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Conserved domains on  [gi|1733464609|gb|QEL30835|]
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murein transglycosylase [Enterobacter hormaechei subsp. xiangfangensis]

Protein Classification

murein transglycosylase( domain architecture ID 11485431)

soluble lytic murein transglycosylase is a murein-degrading enzyme that catalyzes cleavage of glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-645 0e+00

lytic murein transglycosylase; Provisional


:

Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 1331.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609   1 MEKAKRVVWRLLAASVCVMAVSQAVHADSLDEQRSRYAQIKQAWDNRQMDTVQALMPTLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619    1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609  81 PTVTVNNFIQANPTLPPARTLKSRFVNELARREDWRGLLAFSPDKPGATEAQCNYYYAKWATGQQEEAWAGAKELWLTGK 160
Cdd:PRK11619   81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 161 SQPNACDPLFSAWRASGQQDPLSYLERIRLAMKAGNTRLVTVLAGQMPADYQTIASAVIGLANDPNTVLTFARTTGATDF 240
Cdd:PRK11619  161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 241 TRQMAAVAFASVARDDVENARLMIPQLVQAQQLNDDQTQELRDIVAWRLMGTDVTDEQARWRDDAVMRSNSVSLVERRVR 320
Cdd:PRK11619  241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 321 MALGTGDRRGLNTWLARLPMDAKEKDEWRYWQADLLLERGRDDEAKEILHSLMQQRGFYPMAAAQRLGEEYTLKIDKAPA 400
Cdd:PRK11619  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 401 nANPALTQGPEMARVRELMYWNLDNTARSEWANLVTSRTTEEKAQLARYAFDNRWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619  401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 481 KDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPGSSSPSQLLDPETNINIGTSY 560
Cdd:PRK11619  480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 561 LQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKDTLMSDAE 640
Cdd:PRK11619  560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                  ....*
gi 1733464609 641 WQRRY 645
Cdd:PRK11619  640 WQRRY 644
 
Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-645 0e+00

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 1331.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609   1 MEKAKRVVWRLLAASVCVMAVSQAVHADSLDEQRSRYAQIKQAWDNRQMDTVQALMPTLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619    1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609  81 PTVTVNNFIQANPTLPPARTLKSRFVNELARREDWRGLLAFSPDKPGATEAQCNYYYAKWATGQQEEAWAGAKELWLTGK 160
Cdd:PRK11619   81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 161 SQPNACDPLFSAWRASGQQDPLSYLERIRLAMKAGNTRLVTVLAGQMPADYQTIASAVIGLANDPNTVLTFARTTGATDF 240
Cdd:PRK11619  161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 241 TRQMAAVAFASVARDDVENARLMIPQLVQAQQLNDDQTQELRDIVAWRLMGTDVTDEQARWRDDAVMRSNSVSLVERRVR 320
Cdd:PRK11619  241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 321 MALGTGDRRGLNTWLARLPMDAKEKDEWRYWQADLLLERGRDDEAKEILHSLMQQRGFYPMAAAQRLGEEYTLKIDKAPA 400
Cdd:PRK11619  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 401 nANPALTQGPEMARVRELMYWNLDNTARSEWANLVTSRTTEEKAQLARYAFDNRWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619  401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 481 KDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPGSSSPSQLLDPETNINIGTSY 560
Cdd:PRK11619  480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 561 LQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKDTLMSDAE 640
Cdd:PRK11619  560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                  ....*
gi 1733464609 641 WQRRY 645
Cdd:PRK11619  640 WQRRY 644
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 475-627 5.26e-69

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 221.20  E-value: 5.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 475 RFPLAYKDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPgSSSPSQLLDPETNI 554
Cdd:cd13401     1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLP-YYSPRDLFDPEYNI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733464609 555 NIGTSYLQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSaGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:cd13401    80 RLGSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRR-GDLDPDLWIETIPFSETRNYVKRVLENYVVYRA 151
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 398-627 1.57e-52

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 180.96  E-value: 1.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 398 APANANPALTQGPEMARVRELMYWNLDNTARSEWANLVTSRTTEEKAQLARYAFDNRWWDLSVQA----TIAGKLWDHLE 473
Cdd:COG0741    17 AAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAiaalAAELLALAALL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 474 ERFPLAYKDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPgsSSPSQLLDPETN 553
Cdd:COG0741    97 LRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG--PSPDDLFDPETN 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733464609 554 INIGTSYLQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRidavaFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:COG0741   175 IRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGEIIPYAETRNYVKKVLANYAIYRA 243
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 484-600 1.72e-39

