ID A0A1V6UMZ2_9EURO Unreviewed; 692 AA.
AC A0A1V6UMZ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN ORFNames=PENCOP_c006G01238 {ECO:0000313|EMBL:OQE39794.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE39794.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE39794.1}.
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DR EMBL; MDDG01000006; OQE39794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6UMZ2; -.
DR STRING; 36646.A0A1V6UMZ2; -.
DR OrthoDB; 1220009at2759; -.
DR Proteomes; UP000191500; 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; 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; 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; PF13405; EF-hand_6; 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:UP000191500};
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 96..131
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 168..203
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 340..430
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 439..527
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 537..625
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 1..27
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 692 AA; 77029 MW; 7C80E9331F5D6CB6 CRC64;
MASVTEAVKE SLLGSTESPQ LSHQSRSNFV RHAQKDENGE LFMNEENFIN AVAPKQEDYH
KIKREQYGIL FNVADRRRAG KLNITDWASF ENLLAKPDAE YEIAFRLFDF DGTGSVKFEA
VQGLYNMNKS ADSIPFDWNS EWASLYGGRS KSRHDMTYPQ FAQMLRGLQG ERIRQAFHIF
DKDGDGFIQP EDFQRIILET SKHKLSDHVL ENLPTLCNIS TSNRISYANV RAFQNVMREM
DIIDMVVREA TKKSVDGKIT RSDFLNEAAR VTRFSQFTPM EADILFHFAG LDAPSGRLSQ
KDFAKVIDAS WRIPVIAANQ ALSAGQEVAE KTKSLLHGVL ESAHHFALGS IAGAFGAFMV
YPIDLVKTRL QNQRSSRPGE RLYNNSLDCA RKVIRNEGFT GLYSGVIPQL IGVAPEKAIK
LTVNDLVREY FTDKETHRIK YAQEVLAGGT AGACQVVFTN PLEIVKIRLQ VQGEIAKNVE
GVPRRSALWI VKNLGLMGLY KGASACLLRD VPFSAIYFPT YAHLKSDFFG ETATNKLGVL
QLLTAGAIAG MPAAYLTTPC DVIKTRLQVE ARKGDTKYNG LRHCAATVWK EEGLAAFFKG
GPARIMRSSP QFGFTLAAYE VLQKTFPMPG EGDAITPTGH VEPSVGGQGA KAPLPYLRSR
NALKIILDLD QNIGRVQVPR PENWPKFLQS SK
//
