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Conserved domains on  [gi|2183003408|gb|UJP30885|]
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baseplate hub structural protein / lysozyme R [Klebsiella phage Kpn35c1]

Protein Classification

type VI secretion system Vgr family protein( domain architecture ID 11476042)

type VI secretion system Vgr family protein; type VI secretion system tip protein VgrG is a core component and effector of Type VI secretion systems (T6SSs) that are involved in the pathogenicity of several Gram-negative bacteria

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
5 PHA02596
baseplate hub subunit and tail lysozyme; Provisional
 3-589 0e+00

baseplate hub subunit and tail lysozyme; Provisional


:

Pssm-ID: 222900 [Multi-domain]  Cd Length: 576  Bit Score: 1052.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408   3 LGGNLHSPFFDGVVENVDDPRGLGRVQVRVFGQHPAQKQKSDAIGVPVEDLPWMMPIQDIRSAAISGVGFSPTGITRGSF 82
Cdd:PHA02596    1 EMINNNLKWFVGVVEDRMDPLKLGRVRVRVHGIHPAQKAKGDVYGIPTEDLPWMSVIQPITSAAISGIGQSPTGIVEGTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408  83 VVGYWRDKWHQDGMIIGTVAGEYVEQPDTQKGFCDPMGEYPRYVGNDVNSLALGGLKGKGSSSVIIRDSNTSIAVNPDDR 162
Cdd:PHA02596   81 VYGHFLDKWKQNGLILGTYGGIYREKPNTNEGFSDPTGQYPRYVGNDVNVLARGGEVGYDPSSVVIQDANTDVAINPDDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 163 PLDEIPEDNRPDtggFTIEKMLKQDEGIRTRWYTDSEGYPTIGIGHLLIREKTRDTAKINAAISKAVGREVTNGTITAEE 242
Cdd:PHA02596  161 PLDEIPPDDNPD---FTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKTRDMAQINKLLSKQVGREVTGGRITAEE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 243 VSTLFAQDLAKVRSDIQRTANVREVYVNLNRPRQMAIENMSFQMGVGGVAKFTNTLKAMKNEDWQAAYNGLRNSLWASQT 322
Cdd:PHA02596  238 ASKLFARDLAKVQRDISRHSKVGPVYNKLNRSRQMALENMAFQMGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWANQT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 323 PGRSSRVSKIVLTGNLESYGVQVPDPEGRSLSAAyAAYNGATLSATSPEDPFTPGDTRVMFEEPTSSYNAEYPYNMVFES 402
Cdd:PHA02596  318 PGRASRVSKIILTGNLESYGVMVPDPPGRSLSTI-AAYKTAVATSSDPADPFTPGDTRIMFKEPKSSYSAEYPYNHVMES 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 403 RSGHIQEFDDTPGYERYNRVHPAGSYEEIRPDGTRVVKIVGDDYQIVMQGRKLNVKGNLQVVIEGDAFIYNMGNVQQTVD 482
Cdd:PHA02596  397 ESGHIQEFDDTPGHERYRRVHPTGTYEEIRPDGTRVVKIVGDDYYIVKQDRNVNVKGNLKVVVEGDAIYYNMGNVLQTID 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 483 GNVTEFVRGNVQQTVEgeyvglikGNAELTVNKDATVNVDQNLTANVKQNATVAVTEDATITAK-NAKMEIEETMDIGAK 561
Cdd:PHA02596  477 GNVTIFVRGNVTKTVE--------GNGTLYVKGNVTVQVDGNLDATVKGNATTLVEGNQTNTVNgNYKLKVEGNFDMTVG 548

                         570       580
                  ....*....|....*....|....*...
gi 2183003408 562 DINIKATNNTFIDSGALTKITGGTVQVG 589
Cdd:PHA02596  549 GNWSEQMAGMSSIASGTYTIDGSRIDIG 576
 
