ID U6M7U3_EIMMA Unreviewed; 1060 AA.
AC U6M7U3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
DE Flags: Fragment;
GN ORFNames=EMWEY_00029170 {ECO:0000313|EMBL:CDJ60292.1};
OS Eimeria maxima (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ60292.1};
RN [1] {ECO:0000313|EMBL:CDJ60292.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ60292.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ60292.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ60292.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG721678; CDJ60292.1; -; Genomic_DNA.
DR RefSeq; XP_013336942.1; XM_013481488.1.
DR AlphaFoldDB; U6M7U3; -.
DR EnsemblProtists; CDJ60292; CDJ60292; EMWEY_00029170.
DR GeneID; 25336903; -.
DR VEuPathDB; ToxoDB:EMWEY_00029170; -.
DR OMA; DTCVMLI; -.
DR OrthoDB; 5480493at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 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; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..71
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 81..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1060
FT /evidence="ECO:0000313|EMBL:CDJ60292.1"
SQ SEQUENCE 1060 AA; 112473 MW; 622BA3153EC503EF CRC64;
MPTVSVCELL VGSMTCAACK GAVQRSLIKC SGVIQAEVDL LRETARVAYH SDVISPAELC
KSVESLGFQA QVLQIFVASS NTSPPAERDS GRDSPHARTG AQWDEASQLP VPDGLESGAL
DYEEAGLRHH RHVATPQAHD FNELWTMSNA TLRLAIADSR GLAVESACST LKSSKGVHAC
EVALRGVEGP GTQQLLVTYK PQVKEAVLGH RRAMLSSLLL SILPSLVVIC LSTMARTHNL
PTALLRECLP GMRLSTLLLL ILTTPVQFYG GRSFHRAAFK FSMDLLVSLG SNLAFFYSAL
SCVQSAATTI WCRPLLSAAG ATAAPTHRGA AAPVGHRASP FYELLENAEP QVFFDTCVML
ICIVLLGKLL QLRAKARILE QLHSLHSLQV RTVHLVLRSP DTAVSRCLQH AAPQSSAGGV
KEGADTSSPS PSDLLKIADV VAADSPEVGP LRRPPLPVCW WQKVCAACGV QREGFPTAYN
PLTQPASWGL PDEGDDVVDG RKRSCCCRQK RQTSATIIDA QNATGSNPAE VIISAELLQA
GDVVRIPPQE VLPADGILLA PPVLHVDERL LSGEGRGVCK FAGQRVGDAS VLQTLLRLVQ
TGQQQHQPLQ KAAEMFAAYF IPIVLCITAG AVVTWAVRVF AAADTLPLSP LQQLRQRLRE
LELREGVSGT CPCAIGLAAP AAVAAATAAA AARGVFFKKG KALEAAANVN CLVVDKTGTL
TTGDLRVAAC VLHTKRLERL LLPALEGSKH SLQPSSKPSG ETCCSTSNAG KTTNGIKTAL
CSISSSSSRS TNTRESENTS SPSDSVIGSM TDEAIATLEE ATPPRADISA STTGRGSPSC
CRKKLQGSRG NLERPCLAPL AFCRLDFLWE ASLPTSQESS PRSSISYSST TCSSNGAAHA
SLERETSPKP CTWHSSTAKV YGGEALQVVS AESAATGCFL WALSCLEQGS SHSVGEALVH
AYEKWRRMQQ RGASLASCES WKCLGVWSAA AAAGCLPPPQ ACEKPQLLSR GIEGHFQTKG
NLRLRLRVAS ASPEDDGQNS NDDASSEGEQ LAPEEEIQLQ
//
