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Conserved domains on  [gi|1592995644|gb|TDF28035|]
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flagellar assembly peptidoglycan hydrolase FlgJ [Delftia tsuruhatensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
flgJ super family cl35366
flagellar assembly peptidoglycan hydrolase FlgJ;
22-316 1.32e-95

flagellar assembly peptidoglycan hydrolase FlgJ;


The actual alignment was detected with superfamily member PRK05684:

Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 285.62  E-value: 1.32e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  22 RSLNALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPG-GLSDAIT 100
Cdd:PRK05684   15 QSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQLSAGGGlGLADMMV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 101 RQLARTMGSEAAEDAeISVPSTLSMSRIAWRSTATNANGaaggtaaigawsGSRSSAAQSVNAYAPAPKGRDNFVAHHGD 180
Cdd:PRK05684   95 KQLSPEQSPAPEESA-GAVPMKFDLETVQSYQNQALAQL------------VRKAIPQPPLASDKPLFGSSDDFVARLSP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 181 AAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGS 260
Cdd:PRK05684  162 PAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYDS 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1592995644 261 YEESFRDYARLITSNPRYEkAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQS 316
Cdd:PRK05684  242 YLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQ 296
 
Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
22-316 1.32e-95

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 285.62  E-value: 1.32e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  22 RSLNALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPG-GLSDAIT 100
Cdd:PRK05684   15 QSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQLSAGGGlGLADMMV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 101 RQLARTMGSEAAEDAeISVPSTLSMSRIAWRSTATNANGaaggtaaigawsGSRSSAAQSVNAYAPAPKGRDNFVAHHGD 180
Cdd:PRK05684   95 KQLSPEQSPAPEESA-GAVPMKFDLETVQSYQNQALAQL------------VRKAIPQPPLASDKPLFGSSDDFVARLSP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 181 AAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGS 260
Cdd:PRK05684  162 PAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYDS 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1592995644 261 YEESFRDYARLITSNPRYEkAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQS 316
Cdd:PRK05684  242 YLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQ 296
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 23-316 2.35e-83

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: 254.01  E-value: 2.35e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  23 SLNALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPG-GLSDAITR 101
Cdd:TIGR02541   7 SLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANGGiGLADMIVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 102 QLARTMGSEAAEDAEISVPSTLSMSRIAWRSTATNANGAAGGTAAIGAWSGSrsSAAQSVnayapaPKGRDNFVAHHGDA 181
Cdd:TIGR02541  87 QLTKGQGNEPSEGAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRPRGR--SHAESV------PGHPKSFVNSMLPH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 182 AARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGSY 261
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592995644 262 EESFRDYARLITSNPRYEKAMgKTDSALAYATELQKAGYATDPEYASKLSRAIQS 316
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVL-QQRSAESFARGLQRAGYATDPRYARKLLQVIQS 292
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 26-316 3.86e-68

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 214.45  E-value: 3.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  26 ALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPGGLSDAITRQLAR 105
Cdd:COG1705     2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 106 TMGSEAAEDAEISVPSTLSMSRIAWRStatnangaaggtaaigawSGSRSSAAQSVNAYAPAPKGRDNFVAHHGDAAARV 185
Cdd:COG1705    82 SAAKSATEAGGGLASANAAATSAAALA------------------ASLSGAAALAASATAAASASPEEFIAKIAPAAQKA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 186 AQESGIPAAFMLGQAGHETGWGKSEIknaDGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGSYEESF 265
Cdd:COG1705   144 AKKYGVPASVLIAQAALESGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESF 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1592995644 266 RDYARLITSNPRYEKAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQS 316
Cdd:COG1705   221 RDYARLLKNNPRYAGALANAKDYEAFAKALQKAGYATDPKYADKLISIIES 271
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 165-310 1.47e-30

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: 117.53  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 165 APAPK-GRDNFVAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIknadGSNAHNLFGIKAgKGWTGKVA----EVT 239
Cdd:NF038016  153 PTVPRgTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGL----TREDHNYFGIKC-FGSPGPIAvgcrSYA 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1592995644 240 TTEY-IDGVARKVTAKFRAYGSYEESFRDYARLITSNPRYEKAMGKTDSALAYATELQKAGYATDPEYASKL 310
Cdd:NF038016  228 TFECsPTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKL 299
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 166-315 2.36e-25