Name Accession Description Interval E-value
5 PHA02596
baseplate hub subunit and tail lysozyme; Provisional
 3-589 0e+00

baseplate hub subunit and tail lysozyme; Provisional


Pssm-ID: 222900 [Multi-domain]  Cd Length: 576  Bit Score: 1052.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408   3 LGGNLHSPFFDGVVENVDDPRGLGRVQVRVFGQHPAQKQKSDAIGVPVEDLPWMMPIQDIRSAAISGVGFSPTGITRGSF 82
Cdd:PHA02596    1 EMINNNLKWFVGVVEDRMDPLKLGRVRVRVHGIHPAQKAKGDVYGIPTEDLPWMSVIQPITSAAISGIGQSPTGIVEGTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408  83 VVGYWRDKWHQDGMIIGTVAGEYVEQPDTQKGFCDPMGEYPRYVGNDVNSLALGGLKGKGSSSVIIRDSNTSIAVNPDDR 162
Cdd:PHA02596   81 VYGHFLDKWKQNGLILGTYGGIYREKPNTNEGFSDPTGQYPRYVGNDVNVLARGGEVGYDPSSVVIQDANTDVAINPDDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 163 PLDEIPEDNRPDtggFTIEKMLKQDEGIRTRWYTDSEGYPTIGIGHLLIREKTRDTAKINAAISKAVGREVTNGTITAEE 242
Cdd:PHA02596  161 PLDEIPPDDNPD---FTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKTRDMAQINKLLSKQVGREVTGGRITAEE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 243 VSTLFAQDLAKVRSDIQRTANVREVYVNLNRPRQMAIENMSFQMGVGGVAKFTNTLKAMKNEDWQAAYNGLRNSLWASQT 322
Cdd:PHA02596  238 ASKLFARDLAKVQRDISRHSKVGPVYNKLNRSRQMALENMAFQMGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWANQT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 323 PGRSSRVSKIVLTGNLESYGVQVPDPEGRSLSAAyAAYNGATLSATSPEDPFTPGDTRVMFEEPTSSYNAEYPYNMVFES 402
Cdd:PHA02596  318 PGRASRVSKIILTGNLESYGVMVPDPPGRSLSTI-AAYKTAVATSSDPADPFTPGDTRIMFKEPKSSYSAEYPYNHVMES 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 403 RSGHIQEFDDTPGYERYNRVHPAGSYEEIRPDGTRVVKIVGDDYQIVMQGRKLNVKGNLQVVIEGDAFIYNMGNVQQTVD 482
Cdd:PHA02596  397 ESGHIQEFDDTPGHERYRRVHPTGTYEEIRPDGTRVVKIVGDDYYIVKQDRNVNVKGNLKVVVEGDAIYYNMGNVLQTID 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 483 GNVTEFVRGNVQQTVEgeyvglikGNAELTVNKDATVNVDQNLTANVKQNATVAVTEDATITAK-NAKMEIEETMDIGAK 561
Cdd:PHA02596  477 GNVTIFVRGNVTKTVE--------GNGTLYVKGNVTVQVDGNLDATVKGNATTLVEGNQTNTVNgNYKLKVEGNFDMTVG 548

                         570       580
                  ....*....|....*....|....*...
gi 2183003408 562 DINIKATNNTFIDSGALTKITGGTVQVG 589
Cdd:PHA02596  549 GNWSEQMAGMSSIASGTYTIDGSRIDIG 576
Gp5_OB pfam06714
Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein ...
 34-174 2.23e-70

Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein of bacteriophage T4. This domain binds to the Gp27 protein. This domain has the common OB fold.


Pssm-ID: 148361  Cd Length: 144  Bit Score: 223.12  E-value: 2.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408  34 GQHPAQKQKSDAIGVPVEDLPWMMPIQDIRSAAISGVGFSPTGITRGSFVVGYWRDKWHQDGMIIGTVAGEYVEQPDTQK 113
Cdd:pfam06714   1 GIHPEQKAKGDVQGIPTEDLLWMSPMQPITSAAVSGIGQSPTGIVEGTHVYGHFLDKWYQNGVILGTYPGIYKEKPNFNK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183003408 114 GFCDPMGEYPRYVGNDVNSLALGGLKGK---GSSSVIIRDSNTSIAVNPDDRPLDEIPEDNRPD 174
Cdd:pfam06714  81 GFSDPNGQYPRYVGNDVNVLARGGKDPEvgyGSSSNVIQDSNTDVAINPDDTPLDEIPPDDNPD 144
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 179-340 6.66e-63

bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.


