ID X0CX88_FUSOX Unreviewed; 1112 AA.
AC X0CX88;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=FOQG_01556 {ECO:0000313|EMBL:EXK98761.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK98761.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK98761.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK98761.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR EMBL; JH658363; EXK98761.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CX88; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR Proteomes; UP000030663; 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:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF32; COPPER RESISTANCE P-TYPE ATPASE (EUROFUNG); 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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; SSF55008; HMA, heavy metal-associated domain; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 368..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 412..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 457..479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 499..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 655..678
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 698..725
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1040..1061
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1073..1094
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 191..256
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 142..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 119691 MW; AB1AF8DB2594ADA6 CRC64;
MASTETVVTT SYLLGNLHCP TCVTLIRSLL HDAFGDNVLW VSPNLVTSVV TVEHKENSSA
SVASMHRVLQ DAGFEVCGLN TTARTANDLY RTSQVDGESS RVAERSDGWL DSFFHFWRPQ
VSPLAIEAAR AAHLENCEAC KSEKIPGKSP SDDKSGLVRA SSIVSDTPTR RSSLPYPLQK
VVTEASPTPS WRVTLSVGGM TCAVCVNTIT QEMEKYPWVT KVAVNLVSNS ATIEYTDGDR
AQDIVDAIED LGYDATIDEV VNLQEKRVSA EEREVEVSVD GIFCQRCPER IVTTLKGLAP
GRLQIFQEPT VQNPVLRLRY TPDAPRFTIR QILQAIEAAD ESLKASIYHP PTLEERSRII
RAKHQQALLY RVILTIVFAV PTFVLGIVYM SLLPDSNHGK MYLMKPWVSG LSRLDICLFA
LATPVYFLAA DVFHVRAVKE VRTMWRRGSR VPLMQRFYRF GSMNMLVSLG TSIAYFSSVA
QMIAAGASRR EHHESGAEMY FDSVVFLTLF LLLGRLIEAY SKSKTGDAVE MLGKLRPTTA
LLLEKDKAGG QITSTVPVDQ IDSGDIIRVP HGASPAADGI LVSGGTNFDE SSLTGESRLI
KKTEGDQIFA GTINKAAAVT MRVTGASGQS MLDQIVHVVR EGQTKRAPIE QIADLLTTYF
VPVITLIAVL TWIIWMVLGF SGAVPDHGES SSGGWVVFAL QFAIAVFVVA CPCGLALAAP
TAIFVGGGIA AKHGILAKGG GEAFEKASKI DCVVFDKTGT LTEGGQPKIT DSVLFPDTSS
TEEERGAFLS ALKAVEESSS HPIAKAIVSF CGDAPASNVQ NLEELAGRGM KASFKGVDNQ
EMGMIIGNEL LMREFSVNLS PHISSLLDTW KSEAKSVAII ATKASSADTW TLAAALSISD
PIRRETVPVI RALTSRGIQV WMLSGDNVTT ARAVAQRVGI PSSNVLAEVL PSDKAAKISS
LQASVHARGS ITKRATIAMV GDGINDSPAL TTADVGIAIG TGSDVAISSA AFVLATSQLT
AVVTLLDLSR AVFRRIRVNF AWALVYNMLA VPVAAGCLYP IETSSGERVR LDPVWAALAM
ALSSISVVLS SLSLRTRVPG VGFRSRKVDM EE
//