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 99.05  E-value: 2.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  166 PAPKGRDNFVAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKnadgSNAHNLFGIKAgkGWTGKVAEVTTTEYID 245
Cdd:smart00047   3 LAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLA----KKYNNLFGIKG--AYDGRPVRMGTLEYLN 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1592995644  246 GVARKVTAKFRAYgsYEESFRDYAR-LITSNPRYEKAMGktdsalayATELQKAGYATDPEYASKLSRAIQ 315
Cdd:smart00047  77 GGWVTVKAAFRGY--FGEKFIDYAYvLRGQNPLYKKRWG--------SNALQTAGYATDPDYAKKLIRIIA 137
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 179-274 3.14e-24

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: 94.18  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 179 GDAAARVAQESGIPAAFMLGQAGHETGWGKSEIknadGSNAHNLFGIKAgkGWTGKVAeVTTTEYidgvarKVTAKFRAY 258
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRL----AKESNNLFGIKA--SWKGKVA-YDTDEV------TVAARFRKY 67

                          90
                  ....*....|....*..
gi 1592995644 259 GSYEESFRD-YARLITS 274
Cdd:pfam01832  68 DSVEESIRDyYAEKLIA 84
 
Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
22-316 1.32e-95

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 285.62  E-value: 1.32e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  22 RSLNALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPG-GLSDAIT 100
Cdd:PRK05684   15 QSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQLSAGGGlGLADMMV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 101 RQLARTMGSEAAEDAeISVPSTLSMSRIAWRSTATNANGaaggtaaigawsGSRSSAAQSVNAYAPAPKGRDNFVAHHGD 180
Cdd:PRK05684   95 KQLSPEQSPAPEESA-GAVPMKFDLETVQSYQNQALAQL------------VRKAIPQPPLASDKPLFGSSDDFVARLSP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 181 AAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGS 260
Cdd:PRK05684  162 PAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYDS 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1592995644 261 YEESFRDYARLITSNPRYEkAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQS 316
Cdd:PRK05684  242 YLESFNDYVSLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQ 296
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 23-316 2.35e-83

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: 254.01  E-value: 2.35e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  23 SLNALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPG-GLSDAITR 101
Cdd:TIGR02541   7 SLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANGGiGLADMIVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 102 QLARTMGSEAAEDAEISVPSTLSMSRIAWRSTATNANGAAGGTAAIGAWSGSrsSAAQSVnayapaPKGRDNFVAHHGDA 181
Cdd:TIGR02541  87 QLTKGQGNEPSEGAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRPRGR--SHAESV------PGHPKSFVNSMLPH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 182 AARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGSY 261
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592995644 262 EESFRDYARLITSNPRYEKAMgKTDSALAYATELQKAGYATDPEYASKLSRAIQS 316
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVL-QQRSAESFARGLQRAGYATDPRYARKLLQVIQS 292
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 24-324 2.50e-68

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 216.92  E-value: 2.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  24 LNALKFAAGENSPQAA--KETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPGGLSDAITR 101
Cdd:PRK12713   22 LADLKRDAVKAPDGQRqqTEVARQFEALFLQMMLKRMREATPKEGLFDSQQTEMLQGMADEQLALQLASPGIGLAQALLG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 102 QL----------ARTMGSEAAEDAEISVPSTLSMSRIAWRSTATNANGAAGGTAAIGAWSGSRSSAAQSVNAYAPAPKGR 171
Cdd:PRK12713  102 QMqqgqppvpaaAAAGGDAAAARALAGTAAPAPLVRDLRGNYVQPDPAPRREVNALLDVLRSNRARDRAMAAAEGAPSHV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 172 DNFVAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKV 251
Cdd:PRK12713  182 VDFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVMTTEYVDGVAQKL 261

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1592995644 252 TAKFRAYGSYEESFRDYARLITSNPRYEkAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQSAVQSAARA 324
Cdd:PRK12713  262 VQPFRAYSSYEESFSDYARLIGNSPRYE-AVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRTSVARA 333
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 26-316 3.86e-68

