|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
1-315 |
2.29e-173 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 482.84 E-value: 2.29e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 1 MADMQSLTSSAFDSRSLNELKRQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQE 80
Cdd:PRK05684 1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 81 M-GKRGLGLAETIVKQMQPAT--APDEKAGTVPMKLDNSFILStsgatpLPAQQLEQIVRKAMPRlPPVASPTGLPSDSR 157
Cdd:PRK05684 81 LsAGGGLGLADMMVKQLSPEQspAPEESAGAVPMKFDLETVQS------YQNQALAQLVRKAIPQ-PPLASDKPLFGSSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 158 EFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKVR 237
Cdd:PRK05684 154 DFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVK 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497932201 238 ASFRVYNSYFEALTDYVKLLTKNPRYAAVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQFKSMGDKVVKAYSQD 315
Cdd:PRK05684 234 AAFRVYDSYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHD 311
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
10-302 |
1.34e-120 |
|
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: 348.38 E-value: 1.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 10 SAFDSRSLNELKRQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQEMGKR-GLGL 88
Cdd:TIGR02541 1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANgGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 89 AETIVKQMQPATAPDEKAGTVPMKLDNSFILSTSGATPL--PAQQLEQIVRKAMPRlpPVASPTGLPSDSREFIAQLTQP 166
Cdd:TIGR02541 81 ADMIVAQLTKGQGNEPSEGAARGAAPSPLVYRPRLDPKPrrIVKALIESVELSRPR--GRSHAESVPGHPKSFVNSMLPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 167 AQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKVRASFRVYNSY 246
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 497932201 247 FEALTDYVKLLTKNPRYAAVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQFK 302
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
22-304 |
5.37e-71 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 221.38 E-value: 5.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 22 RQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQEMGKRGLGLAETIVKQMQPATA 101
Cdd:COG1705 2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 102 PDEKAGTVPMKLDNSFILSTSGATPLPAQQLEQIVRKAMPRLPPVASPtglpsdsREFIAQLTQPAQAASQQSGIPHHLI 181
Cdd:COG1705 82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASP-------EEFIAKIAPAAQKAAKKYGVPASVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 182 LAQAALESGWGQRQIltrDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKVRASFRVYNSYFEALTDYVKLLTKNP 261
Cdd:COG1705 155 IAQAALESGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNP 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497932201 262 RYA-AVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQFKSM 304
Cdd:COG1705 232 RYAgALANAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLT 275
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
153-306 |
7.08e-42 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 142.19 E-value: 7.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 153 PSDSREFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQIltrdGKPSYNVFGIKasGDWKGDTTDIMTTEYEQGE 232
Cdd:smart00047 5 GGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKL----AKKYNNLFGIK--GAYDGRPVRMGTLEYLNGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497932201 233 AKKVRASFRVYNSYFEALTDYVkLLTKNPRYAAVTnassaeqGAQALQAAGYATDPKYAQKLVGMIQQFKSMGD 306
Cdd:smart00047 79 WVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKRW-------GSNALQTAGYATDPDYAKKLIRIIALYDEKLK 144
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
98-301 |
4.17e-31 |
|
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: 118.69 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 98 PATAPDEKAGTVPMKLDNSFILSTSGATPLPAQQLEQIVRKAMPRLPPV--ASPTGLPSDSREFIAQLTQPAQAASQQSG 175
Cdd:NF038016 100 VGTVANGATVTVECQVWGQEVDGTGVWYRLGDGRYVSAAYVRRPWLPWCgqDPPTVPRGTPAQFIAAVAPPAQQSQRATG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 176 IPHHLILAQAALESGWGqRQILTRDGKpsyNVFGIKASGDwKGDTT----DIMTTEYEQ-GEAKKVRASFRVYNSYFEAL 250
Cdd:NF038016 180 VPASVTIAQAILESGWG-RSGLTREDH---NYFGIKCFGS-PGPIAvgcrSYATFECSPtGGCFDTTATFRAYASAADSF 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497932201 251 TDYVKLLTKNPRYA-AVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQF 301
Cdd:NF038016 255 RDHGRFLSVNSRYApAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQY 306
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
165-302 |
2.76e-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: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 165 QPAQAASQQSGIPHHLILAQAALESGWGQrqilTRDGKPSYNVFGIKASgdWKGDTTdIMTTEYeqgeakKVRASFRVYN 244
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGT----SRLAKESNNLFGIKAS--WKGKVA-YDTDEV------TVAARFRKYD 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 497932201 245 SYFEALTDYvklltknpryaavtnassaeqgaqalqaagyatdpkYAQKLVGMIQQFK 302
Cdd:pfam01832 69 SVEESIRDY------------------------------------YAEKLIAIIERYN 90
|
|
| KREPA2 |
cd23959 |
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ... |
99-174 |
3.99e-03 |
|
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.
