ID A0A1F8AGZ4_9EURO Unreviewed; 695 AA.
AC A0A1F8AGZ4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Mitochondrial carrier protein {ECO:0000313|EMBL:OGM50568.1};
GN ORFNames=ABOM_000755 {ECO:0000313|EMBL:OGM50568.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM50568.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM50568.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- SUBUNIT: Homodimer (via N-terminus). {ECO:0000256|ARBA:ARBA00038674}.
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}.
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:OGM50568.1}.
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DR EMBL; LYCR01000002; OGM50568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8AGZ4; -.
DR STRING; 109264.A0A1F8AGZ4; -.
DR OrthoDB; 1220009at2759; -.
DR Proteomes; UP000179179; 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:0043490; P:malate-aspartate shuttle; IEA:UniProt.
DR CDD; cd00051; EFh; 1.
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; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45678:SF9; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN ARALAR1; 1.
DR PANTHER; PTHR45678; MITOCHONDRIAL 2-OXODICARBOXYLATE CARRIER 1-RELATED; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF00153; Mito_carr; 3.
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}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 97..132
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 169..204
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 342..432
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 441..529
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 539..627
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 77527 MW; DD3C0BE9516BAA77 CRC64;
MTVKDAVKES LVGSSTDQSQ PSHQAKTNFL RHARKDEDTG DLYMTEDDFV NAIAPKHEDY
HKIKREHYGI LFKVADRKQT GKLSLSDWAT FENLLTKPDA EYEIAFRLFD TDGTGAVKWD
TFKNLYNVNK DKDSIPFDWN SEWASLYTGR TKSRHDMTYP QFAQMLRGLQ GERIRQAFHI
FDKDGDGYIE PEDFQRIILE TSKHKLSDYV LEHLPSLCNI STGTKISYAT VRAFQNIMRE
MDMIDVIVRE ATQKSDDGKI TRADFLNEAA RITRFSLFTP MEADILFHFA GLDAPSGRLA
QKDFAKVIDA SWRMPLAIAG QAAVSTAHKA ADKTKSVLYS VLESAHHFAL GSLAGAFGAF
MVYPIDLVKT RMQNQRSTRV GERLYNNSLD CARKVIRNEG FTGLYSGVVP QLIGVAPEKA
IKLTVNDLVR GHFTNKENGK IWYPHEILAG GAAGGCQVIF TNPLEIVKIR LQVQGEIAKN
VEGAPRRSAL WIVKNLGLVG LYKGASACLL RDVPFSAIYF PTYAHLKSDF FGESPTHKLG
VVQLLTAGAI AGMPAAYLTT PCDVIKTRLQ VEARKGEVGY TGLRHCAQTI LKEEGFKAFF
KGGPARIIRS SPQFGFTLAS YELLQKWLPM PGQEEATPSG QIEPGVGLQG AKAPLPYLRS
RNALKLILDL DENIGRVKIP QADKWPKFMQ TPSTN
//