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 214.45  E-value: 3.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  26 ALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPGGLSDAITRQLAR 105
Cdd:COG1705     2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 106 TMGSEAAEDAEISVPSTLSMSRIAWRStatnangaaggtaaigawSGSRSSAAQSVNAYAPAPKGRDNFVAHHGDAAARV 185
Cdd:COG1705    82 SAAKSATEAGGGLASANAAATSAAALA------------------ASLSGAAALAASATAAASASPEEFIAKIAPAAQKA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 186 AQESGIPAAFMLGQAGHETGWGKSEIknaDGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGSYEESF 265
Cdd:COG1705   144 AKKYGVPASVLIAQAALESGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESF 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1592995644 266 RDYARLITSNPRYEKAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQS 316
Cdd:COG1705   221 RDYARLLKNNPRYAGALANAKDYEAFAKALQKAGYATDPKYADKLISIIES 271
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 25-315 1.18e-64

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 206.70  E-value: 1.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  25 NALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPGGLSDAITRQLA 104
Cdd:PRK12709   22 DALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATPSDGLFDSHTSKMYTSMLDQQLAQQMSSKGIGVADALMKQLL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 105 RTMGSEAAEDAEISVPSTLSMSRIAWRSTATNANGAA-GGTAAIGAWSGSRSSAAQSvnAYAPAPKGR------DNFVAH 177
Cdd:PRK12709  102 RNAGVAAGAQGDAGAGGMGGLGGNEGGLAAMNALAKAyANAANNGALAGTRGYSAGS--ALTPPLKGNggspdaDAFVDK 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 178 HGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAKFRA 257
Cdd:PRK12709  180 LAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVNGKPRRVVAKFRA 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1592995644 258 YGSYEESFRDYARLITSNPRYEKAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQ 315
Cdd:PRK12709  260 YDSYEHAMTDYANLLKNNPRYAGVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQ 317
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 26-315 1.39e-64

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 207.55  E-value: 1.39e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  26 ALKFAA-GENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPGGLSDAITRQLA 104
Cdd:PRK12712   25 ALKHSArGGADAGTLQAAARQFEAVFTQMVLKSMRDATPQDGLFDNEQSKLYMSMMDQQLAQQMSSRGIGLADVMVRQLA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 105 RTMGSE------AAEDAEISVPSTLSMSRIA-WRSTATNANGAAGGTAAIGAWSGSRSSAAQSVNAYAP----------- 166
Cdd:PRK12712  105 RATGTQmppgmnAAGGATAGSAADAEMARLLdGRGAGAADADAGDLPAIGTIVPGQAWNPTAGLRQYQPqayadqgqged 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 167 --------APKGRDNFVAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEV 238
Cdd:PRK12712  185 rlgrlpddAPAHVSAFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGSTTFNVFGIKAGANWKGRVAEV 264

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1592995644 239 TTTEYIDGVARKVTAKFRAYGSYEESFRDYARLITSNPRYeKAMGKTDSALAYATELQKAGYATDPEYASKLSRAIQ 315
Cdd:PRK12712  265 TTTEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRY-AGVVSAASADEAAHGLQRAGYATDPAYGHKLVKIMK 340
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
30-326 7.21e-38

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 138.94  E-value: 7.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  30 AAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLdSAQGNLSTDMLDQQLSVAMS-GQPGGLSDAITRQLARTMG 108
Cdd:PRK12711   12 PSTKADPAKIDKVSRQLEGQFAQMLVKSMRDASSGDPMF-PGENQMFREMYDQQMAKALTdGKGLGLSAMISKQLSGDTG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 109 SEA-------------------AEDAEISVP------------------------STLSMSR----IAWRSTATNANGAA 141
Cdd:PRK12711   91 GPAlntalntakaakayslvagKRDASLPLPardgaaagittssvaaaalsagnlSGIGMSQvldlIAGRTGAGEAGSDD 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 142 GG----TAAIGAWSGSRSSAAQSVNAYAPAPKGR-----------DNFVAHHGDAAARVAQESGIPAAFMLGQAGHETGW 206
Cdd:PRK12711  171 AAalswPSANDRWSDVAASDAADANAAVNASAAStaaaslgertpEGFVAKIWTHAQKAARELGVDPRALVAQAALETGW 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 207 GKSEIknADGSNAHNLFGIKAgKGWTGKVAEVTTTEYIDGVARKVTAKFRAYGSYEESFRDYARLITSNPRYEKAMGKTD 286
Cdd:PRK12711  251 GRRGI--GNGGDSNNLFGIKA-TGWNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGT 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1592995644 287 SALAYATELQKAGYATDPEYASKLSR-----AIQSAVQSAARAQA 326
Cdd:PRK12711  328 DIKGFARGLQQAGYATDPGYAAKIAAiangpTIDRAVAAIGNAAA 372
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 22-310 7.01e-34