Pssm-ID: 381597  Cd Length: 146  Bit Score: 203.76  E-value: 6.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 179 TIEKMLKQDEGIRTRWYTDSEGYPTIGIGHLLIREKTRdtakinaaiskavgreVTNGTITAEEVSTLFAQDLAKVRSDI 258
Cdd:cd00735     1 TIREMLRQDEGYRLKAYKDTEGYPTIGIGHLIGKKGAS----------------LTNGTITKDEAEALFEQDVDRAVRDM 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 259 QRTANVREVYVNLNRPRQMAIENMSFQMGVGGVAKFTNTLKAMKNEDWQAAYNGLRNSLWASQTPGRSSRVSKIVLTGNL 338
Cdd:cd00735    65 LRNPKLAPVYAQLNAARRMALINMAFQMGVGGLAKFKNMLAAIKAGDWEEAADGMLNSLWAKQTPNRANRVSAVMRTGTW 144


                  ..
gi 2183003408 339 ES 340
Cdd:cd00735   145 AP 146
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
183-315 5.43e-11

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 60.62  E-value: 5.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 183 MLKQDEGIRTRWYTDSEGYPTIGIGHLlirektrdtakinaaiskavGREVTNG-TITAEEVSTLFAQDLAKVRSDIQRT 261
Cdd:COG3772    11 LIKEFEGFRLKAYRDPAGVWTIGYGHT--------------------GKDVKPGdTITEEEAEALLAADLAKAEAAVRRL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2183003408 262 anvreVYVNLNRPRQMAIENMSFQMGVGGVAKFTnTLKAMKNEDWQAAYNGLRN 315
Cdd:COG3772    71 -----VKVPLTQNQFDALVSFAYNVGAGAFCRST-LLRKLNAGDYAGACDELLR 118
 
Name Accession Description Interval E-value
5 PHA02596
baseplate hub subunit and tail lysozyme; Provisional
 3-589 0e+00

baseplate hub subunit and tail lysozyme; Provisional


Pssm-ID: 222900 [Multi-domain]  Cd Length: 576  Bit Score: 1052.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408   3 LGGNLHSPFFDGVVENVDDPRGLGRVQVRVFGQHPAQKQKSDAIGVPVEDLPWMMPIQDIRSAAISGVGFSPTGITRGSF 82
Cdd:PHA02596    1 EMINNNLKWFVGVVEDRMDPLKLGRVRVRVHGIHPAQKAKGDVYGIPTEDLPWMSVIQPITSAAISGIGQSPTGIVEGTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408  83 VVGYWRDKWHQDGMIIGTVAGEYVEQPDTQKGFCDPMGEYPRYVGNDVNSLALGGLKGKGSSSVIIRDSNTSIAVNPDDR 162
Cdd:PHA02596   81 VYGHFLDKWKQNGLILGTYGGIYREKPNTNEGFSDPTGQYPRYVGNDVNVLARGGEVGYDPSSVVIQDANTDVAINPDDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 163 PLDEIPEDNRPDtggFTIEKMLKQDEGIRTRWYTDSEGYPTIGIGHLLIREKTRDTAKINAAISKAVGREVTNGTITAEE 242
Cdd:PHA02596  161 PLDEIPPDDNPD---FTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKTRDMAQINKLLSKQVGREVTGGRITAEE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 243 VSTLFAQDLAKVRSDIQRTANVREVYVNLNRPRQMAIENMSFQMGVGGVAKFTNTLKAMKNEDWQAAYNGLRNSLWASQT 322
Cdd:PHA02596  238 ASKLFARDLAKVQRDISRHSKVGPVYNKLNRSRQMALENMAFQMGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWANQT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 323 PGRSSRVSKIVLTGNLESYGVQVPDPEGRSLSAAyAAYNGATLSATSPEDPFTPGDTRVMFEEPTSSYNAEYPYNMVFES 402
Cdd:PHA02596  318 PGRASRVSKIILTGNLESYGVMVPDPPGRSLSTI-AAYKTAVATSSDPADPFTPGDTRIMFKEPKSSYSAEYPYNHVMES 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 403 RSGHIQEFDDTPGYERYNRVHPAGSYEEIRPDGTRVVKIVGDDYQIVMQGRKLNVKGNLQVVIEGDAFIYNMGNVQQTVD 482
Cdd:PHA02596  397 ESGHIQEFDDTPGHERYRRVHPTGTYEEIRPDGTRVVKIVGDDYYIVKQDRNVNVKGNLKVVVEGDAIYYNMGNVLQTID 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 483 GNVTEFVRGNVQQTVEgeyvglikGNAELTVNKDATVNVDQNLTANVKQNATVAVTEDATITAK-NAKMEIEETMDIGAK 561
Cdd:PHA02596  477 GNVTIFVRGNVTKTVE--------GNGTLYVKGNVTVQVDGNLDATVKGNATTLVEGNQTNTVNgNYKLKVEGNFDMTVG 548