Pssm-ID: 467780 [Multi-domain] Cd Length: 424 Bit Score: 38.70 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497932201 99 ATAPDEKAGTV-PMKLDNSFILSTSGATPLPAQQLeQIVRKAMPRLPPVaSPTG-LPSDSREFIAQLTQPAQAASQQS 174
Cdd:cd23959 100 AMAPDESLGPFrAARVPNPFSASSSTQRETHKTAQ-VAPPKAEPQTAPV-TPFGqLPMFGQHPPPAKPLPAAAAAQQS 175
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
1-315 |
2.29e-173 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 482.84 E-value: 2.29e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 1 MADMQSLTSSAFDSRSLNELKRQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQE 80
Cdd:PRK05684 1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 81 M-GKRGLGLAETIVKQMQPAT--APDEKAGTVPMKLDNSFILStsgatpLPAQQLEQIVRKAMPRlPPVASPTGLPSDSR 157
Cdd:PRK05684 81 LsAGGGLGLADMMVKQLSPEQspAPEESAGAVPMKFDLETVQS------YQNQALAQLVRKAIPQ-PPLASDKPLFGSSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 158 EFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKVR 237
Cdd:PRK05684 154 DFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVK 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497932201 238 ASFRVYNSYFEALTDYVKLLTKNPRYAAVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQFKSMGDKVVKAYSQD 315
Cdd:PRK05684 234 AAFRVYDSYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHD 311
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
10-302 |
1.34e-120 |
|
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: 348.38 E-value: 1.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 10 SAFDSRSLNELKRQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQEMGKR-GLGL 88
Cdd:TIGR02541 1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANgGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 89 AETIVKQMQPATAPDEKAGTVPMKLDNSFILSTSGATPL--PAQQLEQIVRKAMPRlpPVASPTGLPSDSREFIAQLTQP 166
Cdd:TIGR02541 81 ADMIVAQLTKGQGNEPSEGAARGAAPSPLVYRPRLDPKPrrIVKALIESVELSRPR--GRSHAESVPGHPKSFVNSMLPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 167 AQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKVRASFRVYNSY 246
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 497932201 247 FEALTDYVKLLTKNPRYAAVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQFK 302
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-300 |
4.64e-89 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 269.95 E-value: 4.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 11 AFDSRSLNELKRQASNDPKGQALQ-VARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQEMGKRGLGLA 89
Cdd:PRK12712 17 ALDTQGFEALKHSARGGADAGTLQaAARQFEAVFTQMVLKSMRDATPQDGLFDNEQSKLYMSMMDQQLAQQMSSRGIGLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 90 ETIVKQMQPATAPDEKAGTVPM---------KLDNSFILSTSGATPLPAQQLEQI----------------VRKAMP--- 141
Cdd:PRK12712 97 DVMVRQLARATGTQMPPGMNAAggatagsaaDAEMARLLDGRGAGAADADAGDLPaigtivpgqawnptagLRQYQPqay 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 142 --------RLPPVasPTGLPSDSREFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKAS 213
Cdd:PRK12712 177 adqgqgedRLGRL--PDDAPAHVSAFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGSTTFNVFGIKAG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 214 GDWKGDTTDIMTTEYEQGEAKKVRASFRVYNSYFEALTDYVKLLTKNPRYAAVTNASSAEQGAQALQAAGYATDPKYAQK 293
Cdd:PRK12712 255 ANWKGRVAEVTTTEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAGYATDPAYGHK 334
|
....*..
