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Database: UniProt
Entry: A0A0A0BAD0_9CELL
LinkDB: A0A0A0BAD0_9CELL
Original site: A0A0A0BAD0_9CELL 
ID   A0A0A0BAD0_9CELL        Unreviewed;       724 AA.
AC   A0A0A0BAD0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=3'-phosphate/5'-hydroxy nucleic acid ligase {ECO:0000256|ARBA:ARBA00012726};
DE            EC=6.5.1.8 {ECO:0000256|ARBA:ARBA00012726};
GN   ORFNames=Q760_09665 {ECO:0000313|EMBL:KGM03062.1};
OS   Cellulomonas cellasea DSM 20118.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM03062.1, ECO:0000313|Proteomes:UP000029833};
RN   [1] {ECO:0000313|EMBL:KGM03062.1, ECO:0000313|Proteomes:UP000029833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM03062.1,
RC   ECO:0000313|Proteomes:UP000029833};
RA   Wang G., Zhuang W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end
CC         dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-
CC         ribonucleotide-RNA + diphosphate + GMP + H(+); Xref=Rhea:RHEA:68080,
CC         Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83064,
CC         ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00029282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-
CC         ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA +
CC         diphosphate + GMP; Xref=Rhea:RHEA:68076, Rhea:RHEA-COMP:10463,
CC         Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58115, ChEBI:CHEBI:83062,
CC         ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=6.5.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00029311};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601233-3};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR601233-3};
CC   -!- SIMILARITY: Belongs to the RtcB family.
CC       {ECO:0000256|ARBA:ARBA00008071}.
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:KGM03062.1}.
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DR   EMBL; AXNT01000026; KGM03062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0BAD0; -.
DR   STRING; 1408250.Q760_09665; -.
DR   Proteomes; UP000029833; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008452; F:RNA ligase activity; IEA:InterPro.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR   Gene3D; 3.90.1860.10; tRNA-splicing ligase RtcB; 2.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR001233; RtcB.
DR   InterPro; IPR036025; RtcB-like_sf.
DR   PANTHER; PTHR43749; RNA-SPLICING LIGASE RTCB; 1.
DR   PANTHER; PTHR43749:SF2; RNA-SPLICING LIGASE RTCB; 1.
DR   Pfam; PF14528; LAGLIDADG_3; 1.
DR   Pfam; PF01139; RtcB; 2.
DR   PRINTS; PR00379; INTEIN.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF55608; Homing endonucleases; 1.
DR   SUPFAM; SSF103365; Hypothetical protein PH1602; 2.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR601233-
KW   2}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR601233-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601233-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR601233-2};
KW   Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029833};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          390..503
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000259|PROSITE:PS50819"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601233-3"
FT   BINDING         173..177
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601233-2"
FT   BINDING         174
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601233-3"
FT   BINDING         191
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601233-3"
SQ   SEQUENCE   724 AA;  78965 MW;  C5891D329BCE9510 CRC64;
     MMSSPFPVAL AGTAAPTLMW AHEHEVEPQA LQQLRNIASL PWVEGLRVMP DVHLGKGATV
     GSVIAMRDAV SPNAVGVDIG CGMIGVRTSL TAADLPDDLH AIRTRIEQAV PVGFHAHDEP
     VDLRRLRPVN GSAGRERLKG ADAFWDRFGG LHRTVQQLEA RARKQLGTLG GGNHFIELCL
     DESDQVWLQL HSGSRNIGKE LAERHVAIAK TLEHNQRIVD RELAVFLAGT PQMDAYLNDL
     WWAQEYAARS RAVMMALVVQ AVRDSFPERE ITFDEGVNCF AGETRVLTGA GIFPIAELAG
     GIHELLTTGG RWVKAPIMSF GKQRVYEVTV GRYGEEKVIR ATGNHRWLLR AKVAHARDEA
     TTQDLRVGDR LAYAFPARVS GMKVDRASVA RGFVFGDGSL CGKQTRARAI FCGDKDESLL
     PYFEGLTTNC VRDYGSVKVL NGFPAEWKTA PVATSSHPDI VYGWLAGYFA ADGDVDKSGR
     PSLSSSRRDH LEAVKALATS IGVGTYGIRT RVRRGIDGRD SELHVMGFMR SDLDLDFFVQ
     DEHRARFATG RGAVERKGWT VRSVEITDDV EEVYCAVVPE TEAFTLEDNI LTRNCHHNYV
     KTEQIDGAEL IVTRKGAIRA GSGEMGLIPG SMGTGSYVVR GLGNPASFQS ASHGAGRRMS
     RTAAKKRFTV EDLAAQTAGV ECRKDAGVVD EIPGAYKDLE SVIAAQTDLV EVVARLRTIV
     CVKG
//
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