|
Name |
Accession |
Description |
Interval |
E-value |
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
12-395 |
9.08e-76 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 251.19 E-value: 9.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 12 SSLSAVSATAYAQNATPNQVGMAMMRLNSALLDQAKAQTFGSGSLWASLRKDFRINEVNTELVRRHENKFAANSAYFDRT 91
Cdd:PRK10783 18 SSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRIREQKQKYLRNKSYLHDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 92 ISRSKPYMYHIANEVKKRNMPAEIALLPFIESAFVTKAKSHVGASGLWQFMPATGRHFGLEKTPLYDGRHDVYAATDAAL 171
Cdd:PRK10783 98 TLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 172 NYLQYLHGMF-GDWSLALAAYNWGEGNVGRAVNRARAQGLEPTYENLRMPNETRNYVPKLLAVRNIVANPQTFGMNISEI 250
Cdd:PRK10783 178 DMMQRLNKMFdGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLALSDILKNSKRYGVRLPTT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 251 SNQPYFKSVSIDKPIDNSTIARFANISESELLALNPGFNAPVFIPKNNRRLLLPVSAVSAFE---------KNYRNANPD 321
Cdd:PRK10783 258 DESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLReslasgeiaAVQSTLVAD 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1090946631 322 -TLMSWDIYTSLGNKKLNAIANDTGMSVAELKRLNGLSGSAISEGRSILVAKNSATQSQdiinfIDKDNtPDTYQ 395
Cdd:PRK10783 338 nTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRL-----ANNSD-SITYR 406
|
|
| MltD-like |
cd16894 |
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ... |
106-233 |
1.01e-61 |
|
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381615 [Multi-domain] Cd Length: 129 Bit Score: 201.98 E-value: 1.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 106 VKKRNMPAEIALLPFIESAFVTKAKSHVGASGLWQFMPATGRHFGLEKTPLYDGRHDVYAATDAALNYLQYLHGMFGDWS 185
Cdd:cd16894 1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFGDWL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1090946631 186 LALAAYNWGEGNVGRAVNRARAQGLEpTYENLRMPNETRNYVPKLLAV 233
Cdd:cd16894 81 LALAAYNAGEGRVRRAIKRAGTDKWE-DYYRLYLPAETRRYVPKFLAA 127
|
|
| MltF |
COG4623 |
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ... |
52-236 |
2.34e-41 |
|
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 443662 [Multi-domain] Cd Length: 421 Bit Score: 155.99 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 52 GSGSLWASLRKDFRINEVNTELVRRHENKFA----ANSAYFDRTISRSKPYMYHIANEVKKRNMPAE-IALLPFIESAFV 126
Cdd:COG4623 214 NDPSLLAALNEFFAKIKKGGTLARLYERYFGhvkrDTRAFLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 127 TKAKSHVGASGLWQFMPATGRHFGLektplyDGRHDVYAATDAALNYLQYLHGMF-------GDWSLALAAYNWGEGNVG 199
Cdd:COG4623 294 PRARSPTGARGLMQLMPATAKELGV------DDRLDPEQSIRAGAKYLRWLYDRFpeaidepDRWWFALAAYNAGPGHVQ 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1090946631 200 RAVNRARAQGLEPTY-------------ENLRMPNETRNYVPKLLAVRNI 236
Cdd:COG4623 368 DARRLAKKQGLDPDRwfdveksqpkyydTGYARGRETVNYVPNIRAYYDI 417
|
|
| SLT |
pfam01464 |
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ... |
102-209 |
1.10e-25 |
|
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
Pssm-ID: 396169 [Multi-domain] Cd Length: 114 Bit Score: 102.00 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 102 IANEVKKRNMPAEIALLPFIESAFVTKAKSHVGASGLWQFMPATGRHFGLEKTPLYDGRHDVYAATDAALNYLQYLHGMF 181
Cdd:pfam01464 2 IKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQY 81
|
90 100
....*....|....*....|....*....
