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Conserved domains on  [gi|480049618|gb|ENV88740|]
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hypothetical protein F939_01458 [Acinetobacter radioresistens DSM 6976 = NBRC 102413 = CIP 103788]

Protein Classification

class D beta-lactamase( domain architecture ID 10006473)

class D beta-lactamase hydrolyzes the amide bond of the beta-lactam ring via the formation of an acyl-enzyme covalent complex

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
1-273 2.36e-106

Beta-lactamase class D [Defense mechanisms];


:

Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 309.12  E-value: 2.36e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618   1 MNKYFTCYVVASLFLSGCTVQHNLINETPSQIVQghnqvihQYFDEKNTSGVLVIQTDKKINLYGNALSRANTEYVPAST 80
Cdd:COG2602    1 MKKLLLLLALLLLLACPANAAAAAANVIERPDLA-------KLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPAST 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  81 FKMLNALIGLENQK-TDINEIFKWKGEKRSFTAWEKDMTLGEAMKLSAVPVYQELARRIGLDLMQKEVERIDFGNAEIGQ 159
Cdd:COG2602   74 FKIPNSLIALETGViKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618 160 QVDNFWLIGPLKVTPIQEVEFVSQLAHTQLPFSEKVQANVKNMLLLEESNGYKIFGKTGWAMDIKPQVGWLTGWVEQPDG 239
Cdd:COG2602  154 GIDTFWLDGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDN 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 480049618 240 kIVAFALNMEMRSEMPASIRNELLMKSLKQLNII 273
Cdd:COG2602  234 -VYFFATNIDIPDEADLPKRKEITRKILKQLGLL 266
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
1-273 2.36e-106

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 309.12  E-value: 2.36e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618   1 MNKYFTCYVVASLFLSGCTVQHNLINETPSQIVQghnqvihQYFDEKNTSGVLVIQTDKKINLYGNALSRANTEYVPAST 80
Cdd:COG2602    1 MKKLLLLLALLLLLACPANAAAAAANVIERPDLA-------KLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPAST 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  81 FKMLNALIGLENQK-TDINEIFKWKGEKRSFTAWEKDMTLGEAMKLSAVPVYQELARRIGLDLMQKEVERIDFGNAEIGQ 159
Cdd:COG2602   74 FKIPNSLIALETGViKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618 160 QVDNFWLIGPLKVTPIQEVEFVSQLAHTQLPFSEKVQANVKNMLLLEESNGYKIFGKTGWAMDIKPQVGWLTGWVEQPDG 239
Cdd:COG2602  154 GIDTFWLDGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDN 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 480049618 240 kIVAFALNMEMRSEMPASIRNELLMKSLKQLNII 273
Cdd:COG2602  234 -VYFFATNIDIPDEADLPKRKEITRKILKQLGLL 266
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
48-249 2.71e-33

Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.


Pssm-ID: 425939 [Multi-domain]  Cd Length: 296  Bit Score: 122.91  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618   48 NTSGVLVI---QTDKKINLYGNALSRA-NTEYVPASTFKMLNALIGLENQKTDINEIFK----WKGEKRSFTAWEKDM-- 117
Cdd:pfam00905   9 KTGEVLAMvgkPSYDPNGFIGPLRNRAvTSRYEPGSTFKPFTALAALDNGVLKPDETIFdwpgKQQGGKSIGDWNQDQvg 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  118 --TLGEAMKLSAVPVYQELARRIGLDLMQKEVERIDFGNA-------EIGQQVDNFWLIGP-------LKVTPIQEVEFV 181
Cdd:pfam00905  89 igTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKtgiglpgENAGYLTPYWLEGAtasfgigLTITPLQQAQAY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  182 SQLAH----------------------TQLPFSEKVQANVKNMLLLEESN----------GYKIFGKTGWAMDIKPQVG- 228
Cdd:pfam00905 169 AAIANggklvpphlvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDgtgtgtaavpGYKVAGKTGTAQVAGPKGGg 248
                         250       260
                  ....*....|....*....|....*....
gi 480049618  229 --------WLTGWVEQpDGKIVAFALNME 249
Cdd:pfam00905 249 yydgaqigWFVGYAPA-DNPKYAFAVLID 276
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
75-185 4.47e-06

penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 274573 [Multi-domain]  Cd Length: 592  Bit Score: 47.52  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618   75 YVPASTFKMLNALIGLENQKTDINEIF----KWKGEKRSFTAWEK----DMTLGEAMKLSAVPVYQELARRIGLDLMQKE 146
Cdd:TIGR03423 304 YPPGSTFKPVVALAALEEGVITPETRIycpgYFQLGGRRFRCWKRgghgRVDLRKAIEESCDVYFYQLALRLGIDKIAEY 383
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480049618  147 VERIDFG-----------------------------------NAEIGQqvdNFWLigplkVTPIQEVEFVSQLA 185
Cdd:TIGR03423 384 AKRFGFGqktgidlpgeksglvpsrewkrkrfgqpwypgdtlNVSIGQ---GYVL-----VTPLQLAVATAALA 449
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
1-273 2.36e-106

