ID A0A177C337_9PLEO Unreviewed; 701 AA.
AC A0A177C337;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=tRNA(His) guanylyltransferase {ECO:0000256|ARBA:ARBA00015443};
DE EC=2.7.7.79 {ECO:0000256|ARBA:ARBA00012511};
DE AltName: Full=tRNA-histidine guanylyltransferase {ECO:0000256|ARBA:ARBA00032480};
GN ORFNames=CC84DRAFT_279923 {ECO:0000313|EMBL:OAG01198.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG01198.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG01198.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG01198.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010113}.
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DR EMBL; KV441558; OAG01198.1; -; Genomic_DNA.
DR RefSeq; XP_018031563.1; XM_018185742.1.
DR AlphaFoldDB; A0A177C337; -.
DR STRING; 1460663.A0A177C337; -.
DR GeneID; 28769228; -.
DR InParanoid; A0A177C337; -.
DR OrthoDB; 239198at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 3.30.70.3000; -; 2.
DR InterPro; IPR025845; Thg1_C_dom.
DR InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR InterPro; IPR007537; tRNAHis_GuaTrfase_Thg1.
DR InterPro; IPR038469; tRNAHis_GuaTrfase_Thg1_sf.
DR PANTHER; PTHR12729:SF6; TRNA(HIS) GUANYLYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR12729; UNCHARACTERIZED; 1.
DR Pfam; PF04446; Thg1; 1.
DR Pfam; PF14413; Thg1C; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 6..136
FT /note="tRNAHis guanylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04446"
FT DOMAIN 140..225
FT /note="Thg1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14413"
FT REGION 220..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 76238 MW; 2E822C5257B5A096 CRC64;
MANSKYEYVR NFEQPDNLLP NTFVVVRIDG RGFTKLTTKY NFVKPNDRRA LDLMNGAAEA
VMKDLPDLVL AYGQSDEFSF VFHKDCMLFE RRASKLVTTI VSTFTANYVL GWAKYFPDHP
LTAPLPSFDG RAVCYPSNTN LRDYLSWRQA DCHINNLYNT TFWALVQQGG LENRVAEKEL
SGTVSGDKNE ILFKRFGINY NNEPDIFKKG SVLYRDFFPT STQSSPTPAK SPIIHHPTPQ
SIARPMSQPL ELTHHDLFRS SPASGTSTAT ASTPRGPTFL STSTTPSPPP SPPTIPMPLF
TEAFKDQTSV GYPSTFSLST FSPLSPSANA SAPRHAALQP IPLPPPTLKP STRPPLSLNP
PNSITHANTS PMPSPYVPSS AAYPSPTISN SKKPVKPISH SASASLSLHP KPLAPSYRPT
PKRSPSLSVL ESGLARGPPQ IPQRFSSIPP EQPPRKLSLP TQKSHALLRQ EASDLAVANP
ANTSSYRGAG RPRTPPSQLM TMKELPSPPT GEYDIGGVRG AVMGSSPQPW SQSPPPPTRG
SAISAGGSSG HGEMENLIVN PVIPPSPPGA SLRSHSRAGS SYSKSYSFPA PPSSGPPTSS
GEQFASFDWG NKEEVEVPPE VPEKSKGRQI KGKGEKGKKV LGIEDEGWKE GLDGRPKTMS
KTQKEKERKK RGKARIVTEH VDIIGDSFWE RRPWILSGRV G
//