gi 1090946631 182 G-DWSLALAAYNWGEGNVGRAVNRARAQG 209
Cdd:pfam01464 82 GgDLWLALAAYNAGPGRVRKWIKNAGAKD 110
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
582-699 |
5.93e-21 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 96.34 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 582 LARVNGQQNTQTAALAVGTHRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRVTAAPAKVRSNPVQN-VSYT 660
Cdd:PRK10783 327 IAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDsITYR 406
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1090946631 661 VRKGDTLNTIASRFNVDINDIRRWNRNTRT-VSPGQRLKL 699
Cdd:PRK10783 407 VRKGDSLSSIAKRHGVNIKDVMRWNSDTAKnLQPGDKLTL 446
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
489-642 |
9.49e-13 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 66.66 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 489 KAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQTVVTAESARAARIA 568
Cdd:COG1388 1 GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1090946631 569 ANTAKQQQRINARLARVNGQQNTQTAAlAVGTHRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRV 642
Cdd:COG1388 81 AAAARYTVKSGDTLSGIARRYGAAAAP-SPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
529-702 |
2.13e-12 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 65.50 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 529 ALVQSQPAEEPAATVAEATSEAKQVQTVVTAESARAARIAANTAKQQQRINARLARVNGQQNTQTAALAVGTHRVADGDT 608
Cdd:COG1388 14 AAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 609 LFNISKRYNlsvadliiannikgnnikkgqilrvtaapakvRSNPVQNVSYTVRKGDTLNTIASRFNVDINDIRRWNR-N 687
Cdd:COG1388 94 LSGIARRYG--------------------------------AAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGlS 141
|
170
....*....|....*
gi 1090946631 688 TRTVSPGQRLKLIGS 702
Cdd:COG1388 142 SDTIRPGQKLKIPAS 156
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
657-699 |
1.70e-11 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 59.42 E-value: 1.70e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1090946631 657 VSYTVRKGDTLNTIASRFNVDINDIRRWNR--NTRTVSPGQRLKL 699
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPliNPDCIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
659-699 |
1.35e-10 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 56.69 E-value: 1.35e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1090946631 659 YTVRKGDTLNTIASRFNVDINDIRRWNR--NTRTVSPGQRLKL 699
Cdd:smart00257 2 YTVKKGDTLSSIARRYGISVSDLLELNNilDPDNLQVGQKLKI 44
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
659-699 |
2.39e-10 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 55.87 E-value: 2.39e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1090946631 659 YTVRKGDTLNTIASRFNVDINDIRRWNR-NTRTVSPGQRLKL 699
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGlSSPNLYVGQKLKI 42
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
395-574 |
6.14e-10 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 62.75 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 395 QSNMP----AMSPIIASS---VAEPVKVAQTTVT--------NIVAPVVPqsSKPVDFIARSKAENVTSVAVTETKAQPQ 459
Cdd:PRK10811 822 QSPMPltvaCASPEMASGkvwIRYPVVRPQDVQVeeqreaeeVQVQPVVA--EVPVAAAVEPVVSAPVVEAVAEVVEEPV 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 460 VANAEVAAPVVAMTHTTAEPAATNVAEAPkaAILADLTAPSVAANDVAPTPAVESVA-VAPVQEERDDLMALVQSQPAEE 538
Cdd:PRK10811 900 VVAEPQPEEVVVVETTHPEVIAAPVTEQP--QVITESDVAVAQEVAEHAEPVVEPQDeTADIEEAAETAEVVVAEPEVVA 977
|
170 180 190
....*....|....*....|....*....|....*.
