ID A0A0C2D6D4_9BILA Unreviewed; 1202 AA.
AC A0A0C2D6D4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE Flags: Fragment;
GN ORFNames=ANCDUO_04501 {ECO:0000313|EMBL:KIH65178.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH65178.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH65178.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH65178.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN727669; KIH65178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2D6D4; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 2.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24093:SF253; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 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 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 955..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1055
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1067..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..114
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 314..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIH65178.1"
SQ SEQUENCE 1202 AA; 131879 MW; 531BD7B99106569F CRC64;
LDYLSKNRSF EPQDFYGLFQ LSTEHDGVDG LCQKLKVDPV RGLPNNAADL DKRRAAFGAN
TIPPAKSKSF ARLVFDACRA DRAFENKRRE SQSLQDPTLI ILVVAGFVNL ALSFYEPEMQ
APVDEDAVTS AALVAGAYLN NTVGFDLLNF TLPLNTTAEP QGEGHGTAWI EGVAILLCVV
VVVLVTAIND YSKERQFRSL QEKIETGQKF SVIRDGEAID VPVSDLVVGD IARVKYGDLI
PADGFLLQGN DLKIDESSLT GESDHIKKTP ESDPVLLSGT YAMEGSGKMV LTAVGVNSQT
GIIMTLLGAG KPGVGGVDDD STSTSSSSSS SSSSSSSSSS SGSSHSSKSS DDDDGLSAKS
VLQSKLSRLA LQIIYCGTTV AAVALIVLVT RFCIEHYVRD GIPFSIADIQ MFVKFFIIAV
TILVISIPEG LPLAIALALT YSVRKMMFDN NLVRHLDACE TMGNATSICS DKTGTLTTNK
MTVVDSYING NHYEGQDNQP SGAALPGNTA HLITEAISVY TFNSSRKCMM TVIRLVENGV
DVGYRVYCKG ASEIILGRCA YLIGSDGKPH TFSADRLKEI TATIISQMAN NGLRTICVAY
KDYIRKNVRE ADRTEIAFEK DEDIDWSDED EMYKNFVGIA ICGIQDPVRP EVPAAIENAY
NSMIVEPTKV GEQVQQLGNK TECGLLGFVQ KLGGDYATIR KKFPEESFVK DPVRPEVPAA
IEKCKRAGIT VRMVTGDNIN TARAIAMSCK ILEPGEDFLA LEGKEFNERI REPDGKVSQA
KLDQIWPRLR VLARAQPADK YTLVKGIIDS KVTPQREIVA VTGDGTNDGP ALKKADVGFA
MGIAGTDVAK EASDIILTDD NFTSIVKAVM WGRNVYDSIS KFLQFQLTVN VVAVLTAFVG
AVTVSDSPLK AVHMLWINLI MDTLASLALA TEVPTDELLN RKPYGRKKSL ISRTMVKNIL
CHALYQLLIL FTIFYYGDRI FHIKSGLYAP LFAPPSQHFT IVFNAFVMMT LFNEINARKV
HGERNVFKGL ASNRVFCVIW LSTFIGQILI TQFGGAWFST APLNGKQWIA CLALGLSTLV
WGQVVATIPS KKLPKTWKVG RGEVEPSKIH INGDYNVRAR SRALTVRRTG KSLWMRGMFL
MGQHLRVLRA FRMRDKNFGK TAPTMTAEAA ERWRSSYRKY RHQKHQEKKN LPGSYHIGRY
PM
//