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Conserved domains on  [gi|1125233871|gb|OLB81478|]
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hypothetical protein AUI14_03275 [Actinobacteria bacterium 13_2_20CM_2_71_6]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
43-296 2.05e-133

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


:

Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 380.63  E-value: 2.05e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871  43 LNLRAAATTRSATVGRLANRARVTLVCKVAGEKVKGKVRTSNQWDRTASGGYVSHAYVRSNSSLPTCPAPVVPQVTVASV 122
Cdd:NF038016    1 LNVRSGPATDSAVVGTLANGAKVTVVCKVRGEQIRGTVRTTSQWDRLGSGRYVSHAYVRWSPSLPTCPWCAPKAATVATV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 123 -----------GPYTGPVVLGTVAGG-----------------------------------------------PNGTMTN 144
Cdd:NF038016   81 ttgggalnvraAAGTGAARVGTVANGatvtvecqvwgqevdgtgvwyrlgdgryvsaayvrrpwlpwcgqdppTVPRGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCFtPVPGPISIGCHSYATYEFV-NGHYVA 223
Cdd:NF038016  161 AQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKCF-GSPGPIAVGCRSYATFECSpTGGCFD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125233871 224 TTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQYD 296
Cdd:NF038016  240 TTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
 
Name Accession Description Interval E-value
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
43-296 2.05e-133

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 380.63  E-value: 2.05e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871  43 LNLRAAATTRSATVGRLANRARVTLVCKVAGEKVKGKVRTSNQWDRTASGGYVSHAYVRSNSSLPTCPAPVVPQVTVASV 122
Cdd:NF038016    1 LNVRSGPATDSAVVGTLANGAKVTVVCKVRGEQIRGTVRTTSQWDRLGSGRYVSHAYVRWSPSLPTCPWCAPKAATVATV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 123 -----------GPYTGPVVLGTVAGG-----------------------------------------------PNGTMTN 144
Cdd:NF038016   81 ttgggalnvraAAGTGAARVGTVANGatvtvecqvwgqevdgtgvwyrlgdgryvsaayvrrpwlpwcgqdppTVPRGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCFtPVPGPISIGCHSYATYEFV-NGHYVA 223
Cdd:NF038016  161 AQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKCF-GSPGPIAVGCRSYATFECSpTGGCFD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125233871 224 TTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQYD 296
Cdd:NF038016  240 TTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
138-294 8.25e-51

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 168.99  E-value: 8.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 138 PNGTMTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLT-VNDKNFFGIKCFTPVPGPisigCHSYATYEF 216
Cdd:COG1705   123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSWQGK----SVEVTTTEY 198
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125233871 217 VNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:COG1705   199 VNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALANAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
142-294 1.78e-26

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 105.73  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 142 MTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSG-LTVNDK---NFFGIKCFTPVPGPISigchSYATYEFV 217
Cdd:PRK05684  150 GSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREiRTADGSpshNLFGIKADGSWKGPVT----EITTTEYE 225
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:PRK05684  226 NGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMG 301
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
133-289 8.99e-25

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 100.70  E-value: 8.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 133 TVAGGPNgtmtnaDFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigc 208
Cdd:TIGR02541 143 SVPGHPK------SFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGspsyNLFGIKASGSWQGKVV--- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 209 hSYATYEFVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMH 288
Cdd:TIGR02541 214 -TTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARLLNNNPRYE-AVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQ 291

                  .
gi 1125233871 289 Q 289
Cdd:TIGR02541 292 S 292
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
155-241 1.80e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 86.47  E-value: 1.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 155 AQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCftpvpgpisigchSYATYEFVNGHYVATTAAFRTYASA 234
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKA-------------SWKGKVAYDTDEVTVAARFRKYDSV 70

                  ....*..
gi 1125233871 235 LDSFRDH 241
Cdd:pfam01832  71 EESIRDY 77
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
145-296 4.55e-20

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 84.41  E-value: 4.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871  145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKcfTPVPGPISigchSYATYEFVNGHYVAT 224
Cdd:smart00047   9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIK--GAYDGRPV----RMGTLEYLNGGWVTV 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125233871  225 TAAFRTYASAldSFRDHGRFLV-VNDRYAPAFAYTGnadqflyqIWKAGYATSPTYVANVQALMHQFN--LYQYD 296
Cdd:smart00047  83 KAAFRGYFGE--KFIDYAYVLRgQNPLYKKRWGSNA--------LQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
 
Name Accession Description Interval E-value
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
43-296 2.05e-133

