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Database: UniProt
Entry: A0A093JDW6_FULGA
LinkDB: A0A093JDW6_FULGA
Original site: A0A093JDW6_FULGA 
ID   A0A093JDW6_FULGA        Unreviewed;       417 AA.
AC   A0A093JDW6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Calcium-binding mitochondrial carrier protein SCaMC-1 {ECO:0000313|EMBL:KFW10052.1};
DE   Flags: Fragment;
GN   ORFNames=N327_01894 {ECO:0000313|EMBL:KFW10052.1};
OS   Fulmarus glacialis (Northern fulmar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC   Fulmarus.
OX   NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW10052.1, ECO:0000313|Proteomes:UP000053806};
RN   [1] {ECO:0000313|EMBL:KFW10052.1, ECO:0000313|Proteomes:UP000053806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW10052.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-AMP(in) + ADP(out) + H(+)(out) = 3'-AMP(out) + ADP(in) +
CC         H(+)(in); Xref=Rhea:RHEA:73679, ChEBI:CHEBI:15378, ChEBI:CHEBI:60880,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036310};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-AMP(out) + phosphate(in) = 3'-AMP(in) + phosphate(out);
CC         Xref=Rhea:RHEA:73691, ChEBI:CHEBI:43474, ChEBI:CHEBI:60880;
CC         Evidence={ECO:0000256|ARBA:ARBA00036289};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + ATP(in) + H(+)(out) + Mg(2+)(in) = ADP(in) +
CC         ATP(out) + H(+)(in) + Mg(2+)(out); Xref=Rhea:RHEA:73659,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036612};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) +
CC         phosphate(out); Xref=Rhea:RHEA:65844, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036415};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out);
CC         Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + dAMP(in) + H(+)(out) = ADP(in) + dAMP(out) +
CC         H(+)(in); Xref=Rhea:RHEA:73675, ChEBI:CHEBI:15378, ChEBI:CHEBI:58245,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036316};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + diphosphate(in) = ADP(in) + diphosphate(out);
CC         Xref=Rhea:RHEA:73671, ChEBI:CHEBI:33019, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036630};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP(out) + phosphate(in) = AMP(in) + phosphate(out);
CC         Xref=Rhea:RHEA:70259, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00036908};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP(out) + 2 H(+)(out) + phosphate(in) = ATP(in) + 2 H(+)(in)
CC         + phosphate(out); Xref=Rhea:RHEA:72035, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000256|ARBA:ARBA00036970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in)
CC         + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000256|ARBA:ARBA00034993};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dADP(out) + H(+)(out) + phosphate(in) = dADP(in) + H(+)(in) +
CC         phosphate(out); Xref=Rhea:RHEA:73695, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57667;
CC         Evidence={ECO:0000256|ARBA:ARBA00036766};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dAMP(out) + phosphate(in) = dAMP(in) + phosphate(out);
CC         Xref=Rhea:RHEA:73687, ChEBI:CHEBI:43474, ChEBI:CHEBI:58245;
CC         Evidence={ECO:0000256|ARBA:ARBA00036282};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
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DR   EMBL; KK607613; KFW10052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093JDW6; -.
DR   Proteomes; UP000053806; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd00051; EFh; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR002167; GDC-like.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR24089:SF262; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-1; 1.
DR   PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00928; GRAVESDC.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053806};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   DOMAIN          28..63
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          64..99
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          134..220
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          228..313
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          325..413
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW10052.1"
FT   NON_TER         417
FT                   /evidence="ECO:0000313|EMBL:KFW10052.1"
SQ   SEQUENCE   417 AA;  46311 MW;  830290A1F42013E3 CRC64;
     SQQKIFKAGD TNQDGQLDFE EFMRYLKDHE KKMKLAFKSL DKNNDGKIEA SEVVQSLKIL
     GISISEKQAE KILQSIDADG TMTVDWNEWR DHFMFNPATD IEEIIRYWKH STVLDIGDSL
     TVPDEFTEEE KKTGQWWKQL LAGGVAGAVS RTGTAPLDRL KVMMQVHGSK SNKMNIASSF
     KQMLKEGGVR SLWRGNGVNV VKIAPETAIK FWAYEQYKKI LTKNDGKLGT VERFISGSLA
     GATAQTSIYP MEVLKTRLAV GKTGQYTGMF DCAKKILKRE GVKAFYKGYI PNILGIIPYA
     GIDLAVYELL KSTWLEHYAS SSANPGVFVL LGCGTVSSTC GQLASYPLAL IRTRMQAQAS
     VEGAPQLNMV GLFQRIIAVE GIRGLYRGIA PNFMKVLPAV SISYVVYEKM KQNLGIA
//
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