gi 1090946631 539 PAATVAEATSEAKQVQTVVTAESARAARIAANTAKQ 574
Cdd:PRK10811 978 QPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEH 1013
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
429-559 |
1.34e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 48.56 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 429 PQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMthTTAEPAATNVAEAPKAAIladltAPSVAANDVAP 508
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAA--AASAPAAPPAAAPPAPVA-----APAAAAPAAAP 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1090946631 509 TPAVESVAVAPVQEERD-DLMALVQSQPAEEPAATVAEATSEAKQVQTVVTA 559
Cdd:PRK14951 439 AAAPAAVALAPAPPAQAaPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
316-559 |
1.21e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 45.34 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 316 RNANPDTLMSWDIYTSLGNKKLNAIANDTGMSVAelkrlnglSGSAISEGRSILVAKNSATQSQDIINFIDKDNTPDTYQ 395
Cdd:pfam17823 40 QNASGDAVPRADNKSSEQ*NFCAATAAPAPVTLT--------KGTSAAHLNSTEVTAEHTPHGTDLSEPATREGAADGAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 396 SNMPAmspiiASSVAEPVKVAQTTVTNIVAPVVPQSSKPvdfiarskaenVTSVAVTETKAQPQVANAEVAAPVVAMTHT 475
Cdd:pfam17823 112 SRALA-----AAASSSPSSAAQSLPAAIAALPSEAFSAP-----------RAAACRANASAAPRAAIAAASAPHAASPAP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 476 TAEPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQT 555
Cdd:pfam17823 176 RTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALAT 255
|
....
gi 1090946631 556 VVTA 559
Cdd:pfam17823 256 LAAA 259
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
442-570 |
5.91e-03 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 39.49 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 442 KAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTTAEPAA--TNVAEAPKAAiladlTAPSVAANDVAPTPAVESVAVAP 519
Cdd:TIGR00601 65 KEKDFVVVMVSKPKTGTGKVAPPAATPTSAPTPTPSPPASpaSGMSAAPASA-----VEEKSPSEESATATAPESPSTSV 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1090946631 520 VQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQtvvtaesaRAARIAAN 570
Cdd:TIGR00601 140 PSSGSDAASTLVVGSERETTIEEIMEMGYEREEVE--------RALRAAFN 182
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
12-395 |
9.08e-76 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 251.19 E-value: 9.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 12 SSLSAVSATAYAQNATPNQVGMAMMRLNSALLDQAKAQTFGSGSLWASLRKDFRINEVNTELVRRHENKFAANSAYFDRT 91
Cdd:PRK10783 18 SSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRIREQKQKYLRNKSYLHDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 92 ISRSKPYMYHIANEVKKRNMPAEIALLPFIESAFVTKAKSHVGASGLWQFMPATGRHFGLEKTPLYDGRHDVYAATDAAL 171
Cdd:PRK10783 98 TLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 172 NYLQYLHGMF-GDWSLALAAYNWGEGNVGRAVNRARAQGLEPTYENLRMPNETRNYVPKLLAVRNIVANPQTFGMNISEI 250
Cdd:PRK10783 178 DMMQRLNKMFdGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLALSDILKNSKRYGVRLPTT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 251 SNQPYFKSVSIDKPIDNSTIARFANISESELLALNPGFNAPVFIPKNNRRLLLPVSAVSAFE---------KNYRNANPD 321
Cdd:PRK10783 258 DESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLReslasgeiaAVQSTLVAD 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1090946631 322 -TLMSWDIYTSLGNKKLNAIANDTGMSVAELKRLNGLSGSAISEGRSILVAKNSATQSQdiinfIDKDNtPDTYQ 395
