDPNKE
     ISTIAPYVSQ KHKMTITNDS GSSTLGEVSA EDTCDKEAYQ STTSNKTADS TALLLSGVDL
     LTLNDNQWEQ VCQYEEIVFA RTSPDQKLRI IKEFQRRDNV VGMTGDGVND SPALRAADVG
     IAMGNGSDVA IEAADMVLLD KFSSILVAIE NGRLVFDNLK KVIIYLLPAG SWSELFPVLV
     NIFLGSPQTL SSFQMIVICV LTDLMPSMAI MMEKPEAGLL HRAPRRPKHD RLVNSRLLLQ
     AYGFIGLMEM LSSMFMFYYF LSTHGLPPAT VFLSFSNFNS PQGYMGYTSD EVTALLNTAQ
     SIYFVNLVIC QWGNVLSSRT RRLPLTRANP LWGPNKNLYL FAAMLGSLAI TLIILYVPVF
     NIYLGTSPIP IHFWFIPFGW AATIMVADEL RKLLLTRFPH SLFGYLAW
//
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