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 140.52  E-value: 1.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 484 FDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIpgssSPSQLLDPETNINIGTSYLQY 563
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNP----GVDDLFDPEKNIKAGTKYLKE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1733464609 564 VYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRIDAV 600
Cdd:pfam01464  77 LYKQYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKL 113
 
Name Accession Description Interval E-value
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 1-645 0e+00

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 1331.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609   1 MEKAKRVVWRLLAASVCVMAVSQAVHADSLDEQRSRYAQIKQAWDNRQMDTVQALMPTLKDYPLYPYLEYRQITDDLMNQ 80
Cdd:PRK11619    1 MEKAKMGKWRLLAAGVCLLTVSGVARADSLDEQRQRYQQIKQAWDNRQMDVVEQLMPTLKDYPLYPYLEYRQLTQDLMNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609  81 PTVTVNNFIQANPTLPPARTLKSRFVNELARREDWRGLLAFSPDKPGATEAQCNYYYAKWATGQQEEAWAGAKELWLTGK 160
Cdd:PRK11619   81 PAVQVTNFIRANPTLPPARSLQSRFVNELARREDWRGLLAFSPEKPKPVEARCNYYYAKWATGQQQEAWQGAKELWLTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 161 SQPNACDPLFSAWRASGQQDPLSYLERIRLAMKAGNTRLVTVLAGQMPADYQTIASAVIGLANDPNTVLTFARTTGATDF 240
Cdd:PRK11619  161 SLPNACDKLFSVWQQSGKQDPLAYLERIRLAMKAGNTGLVTYLAKQLPADYQTIASALIKLQNDPNTVETFARTTGPTDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 241 TRQMAAVAFASVARDDVENARLMIPQLVQAQQLNDDQTQELRDIVAWRLMGTDVTDEQARWRDDAVMRSNSVSLVERRVR 320
Cdd:PRK11619  241 TRQMAAVAFASVARQDAENARLMIPSLVRAQKLNEDQRQELRDIVAWRLMGNDVTDEQAKWRDDVIMRSQSTSLLERRVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 321 MALGTGDRRGLNTWLARLPMDAKEKDEWRYWQADLLLERGRDDEAKEILHSLMQQRGFYPMAAAQRLGEEYTLKIDKAPA 400
Cdd:PRK11619  321 MALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLEQGRKAEAEEILRQLMQQRGFYPMVAAQRLGEEYPLKIDKAPK 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 401 nANPALTQGPEMARVRELMYWNLDNTARSEWANLVTSRTTEEKAQLARYAFDNRWWDLSVQATIAGKLWDHLEERFPLAY 480
Cdd:PRK11619  401 -PDSALTQGPEMARVRELMYWNMDNTARSEWANLVASRSKTEQAQLARYAFNQQWWDLSVQATIAGKLWDHLEERFPLAW 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 481 KDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPGSSSPSQLLDPETNINIGTSY 560
Cdd:PRK11619  480 NDEFRRYTSGKGIPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTATHTVKMFSIPGYSSSSQLLDPETNINIGTSY 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 561 LQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKDTLMSDAE 640
Cdd:PRK11619  560 LEYVYQQFGNNRILASAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGQKPTLLSDAE 639


                  ....*
gi 1733464609 641 WQRRY 645
Cdd:PRK11619  640 WQRRY 644
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 475-627 5.26e-69

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 221.20  E-value: 5.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 475 RFPLAYKDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPgSSSPSQLLDPETNI 554
Cdd:cd13401     1 RYPLPYRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLP-YYSPRDLFDPEYNI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733464609 555 NIGTSYLQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSaGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:cd13401    80 RLGSAYLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRR-GDLDPDLWIETIPFSETRNYVKRVLENYVVYRA 151
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 398-627 1.57e-52

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 180.96  E-value: 1.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 398 APANANPALTQGPEMARVRELMYWNLDNTARSEWANLVTSRTTEEKAQLARYAFDNRWWDLSVQA----TIAGKLWDHLE 473
Cdd:COG0741    17 AAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAiaalAAELLALAALL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 474 ERFPLAYKDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPgsSSPSQLLDPETN 553
Cdd:COG0741    97 LRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLG--PSPDDLFDPETN 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733464609 554 INIGTSYLQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRidavaFVESIPFSETRGYVKNVLAYDAYYRY 627
Cdd:COG0741   175 IRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGEIIPYAETRNYVKKVLANYAIYRA 243
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 477-621 1.43e-44

