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Database: UniProt
Entry: C0NM44_AJECG
LinkDB: C0NM44_AJECG
Original site: C0NM44_AJECG 
ID   C0NM44_AJECG            Unreviewed;       612 AA.
AC   C0NM44;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=tRNA pseudouridine synthase {ECO:0000313|EMBL:EEH07695.1};
GN   ORFNames=HCBG_04574 {ECO:0000313|EMBL:EEH07695.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH07695.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000256|ARBA:ARBA00009375}.
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DR   EMBL; GG663367; EEH07695.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NM44; -.
DR   STRING; 447093.C0NM44; -.
DR   VEuPathDB; FungiDB:I7I50_11172; -.
DR   HOGENOM; CLU_021971_1_0_1; -.
DR   InParanoid; C0NM44; -.
DR   OrthoDB; 12038at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:InterPro.
DR   CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR   Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR   Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR001406; PsdUridine_synth_TruA.
DR   InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR   InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR   InterPro; IPR041708; PUS1/PUS2-like.
DR   InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   NCBIfam; TIGR00071; hisT_truA; 1.
DR   PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11142:SF4; PSEUDOURIDYLATE SYNTHASE 1 HOMOLOG; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          399..504
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
SQ   SEQUENCE   612 AA;  68519 MW;  D50ABBE5F983AC2C CRC64;
     MDTQQQSPNP NRPSNSAPDQ QAMFPAGYSQ EQEVSQPRPD GDAKRKKEPN SGGGGRGGRK
     NKRKDLGRKA WSRQIPDKRA RAEASQESKR RKLENGEKAL PIYATEFSKE DIEADQRRPK
     KKVAVMLGYS GSGYKGMQLS ETEKTIEGDL FTAFVAAGAI SKANATDPKK SSLVRCARTD
     KGVHAAGNVV SLKLIVEDPN VVQKINGHLS PQIRVWGIEI TNKSFSSYHL CDSRIYEYLI
     PSHCFLPPHP STHLGQQLVE IAEQENDLEG YQQRQAEVAH YWEEVDEKYI KPILERLPEV
     TRNRVKQALI IKSGTDPADN STSQGEQDQL DPSDEQDGEV TSKEASASTN ENKDLSSGDE
     QTVHTTNEAI RIIRAAYLGA KKAYRIPRER MDRINDALGM YVGTRNFHNY TIQKSFRDAS
     AKRHIKSFKI SREPLIINGT EWLSLKVHGQ SFMMHQIRKM VAMAALIVRC GCDIKLVPET
     YGDQKIAIPK APGLGLLLER PIFDSYNKRT VVEYGKNPID FSKHEKEIEE FKQREIYERI
     FREEEESNSF GNFFNHIDTF QDNAFLFVTS RGIPASKPSG GSAKAPMSGK AALKEVESES
     DDDLVNGGEE GG
//
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