ID U1HH31_ENDPU Unreviewed; 300 AA.
AC U1HH31;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Nucleotidyl transferase domain-containing protein {ECO:0000259|Pfam:PF00483};
GN ORFNames=EPUS_07290 {ECO:0000313|EMBL:ERF69475.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF69475.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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 ---------------------------------------------------------------------------
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; KE721405; ERF69475.1; -; Genomic_DNA.
DR RefSeq; XP_007804887.1; XM_007806696.1.
DR AlphaFoldDB; U1HH31; -.
DR GeneID; 19242175; -.
DR eggNOG; KOG1460; Eukaryota.
DR HOGENOM; CLU_029499_3_1_1; -.
DR OMA; SSMMKNG; -.
DR OrthoDB; 5486038at2759; -.
DR Proteomes; UP000019373; 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 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:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..71
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 300 AA; 32980 MW; FFA01782F1442F93 CRC64;
MLKLFEEKDA EAVILGTRVS NDAATNFGCI VSDGHTKRVL HYVEKPESHI SNLINCGVYL
FATECIFPSI RSAIKRRSDR PRIVSYPSSE NLESSFFRDQ DDDAEKNEVL RLEQDILSDL
ADSNRFFVHE TKDFWRQIKT AGSAVPANAL YLQKAFQSQS EELAAPSANI LPPVFIHPTA
TVDPTAKLGP NVSIGPKAVI GAGARVKESI VLEEAEIKHD ACVLYSIIGW NSRVGAWARV
EGSPTPVGNH TTSIVKNGVK VQSITILGKE CGVGDEVRVQ NCVCLPYKEL KRDVANEVIM
//