|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
12-392 |
7.93e-134 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 385.77 E-value: 7.93e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 12 PDSGSYSDLNRLNQLKVGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATevmAKDNPFNSQASKQYQDMHDQQLSVTLS 91
Cdd:PRK05684 6 SDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDAN---PKDGLMNSQQTKLYTSMYDQQIAQQLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 92 KeGGGIGLADVLIRQLSKQQEPSekpnpfaqvaqtegakwssnpnskiapvdptrndsqllnqrrlalpgrLAERAHAQV 171
Cdd:PRK05684 83 A-GGGLGLADMMVKQLSPEQSPA------------------------------------------------PEESAGAVP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 172 APANAQADQASQTGAIQPLVDLdwkpaiafAAPQdapltingveatAPSAPSKTRFSSPAEFIATMLPMAEKAAKRLGVE 251
Cdd:PRK05684 114 MKFDLETVQSYQNQALAQLVRK--------AIPQ------------PPLASDKPLFGSSDDFVARLSPPAQKAAQQSGVP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 252 PRFLVAQAALETGWGKSIIKQKDGTNSHNLFGIKATG-WNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLL 330
Cdd:PRK05684 174 HHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGsWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLL 253
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518172594 331 ENNDRYKpALQVAsasGNSERFVNELQRAGYATDPQYARKINQIARKVQTYQTIADASTSPA 392
Cdd:PRK05684 254 TNNPRYA-AVTQA---ASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHD 311
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
19-378 |
8.95e-87 |
|
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: 265.18 E-value: 8.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 19 DLNRLNQLKVGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATEvmaKDNPFNSQASKQYQDMHDQQLSVTLSkEGGGIG 98
Cdd:TIGR02541 4 DAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATP---KDGLFDSQQTRFYTQMLDQQMAQQLS-ANGGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 99 LADVLIRQLSKQQ--EPSEkpnpfaqvAQTEGAKWSSNPNSKIAPVDPTRNDSQLLNQRRLALPGRlaerahaqvapana 176
Cdd:TIGR02541 80 LADMIVAQLTKGQgnEPSE--------GAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRPRG-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 177 qadqasqtgaiqplvdldwkpaiafaapqdapltingveatapSAPSKTRFSSPAEFIATMLPMAEKAAKRLGVEPRFLV 256
Cdd:TIGR02541 138 -------------------------------------------RSHAESVPGHPKSFVNSMLPHARKAAQQLGVPPHLIL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 257 AQAALETGWGKSIIKQKDGTNSHNLFGIKATG-WNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLENNDR 335
Cdd:TIGR02541 175 AQAALESGWGQRQIRNADGSPSYNLFGIKASGsWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARLLNNNPR 254
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 518172594 336 YKPALQvasaSGNSERFVNELQRAGYATDPQYARKINQIARKV 378
Cdd:TIGR02541 255 YEAVLQ----QRSAESFARGLQRAGYATDPRYARKLLQVIQSL 293
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
146-382 |
1.16e-67 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 215.60 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 146 RNDSQLLNQRRLALPGRLAERAHAQVAPANAQADQASQTGAIQPLVdldwKPAIAFAAPQDAPLTINGVEATAPSAPSKT 225
Cdd:COG1705 49 SKGASSSQSLEGLASALGGGASALSSAAALALKSAAKSATEAGGGL----ASANAAATSAAALAASLSGAAALAASATAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 226 RFSSPAEFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWGKSIIkqkDGTNSHNLFGIKAT-GWNGASAKVTTTEYVNG 304
Cdd:COG1705 125 ASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSEL---DGSPSNNLFGIKAGgSWQGKSVEVTTTEYVNG 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518172594 305 KATKEVAGFRAYDSFEHSFNDYVRLLENNDRYKPALQVAsasGNSERFVNELQRAGYATDPQYARKINQIARKVQTYQ 382
Cdd:COG1705 202 KAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALANA---KDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
218-382 |
7.63e-36 |
|
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: 133.33 E-value: 7.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 218 APSAPSKTrfssPAEFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWGKSIIKQKDgtnsHNLFGIKATGWNGASA--- 294
