ID S7ZQ06_PENO1 Unreviewed; 433 AA.
AC S7ZQ06;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN ORFNames=PDE_07444 {ECO:0000313|EMBL:EPS32484.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS32484.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS32484.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the GcvT family. CAF17 subfamily.
CC {ECO:0000256|ARBA:ARBA00007270}.
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DR EMBL; KB644414; EPS32484.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZQ06; -.
DR STRING; 933388.S7ZQ06; -.
DR eggNOG; KOG2929; Eukaryota.
DR HOGENOM; CLU_007884_7_0_1; -.
DR OrthoDB; 2874334at2759; -.
DR PhylomeDB; S7ZQ06; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR InterPro; IPR045179; YgfZ/GcvT.
DR InterPro; IPR017703; YgfZ/GcvT_CS.
DR NCBIfam; TIGR03317; ygfZ_signature; 1.
DR PANTHER; PTHR22602:SF0; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR22602; UNCHARACTERIZED; 1.
DR Pfam; PF01571; GCV_T; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 45..138
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT REGION 400..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 47752 MW; 85863EE7896422C3 CRC64;
MIRPRPSICG RCLARKRLFT TSSCKSEQIQ NAPHPPDVGY SRLTNRGLIS ITGADSTSFL
QGLITQNMLV ANDPNKRVRQ TGTYAAFLNS QGRILNDVFI YPLPSPNGDH AEREWLVEVD
QNELSTLLKH LKKHKLRAKL KLRALDMGER TVWSSWKNHS EPRWAAYNLE AETASPFASS
PNVVGCIDSR APGFGSRLVT PGSEDLRSHL PDESQLAGSE VDLDSYIVRR ILHGIAEGQG
EIIRESALPL ESNMDLGRAI DFRKGCYVGQ ELTIRTHHTG VVRKRILPVQ LYTGAAPSAS
GPIYDPSAQI SLPAQGSNIN KAGGRRGRSA GKFLSGVGNI GLALCRLEMM TDIALTGEGS
QYSPDNEFKV SWENQSDQQP QEVKLQAFVP AWTREFILAG SAKKTPARSG DVEGERARTL
VEQLEEEEAQ RRE
//