Cdd:PRK10783 338 nTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRL-----ANNSD-SITYR 406
|
|
| MltD-like |
cd16894 |
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ... |
106-233 |
1.01e-61 |
|
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381615 [Multi-domain] Cd Length: 129 Bit Score: 201.98 E-value: 1.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 106 VKKRNMPAEIALLPFIESAFVTKAKSHVGASGLWQFMPATGRHFGLEKTPLYDGRHDVYAATDAALNYLQYLHGMFGDWS 185
Cdd:cd16894 1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFGDWL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1090946631 186 LALAAYNWGEGNVGRAVNRARAQGLEpTYENLRMPNETRNYVPKLLAV 233
Cdd:cd16894 81 LALAAYNAGEGRVRRAIKRAGTDKWE-DYYRLYLPAETRRYVPKFLAA 127
|
|
| MltF |
COG4623 |
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ... |
52-236 |
2.34e-41 |
|
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 443662 [Multi-domain] Cd Length: 421 Bit Score: 155.99 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 52 GSGSLWASLRKDFRINEVNTELVRRHENKFA----ANSAYFDRTISRSKPYMYHIANEVKKRNMPAE-IALLPFIESAFV 126
Cdd:COG4623 214 NDPSLLAALNEFFAKIKKGGTLARLYERYFGhvkrDTRAFLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 127 TKAKSHVGASGLWQFMPATGRHFGLektplyDGRHDVYAATDAALNYLQYLHGMF-------GDWSLALAAYNWGEGNVG 199
Cdd:COG4623 294 PRARSPTGARGLMQLMPATAKELGV------DDRLDPEQSIRAGAKYLRWLYDRFpeaidepDRWWFALAAYNAGPGHVQ 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1090946631 200 RAVNRARAQGLEPTY-------------ENLRMPNETRNYVPKLLAVRNI 236
Cdd:COG4623 368 DARRLAKKQGLDPDRwfdveksqpkyydTGYARGRETVNYVPNIRAYYDI 417
|
|
| MltE |
COG0741 |
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ... |
82-236 |
1.31e-36 |
|
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440504 [Multi-domain] Cd Length: 244 Bit Score: 137.82 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 82 AANSAYFDRTISRSKPYMYHIANEVKKRNMPAE-IALLPFIESAFVTKAKSHVGASGLWQFMPATGRHFGLE--KTPLYD 158
Cdd:COG0741 87 AELLALAALLLRRPLPYLPLIEEAAKKYGVDPAlVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKlgLGPSPD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 159 GRHDVYAATDAALNYLQYLHGMF-GDWSLALAAYNWGEGNVGRAVNRARAQGLEptyenlRMP-NETRNYVPKLLAVRNI 236
Cdd:COG0741 167 DLFDPETNIRAGAAYLRELLDRFdGDLVLALAAYNAGPGRVRRWLRRNGDRDGE------IIPyAETRNYVKKVLANYAI 240
|
|
| SLT |
pfam01464 |
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ... |
102-209 |
1.10e-25 |
|
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
Pssm-ID: 396169 [Multi-domain] Cd Length: 114 Bit Score: 102.00 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 102 IANEVKKRNMPAEIALLPFIESAFVTKAKSHVGASGLWQFMPATGRHFGLEKTPLYDGRHDVYAATDAALNYLQYLHGMF 181
Cdd:pfam01464 2 IKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQY 81
|
90 100
....*....|....*....|....*....
gi 1090946631 182 G-DWSLALAAYNWGEGNVGRAVNRARAQG 209
Cdd:pfam01464 82 GgDLWLALAAYNAGPGRVRKWIKNAGAKD 110
|
|
| LT-like |
cd00254 |
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ... |
122-232 |
3.29e-21 |
|
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381594 [Multi-domain] Cd Length: 111 Bit Score: 89.19 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 122 ESAFVTKAKSHVGASGLWQFMPATGRHFGLEktpLYDGRHDVYAATDAALNYLQYLHGMF-GDWSLALAAYNWGEGNVGR 200
Cdd:cd00254 11 ESGFNPRAVSPAGARGLMQLMPGTARDLGRR---GVDDLFDPEENIRAGARYLRELLDRFgGDLELALAAYNAGPGAVDR 87
|
90 100 110
....*....|....*....|....*....|..