gi 497932201 294 LVGMIQQ 300
Cdd:PRK12712 335 LVKIMKK 341
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
10-303 |
5.51e-85 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 259.29 E-value: 5.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 10 SAFDSRSLNELKRQASNDPKGQALQ--VARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQEMGKRGLG 87
Cdd:PRK12713 15 SVFDLGRLADLKRDAVKAPDGQRQQteVARQFEALFLQMMLKRMREATPKEGLFDSQQTEMLQGMADEQLALQLASPGIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 88 LAETIVKQMQ---------PATAPDEK-----AGTV-PMKLDNSFILSTSGATPLPAQQ---LEQIVRKAMPRLPPVASP 149
Cdd:PRK12713 95 LAQALLGQMQqgqppvpaaAAAGGDAAaaralAGTAaPAPLVRDLRGNYVQPDPAPRREvnaLLDVLRSNRARDRAMAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 150 TGLPSDSREFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKASGDWKGDTTDIMTTEYE 229
Cdd:PRK12713 175 EGAPSHVVDFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVMTTEYV 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497932201 230 QGEAKKVRASFRVYNSYFEALTDYVKLLTKNPRYAAVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQFKS 303
Cdd:PRK12713 255 DGVAQKLVQPFRAYSSYEESFSDYARLIGNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRT 328
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-300 |
2.42e-82 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 252.15 E-value: 2.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 11 AFDSRSLNELKRQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQEMGKRGLGLAE 90
Cdd:PRK12709 15 ALDVQGFDALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATPSDGLFDSHTSKMYTSMLDQQLAQQMSSKGIGVAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 91 TIVKQ------MQPATAPDEKAGTVPMKLDNSFILSTSGATPLPAQQLEQIVRKAMPR--------LPPVASPTGLPsDS 156
Cdd:PRK12709 95 ALMKQllrnagVAAGAQGDAGAGGMGGLGGNEGGLAAMNALAKAYANAANNGALAGTRgysagsalTPPLKGNGGSP-DA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 157 REFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKV 236
Cdd:PRK12709 174 DAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVNGKPRRV 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497932201 237 RASFRVYNSYFEALTDYVKLLTKNPRYAAVTNAS-SAEQGAQALQAAGYATDPKYAQKLVGMIQQ 300
Cdd:PRK12709 254 VAKFRAYDSYEHAMTDYANLLKNNPRYAGVLNASrSVEGFAHGMQKAGYATDPHYAKKLISIMQQ 318
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
22-304 |
5.37e-71 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 221.38 E-value: 5.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 22 RQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQEMGKRGLGLAETIVKQMQPATA 101
Cdd:COG1705 2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 102 PDEKAGTVPMKLDNSFILSTSGATPLPAQQLEQIVRKAMPRLPPVASPtglpsdsREFIAQLTQPAQAASQQSGIPHHLI 181
Cdd:COG1705 82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASP-------EEFIAKIAPAAQKAAKKYGVPASVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 182 LAQAALESGWGQRQIltrDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKVRASFRVYNSYFEALTDYVKLLTKNP 261
Cdd:COG1705 155 IAQAALESGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNP 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497932201 262 RYA-AVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQFKSM 304
Cdd:COG1705 232 RYAgALANAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLT 275
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
153-306 |
7.08e-42 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 142.19 E-value: 7.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 153 PSDSREFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQIltrdGKPSYNVFGIKasGDWKGDTTDIMTTEYEQGE 232
Cdd:smart00047 5 GGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKL----AKKYNNLFGIK--GAYDGRPVRMGTLEYLNGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497932201 233 AKKVRASFRVYNSYFEALTDYVkLLTKNPRYAAVTnassaeqGAQALQAAGYATDPKYAQKLVGMIQQFKSMGD 306
Cdd:smart00047 79 WVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKRW-------GSNALQTAGYATDPDYAKKLIRIIALYDEKLK 144
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
7-294 |
5.92e-41 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 147.03 E-value: 5.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 7 LTSSAFDsrslneLKRQASNDPkGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQtKLFTSMYDQQIAQEMGK-RG 85
Cdd:PRK12711 3 IAASPID------LNPSTKADP-AKIDKVSRQLEGQFAQMLVKSMRDASSGDPMFPGEN-QMFREMYDQQMAKALTDgKG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 86 LGLAETIVKQMQPAT-APDEKAGTVPMKLDNSFILST---SGATPLPAQQLEQIVRKAMPR------------------L 143
Cdd:PRK12711 75 LGLSAMISKQLSGDTgGPALNTALNTAKAAKAYSLVAgkrDASLPLPARDGAAAGITTSSVaaaalsagnlsgigmsqvL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 144 PPVASPTG------------------------LPSDSRE------------------------FIAQLTQPAQAASQQSG 175
Cdd:PRK12711 155 DLIAGRTGageagsddaaalswpsandrwsdvAASDAADanaavnasaastaaaslgertpegFVAKIWTHAQKAARELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 176 IPHHLILAQAALESGWGQRQIltRDGKPSYNVFGIKASGdWKGDTTDIMTTEYEQGEAKKVRASFRVYNSYFEALTDYVK 255
Cdd:PRK12711 235 VDPRALVAQAALETGWGRRGI--GNGGDSNNLFGIKATG-WNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVR 311
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 497932201 256 LLTKNPRYAAVTNASSAEQG-AQALQAAGYATDPKYAQKL 294
Cdd:PRK12711 312 LLKNNSRYQQALQAGTDIKGfARGLQQAGYATDPGYAAKI 351
|
|
| FlgJ1 |
COG3951 |
Rod binding protein domain [Cell motility]; |
1-105 |
1.63e-35 |
|
Rod binding protein domain [Cell motility];
Pssm-ID: 443151 [Multi-domain] Cd Length: 107 Bit Score: 124.26 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 1 MADMQSLTSS-AFDSRSLNELKRQASNDPKGQALQVARQVEGMFVQMMLKSMREALPQDGIMGNEQTKLFTSMYDQQIAQ 79
Cdd:COG3951 1 MSISSSLSSSlALDAQSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVPEDGLFGSQAEDMFRDMLDQQLAK 80
|
90 100
....*....|....*....|....*..
