ID A0A094EL12_9PEZI Unreviewed; 999 AA.
AC A0A094EL12;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0000259|PROSITE:PS50048};
GN ORFNames=V499_01635 {ECO:0000313|EMBL:KFY79371.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY79371.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY79371.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY79371.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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:KFY79371.1}.
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; JPKB01000214; KFY79371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EL12; -.
DR HOGENOM; CLU_010001_1_0_1; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR31845; FINGER DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR31845:SF33; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR Pfam; PF00153; Mito_carr; 3.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS50920; SOLCAR; 3.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REPEAT 1..54
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 68..155
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 179..265
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT DOMAIN 301..333
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 398..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 108818 MW; 0EDC3E211BBC662A CRC64;
MQVLSERKPM LHTLYMFASR NGIHSLWTGI SASILRQSTY STTRFGLYNY LTSVMKRAYD
VRDLSAASTI VCAGAAGGVA GMLGNPTEIV LVRMCADGAK APVDRYGYAH ALDGFVRIGR
EEGMKAFSKG LGPNIVRSVL MNRSVSTYPP SSLSSGAYRF SYTSAKAKLL SASWLKMNDG
IMLHITASIA AGTVATTVCA PADVLKSRMQ NAAAVGGKSA GLVHIVAESM RKEGPRFLMK
GWLPAWLRLT DNCPRTSDPD RNRLWIVISP ATEGAAAANG MDERSESAEA ASNSGTTKQA
ACLSCRRSKI RCHRGAGDPK CRRCNQANSE CIIPKYHPGR QKGVKNKRTG LEKAVYRIGQ
AIARTKANGG ELEDEQAAVN LQHLLSSTVG LLPRSTISQE PAQSPQMQAP TSMPTHHGIT
VTTSPGYPTH NNVRASPGYP LHRSRNNNYS VDDAENPLQL LASASDMAVS PPETLANTQA
PASSGPFCPA KEDEDKDLQT FFGRFIPNLD VSEDIDPIDM GFITNGETVA LFNLIYPTRD
GDLILSYTLP TSALFLPSTD ALSKRLSVHC KKLAYYVMEK RYRSPEIVLA FIINVPWMAP
GKHWADDETC AYMAMALSVA MDLSLNKLIV PAPGFPQREI PDHVPKSDCI TAKKALLLDG
FDDVDPYSSW GQRLLRRRER IWLSLFVLDR GVCLARGRTF TVHMTPLVES CDQWHISDMA
DTWDQSIISS AVLRRDLVTL IADIKSTCDV VADGVSIVHV LKDMIEGFFD RWFSVWAVAV
GSKHHVLPPY VEILVSHTRL STYSSVINHP TAPVEVKRFF RAAGLSSALN VMRAAVQGEG
RLKSMPNNTA IMISFAACFA LSISTMTEGN TLSLAPSIRI LVEEAAGMLE RIGCSPSHRN
GTSSLYGRHL RKIIRNNFAA PDRDVPAAAL PIGQDVAVGG YDAQNGQSLG GFAEFQPVLF
SAMSNDQVTA AIDSASQELD VWLSTFQMDD NAGLDWLDW
//