gi 1090946631 201 AVNRARaqgleptyenlRMPNETRNYVPKLLA 232
Cdd:cd00254 88 WGGGEV-----------PPYKETRNYVQRVLA 108
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
582-699 |
5.93e-21 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 96.34 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 582 LARVNGQQNTQTAALAVGTHRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRVTAAPAKVRSNPVQN-VSYT 660
Cdd:PRK10783 327 IAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDsITYR 406
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1090946631 661 VRKGDTLNTIASRFNVDINDIRRWNRNTRT-VSPGQRLKL 699
Cdd:PRK10783 407 VRKGDSLSSIAKRHGVNIKDVMRWNSDTAKnLQPGDKLTL 446
|
|
| Slt70-like |
cd13401 |
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ... |
122-232 |
4.92e-18 |
|
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.
Pssm-ID: 381604 [Multi-domain] Cd Length: 152 Bit Score: 81.37 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 122 ESAFVTKAKSHVGASGLWQFMPATGRH----FGLEktplYDGRHDVYaatDAALN------YLQYLHGMF-GDWSLALAA 190
Cdd:cd13401 31 ESAFDPDAVSPAGALGLMQLMPATAKDvakkLGLP----YYSPRDLF---DPEYNirlgsaYLAELLDRFdGNPVLALAA 103
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1090946631 191 YNWGEGNVGRAVNRARAQGLEPTYENlrMP-NETRNYVPKLLA 232
Cdd:cd13401 104 YNAGPGRVRRWLKRRGDLDPDLWIET--IPfSETRNYVKRVLE 144
|
|
| LT_Slt70-like |
cd16896 |
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ... |
122-236 |
3.02e-17 |
|
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381617 [Multi-domain] Cd Length: 146 Bit Score: 79.09 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 122 ESAFVTKAKSHVGASGLWQFMPATGRH----FGLEKTPLYDgrhdvyaATDAALN------YLQYLHGMF-GDWSLALAA 190
Cdd:cd16896 29 ESNFNPNAVSSKGAIGLMQIMPETAEWiaekLGLEDFSEDD-------LYDPETNirlgtwYLSYLLKEFdGNLVLALAA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1090946631 191 YNWGEGNVGRAVNRARAQGLEPTYENLRMPnETRNYVPKLLAVRNI 236
Cdd:cd16896 102 YNAGPGNVDKWLKDGGWSGDGKTLDQIPFP-ETRHYVKKVLKNYKI 146
|
|
| MLTF-like |
cd13403 |
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ... |
122-212 |
6.03e-15 |
|
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381606 [Multi-domain] Cd Length: 161 Bit Score: 72.95 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 122 ESAFVTKAKSHVGASGLWQFMPATGRHFGLekTPLYDGRHDVYAATdaalNYLQYLHGMFGD-------WSLALAAYNWG 194
Cdd:cd13403 22 ESRFNPNARSPAGARGLMQLMPSTARELGV--NDRLDPEQNIHAGA----KYLRYLRDRFPPdidepdrLKFALAAYNAG 95
|
90
....*....|....*...
gi 1090946631 195 EGNVGRAVNRARAQGLEP 212
Cdd:cd13403 96 PGHVRDARRLAKKYGLNP 113
|
|
| Slt35-like |
cd13399 |
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ... |
110-202 |
2.26e-13 |
|
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381602 [Multi-domain] Cd Length: 108 Bit Score: 66.56 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 110 NMPAEI--ALLpFIESAFVTKA-KSHVGASGLWQFMPATGRHFGLEKTplYDGRHDVYAATDAALNYLQYLHGMFG---- 182
Cdd:cd13399 2 GVPPGIlaAIL-GVESGFGPNAgGSPAGAQGIAQFMPSTWKAYGVDGN--GDGKADPFNPEDAIASAANYLCRHGWdlna 78
|
90 100
....*....|....*....|....