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 126.06  E-value: 7.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  22 RSLNALKFAAGENSPQAAKETAKQLESLFMREMIKSMReatMKSGLLDSAQ----GNLST--DMLDQQLSVAMSGQPG-G 94
Cdd:PRK12710   12 QGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMR---MGQHFLDESSpfsgKNEATfqEMLDTQYASTIAESKGiG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  95 LSDAITRQLARTMGSEAaeDAEISVPSTLSMSRIawrstatnangaaggtaaigawsgsrSSAAQSVNAYapapkgrDNF 174
Cdd:PRK12710   89 LAALLAKQLENSVGDKA--NNPVNSSTEVSNTKV--------------------------TNSEESLSVV-------DDF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 175 VAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNAHNLFGIKAGKGWTGKVAEVTTTEYIDGVARKVTAK 254
Cdd:PRK12710  134 VKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKINAS 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1592995644 255 FRAYGSYEESFRDYARLITSNPRYEKAMGKTDSALAYATELQKAGYATDPEYASKL 310
Cdd:PRK12710  214 FRKYPSIEHSFHDYVSLIKGSERYQMALANAENPEIYVSELNKAGYATDPNYSNKI 269
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 165-310 1.47e-30

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: 117.53  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 165 APAPK-GRDNFVAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIknadGSNAHNLFGIKAgKGWTGKVA----EVT 239
Cdd:NF038016  153 PTVPRgTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGL----TREDHNYFGIKC-FGSPGPIAvgcrSYA 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1592995644 240 TTEY-IDGVARKVTAKFRAYGSYEESFRDYARLITSNPRYEKAMGKTDSALAYATELQKAGYATDPEYASKL 310
Cdd:NF038016  228 TFECsPTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQFAREIHKAGYATDPTYADKL 299
FlgJ1 COG3951
Rod binding protein domain [Cell motility];
22-112 3.27e-30

Rod binding protein domain [Cell motility];


Pssm-ID: 443151 [Multi-domain]  Cd Length: 107  Bit Score: 110.40  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  22 RSLNALKFAAGENSPQAAKETAKQLESLFMREMIKSMREATMKSGLLDSAQGNLSTDMLDQQLSVAMSGQPG-GLSDAIT 100
Cdd:COG3951    16 QSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVPEDGLFGSQAEDMFRDMLDQQLAKELAKGGGlGLADMIY 95

                          90
                  ....*....|..
gi 1592995644 101 RQLARTMGSEAA 112
Cdd:COG3951    96 RQLSRQQEAAAA 107
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 166-315 2.36e-25

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 99.05  E-value: 2.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644  166 PAPKGRDNFVAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKnadgSNAHNLFGIKAgkGWTGKVAEVTTTEYID 245
Cdd:smart00047   3 LAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLA----KKYNNLFGIKG--AYDGRPVRMGTLEYLN 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1592995644  246 GVARKVTAKFRAYgsYEESFRDYAR-LITSNPRYEKAMGktdsalayATELQKAGYATDPEYASKLSRAIQ 315
Cdd:smart00047  77 GGWVTVKAAFRGY--FGEKFIDYAYvLRGQNPLYKKRWG--------SNALQTAGYATDPDYAKKLIRIIA 137
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 179-274 3.14e-24

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: 94.18  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 179 GDAAARVAQESGIPAAFMLGQAGHETGWGKSEIknadGSNAHNLFGIKAgkGWTGKVAeVTTTEYidgvarKVTAKFRAY 258
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRL----AKESNNLFGIKA--SWKGKVA-YDTDEV------TVAARFRKY 67