Cdd:NF038016 152 PPTVPRGT----PAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTRED----HNYFGIKCFGSPGPIAvgc 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 295 -KVTTTEYV-NGKATKEVAGFRAYDSFEHSFNDYVRLLENNDRYKPALQVAsasGNSERFVNELQRAGYATDPQYARKIN 372
Cdd:NF038016 224 rSYATFECSpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYT---DDPDQFAREIHKAGYATDPTYADKLI 300
|
170
....*....|
gi 518172594 373 QIARKVQTYQ 382
Cdd:NF038016 301 GLMKQYNLYQ 310
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
229-374 |
4.09e-31 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 116.00 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 229 SPAEFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWGKSIIKqkdgTNSHNLFGIKATgWNGASAKVTTTEYVNGKATK 308
Cdd:smart00047 7 STLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLA----KKYNNLFGIKGA-YDGRPVRMGTLEYLNGGWVT 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518172594 309 EVAGFRAYdsFEHSFNDYVRLL-ENNDRYKPALQvasasgnserfVNELQRAGYATDPQYARKINQI 374
Cdd:smart00047 82 VKAAFRGY--FGEKFIDYAYVLrGQNPLYKKRWG-----------SNALQTAGYATDPDYAKKLIRI 135
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
239-326 |
1.79e-23 |
|
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: 93.41 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 239 PMAEKAAKRLGVEPRFLVAQAALETGWGKSiikqKDGTNSHNLFGIKAtGWNGASAkVTTTEYvngkatKEVAGFRAYDS 318
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGTS----RLAKESNNLFGIKA-SWKGKVA-YDTDEV------TVAARFRKYDS 69
|
....*...
gi 518172594 319 FEHSFNDY 326
Cdd:pfam01832 70 VEESIRDY 77
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
12-392 |
7.93e-134 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 385.77 E-value: 7.93e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 12 PDSGSYSDLNRLNQLKVGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATevmAKDNPFNSQASKQYQDMHDQQLSVTLS 91
Cdd:PRK05684 6 SDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDAN---PKDGLMNSQQTKLYTSMYDQQIAQQLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 92 KeGGGIGLADVLIRQLSKQQEPSekpnpfaqvaqtegakwssnpnskiapvdptrndsqllnqrrlalpgrLAERAHAQV 171
Cdd:PRK05684 83 A-GGGLGLADMMVKQLSPEQSPA------------------------------------------------PEESAGAVP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 172 APANAQADQASQTGAIQPLVDLdwkpaiafAAPQdapltingveatAPSAPSKTRFSSPAEFIATMLPMAEKAAKRLGVE 251
Cdd:PRK05684 114 MKFDLETVQSYQNQALAQLVRK--------AIPQ------------PPLASDKPLFGSSDDFVARLSPPAQKAAQQSGVP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 252 PRFLVAQAALETGWGKSIIKQKDGTNSHNLFGIKATG-WNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLL 330
Cdd:PRK05684 174 HHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGsWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLL 253
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518172594 331 ENNDRYKpALQVAsasGNSERFVNELQRAGYATDPQYARKINQIARKVQTYQTIADASTSPA 392
Cdd:PRK05684 254 TNNPRYA-AVTQA---ASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHD 311
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
19-378 |
8.95e-87 |
|
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: 265.18 E-value: 8.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 19 DLNRLNQLKVGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATEvmaKDNPFNSQASKQYQDMHDQQLSVTLSkEGGGIG 98
Cdd:TIGR02541 4 DAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATP---KDGLFDSQQTRFYTQMLDQQMAQQLS-ANGGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 99 LADVLIRQLSKQQ--EPSEkpnpfaqvAQTEGAKWSSNPNSKIAPVDPTRNDSQLLNQRRLALPGRlaerahaqvapana 176
Cdd:TIGR02541 80 LADMIVAQLTKGQgnEPSE--------GAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRPRG-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 177 qadqasqtgaiqplvdldwkpaiafaapqdapltingveatapSAPSKTRFSSPAEFIATMLPMAEKAAKRLGVEPRFLV 256
