ID   A0A2N3NKF6_9PEZI        Unreviewed;       776 AA.
AC   A0A2N3NKF6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PKS12909.1};
GN   ORFNames=jhhlp_000249 {ECO:0000313|EMBL:PKS12909.1};
OS   Lomentospora prolificans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX   NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS12909.1, ECO:0000313|Proteomes:UP000233524};
RN   [1] {ECO:0000313|EMBL:PKS12909.1, ECO:0000313|Proteomes:UP000233524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS12909.1,
RC   ECO:0000313|Proteomes:UP000233524};
RX   PubMed=28963165; DOI=10.1534/g3.117.300107;
RA   Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA   Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT   "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT   prolificans (Formerly Scedosporium prolificans).";
RL   G3 (Bethesda) 7:3831-3836(2017).
CC   -!- FUNCTION: Involved in the partitioning of the mitochondrial organelle
CC       and mitochondrial DNA (mtDNA) inheritance.
CC       {ECO:0000256|ARBA:ARBA00003757}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
CC   -!- SIMILARITY: Belongs to the misato family.
CC       {ECO:0000256|ARBA:ARBA00008507}.
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:PKS12909.1}.
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DR   EMBL; NLAX01000002; PKS12909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3NKF6; -.
DR   STRING; 41688.A0A2N3NKF6; -.
DR   VEuPathDB; FungiDB:jhhlp_000249; -.
DR   InParanoid; A0A2N3NKF6; -.
DR   OrthoDB; 345661at2759; -.
DR   Proteomes; UP000233524; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR029209; DML1/Misato_tubulin.
DR   InterPro; IPR019605; Misato_II_tubulin-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF10644; Misat_Tub_SegII; 1.
DR   Pfam; PF14881; Tubulin_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233524}.
FT   DOMAIN          494..605
FT                   /note="Misato Segment II tubulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF10644"
FT   DOMAIN          610..765
FT                   /note="DML1/Misato tubulin"
FT                   /evidence="ECO:0000259|Pfam:PF14881"
SQ   SEQUENCE   776 AA;  84765 MW;  805A1C4C192346DC CRC64;
     MGAYSLPDGT LASHQRTSQI IRALETPQTL EKQVACPSGS SRPVVVSAQG HRLFLEDGRE
     ILDACGGAAV SCLGYGDREV LETLANQAAE VPYVPWAFFD THSTRQLSDW LIKSTGRAMG
     KVYIMSSGSD AVEGALKLAR EYFVWKDQPK RVNFIARHGS YHGTTLGALS LSGHVARRAP
     FEDLLSRHVH RVSSCNAYRQ RRAGESDAAF CARKARELED VFIKLGPETV AAFVVEPVVG
     AALGCVPAVP GYLKAMKAVC DKYGALFVLD EIMSGMGRTG TLHAWEQEGV VPDIQTIGKG
     LGAGYQPVSA VLAGRRIVEE MEKAGTAFNN GHTYQDFPVA AATALKVQEI IQERNLLQNV
     VAQGEVLGRK LQERLGHHPN VGDIRGRGLF WGVEFVKDRT TKEPFDESLR VSKRIHDAAL
     GEPYNIMVYH GQGCAGGWKG DHIMLCPAYD VSAEEVEVMV DRVSGAVEEV FASLVKLEKL
     VRYIAAYTGR AMVREIITLQ LGELSNYVAT HFWNAQESYF TYGDEEKSPV DHNVHWRQGI
     GADGSETFLP RALIYDFRSN YGPLGRSNPL YENEDDDPNR HLWHGNAAIH KQPPIPKSPY
     HAALEAGTVP ALTTASVRYW SDFTRPYFHP RSIVQLSDLE GTPAQSAGGG TGGAPTLDSF
     EHGKELFKAV DAADDVLDGQ LRAFVEECDL LQGMQVVVGG EDGWSGFGAG LLERVRDEYG
     KSCVWVWMPD GGAGGNKKEK QLLRLINKAK SLTDSLPLAS TLIPSPYPRA SDPLTP
//