                          90
                  ....*....|....*..
gi 1592995644 259 GSYEESFRD-YARLITS 274
Cdd:pfam01832  68 DSVEESIRDyYAEKLIA 84
PRK08581 PRK08581
amidase domain-containing protein;
174-315 1.27e-14

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 74.44  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 174 FVAHHGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKNadgSNAHNLFGIKAGkgWTGKVAEVTTTEYIDGVARKVTA 253
Cdd:PRK08581  323 FIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAK---SPNHNLFGIKGA--YEGNSVSFNTLEADGNQLYSINA 397

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1592995644 254 KFRAYGSYEESFRDYARL----ITSNPRYEKAMGKTDsALAY--ATELQKAGYATDPEYASKLSRAIQ 315
Cdd:PRK08581  398 GFRKYPSTKESLEDYADLikngIDGNSTIYKPTWKSE-AKSYkdATSHLSKTYATDPNYAKKLNSIIK 464
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
181-314 1.84e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 70.88  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 181 AAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGsnaHNLFGIKA---GKGWTGKVAEVTTTeyidGVARKVTAKFRA 257
Cdd:PRK06347  160 SSSQIAAENDLYASVMIAQAILESAYGTSELGSAPN---YNLFGIKGaynGQSYTKQTLEDDGK----GNYYTITAKFRK 232

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1592995644 258 YGSYEESFRDYARLITSNPR-----YEKAMGKTDSALAYATELQKAGYATDPEYASKLSRAI 314
Cdd:PRK06347  233 YPSYHQSLEDYAQVIRKGPSwnpnyYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLI 294
Rod-binding pfam10135
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ...
 56-102 4.56e-08

Rod binding protein; Members of this family are involved in the assembly of the prokaryotic flagellar rod.


Pssm-ID: 431078 [Multi-domain]  Cd Length: 50  Bit Score: 48.74  E-value: 4.56e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592995644  56 KSMREAT-MKSGLLD-SAQGNLSTDMLDQQLSVAMSGQPG-GLSDAITRQ 102
Cdd:pfam10135   1 KSMRKTVpKEDGLFDgSEAEDMFRDMLDQQLAKQLAKGGGlGLADMLYRQ 50
LytD COG4193
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
178-227 1.65e-05

Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 443347 [Multi-domain]  Cd Length: 423  Bit Score: 46.12  E-value: 1.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1592995644 178 HGDAAARVAQESGIPAAFMLGQAGHETGWGKSEIKNADGSNA---HNLFGIKA 227
Cdd:COG4193   274 KGQAFIEAAKKYGVNPLYLASHALLETGNGTSKLAKGVEVNGktyYNLFGIGA 326
flgJ PRK12708
peptidoglycan hydrolase; Reviewed
 38-110 5.47e-05

peptidoglycan hydrolase; Reviewed


Pssm-ID: 139168 [Multi-domain]  Cd Length: 134  Bit Score: 42.52  E-value: 5.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1592995644  38 AAKETAKQLESLFMREMIKSMREAT----MKSGLLDSAQGNLSTDMLDQQLSVAMSGQPG-GLSDAITRQLARTMGSE 110
Cdd:PRK12708   27 ALKLAAQQFEAQFLQTVLKQMRSASdvmaDEDDPFNSKNQGMYRDFYDAELASRLSSQRSmGLAEVMIKQLSSKLKSA 104
PRK10356 PRK10356
protein bax;
191-279 6.05e-04

protein bax;


Pssm-ID: 182404  Cd Length: 274  Bit Score: 41.01  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592995644 191 IPAAFMLGQAGHETGWGKSEIknadGSNAHNLFGIKAGKGWTGKvaevtTTEYIDGvarkvtakFRAYGSYEESFRDYAR 270
Cdd:PRK10356  149 IPTSMVATMAAAESGWGTSKL----ARNNNNLFGMKCMKGRCTN-----APGKVKG--------YSQFSSVKESVSAYVT 211


                  ....*....
gi 1592995644 271 LITSNPRYE 279
Cdd:PRK10356  212 NLNTHPAYS 220
 
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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