Cdd:TIGR02541 138 -------------------------------------------RSHAESVPGHPKSFVNSMLPHARKAAQQLGVPPHLIL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 257 AQAALETGWGKSIIKQKDGTNSHNLFGIKATG-WNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLENNDR 335
Cdd:TIGR02541 175 AQAALESGWGQRQIRNADGSPSYNLFGIKASGsWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARLLNNNPR 254
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 518172594 336 YKPALQvasaSGNSERFVNELQRAGYATDPQYARKINQIARKV 378
Cdd:TIGR02541 255 YEAVLQ----QRSAESFARGLQRAGYATDPRYARKLLQVIQSL 293
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
146-382 |
1.16e-67 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 215.60 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 146 RNDSQLLNQRRLALPGRLAERAHAQVAPANAQADQASQTGAIQPLVdldwKPAIAFAAPQDAPLTINGVEATAPSAPSKT 225
Cdd:COG1705 49 SKGASSSQSLEGLASALGGGASALSSAAALALKSAAKSATEAGGGL----ASANAAATSAAALAASLSGAAALAASATAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 226 RFSSPAEFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWGKSIIkqkDGTNSHNLFGIKAT-GWNGASAKVTTTEYVNG 304
Cdd:COG1705 125 ASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSEL---DGSPSNNLFGIKAGgSWQGKSVEVTTTEYVNG 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518172594 305 KATKEVAGFRAYDSFEHSFNDYVRLLENNDRYKPALQVAsasGNSERFVNELQRAGYATDPQYARKINQIARKVQTYQ 382
Cdd:COG1705 202 KAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALANA---KDYEAFAKALQKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
16-391 |
6.99e-64 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 208.06 E-value: 6.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 16 SYSDLNRLNQLK--VGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATevmAKDNPFNSQASKQYQDMHDQQLSVTLSKE 93
Cdd:PRK12713 15 SVFDLGRLADLKrdAVKAPDGQRQQTEVARQFEALFLQMMLKRMREAT---PKEGLFDSQQTEMLQGMADEQLALQLASP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 94 GggIGLADVLIRQLSKQQepsekPNPFAQVAQTEGAKWSSNPNSKIAPVDPTRNdsqllnqrrlaLPGRLAERAHAQVAP 173
Cdd:PRK12713 92 G--IGLAQALLGQMQQGQ-----PPVPAAAAAGGDAAAARALAGTAAPAPLVRD-----------LRGNYVQPDPAPRRE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 174 ANAQADQASQTGAIQPlvdldwkpaiAFAAPQDAPltingveatapsapsktrfSSPAEFIATMLPMAEKAAKRLGVEPR 253
Cdd:PRK12713 154 VNALLDVLRSNRARDR----------AMAAAEGAP-------------------SHVVDFVSRMSRAANVAAQQSGVPAR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 254 FLVAQAALETGWGKSIIKQKDGTNSHNLFGIKA-TGWNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLEN 332
Cdd:PRK12713 205 LILGQAALESGWGRRELRHEDGSTSYNLFGIKAgASWKGKVVNVMTTEYVDGVAQKLVQPFRAYSSYEESFSDYARLIGN 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 518172594 333 NDRYKPALQvasaSGNSERFVNELQRAGYATDPQYARKINQIARKVQTYQTIADASTSP 391
Cdd:PRK12713 285 SPRYEAVTQ----AGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRTSVARADFSGGL 339
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
38-375 |
8.26e-63 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 206.74 E-value: 8.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 38 VRKVAQEFESLFMNEMLKSMRSATevmAKDNPFNSQaSKQYQDMHDQQLSVTLSkEGGGIGLADVLIRQLSKQqepSEKP 117
Cdd:PRK12711 21 IDKVSRQLEGQFAQMLVKSMRDAS---SGDPMFPGE-NQMFREMYDQQMAKALT-DGKGLGLSAMISKQLSGD---TGGP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 118 NPFAQVAQTEGAK-WSSNPNSKIAPVD-PTRNDSQLLNQRRLALPGRLaERAHAQVAPANAQADQ-ASQTGAIQPLVD-- 192
Cdd:PRK12711 93 ALNTALNTAKAAKaYSLVAGKRDASLPlPARDGAAAGITTSSVAAAAL-SAGNLSGIGMSQVLDLiAGRTGAGEAGSDda 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 193 --LDWKPA---IAFAAPQDAPLTINGVEATAPS-APSKTRFSSPAEFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWG 266
Cdd:PRK12711 172 aaLSWPSAndrWSDVAASDAADANAAVNASAAStAAASLGERTPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 267 KSIIKqkDGTNSHNLFGIKATGWNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLENNDRYKPALQvasAS 346
Cdd:PRK12711 252 RRGIG--NGGDSNNLFGIKATGWNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQ---AG 326
|
330 340
....*....|....*....|....*....