                         570       580
                  ....*....|....*....|....*...
gi 2183003408 562 DINIKATNNTFIDSGALTKITGGTVQVG 589
Cdd:PHA02596  549 GNWSEQMAGMSSIASGTYTIDGSRIDIG 576
Gp5_OB pfam06714
Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein ...
 34-174 2.23e-70

Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein of bacteriophage T4. This domain binds to the Gp27 protein. This domain has the common OB fold.


Pssm-ID: 148361  Cd Length: 144  Bit Score: 223.12  E-value: 2.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408  34 GQHPAQKQKSDAIGVPVEDLPWMMPIQDIRSAAISGVGFSPTGITRGSFVVGYWRDKWHQDGMIIGTVAGEYVEQPDTQK 113
Cdd:pfam06714   1 GIHPEQKAKGDVQGIPTEDLLWMSPMQPITSAAVSGIGQSPTGIVEGTHVYGHFLDKWYQNGVILGTYPGIYKEKPNFNK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183003408 114 GFCDPMGEYPRYVGNDVNSLALGGLKGK---GSSSVIIRDSNTSIAVNPDDRPLDEIPEDNRPD 174
Cdd:pfam06714  81 GFSDPNGQYPRYVGNDVNVLARGGKDPEvgyGSSSNVIQDSNTDVAINPDDTPLDEIPPDDNPD 144
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 179-340 6.66e-63

bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.


Pssm-ID: 381597  Cd Length: 146  Bit Score: 203.76  E-value: 6.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 179 TIEKMLKQDEGIRTRWYTDSEGYPTIGIGHLLIREKTRdtakinaaiskavgreVTNGTITAEEVSTLFAQDLAKVRSDI 258
Cdd:cd00735     1 TIREMLRQDEGYRLKAYKDTEGYPTIGIGHLIGKKGAS----------------LTNGTITKDEAEALFEQDVDRAVRDM 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 259 QRTANVREVYVNLNRPRQMAIENMSFQMGVGGVAKFTNTLKAMKNEDWQAAYNGLRNSLWASQTPGRSSRVSKIVLTGNL 338
Cdd:cd00735    65 LRNPKLAPVYAQLNAARRMALINMAFQMGVGGLAKFKNMLAAIKAGDWEEAADGMLNSLWAKQTPNRANRVSAVMRTGTW 144


                  ..
gi 2183003408 339 ES 340
Cdd:cd00735   145 AP 146
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 201-325 2.73e-12

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 63.53  E-value: 2.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 201 YPTIGIGHLlirEKTRDTAKInaaiskavgrevtngtITAEEVSTLFAQDLAKVRSDIQRTANVRevyvNLNRPRQMAIE 280
Cdd:pfam00959   1 YWTIGIGHN---GKDVSPHPR----------------ATKSEAAGRLQIDLDTAERCINQYHKVK----DFNPNQQDALV 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2183003408 281 NMSFQMGVGGvAKFTNTLKAMKNEDWQAAYNGLRNSL----WASQTPGR 325
Cdd:pfam00959  58 SLAFNVGCGK-RGFSTLLRAGNIGQWIKACSAIWKSLkagkVYNGLVNR 105
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
183-315 5.43e-11

