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Database: UniProt
Entry: U1HH31_ENDPU
LinkDB: U1HH31_ENDPU
Original site: U1HH31_ENDPU 
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}.
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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
//
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