gi 518172594 347 GNSERFVNELQRAGYATDPQYARKINQIA 375
Cdd:PRK12711 327 TDIKGFARGLQQAGYATDPGYAAKIAAIA 355
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
19-378 |
3.09e-62 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 202.85 E-value: 3.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 19 DLNRLNQLKVGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATevmAKDNPFNSQASKQYQDMHDQQLSVTLSKEGggIG 98
Cdd:PRK12709 17 DVQGFDALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDAT---PSDGLFDSHTSKMYTSMLDQQLAQQMSSKG--IG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 99 LADVLIRQLSKQQEPSEKPNPFAQVAQTEGAKWssnpnskiapvdptrndsqllNQRRLALPGRLAErahaqvAPANAQA 178
Cdd:PRK12709 92 VADALMKQLLRNAGVAAGAQGDAGAGGMGGLGG---------------------NEGGLAAMNALAK------AYANAAN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 179 DQASQTGAiqplvdldwkpaiAFAApqdapltingveATAPSAPSKTRFSSPAE--FIATMLPMAEKAAKRLGVEPRFLV 256
Cdd:PRK12709 145 NGALAGTR-------------GYSA------------GSALTPPLKGNGGSPDAdaFVDKLAAPAQAASAATGIPARFIV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 257 AQAALETGWGKSIIKQKDGTNSHNLFGIKAT-GWNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLENNDR 335
Cdd:PRK12709 200 GQAALESGWGKREIRGADGSTSYNVFGIKATkGWTGRTVSAVTTEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKNNPR 279
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 518172594 336 YKpalQVASASGNSERFVNELQRAGYATDPQYARKINQIARKV 378
Cdd:PRK12709 280 YA---GVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQI 319
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
24-380 |
2.21e-57 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 190.99 E-value: 2.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 24 NQLKVGKDrdgAENVRKVAQEFESLFMNEMLKSMRSATevmAKDNPFNSQASKQYQDMHDQQLSVTLSKEGggIGLADVL 103
Cdd:PRK12712 28 HSARGGAD---AGTLQAAARQFEAVFTQMVLKSMRDAT---PQDGLFDNEQSKLYMSMMDQQLAQQMSSRG--IGLADVM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 104 IRQLSKQQEPSEKPNpfaqVAQTEGAKWSSNPNSKIApvdptrndsqllnqrRLaLPGRLAerahaqvAPANAQADQASQ 183
Cdd:PRK12712 100 VRQLARATGTQMPPG----MNAAGGATAGSAADAEMA---------------RL-LDGRGA-------GAADADAGDLPA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 184 TGAIQPlvDLDWKPAIAFAA--PQDAPLTINGVEATAP---SAPSKTrfsspAEFIATMLPMAEKAAKRLGVEPRFLVAQ 258
Cdd:PRK12712 153 IGTIVP--GQAWNPTAGLRQyqPQAYADQGQGEDRLGRlpdDAPAHV-----SAFVARMAGPAEAASRASGVPARLIVGQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 259 AALETGWGKSIIKQKDGTNSHNLFGIKA-TGWNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLENNDRYK 337
Cdd:PRK12712 226 AALESGWGRREITHADGSTTFNVFGIKAgANWKGRVAEVTTTEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 518172594 338 PALQVASAsgnsERFVNELQRAGYATDPQYARKINQIARKVQT 380
Cdd:PRK12712 306 GVVSAASA----DEAAHGLQRAGYATDPAYGHKLVKIMKKVSA 344
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-390 |
6.92e-43 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 151.48 E-value: 6.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 11 TPDSGSYSDLNRLNQLKVGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATEVMAKDNPFNSQASKQYQDMHDQQLSVTL 90
Cdd:PRK12710 2 TIQSIATSDFQGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGQHFLDESSPFSGKNEATFQEMLDTQYASTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 91 SkEGGGIGLADVLIRQLSkqqepsekpnpfaqvaqtegakwssnpnskiapvdptrndsqllnqrrlalpgrlaerahaq 170
