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Conserved domains on  [gi|502714104|ref|WP_012949181|]
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glutaminyl-peptide cyclotransferase [Geodermatophilus obscurus]

Protein Classification

glutaminyl-peptide cyclotransferase( domain architecture ID 11467365)

glutaminyl-peptide cyclotransferase converts glutamine and N-terminal glutamyl residues in peptides to 5-oxoproline and 5-oxoproline residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3823 COG3823
Glutamine cyclotransferase [Posttranslational modification, protein turnover, chaperones];
38-273 4.68e-133

Glutamine cyclotransferase [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443035 [Multi-domain]  Cd Length: 237  Bit Score: 375.65  E-value: 4.68e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104  38 AITGGSAQSFPVLRPEVLAEVPHDPSAFTQGLELHEGTLYEGTGLEGKSQLRVLDPATGEVLRAQSLPGQLFGEGIAVAG 117
Cdd:COG3823    1 AIAVAAAAAPEVYTYEVVNTYPHDPTAFTQGLEFHDGTLYESTGLYGQSSLRKVDLETGEVLQRVDLPDRYFGEGITILG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104 118 DRIWQLTWQDGVVLEWDRATLTLRQQLPLDGEGWGLCHDGTRLVRSDGTDRLRFHDPVTFAETGSVTVTIDGEPVTQLNE 197
Cdd:COG3823   81 DKLYQLTWQSGVGFVYDLATFELLGTFPYPGEGWGLTNDGKRLIMSDGSSTLRFLDPETFAEVRTIQVTDNGRPVDRLNE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502714104 198 LECVDGQVWANVWPSDVLVRIDPARGRVTAAVDAAGLLDPEQRANADAVLNGIAALGD-DEYLLSGKLWPVSFRVRF 273
Cdd:COG3823  161 LEYVDGKIYANVWQTDRIVRIDPATGAVTGVIDLSGLLPEVKRTPGEDVLNGIAYDPEtDRLFVTGKLWPKLFEVRL 237
 
Name Accession Description Interval E-value
COG3823 COG3823
Glutamine cyclotransferase [Posttranslational modification, protein turnover, chaperones];
38-273 4.68e-133

Glutamine cyclotransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443035 [Multi-domain]  Cd Length: 237  Bit Score: 375.65  E-value: 4.68e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104  38 AITGGSAQSFPVLRPEVLAEVPHDPSAFTQGLELHEGTLYEGTGLEGKSQLRVLDPATGEVLRAQSLPGQLFGEGIAVAG 117
Cdd:COG3823    1 AIAVAAAAAPEVYTYEVVNTYPHDPTAFTQGLEFHDGTLYESTGLYGQSSLRKVDLETGEVLQRVDLPDRYFGEGITILG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104 118 DRIWQLTWQDGVVLEWDRATLTLRQQLPLDGEGWGLCHDGTRLVRSDGTDRLRFHDPVTFAETGSVTVTIDGEPVTQLNE 197
Cdd:COG3823   81 DKLYQLTWQSGVGFVYDLATFELLGTFPYPGEGWGLTNDGKRLIMSDGSSTLRFLDPETFAEVRTIQVTDNGRPVDRLNE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502714104 198 LECVDGQVWANVWPSDVLVRIDPARGRVTAAVDAAGLLDPEQRANADAVLNGIAALGD-DEYLLSGKLWPVSFRVRF 273
Cdd:COG3823  161 LEYVDGKIYANVWQTDRIVRIDPATGAVTGVIDLSGLLPEVKRTPGEDVLNGIAYDPEtDRLFVTGKLWPKLFEVRL 237
Glu_cyclase_2 pfam05096
Glutamine cyclotransferase; This family of enzymes EC:2.3.2.5 catalyze the cyclization of free ...
10-273 7.53e-128

Glutamine cyclotransferase; This family of enzymes EC:2.3.2.5 catalyze the cyclization of free L-glutamine and N-terminal glutaminyl residues in proteins to pyroglutamate (5-oxoproline) and pyroglutamyl residues respectively. This family includes plant and bacterial enzymes and seems unrelated to the mammalian enzymes.


Pssm-ID: 428301 [Multi-domain]  Cd Length: 249  Bit Score: 363.06  E-value: 7.53e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104   10 VLTTAVLCGCSSGDGAEAAAEGqpavreaitggsaqsfPVLRPEVLAEVPHDPSAFTQGLELHEGTLYEGTGLEGKSQLR 89
Cdd:pfam05096   1 LLLALALAGCAAAPAAAAAPPA----------------PVLGYEVVATYPHDPTAFTQGLEYDDGVLYESTGLYGRSSLR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104   90 VLDPATGEVLRAQSLPGQLFGEGIAVAGDRIWQLTWQDGVVLEWDRATLTLRQQLPLDGEGWGLCHDGTRLVRSDGTDRL 169
Cdd:pfam05096  65 KVDLATGEVLQSVPLPPRLFGEGITLLGDKLYQLTWKDGVGFVYDAATLEEIGRFSYEGEGWGLTTDGKRLIMSDGSSTL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104  170 RFHDPVTFAETGSVTVTIDGEPVTQLNELECVDGQVWANVWPSDVLVRIDPARGRVTAAVDAAGLLDPEQRANADAVLNG 249
Cdd:pfam05096 145 TFRDPKTFAETGTVQVTDDGRPVRNLNELEYVKGEIYANVWQTDRIARIDPATGRVTGWIDLSGLRNEAAPAGAEDVLNG 224
                         250       260
                  ....*....|....*....|....*
gi 502714104  250 IAAL-GDDEYLLSGKLWPVSFRVRF 273
Cdd:pfam05096 225 IAYDpATDRFFVTGKLWPKLFEVKL 249
 