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 60.62  E-value: 5.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 183 MLKQDEGIRTRWYTDSEGYPTIGIGHLlirektrdtakinaaiskavGREVTNG-TITAEEVSTLFAQDLAKVRSDIQRT 261
Cdd:COG3772    11 LIKEFEGFRLKAYRDPAGVWTIGYGHT--------------------GKDVKPGdTITEEEAEALLAADLAKAEAAVRRL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2183003408 262 anvreVYVNLNRPRQMAIENMSFQMGVGGVAKFTnTLKAMKNEDWQAAYNGLRN 315
Cdd:COG3772    71 -----VKVPLTQNQFDALVSFAYNVGAGAFCRST-LLRKLNAGDYAGACDELLR 118
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 183-309 1.41e-10

endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381599 [Multi-domain]  Cd Length: 136  Bit Score: 59.45  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 183 MLKQDEGIRTRWYTDSEGYPTIGIGHLLirektrdtakinaaisKAVGREvtNGTITAEEVSTLFAQDLAKVRSDIqrta 262
Cdd:cd00737     4 LIKEFEGLRLKAYRDPAGVWTIGYGHTG----------------GVVVKP--GDTITEAQAEALLRQDLARFEAAV---- 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2183003408 263 nVREVYVNLNRPRQMAIENMSFQMGVGGVAKFTNtLKAMKNEDWQAA 309
Cdd:cd00737    62 -NRLVKVPLNQNQFDALVSFAFNVGAGAFKSSTL-LRKLNAGDYAGA 106
VgrG COG3501
Uncharacterized conserved protein VgrG, implicated in type VI secretion and phage assembly ...
 390-589 5.37e-07

Uncharacterized conserved protein VgrG, implicated in type VI secretion and phage assembly [Intracellular trafficking, secretion, and vesicular transport, Mobilome: prophages, transposons, General function prediction only];


Pssm-ID: 442724 [Multi-domain]  Cd Length: 743  Bit Score: 52.84  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 390 YNAEY--PYN-------MVFESRS----GHIQ-EFDDTPGYERYnRVH-PAGSYEEIRPDGTRVVK------IVGDDYQI 448
Cdd:COG3501   452 YNGANmpPYTlpanktrSGIRTRSspggGFNElRFDDKAGQEEI-FLHaEKDMNTLVDNDETITVGndrteeVGTDETGT 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 449 VMQGRKLNVKGNLQVVIEGDAFIYNMGNVQQTVDGNVTEFVRGNVQQTVEGEYVGLIKGNAELTVNKDATVNVDQNLTAN 528
Cdd:COG3501   531 VAGNQGLTVSGDQTVVVGGNQTLVVGGARTLVVGGNLAAVVGGAAATAGGAQATLVAGALLLLAAGGALTTVGGGGTTTG 610

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183003408 529 VKQNATVAVTEDATITAKNAKMEIEETMDIGAKDINIKATNNTFIDSGALTKITGGTVQVG 589
Cdd:COG3501   611 GGAAATAGGGGAGAAAGGAATAAAGAAATSAAGGASSAAAAAGGAAGAGGGGLAAAGGGGA 671
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 183-309 8.70e-07

P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381620 [Multi-domain]  Cd Length: 140  Bit Score: 48.37  E-value: 8.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 183 MLKQDEGIRTRWYTDSEGYPTIGIGHllirektrdTAKInaaiskavgreVTNGTITAEEVstlfAQDLAKvrsDIQRTA 262
Cdd:cd16901     9 LIANAEGCRRDPYKCPAGVPTIGIGS---------THGV-----------KPGDRYTDEQA----AKRLAK---DIKKAE 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2183003408 263 NVREVYVNLNRPRQMAIENM---SFQMGVGGVAKfTNTLKAMKNEDWQAA 309
Cdd:cd16901    62 RCVNRCFNGVPLPQGEFDAYvsfAFNVGCGAFCK-STIYKKLQAGDYAAA 110
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 450-557 7.68e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 49.01  E-value: 7.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408  450 MQGRKLNVKGNLQVVIEGDAFIYNMGNVQQTVDGNVTEFVRGNVQQTVEGEYVGLIKGNAELTVNKDATVNVDQNLTANV 529
Cdd:PTZ00341   928 LKNQNENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEENV 1007