Cdd:PRK12710 82 A-ESKGIGLAALLAKQLE-------------------------------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 171 vapaNAQADQASqtgaiqplvdldwkpaiafaAPQDAPLTINGVEATApsapSKTRFSSPAEFIATMLPMAEKAAKRLGV 250
Cdd:PRK12710 99 ----NSVGDKAN--------------------NPVNSSTEVSNTKVTN----SEESLSVVDDFVKSVWPTAKQAASLIGL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 251 EPRFLVAQAALETGWGKSIIKQKDGTNSHNLFGIKaTGWNG--ASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVR 328
Cdd:PRK12710 151 DPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIK-TGSHSevESIQVKTTEYIADTPIKINASFRKYPSIEHSFHDYVS 229
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518172594 329 LLENNDRYKPALQVASasgNSERFVNELQRAGYATDPQYARKINQIARKVQTYQTIADASTS 390
Cdd:PRK12710 230 LIKGSERYQMALANAE---NPEIYVSELNKAGYATDPNYSNKILSIYHGDELNQAIQRCESS 288
|
|
| FlgJ1 |
COG3951 |
Rod binding protein domain [Cell motility]; |
11-116 |
9.64e-38 |
|
Rod binding protein domain [Cell motility];
Pssm-ID: 443151 [Multi-domain] Cd Length: 107 Bit Score: 131.97 E-value: 9.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 11 TPDSGSYSDLNRLNQLKVGKDRDGAENVRKVAQEFESLFMNEMLKSMRSATEvmaKDNPFNSQASKQYQDMHDQQLSVTL 90
Cdd:COG3951 6 SLSSSLALDAQSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVP---EDGLFGSQAEDMFRDMLDQQLAKEL 82
|
90 100
....*....|....*....|....*.
gi 518172594 91 SKeGGGIGLADVLIRQLSKQQEPSEK 116
Cdd:COG3951 83 AK-GGGLGLADMIYRQLSRQQEAAAA 107
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
218-382 |
7.63e-36 |
|
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: 133.33 E-value: 7.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 218 APSAPSKTrfssPAEFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWGKSIIKQKDgtnsHNLFGIKATGWNGASA--- 294
Cdd:NF038016 152 PPTVPRGT----PAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTRED----HNYFGIKCFGSPGPIAvgc 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 295 -KVTTTEYV-NGKATKEVAGFRAYDSFEHSFNDYVRLLENNDRYKPALQVAsasGNSERFVNELQRAGYATDPQYARKIN 372
Cdd:NF038016 224 rSYATFECSpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAYT---DDPDQFAREIHKAGYATDPTYADKLI 300
|
170
....*....|
gi 518172594 373 QIARKVQTYQ 382
Cdd:NF038016 301 GLMKQYNLYQ 310
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
229-374 |
4.09e-31 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 116.00 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 229 SPAEFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWGKSIIKqkdgTNSHNLFGIKATgWNGASAKVTTTEYVNGKATK 308
Cdd:smart00047 7 STLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLA----KKYNNLFGIKGA-YDGRPVRMGTLEYLNGGWVT 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518172594 309 EVAGFRAYdsFEHSFNDYVRLL-ENNDRYKPALQvasasgnserfVNELQRAGYATDPQYARKINQI 374
Cdd:smart00047 82 VKAAFRGY--FGEKFIDYAYVLrGQNPLYKKRWG-----------SNALQTAGYATDPDYAKKLIRI 135
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
239-326 |
1.79e-23 |
|
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: 93.41 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 239 PMAEKAAKRLGVEPRFLVAQAALETGWGKSiikqKDGTNSHNLFGIKAtGWNGASAkVTTTEYvngkatKEVAGFRAYDS 318
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGTS----RLAKESNNLFGIKA-SWKGKVA-YDTDEV------TVAARFRKYDS 69
|
....*...