gi 497932201 80 EM-GKRGLGLAETIVKQMQPATAPDEK 105
Cdd:COG3951 81 ELaKGGGLGLADMIYRQLSRQQEAAAA 107
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
4-297 |
1.15e-33 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 125.29 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 4 MQSLTSSAFdsRSLNELKRQASNDPKGQALQVARQVEGMFVQMMLKSMREA---LPQDGIMGNEQTKLFTSMYDQQIAQE 80
Cdd:PRK12710 3 IQSIATSDF--QGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGqhfLDESSPFSGKNEATFQEMLDTQYAST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 81 MGK-RGLGLAETIVKQMQpatapdEKAGTVPMKLDNSfilSTSGATPLPAQQLEQIvrkamprlppvasptglpSDSREF 159
Cdd:PRK12710 81 IAEsKGIGLAALLAKQLE------NSVGDKANNPVNS---STEVSNTKVTNSEESL------------------SVVDDF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 160 IAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQILTRDGKPSYNVFGIKASGDWKGDTTDIMTTEYEQGEAKKVRAS 239
Cdd:PRK12710 134 VKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKINAS 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 497932201 240 FRVYNSYFEALTDYVKLLTKNPRYA-AVTNASSAEQGAQALQAAGYATDPKYAQKLVGM 297
Cdd:PRK12710 214 FRKYPSIEHSFHDYVSLIKGSERYQmALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
98-301 |
4.17e-31 |
|
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: 118.69 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 98 PATAPDEKAGTVPMKLDNSFILSTSGATPLPAQQLEQIVRKAMPRLPPV--ASPTGLPSDSREFIAQLTQPAQAASQQSG 175
Cdd:NF038016 100 VGTVANGATVTVECQVWGQEVDGTGVWYRLGDGRYVSAAYVRRPWLPWCgqDPPTVPRGTPAQFIAAVAPPAQQSQRATG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 176 IPHHLILAQAALESGWGqRQILTRDGKpsyNVFGIKASGDwKGDTT----DIMTTEYEQ-GEAKKVRASFRVYNSYFEAL 250
Cdd:NF038016 180 VPASVTIAQAILESGWG-RSGLTREDH---NYFGIKCFGS-PGPIAvgcrSYATFECSPtGGCFDTTATFRAYASAADSF 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497932201 251 TDYVKLLTKNPRYA-AVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQF 301
Cdd:NF038016 255 RDHGRFLSVNSRYApAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQY 306
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
154-301 |
7.43e-22 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 96.01 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 154 SDSREFIAQLTQPAQAASQQSGIPHHLILAQAALESGWGQRQiLTRdgKPSYNVFGIKasGDWKGDTTDIMTTEYEQGEA 233
Cdd:PRK08581 318 KDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSA-LAK--SPNHNLFGIK--GAYEGNSVSFNTLEADGNQL 392
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497932201 234 KKVRASFRVYNSYFEALTDYVKLLTK----NPRYAAVT---NASSAEQGAQALQAAgYATDPKYAQKLVGMIQQF 301
Cdd:PRK08581 393 YSINAGFRKYPSTKESLEDYADLIKNgidgNSTIYKPTwksEAKSYKDATSHLSKT-YATDPNYAKKLNSIIKHY 466
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
165-302 |
2.76e-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: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 165 QPAQAASQQSGIPHHLILAQAALESGWGQrqilTRDGKPSYNVFGIKASgdWKGDTTdIMTTEYeqgeakKVRASFRVYN 244
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGT----SRLAKESNNLFGIKAS--WKGKVA-YDTDEV------TVAARFRKYD 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 497932201 245 SYFEALTDYvklltknpryaavtnassaeqgaqalqaagyatdpkYAQKLVGMIQQFK 302
Cdd:pfam01832 69 SVEESIRDY------------------------------------YAEKLIAIIERYN 90
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