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 380.63  E-value: 2.05e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871  43 LNLRAAATTRSATVGRLANRARVTLVCKVAGEKVKGKVRTSNQWDRTASGGYVSHAYVRSNSSLPTCPAPVVPQVTVASV 122
Cdd:NF038016    1 LNVRSGPATDSAVVGTLANGAKVTVVCKVRGEQIRGTVRTTSQWDRLGSGRYVSHAYVRWSPSLPTCPWCAPKAATVATV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 123 -----------GPYTGPVVLGTVAGG-----------------------------------------------PNGTMTN 144
Cdd:NF038016   81 ttgggalnvraAAGTGAARVGTVANGatvtvecqvwgqevdgtgvwyrlgdgryvsaayvrrpwlpwcgqdppTVPRGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCFtPVPGPISIGCHSYATYEFV-NGHYVA 223
Cdd:NF038016  161 AQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKCF-GSPGPIAVGCRSYATFECSpTGGCFD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125233871 224 TTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQYD 296
Cdd:NF038016  240 TTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
138-294 8.25e-51

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 168.99  E-value: 8.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 138 PNGTMTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLT-VNDKNFFGIKCFTPVPGPisigCHSYATYEF 216
Cdd:COG1705   123 AAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSWQGK----SVEVTTTEY 198
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125233871 217 VNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:COG1705   199 VNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALANAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
142-294 1.78e-26

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 105.73  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 142 MTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSG-LTVNDK---NFFGIKCFTPVPGPISigchSYATYEFV 217
Cdd:PRK05684  150 GSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREiRTADGSpshNLFGIKADGSWKGPVT----EITTTEYE 225
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:PRK05684  226 NGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMG 301
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
133-289 8.99e-25

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 100.70  E-value: 8.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 133 TVAGGPNgtmtnaDFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigc 208
Cdd:TIGR02541 143 SVPGHPK------SFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGspsyNLFGIKASGSWQGKVV--- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 209 hSYATYEFVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMH 288
Cdd:TIGR02541 214 -TTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARLLNNNPRYE-AVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQ 291

                  .
gi 1125233871 289 Q 289
Cdd:TIGR02541 292 S 292
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
155-241 1.80e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 86.47  E-value: 1.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 155 AQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKCftpvpgpisigchSYATYEFVNGHYVATTAAFRTYASA 234
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKA-------------SWKGKVAYDTDEVTVAARFRKYDSV 70

                  ....*..
gi 1125233871 235 LDSFRDH 241
Cdd:pfam01832  71 EESIRDY 77
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
145-296 4.55e-20

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 84.41  E-value: 4.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871  145 ADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDKNFFGIKcfTPVPGPISigchSYATYEFVNGHYVAT 224
Cdd:smart00047   9 LEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIK--GAYDGRPV----RMGTLEYLNGGWVTV 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125233871  225 TAAFRTYASAldSFRDHGRFLV-VNDRYAPAFAYTGnadqflyqIWKAGYATSPTYVANVQALMHQFN--LYQYD 296
Cdd:smart00047  83 KAAFRGYFGE--KFIDYAYVLRgQNPLYKKRWGSNA--------LQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
140-288 5.30e-20

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 88.87  E-value: 5.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 140 GTMTNADFIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLT--VNDKNFFGIKCFTPVPGPISIGCHsyatyEFV 217
Cdd:PRK12711  211 GERTPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGngGDSNNLFGIKATGWNGDKVTTGTH-----EYV 285
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMH 288
Cdd:PRK12711  286 NGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGTDIKGFARGLQQAGYATDPGYAAKIAAIAN 356
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
147-279 1.46e-18

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 84.29  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 147 FIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigchSYATYEFVNGHYV 222
Cdd:PRK12712  200 FVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGsttfNVFGIKAGANWKGRVA----EVTTTEYVDGQPQ 275
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1125233871 223 ATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAyTGNADQFLYQIWKAGYATSPTY 279
Cdd:PRK12712  276 KVRARFRAYGSYDEACADYARLLTSNPRYAGVVS-AASADEAAHGLQRAGYATDPAY 331
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
146-290 5.46e-17

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 79.79  E-value: 5.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 146 DFIA----AAVIPAQQSQrefrVPASVTIAQSILESGWGRSGLTVNDK----NFFGIKCFTPVPGPISigchSYATYEFV 217
Cdd:PRK12713  183 DFVSrmsrAANVAAQQSG----VPARLILGQAALESGWGRRELRHEDGstsyNLFGIKAGASWKGKVV----NVMTTEYV 254
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125233871 218 NGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYApAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQF 290
Cdd:PRK12713  255 DGVAQKLVQPFRAYSSYEESFSDYARLIGNSPRYE-AVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQL 326
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
139-289 1.91e-15

