ID A0A135LGQ9_PENPA Unreviewed; 617 AA.
AC A0A135LGQ9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:KXG48171.1};
GN ORFNames=PGRI_020410 {ECO:0000313|EMBL:KXG48171.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG48171.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG48171.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG48171.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC glycosylation. Involved in cell cycle progression through cell-size
CC checkpoint. {ECO:0000256|ARBA:ARBA00024813}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274}.
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:KXG48171.1}.
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DR EMBL; LHQR01000065; KXG48171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LGQ9; -.
DR STRING; 5078.A0A135LGQ9; -.
DR OMA; MPVPNWW; -.
DR OrthoDB; 5486038at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR CDD; cd06428; M1P_guanylylT_A_like_N; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR22572:SF104; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE ALPHA; 1.
DR PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXG48171.1}.
FT DOMAIN 194..387
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 617 AA; 69260 MW; D090A3C26749B698 CRC64;
MKALLPHFSN KDHREGPFLY RLTDLHPSNI FVDSDWNVKF FNDLEWACSL PAETLRPPYW
LTGCSVDELT DDHLETFSKA HEEFVGVFEE EEKQFSPINN DHSYRTNLMR NGWKIGNLWY
FHALDSPKGL FNLFSQHIYP IFAPSSQSKD DFARVISDFW APDVGKVLAA KLRDKEEYEK
SLCRRFEDAV ASTKAVILVG GPSRGTRFRP LSLDVPKPLF EVAGHPIIHH CLKAVAKVPD
VREVILVGYY DESVFRDFIK DASKEFPQLR ILYLREYTAL GTAGGLYHFR DAILKGKPER
LLVLNADVCC SFPLGEMMRL FEEKDAEAVI LGTRVSNDTA TNFGCIVSDS HTKRVLHYVE
KPESHISNLI NCGVYLFATE CIFPAIRSAI KRRTTRPRLL SYPSSDNLES SFIATGDDED
AEKSEVLRLE QDILSDLADS NRFFVHETKD FWRQIKTAGS AVPANALYLQ KAFQAESPEL
TPPSATIVPP VYIHPTASVD PTAKLGPNVS IGPRVVVGAG ARIKDSIVLE DTEIRHDACV
MHSIIGWSSR VGAWARVEGT PIPVGSHSTS IVKQGIKVQS ITILGKECGV GDEVRVQNCV
CLPYKELKRD VCNEVIM
//