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 155.75  E-value: 1.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 477 PLAYKDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPgSSSPSQLLDPETNINI 556
Cdd:cd16896     1 PLKYREYIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAEWIAEKLGLE-DFSEDDLYDPETNIRL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733464609 557 GTSYLQYVYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRIDAVAfVESIPFSETRGYVKNVLAY 621
Cdd:cd16896    80 GTWYLSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKT-LDQIPFPETRHYVKKVLKN 143
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 484-600 1.72e-39

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 140.52  E-value: 1.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 484 FDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIpgssSPSQLLDPETNINIGTSYLQY 563
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNP----GVDDLFDPEKNIKAGTKYLKE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1733464609 564 VYQQFGNNRIFASAAYNAGPGRVRTWLGNSAGRIDAV 600
Cdd:pfam01464  77 LYKQYGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKL 113
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 499-621 4.16e-37

lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381594 [Multi-domain]  Cd Length: 111  Bit Score: 133.88  E-value: 4.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 499 MAIARQESAWNPKVRSPVGASGLMQIMPGTATHtvkmfniPGSSSPSQLLDPETNINIGTSYLQYVYQQFGNNRIFASAA 578
Cdd:cd00254     5 LAVIRVESGFNPRAVSPAGARGLMQLMPGTARD-------LGRRGVDDLFDPEENIRAGARYLRELLDRFGGDLELALAA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1733464609 579 YNAGPGRVRTWLGNsagridavafvESIPFSETRGYVKNVLAY 621
Cdd:cd00254    78 YNAGPGAVDRWGGG-----------EVPPYKETRNYVQRVLAY 109
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 471-627 1.00e-27

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 116.31  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 471 HLEERFPlAYKDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTAthtvKMFNIpgssspSQLLDP 550
Cdd:COG4623   256 RIEGRLP-PYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATA----KELGV------DDRLDP 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 551 ETNINIGTSYLQYVYQQFG-----NNRI-FASAAYNAGPGRVR--------------TWLGN--SAGRIDAVAFVESipf 608
Cdd:COG4623   325 EQSIRAGAKYLRWLYDRFPeaidePDRWwFALAAYNAGPGHVQdarrlakkqgldpdRWFDVekSQPKYYDTGYARG--- 401

                         170       180
                  ....*....|....*....|
gi 1733464609 609 SETRGYVKNVLA-YDAYYRY 627
Cdd:COG4623   402 RETVNYVPNIRAyYDIYKRL 421
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 492-621 1.41e-26

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 106.10  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 492 DIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTV--KMFNIPGSSSPSQLLDPETNINIGTSY---LQYVYQ 566
Cdd:cd16893    11 GVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVyrLLGGKGGLPSKSYLFDPENNIDIGTAYlhiLQNRYL 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 567 QFGNN---RIFAS-AAYNAGPGRV-RTWLGN---SAGRI---DAVAFVESI----PFSETRGYVKNVLAY 621
Cdd:cd16893    91 KGIKNpksREYCAiAAYNGGAGNVlRTFSSDrkkAISKInrlSPDEVYQHLtkklPAAETRNYLKKVLKA 160
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 499-624 1.32e-25

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 103.38  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 499 MAIARQESAWNPKVRSPVGASGLMQIMPGTAthtvKMFNIpgssspSQLLDPETNINIGTSYLQYVYQQF-----GNNRI 573
Cdd:cd13403    16 AAQAYQESRFNPNARSPAGARGLMQLMPSTA----RELGV------NDRLDPEQNIHAGAKYLRYLRDRFppdidEPDRL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733464609 574 -FASAAYNAGPGRVR--------------TWLGN-------SAGRIDAVAFVESIPFSETRGYVKNVLA-YDAY 624
Cdd:cd13403    86 kFALAAYNAGPGHVRdarrlakkyglnpnVWFDNvevlpllKSPYYDPVVKYGYARGRETVNYVRNIRKyYDAY 159
SLT_L pfam14718
Soluble lytic murein transglycosylase L domain; Soluble lytic murein transglycosylase (SLT) ...
 408-472 8.04e-22

Soluble lytic murein transglycosylase L domain; Soluble lytic murein transglycosylase (SLT) consists of three domains, an N-terminal U domain, an L domain (linker domain) and a C-terminal domain (C). The L domain may be involved in the interaction of the enzyme with peptidoglycan.