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 75.35  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 139 NGTMTNAD-FIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVND----KNFFGIKCFTPVPGPISigchSYAT 213
Cdd:PRK12709  167 NGGSPDADaFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADgstsYNVFGIKATKGWTGRTV----SAVT 242
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125233871 214 YEFVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQ 289
Cdd:PRK12709  243 TEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRYAGVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQ 318
PRK08581 PRK08581
amidase domain-containing protein;
125-297 1.72e-13

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 70.59  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 125 YTGPVVLGTVAGGPNGTMTNAD---FIAAAVIPAQQSQREFRVPASVTIAQSILESGWGRSGLTVNDK-NFFGIKcftpv 200
Cdd:PRK08581  298 ETGPSLSNNDDSGSFNVVDSKDtrqFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSPNhNLFGIK----- 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 201 pGPISIGCHSYATYEFVNGHYVATTAAFRTYASALDSFRDHGRfLVVN------DRYAPAF---AYT-GNADQFLYQIwk 270
Cdd:PRK08581  373 -GAYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYAD-LIKNgidgnsTIYKPTWkseAKSyKDATSHLSKT-- 448
                         170       180
                  ....*....|....*....|....*..
gi 1125233871 271 agYATSPTYVANVQALMHQFNLYQYDL 297
Cdd:PRK08581  449 --YATDPNYAKKLNSIIKHYNLTQFDD 473
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
146-294 4.85e-12

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 65.20  E-value: 4.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 146 DFIAAAVIPAQQSQREFRVPASVTIAQSILESGWG----RSGLTVNDKNFFGIKcftpvpgpisIGCHS------YATYE 215
Cdd:PRK12710  132 DFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGkfvtRDADGSSSNNLFNIK----------TGSHSevesiqVKTTE 201
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125233871 216 FVNGHYVATTAAFRTYASALDSFRDHGRFLVVNDRYAPAFAYTGNADQFLYQIWKAGYATSPTYVANVQALMHQFNLYQ 294
Cdd:PRK12710  202 YIADTPIKINASFRKYPSIEHSFHDYVSLIKGSERYQMALANAENPEIYVSELNKAGYATDPNYSNKILSIYHGDELNQ 280
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
107-296 8.76e-10

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 59.32  E-value: 8.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 107 PTCPAPVVPQVTVASVGPytgpvvlGTVAGGPNGT-------------------MTNADFIAAAVIPAQQSQREFRVPAS 167
Cdd:PRK06347  101 PEEKQPAAKQVEKAPAEP-------ATVSNPDNATssstpatynllqksalrsgATVQSFIQTIQASSSQIAAENDLYAS 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 168 VTIAQSILESGWGRSGL-TVNDKNFFGIKcftpvpGPISIGCHSYATYE-FVNGHYVATTAAFRTYASALDSFRDHGRFL 245
Cdd:PRK06347  174 VMIAQAILESAYGTSELgSAPNYNLFGIK------GAYNGQSYTKQTLEdDGKGNYYTITAKFRKYPSYHQSLEDYAQVI 247
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125233871 246 vvndRYAPAFaytgNADqFLYQIWKAG--------------YATSPTYVANVQALMHQFNLYQYD 296
Cdd:PRK06347  248 ----RKGPSW----NPN-YYSKVWKSNttsykdatkaltgtYATDTAYATKLNDLISRYNLTQYD 303
PRK10356 PRK10356
protein bax;
164-239 2.11e-05

protein bax;


Pssm-ID: 182404  Cd Length: 274  Bit Score: 45.25  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871 164 VPASVTIAQSILESGWGRSGLTVNDKNFFGIKCF----TPVPGPISigchSYATYEFVNGHYVATTAAFRTYaSALDSFR 239
Cdd:PRK10356  149 IPTSMVATMAAAESGWGTSKLARNNNNLFGMKCMkgrcTNAPGKVK----GYSQFSSVKESVSAYVTNLNTH-PAYSSFR 223
SH3_3 pfam08239
Bacterial SH3 domain;
41-100 2.49e-03

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 35.30  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125233871  41 GPLNLRAAATTRSATVGRLANRARVTLVCKVAGEKVkgKVRTSNqwDRTasgGYVSHAYV 100
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGGWY--KVRTYD--GYE---GWVSSSYL 53
 
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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