97-301 |
1.91e-15 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 76.66 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 97 QPATAPDEKAGTVPMKLDNSFILsTSGATPLPAQQLEQivrkamprlppvaspTGLPSDSRefIAQLTQPAQAASQQSGI 176
Cdd:PRK06347 105 QPAAKQVEKAPAEPATVSNPDNA-TSSSTPATYNLLQK---------------SALRSGAT--VQSFIQTIQASSSQIAA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 177 PHHL----ILAQAALESGWGQRQIltrDGKPSYNVFGIKasGDWKGDTTDIMTTEYE-QGEAKKVRASFRVYNSYFEALT 251
Cdd:PRK06347 167 ENDLyasvMIAQAILESAYGTSEL---GSAPNYNLFGIK--GAYNGQSYTKQTLEDDgKGNYYTITAKFRKYPSYHQSLE 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497932201 252 DYVKLLTKNPR-----YAAV--TNASSAEQGAQALQAAgYATDPKYAQKLVGMIQQF 301
Cdd:PRK06347 242 DYAQVIRKGPSwnpnyYSKVwkSNTTSYKDATKALTGT-YATDTAYATKLNDLISRY 297
|
|
| Rod-binding |
pfam10135 |
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ... |
49-95 |
1.66e-10 |
|
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: 55.68 E-value: 1.66e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 497932201 49 KSMREALPQDGIM--GNEQTKLFTSMYDQQIAQEM-GKRGLGLAETIVKQ 95
Cdd:pfam10135 1 KSMRKTVPKEDGLfdGSEAEDMFRDMLDQQLAKQLaKGGGLGLADMLYRQ 50
|
|
| LytD |
COG4193 |
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]; |
170-307 |
1.97e-07 |
|
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
Pssm-ID: 443347 [Multi-domain] Cd Length: 423 Bit Score: 51.90 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 170 ASQQSGI-PHHLIlAQAALESGWGQRQI---LTRDGKPSYNVFGIKAsgdwkgdtTDimTTEYEQGE--AKKvRASFRVY 243
Cdd:COG4193 281 AAKKYGVnPLYLA-SHALLETGNGTSKLakgVEVNGKTYYNLFGIGA--------YD--SNPLENGAkyAYK-QGWTSPE 348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497932201 244 NSYFEA----LTDYVklltKNPRYAAVTNASSAEQGAQALQAAGYATDPKYAQKLVGMIQQF-KSMGDK 307
Cdd:COG4193 349 KAIVGGakfiGSNYI----NNTGYGQNTLYKMRWNPVNPGTNHQYATDPFWAEKIAGHMYRAyKKLKDY 413
|
|
| flgJ |
PRK12708 |
peptidoglycan hydrolase; Reviewed |
23-99 |
2.78e-05 |
|
peptidoglycan hydrolase; Reviewed
Pssm-ID: 139168 [Multi-domain] Cd Length: 134 Bit Score: 43.29 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497932201 23 QASNDPKGQALQVARQVEGMFVQMMLKSMREA----LPQDGIMGNEQTKLFTSMYDQQIAQEMGK-RGLGLAETIVKQMQ 97
Cdd:PRK12708 19 IPQNLEQGALKLAAQQFEAQFLQTVLKQMRSAsdvmADEDDPFNSKNQGMYRDFYDAELASRLSSqRSMGLAEVMIKQLS 98
|
..
gi 497932201 98 PA 99
Cdd:PRK12708 99 SK 100
|
|
| Bax |
COG2992 |
Uncharacterized FlgJ-related protein [General function prediction only]; |
176-210 |
3.29e-03 |
|
Uncharacterized FlgJ-related protein [General function prediction only];
Pssm-ID: 442231 Cd Length: 253 Bit Score: 38.37 E-value: 3.29e-03
10 20 30
....*....|....*....|....*....|....*.
gi 497932201 176 IPHHLILAQAALESGWGQ-RqiLTRDGkpsYNVFGI 210
Cdd:COG2992 119 IPPSLVLAQAANESGWGTsR--FAREG---NNLFGQ 149
|
|
| KREPA2 |
cd23959 |
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ... |
99-174 |
3.99e-03 |
|
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.
Pssm-ID: 467780 [Multi-domain] Cd Length: 424 Bit Score: 38.70 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497932201 99 ATAPDEKAGTV-PMKLDNSFILSTSGATPLPAQQLeQIVRKAMPRLPPVaSPTG-LPSDSREFIAQLTQPAQAASQQS 174
Cdd:cd23959 100 AMAPDESLGPFrAARVPNPFSASSSTQRETHKTAQ-VAPPKAEPQTAPV-TPFGqLPMFGQHPPPAKPLPAAAAAQQS 175
|
|
| |