gi 518172594 319 FEHSFNDY 326
Cdd:pfam01832 70 VEESIRDY 77
|
|
| flgJ |
PRK12708 |
peptidoglycan hydrolase; Reviewed |
9-130 |
1.36e-21 |
|
peptidoglycan hydrolase; Reviewed
Pssm-ID: 139168 [Multi-domain] Cd Length: 134 Bit Score: 89.51 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 9 RRTPDSGSYSDLNRLNQLKVGKDRDGAenVRKVAQEFESLFMNEMLKSMRSATEVMA-KDNPFNSQASKQYQDMHDQQLS 87
Cdd:PRK12708 1 MAINNSSPYLPGLNAGDLIPQNLEQGA--LKLAAQQFEAQFLQTVLKQMRSASDVMAdEDDPFNSKNQGMYRDFYDAELA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 518172594 88 VTLSKEgGGIGLADVLIRQLSKQQEPSEKPNPFAQVAQTEGAK 130
Cdd:PRK12708 79 SRLSSQ-RSMGLAEVMIKQLSSKLKSAPEVVALESQTLTTTAM 120
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
108-374 |
1.24e-14 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 75.59 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 108 SKQQEPS--EKPNPFAQVAQTEGAKWSSNPNSKIAP------VDPTRNDSQLLNQRRLALPGRLAERAHAQVAPANAQAD 179
Cdd:PRK08581 191 PNSPKPTqpNQSNSQPASDDTANQKSSSKDNQSMSDsaldsiLDQYSEDAKKTQKDYASQSKKDKTETSNTKNPQLPTQD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 180 QASQTGAIQPLVDLDWK--PAIAFAAPQDAPlTINGVEATAPSapSKTRFSSPAEFIATMLPMAEKAAKRLGVEPRFLVA 257
Cdd:PRK08581 271 ELKHKSKPAQSFENDVNqsNTRSTSLFETGP-SLSNNDDSGSF--NVVDSKDTRQFIKSIAKDAHRIGQDNDIYASVMIA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 258 QAALETGWGKSIIKQKDgtnSHNLFGIKATgWNGASAKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLE-----N 332
Cdd:PRK08581 348 QAILESDSGQSALAKSP---NHNLFGIKGA-YEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLIKngidgN 423
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518172594 333 NDRYKPALQvaSASGNSERFVNELQRAgYATDPQYARKINQI 374
Cdd:PRK08581 424 STIYKPTWK--SEAKSYKDATSHLSKT-YATDPNYAKKLNSI 462
|
|
| Rod-binding |
pfam10135 |
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ... |
55-106 |
2.06e-13 |
|
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: 64.15 E-value: 2.06e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 518172594 55 KSMRSATEvmAKDNPFN-SQASKQYQDMHDQQLSVTLSKeGGGIGLADVLIRQ 106
Cdd:pfam10135 1 KSMRKTVP--KEDGLFDgSEAEDMFRDMLDQQLAKQLAK-GGGLGLADMLYRQ 50
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
197-374 |
7.32e-10 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 60.48 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 197 PAIAFAAPQDAPLTI-NGVEATAPSAPS------KTRFSSPA---EFIATMLPMAEKAAKRLGVEPRFLVAQAALETGWG 266
Cdd:PRK06347 107 AAKQVEKAPAEPATVsNPDNATSSSTPAtynllqKSALRSGAtvqSFIQTIQASSSQIAAENDLYASVMIAQAILESAYG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 267 KSiikQKDGTNSHNLFGIKAtGWNGAS-AKVTTTEYVNGKATKEVAGFRAYDSFEHSFNDYVRLLENNDRYKPAL--QVA 343
Cdd:PRK06347 187 TS---ELGSAPNYNLFGIKG-AYNGQSyTKQTLEDDGKGNYYTITAKFRKYPSYHQSLEDYAQVIRKGPSWNPNYysKVW 262
|
170 180 190
....*....|....*....|....*....|.