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 309.12  E-value: 2.36e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618   1 MNKYFTCYVVASLFLSGCTVQHNLINETPSQIVQghnqvihQYFDEKNTSGVLVIQTDKKINLYGNALSRANTEYVPAST 80
Cdd:COG2602    1 MKKLLLLLALLLLLACPANAAAAAANVIERPDLA-------KLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPAST 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  81 FKMLNALIGLENQK-TDINEIFKWKGEKRSFTAWEKDMTLGEAMKLSAVPVYQELARRIGLDLMQKEVERIDFGNAEIGQ 159
Cdd:COG2602   74 FKIPNSLIALETGViKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618 160 QVDNFWLIGPLKVTPIQEVEFVSQLAHTQLPFSEKVQANVKNMLLLEESNGYKIFGKTGWAMDIKPQVGWLTGWVEQPDG 239
Cdd:COG2602  154 GIDTFWLDGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDN 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 480049618 240 kIVAFALNMEMRSEMPASIRNELLMKSLKQLNII 273
Cdd:COG2602  234 -VYFFATNIDIPDEADLPKRKEITRKILKQLGLL 266
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
48-249 2.71e-33

Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.


Pssm-ID: 425939 [Multi-domain]  Cd Length: 296  Bit Score: 122.91  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618   48 NTSGVLVI---QTDKKINLYGNALSRA-NTEYVPASTFKMLNALIGLENQKTDINEIFK----WKGEKRSFTAWEKDM-- 117
Cdd:pfam00905   9 KTGEVLAMvgkPSYDPNGFIGPLRNRAvTSRYEPGSTFKPFTALAALDNGVLKPDETIFdwpgKQQGGKSIGDWNQDQvg 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  118 --TLGEAMKLSAVPVYQELARRIGLDLMQKEVERIDFGNA-------EIGQQVDNFWLIGP-------LKVTPIQEVEFV 181
Cdd:pfam00905  89 igTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKtgiglpgENAGYLTPYWLEGAtasfgigLTITPLQQAQAY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  182 SQLAH----------------------TQLPFSEKVQANVKNMLLLEESN----------GYKIFGKTGWAMDIKPQVG- 228
Cdd:pfam00905 169 AAIANggklvpphlvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDgtgtgtaavpGYKVAGKTGTAQVAGPKGGg 248
                         250       260
                  ....*....|....*....|....*....
gi 480049618  229 --------WLTGWVEQpDGKIVAFALNME 249
Cdd:pfam00905 249 yydgaqigWFVGYAPA-DNPKYAFAVLID 276
FtsI COG0768
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell ...
75-153 4.22e-07

Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440531 [Multi-domain]  Cd Length: 568  Bit Score: 50.59  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618  75 YVPASTFKMLNALIGLENQKTDINEIF----KWKGEKRSFTAWEK----DMTLGEAMKLSAVPVYQELARRIGLDLMQKE 146
Cdd:COG0768  292 YEPGSTFKPFTAAAALEEGVITPDTTFdcpgYYRVGGRTIRDWDRgghgTLTLTEALAKSSNVGFYKLALRLGIDKLYDY 371

                 ....*..
gi 480049618 147 VERIDFG 153
Cdd:COG0768  372 LKKFGLG 378
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
75-185 4.47e-06

penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 274573 [Multi-domain]  Cd Length: 592  Bit Score: 47.52  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480049618   75 YVPASTFKMLNALIGLENQKTDINEIF----KWKGEKRSFTAWEK----DMTLGEAMKLSAVPVYQELARRIGLDLMQKE 146
Cdd:TIGR03423 304 YPPGSTFKPVVALAALEEGVITPETRIycpgYFQLGGRRFRCWKRgghgRVDLRKAIEESCDVYFYQLALRLGIDKIAEY 383
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480049618  147 VERIDFG-----------------------------------NAEIGQqvdNFWLigplkVTPIQEVEFVSQLA 185
Cdd:TIGR03423 384 AKRFGFGqktgidlpgeksglvpsrewkrkrfgqpwypgdtlNVSIGQ---GYVL-----VTPLQLAVATAALA 449
 
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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