Pssm-ID: 434154 [Multi-domain]  Cd Length: 68  Bit Score: 89.20  E-value: 8.04e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733464609 408 QGPEMARVRELMYWNLDNTARSEWANLVTSRTTEEKAQLARYAFDNRWWDLSVQATIAGKLWDHL 472
Cdd:pfam14718   4 QLPALARIRELLALGRDAEARREWRHLLARLDKEQQLALARLALDWGWHDLAIQATIQAKLWDDL 68
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 501-621 1.54e-16

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 76.40  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 501 IARQESAWNPKVRSPVGASGLMQIMPGTAthtvKMFNIPGSSSPSQLLDPETNINIGTSYLQYVYQQFGNNRIfASAAYN 580
Cdd:cd16894    13 LALVESGFNPDAVSSAGAAGLWQFMPATA----REYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFGDWLL-ALAAYN 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1733464609 581 AGPGRVRTWLGNSAGRIDAVAFVESIPFsETRGYVKNVLAY 621
Cdd:cd16894    88 AGEGRVRRAIKRAGTDKWEDYYRLYLPA-ETRRYVPKFLAA 127
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
470-586 2.65e-12

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 68.54  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 470 DHLEERfplAYKDL-FDRYTSGK-DIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTV-KMFNIPGSSSPSQ 546
Cdd:PRK11671  183 NHLDKR---AHKYLpMVRKASRKyGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVfRMKGKSGQPSRSY 259

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1733464609 547 LLDPETNINIGTSY---LQYVYQQFGNN---RIFAS-AAYNAGPGRV 586
Cdd:PRK11671  260 LFDPANNIDTGTAYlaiLQNVYLGGITNptsRRYAViTAYNGGAGSV 306
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
471-587 8.30e-12

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 67.98  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 471 HLEERFPlAYKDLFDRYTSGKDipqsYAM--AIARQESAWNPKVRSPVGASGLMQIMPGTAthtvKMFNIpgssspSQLL 548
Cdd:PRK10859  282 AIDNRLP-KYQPLFEKYAGELD----WRLlaAIAYQESHWNPQATSPTGVRGLMMLTRNTA----QSMGV------TDRL 346

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1733464609 549 DPETNINIGTSYLQYVYQQF-----GNNRI-FASAAYNAGPGRVR 587
Cdd:PRK10859  347 DPEQSIRGGARYLQDLMERLpesipEPERIwFALAAYNIGYGHML 391
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 497-560 8.67e-10

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 54.72  E-value: 8.67e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733464609 497 YAMAIARQESAWNPKVR--SPVGASGLMQIMPGTATHTVKmfnipgsSSPSQLLDPETNINIGTSY 560
Cdd:cd00442     1 VLAAIIGQESGGNKPANagSGSGAAGLFQFMPGTWKAYGK-------NSSSDLNDPEASIEAAAKY 59
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 500-584 3.87e-09

Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381602 [Multi-domain]  Cd Length: 108  Bit Score: 54.62  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 500 AIARQESAWNPK-VRSPVGASGLMQIMPGTAthtvKMFNIPGSSSPSQLL-DPETNInigTSYLQYVYQQFGNNRIF--- 574
Cdd:cd13399    10 AILGVESGFGPNaGGSPAGAQGIAQFMPSTW----KAYGVDGNGDGKADPfNPEDAI---ASAANYLCRHGWDLNAFlge 82

                          90
                  ....*....|....
gi 1733464609 575 ----ASAAYNAGPG 584
Cdd:cd13399    83 dnflALAAYNAGPG 96
PHA00658 PHA00658
putative lysin
 502-623 5.19e-09

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 59.45  E-value: 5.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 502 ARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPGSSSPSQLlDPETNINIGTSYLQYVYQQFGNNRIFASAAYNA 581
Cdd:PHA00658  314 GRQFGADGKPLTSPKGAVGIAQVMPDTAPEAAKLAGLPWDENRYRN-DAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNA 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1733464609 582 GPGRVRTWLGNSAGRidavAFVESIPfSETRGY-VKNVLAYDA 623
Cdd:PHA00658  393 GPGALQSALKDAKDG----NWLALLP-KETQDYvVKNMQAYNA 430
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 500-589 1.73e-07