Name Accession Description Interval E-value
COG3823 COG3823
Glutamine cyclotransferase [Posttranslational modification, protein turnover, chaperones];
38-273 4.68e-133

Glutamine cyclotransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443035 [Multi-domain]  Cd Length: 237  Bit Score: 375.65  E-value: 4.68e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104  38 AITGGSAQSFPVLRPEVLAEVPHDPSAFTQGLELHEGTLYEGTGLEGKSQLRVLDPATGEVLRAQSLPGQLFGEGIAVAG 117
Cdd:COG3823    1 AIAVAAAAAPEVYTYEVVNTYPHDPTAFTQGLEFHDGTLYESTGLYGQSSLRKVDLETGEVLQRVDLPDRYFGEGITILG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104 118 DRIWQLTWQDGVVLEWDRATLTLRQQLPLDGEGWGLCHDGTRLVRSDGTDRLRFHDPVTFAETGSVTVTIDGEPVTQLNE 197
Cdd:COG3823   81 DKLYQLTWQSGVGFVYDLATFELLGTFPYPGEGWGLTNDGKRLIMSDGSSTLRFLDPETFAEVRTIQVTDNGRPVDRLNE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502714104 198 LECVDGQVWANVWPSDVLVRIDPARGRVTAAVDAAGLLDPEQRANADAVLNGIAALGD-DEYLLSGKLWPVSFRVRF 273
Cdd:COG3823  161 LEYVDGKIYANVWQTDRIVRIDPATGAVTGVIDLSGLLPEVKRTPGEDVLNGIAYDPEtDRLFVTGKLWPKLFEVRL 237
Glu_cyclase_2 pfam05096
Glutamine cyclotransferase; This family of enzymes EC:2.3.2.5 catalyze the cyclization of free ...
10-273 7.53e-128

Glutamine cyclotransferase; This family of enzymes EC:2.3.2.5 catalyze the cyclization of free L-glutamine and N-terminal glutaminyl residues in proteins to pyroglutamate (5-oxoproline) and pyroglutamyl residues respectively. This family includes plant and bacterial enzymes and seems unrelated to the mammalian enzymes.


Pssm-ID: 428301 [Multi-domain]  Cd Length: 249  Bit Score: 363.06  E-value: 7.53e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104   10 VLTTAVLCGCSSGDGAEAAAEGqpavreaitggsaqsfPVLRPEVLAEVPHDPSAFTQGLELHEGTLYEGTGLEGKSQLR 89
Cdd:pfam05096   1 LLLALALAGCAAAPAAAAAPPA----------------PVLGYEVVATYPHDPTAFTQGLEYDDGVLYESTGLYGRSSLR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104   90 VLDPATGEVLRAQSLPGQLFGEGIAVAGDRIWQLTWQDGVVLEWDRATLTLRQQLPLDGEGWGLCHDGTRLVRSDGTDRL 169
Cdd:pfam05096  65 KVDLATGEVLQSVPLPPRLFGEGITLLGDKLYQLTWKDGVGFVYDAATLEEIGRFSYEGEGWGLTTDGKRLIMSDGSSTL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104  170 RFHDPVTFAETGSVTVTIDGEPVTQLNELECVDGQVWANVWPSDVLVRIDPARGRVTAAVDAAGLLDPEQRANADAVLNG 249
Cdd:pfam05096 145 TFRDPKTFAETGTVQVTDDGRPVRNLNELEYVKGEIYANVWQTDRIARIDPATGRVTGWIDLSGLRNEAAPAGAEDVLNG 224
                         250       260
                  ....*....|....*....|....*
gi 502714104  250 IAAL-GDDEYLLSGKLWPVSFRVRF 273
Cdd:pfam05096 225 IAYDpATDRFFVTGKLWPKLFEVKL 249
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
84-223 2.00e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 41.93  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104  84 GKSQLRVLDPATGEVLRAQSLPGQLFGEGIAVAGD-RIWQLTWQDGVVLEWDRATLTLRQ-QLPLDG---EGWGLCHDGT 158
Cdd:COG4257  121 GGNRIGRLDPATGEVTEFPLPTGGAGPYGIAVDPDgNLWVTDFGANAIGRIDPDTGTLTEyALPTPGagpRGLAVDPDGN 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502714104 159 RLVRSDGTDRLRFHDPVTFAETGSVTVTIDGEP----VTQlnelecvDGQVWANVWPSDVLVRIDPARG 223
Cdd:COG4257  201 LWVADTGSGRIGRFDPKTGTVTEYPLPGGGARPygvaVDG-------DGRVWFAESGANRIVRFDPDTE 262
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1-185 7.83e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 40.06  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104   1 MTHHRTLGVVLTTAVLCGCSSGDGAEAAAEGQPAVREAITGGSAQSFPVLRPEVLAEVPHDPSAFTQGLELHEGTLYEGT 80
Cdd:COG3391    7 LLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVAN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502714104  81 GLEGksQLRVLDPATGEVLRAQSLPGQLFGEGIAVAGDRIWQLTWQDGVVLEWDRATLTLRQQLPLDGEGWGLC--HDGT 158
Cdd:COG3391   87 SGSG--RVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAvdPDGK 164
                        170       180       190
                 ....*....|....*....|....*....|..
gi 502714104 159 RLVRSDGTDR-----LRFHDPVTFAETGSVTV 185
Cdd:COG3391  165 RLYVANSGSNtvsviVSVIDTATGKVVATIPV 196
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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