ID A0A179HK98_PURLI Unreviewed; 1207 AA.
AC A0A179HK98;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Vacuolar protein sorting-associated protein 45 {ECO:0000313|EMBL:OAQ90707.1};
GN ORFNames=VFPFJ_04866 {ECO:0000313|EMBL:OAQ90707.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ90707.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ90707.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ90707.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC {ECO:0000256|ARBA:ARBA00002739}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the MnmG family.
CC {ECO:0000256|ARBA:ARBA00007653}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
CC {ECO:0000256|ARBA:ARBA00009884}.
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:OAQ90707.1}.
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DR EMBL; LSBI01000004; OAQ90707.1; -; Genomic_DNA.
DR RefSeq; XP_018179426.1; XM_018321946.1.
DR AlphaFoldDB; A0A179HK98; -.
DR STRING; 33203.A0A179HK98; -.
DR GeneID; 28886995; -.
DR KEGG; plj:VFPFJ_04866; -.
DR OMA; MHAILRQ; -.
DR OrthoDB; 49088at2759; -.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR Pfam; PF00995; Sec1; 1.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000078340}.
FT DOMAIN 1118..1189
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 1207 AA; 132491 MW; 1FC4E030A8706313 CRC64;
MDVSQAVAGY IAKIVSPPGE ASSSKMKILL LDRETVSIVS TAVTQSALLN HEVYLIDRLD
NAGREKMRHL RCLCLVRPSP ETVQLLVDEL RDPKYGEYHL YFTNVAKKSS LERLAEADDH
EIVKVVQEHF ADYTVINPDL FALGVSLPQW RIWSGTPDTW NPDALQRCAE GLIAVLLSLK
KKPLVRYQKN SSLAKKLASE VRYLMSQEDQ LFDFRKVDTP PILLVLDRRE DPVTPLLTQW
TYQAMVHNLL GIQNGRVDLS QVPDIRPELR EIVLSQDQDP FFKKNMFLNF GDLGGTIKEY
VEQYQSKTKS NTNIDSISDM KRFIEEYPEF RKLSGNVSKH VTLVSELSRR VADERLLENI
QNLIQTPTVT PEAKVGLVAL YALRYHKQPS NALPMLADLL VAAGGVTPRQ ADAVKAVLSY
HTSLPSSQSQ GGISELFESA GIFSGASSRF KGLKGVENVY TQHTTLLEST LQSLIKGKLR
EQQYPFVDGG GSTRDKPQDI IVFMVGGATY EEAKMIAGVN ASTPGVRVVL GGTSIHNAAT
FLEEASPQTG DNWVFVAGPV VVDRHFGRVP FDVVVIGGGH AGAEACAAAA RAGARTALVT
PKMDNLGTCS CNPSFGGIGK GTIIREIDAL DGLAGRIIDQ AGVQFHMLNR RKGPAVWGPR
AQIDRGLYKK HMRDELSLYP NLSIILGSVS DIVVSTHDSP PVGGAQKSIA GVRLESGRVL
PTTKVIITTG TFLGGEIHIG LQSYPAGRLG EAATFGLSQS LHDAGFRLGR LKTGTPPRLD
RGTINFDALQ KQLGDEPPTP FSYLNDSVSV RDQLTCSITY TNDATHSVVR QNLDKTIHIR
ETIKGPRYCP SLESKIIRFA DKERHIVWLE PEGFDNPVVY PNGLSMTIPA EAQEQALRTI
EGLEHVKMLQ PGYGVEYDYV DPRGLKASLE TKAITGLYLA GQINGTTGYE EAAGQGIVAG
INAGRSALGL PAMSLSRSDG YIGIMIDDLI TKGVTEPYRM FTSRSEFRLG ARADNADLRL
TEKGRTWGVV SDKRWQAFRD ERQQIADLTA SLATLSLTPE QWLQSGFRLK KGSRRRSGMD
MLRLSNSSSR VELDHLSAAC PEIMAYPARI RNRVAVEASY APYVKMQAAE RGQLTGDEAL
RIPLNLDYDA IPGLALSEKE VLKATRPETL AQARRVEGVT PSGSLRLLAH VRRQPTEGRP
EASPDLP
//