                           90       100
                   ....*....|....*....|....*...
gi 2183003408  530 KQNATVAVTEDATITAKNAKMEIEETMD 557
Cdd:PTZ00341  1008 EENVEENIEENVEEYDEENVEEVEENVE 1035
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 439-557 3.34e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.09  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408  439 VKIVGDDYQIVMQGRKLNVKGNLQVVIEGDA---FIYNMG-NVQQTVDGNVTEFVRGNVQQTVEGEYVGLIKGNAELTVN 514
Cdd:PTZ00341   921 INLINKELKNQNENVPEHLKEHAEANIEEDAeenVEEDAEeNVEENVEENVEENVEENVEENVEENVEENVEENVEENVE 1000

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2183003408  515 KDATVNVDQNLTANVKQNATVAVTEDATITAKNAKMEIEETMD 557
Cdd:PTZ00341  1001 ENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVE 1043
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 183-314 2.08e-03

endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381619 [Multi-domain]  Cd Length: 142  Bit Score: 38.69  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 183 MLKQDEGIRTRWYTDSEGYPTIGIGHllirekTRDTAKINAaiskavgrevtngTITAEEVSTLFAQDLAKVRSDIQRTa 262
Cdd:cd16900    11 LVGPWEGLRLTAYRDPVGVWTVCYGH------TGGDVKPGM-------------RYTPAECDALLAKDLQEAAAAVDRC- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2183003408 263 nvreVYVNLNRPRQMAIENMSFQMGVGGVAKFTnTLKAMKNEDWQAAYNGLR 314
Cdd:cd16900    71 ----VKVPLPDPQRAALASFAYNVGVGAFCRST-LLRKLNAGDRRGACDELT 117
fliD PRK08032
flagellar capping protein; Reviewed
 438-582 2.38e-03

flagellar capping protein; Reviewed


Pssm-ID: 236141 [Multi-domain]  Cd Length: 462  Bit Score: 40.83  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 438 VVKIVGDDYQIVMQGRKLNVKGNLQVVIEGDAFIYNMGNVQQTVDGnvtefvrGNVQQTVEGEyvglikgNAELTVN--- 514
Cdd:PRK08032  169 IIKVGDGEYRLVLTSKDTGTDNAMTISVEGDSKLNDFLNYDSSTGS-------GNMTQSVAAQ-------NAKLTVNgia 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183003408 515 --------KDATVNVDQNLTANVKQNATVAVTEDATiTAKNAkmeieetmdigakdinIKA---TNNTFIDS-GALTKIT 582
Cdd:PRK08032  235 ierqsntiTDAPEGITLNLKKVTTGNQTLTITKDTT-KAKEA----------------IKDwvdAYNSLQDTfSSLTKYT 297
Gp5_C pfam06715
Gp5 C-terminal repeat (3 copies); This repeat composes the C-terminal part of the ...
 467-490 7.78e-03

Gp5 C-terminal repeat (3 copies); This repeat composes the C-terminal part of the bacteriophage T4 baseplate protein Gp5. This region of the protein forms a needle like projection from the baseplate that is presumed to puncture the bacterial cell membrane. Structurally three copies of the repeated region trimerize to form a beta solenoid type structure. This family also includes repeats from bacterial Vgr proteins.


Pssm-ID: 310962 [Multi-domain]  Cd Length: 24  Bit Score: 34.18  E-value: 7.78e-03
                          10        20
                  ....*....|....*....|....
gi 2183003408 467 GDAFIYNMGNVQQTVDGNVTEFVR 490
Cdd:pfam06715   1 GNETETVGGNRTVTVGGNETETVG 24
 
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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