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 49.83  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 500 AIARQESAWNPKV--RSPVG--ASGLMQImpgtATHTVKMFNIPGSSSPSQLLDPETNINIGTSYLQYVYQQFGNNrIFA 575
Cdd:cd13400    10 AIAKVESGFNPNAinRNKNGsyDIGLMQI----NSIWLPELARYGITREELLNDPCTNIYVGAWILARNIKRYGNT-WKA 84

                          90
                  ....*....|....
gi 1733464609 576 SAAYNAGPGRVRTW 589
Cdd:cd13400    85 VGAYNSGTPKKNDK 98
PHA00368 PHA00368
internal virion protein D
 477-619 4.49e-07

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 53.25  E-value: 4.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609  477 PLAYKDLFDRYTSGKDIPQSYAMAIARQESAWNPKVRSPVGASGLMQIMPGTATHTVKMFNIPGSsspsqlLDPETNINI 556
Cdd:PHA00368     8 PSEYDGLFQKAADAHGVSYDLLRKVGWDESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDDDDR------LDPELAIDA 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733464609  557 GTSYLQYVYQQFGNNRIFASAAYNAGPGRvrtwlgNSAGRIDAVAFVESIPFSET-RGYVKNVL 619
Cdd:PHA00368    82 GARYLADLVGKYDGDELKAALAYNQGEGR------LGAPQLEAYDKGDFASISEEgRNYLRNLL 139
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
500-561 3.32e-06

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 48.42  E-value: 3.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733464609 500 AIARQESAWNPKVRSPVGASGLMQIMPGTATHTV-KMFNIPGSSSPSQLLDPETNINIGTSYL 561
Cdd:PRK15470   59 AIIAIESGGNPNAVSKSNAIGLMQLKASTSGRDVyRRMGWSGEPTTSELKNPERNISMGAAYL 121
Cucumo_coat pfam00760
Cucumovirus coat protein;
153-204 1.42e-04

Cucumovirus coat protein;


Pssm-ID: 395617  Cd Length: 175  Bit Score: 43.20  E-value: 1.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1733464609 153 KELWLTGKSQPNACDPLFSAWRA--SGQQDPLSYLERIRLAMKAGNTRLVTVLA 204
Cdd:pfam00760  83 EQLWLTGKKLPASCDLLFAAINAmfADGASNSLIQQRAALAFDANNVGLLTDLS 136
CwlT-like cd16891
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
 480-596 6.98e-03

CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381612 [Multi-domain]  Cd Length: 151  Bit Score: 37.58  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 480 YKDLFDRYTSGKDIP--QSYAMAIARQESawnpKVRSPvgasGLMQimpgtathtvkmfnipgsSSPSQ------LLDPE 551
Cdd:cd16891     1 YRPLVEKEAKKYGIPeyVPLILAIIMQES----GGKGP----DIMQ------------------SSESAglppntITDPE 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1733464609 552 TNINIGTSYLQYVY---QQFGNNRIFASAAYNAGPGRVrTWLGNSAGR 596
Cdd:cd16891    55 ESIEQGVKYFADVLkkaKGKGVDIWTAVQAYNFGGGYI-DYVAKNGGK 101
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 195-359 8.87e-03

SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid.


Pssm-ID: 238861  Cd Length: 259  Bit Score: 38.59  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 195 GNTRLVTVLAGQMPADYQTIASAVIGLANDPNTVLTFARTTGATDFTRQ-----MAAVafASVARDDVENARLMIpqLVQ 269
Cdd:cd01823    79 PDTDLVTITIGGNDLGFADVVKACILTGGGSSLAQEKGAADGARDAALDevgarLKAV--LDRIRERAPNARVVV--VGY 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733464609 270 AQQLNDDQTQELRDIvawrLMGTDVTDEQARWRDDAVMRSNSVslVERRVRmALGTGDRRGLNTWLARLPMDAKEKDEWR 349
Cdd:cd01823   155 PRLFPPDGGDCDKSC----SPGTPLTPADRPELNQLVDKLNAL--IRRAAA-DAGDYKVRFVDTDAPFAGHRACSPDPWS 227

                         170
                  ....*....|
gi 1733464609 350 YWQADLLLER 359
Cdd:cd01823   228 RSVLDLLPTR 237
 
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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