gi 518172594 344 SASGNSERFVNELQRAGYATDPQYARKINQI 374
Cdd:PRK06347 263 KSNTTSYKDATKALTGTYATDTAYATKLNDL 293
|
|
| LytD |
COG4193 |
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]; |
243-374 |
2.75e-08 |
|
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
Pssm-ID: 443347 [Multi-domain] Cd Length: 423 Bit Score: 55.36 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 243 KAAKRLGVEPRFLVAQAALETGWGKSII---KQKDGTNSHNLFGIKATgwngasakvTTTEYVNGKATkevAGFRAYDSF 319
Cdd:COG4193 280 EAAKKYGVNPLYLASHALLETGNGTSKLakgVEVNGKTYYNLFGIGAY---------DSNPLENGAKY---AYKQGWTSP 347
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518172594 320 EHSF--------NDYVrlleNNDRYKpalqvasasGN---SERF--VNELQRAGYATDPQYARKINQI 374
Cdd:COG4193 348 EKAIvggakfigSNYI----NNTGYG---------QNtlyKMRWnpVNPGTNHQYATDPFWAEKIAGH 402
|
|
| PRK10927 |
PRK10927 |
cell division protein FtsN; |
94-225 |
1.72e-04 |
|
cell division protein FtsN;
Pssm-ID: 236797 [Multi-domain] Cd Length: 319 Bit Score: 43.13 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 94 GGGIGLADVLI---RQLSKQQEPSEKPNPfaqvAQTEGAKWSSN-PNSKIAPVDPTRNDSQLLNQRRLALPGRLAERAH- 168
Cdd:PRK10927 105 GGEVKTPEQLTpeqRQLLEQMQADMRQQP----TQLVEVPWNEQtPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWq 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518172594 169 -----AQVAPANAQADQASQTGAIQPLVDLDWKPAIAFA---APQDAPLTingveaTAPSAPSKT 225
Cdd:PRK10927 181 qqtrtSQAAPVQAQPRQSKPASTQQPYQDLLQTPAHTTAqskPQQAAPVT------RAADAPKPT 239
|
|
| PRK12790 |
PRK12790 |
flagellar rod assembly protein FlgJ; |
39-111 |
2.31e-04 |
|
flagellar rod assembly protein FlgJ;
Pssm-ID: 237203 [Multi-domain] Cd Length: 115 Bit Score: 40.57 E-value: 2.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518172594 39 RKVAQEFESLFMNEMLKSMRSAtevMAKDNPF-NSQASKQYQDMHDQQLSVTLSKeGGGIGLADVLIRQLSKQQ 111
Cdd:PRK12790 41 KATATDFEAMFLNSMFSQMTSG---LKGEGPFgDTVGTGVWRSMLTEQYSKSFAK-AGGVGISDDVFRTLILQQ 110
|
|
| PRK10356 |
PRK10356 |
protein bax; |
247-336 |
1.22e-03 |
|
protein bax;
Pssm-ID: 182404 Cd Length: 274 Bit Score: 40.24 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172594 247 RLGVEPRFLVA-QAALETGWGKSIIKQkdgtNSHNLFGIKATGWNGASAKvttteyvnGKatkeVAGFRAYDSFEHSFND 325
Cdd:PRK10356 145 RVDIIPTSMVAtMAAAESGWGTSKLAR----NNNNLFGMKCMKGRCTNAP--------GK----VKGYSQFSSVKESVSA 208
|
90
....*....|.
gi 518172594 326 YVRLLENNDRY 336
Cdd:PRK10356 209 YVTNLNTHPAY 219
|
|
|