gi 1090946631 183 ----DWSLALAAYNWGEGNVGRAV 202
Cdd:cd13399 79 flgeDNFLALAAYNAGPGAYANAV 102
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
489-642 |
9.49e-13 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 66.66 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 489 KAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQTVVTAESARAARIA 568
Cdd:COG1388 1 GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1090946631 569 ANTAKQQQRINARLARVNGQQNTQTAAlAVGTHRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRV 642
Cdd:COG1388 81 AAAARYTVKSGDTLSGIARRYGAAAAP-SPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
529-702 |
2.13e-12 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 65.50 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 529 ALVQSQPAEEPAATVAEATSEAKQVQTVVTAESARAARIAANTAKQQQRINARLARVNGQQNTQTAALAVGTHRVADGDT 608
Cdd:COG1388 14 AAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 609 LFNISKRYNlsvadliiannikgnnikkgqilrvtaapakvRSNPVQNVSYTVRKGDTLNTIASRFNVDINDIRRWNR-N 687
Cdd:COG1388 94 LSGIARRYG--------------------------------AAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGlS 141
|
170
....*....|....*
gi 1090946631 688 TRTVSPGQRLKLIGS 702
Cdd:COG1388 142 SDTIRPGQKLKIPAS 156
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
600-699 |
5.06e-12 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 68.95 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 600 THRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRVTAAPAKVRSN---PVQNVS--------------YTVR 662
Cdd:PRK06347 332 IYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNtskPSTGTStskpstgtstnakvYTVV 411
|
90 100 110
....*....|....*....|....*....|....*...
gi 1090946631 663 KGDTLNTIASRFNVDINDIRRWNR-NTRTVSPGQRLKL 699
Cdd:PRK06347 412 KGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKLKV 449
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
586-699 |
1.13e-11 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 67.80 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 586 NGQQNTQTAALAVGTHRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRVTAAP-------AKVRSNPVQNVS 658
Cdd:PRK06347 467 NTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSttnntntAKPSTNKPSNST 546
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1090946631 659 ---YTVRKGDTLNTIASRFNVDINDIRRWNRNT-RTVSPGQRLKL 699
Cdd:PRK06347 547 vktYTVKKGDSLWAISRQYKTTVDNIKAWNKLTsNMIHVGQKLTI 591
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
586-699 |
1.51e-11 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 67.41 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 586 NGQQNTQTAALAVGTHRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRVTAAP---------------AKVR 650
Cdd:PRK06347 393 STSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGStsntntskpstntntSKPS 472
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1090946631 651 SNPVQNV-SYTVRKGDTLNTIASRFNVDINDIRRWNR-NTRTVSPGQRLKL 699
Cdd:PRK06347 473 TNTNTNAkVYTVAKGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKLKV 523
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
657-699 |
1.70e-11 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 59.42 E-value: 1.70e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1090946631 657 VSYTVRKGDTLNTIASRFNVDINDIRRWNR--NTRTVSPGQRLKL 699
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPliNPDCIYPGQKLKI 45
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
600-642 |
1.22e-10 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 56.72 E-value: 1.22e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1090946631 600 THRVADGDTLFNISKRYNLSVADLIIANNIKGNN-IKKGQILRV 642
Cdd:cd00118 2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
659-699 |
1.35e-10 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 56.69 E-value: 1.35e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1090946631 659 YTVRKGDTLNTIASRFNVDINDIRRWNR--NTRTVSPGQRLKL 699
Cdd:smart00257 2 YTVKKGDTLSSIARRYGISVSDLLELNNilDPDNLQVGQKLKI 44
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
659-699 |
2.39e-10 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 55.87 E-value: 2.39e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1090946631 659 YTVRKGDTLNTIASRFNVDINDIRRWNR-NTRTVSPGQRLKL 699
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGlSSPNLYVGQKLKI 42
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
601-643 |
3.50e-10 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 55.48 E-value: 3.50e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1090946631 601 HRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRVT 643
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
395-574 |
6.14e-10 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 62.75 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 395 QSNMP----AMSPIIASS---VAEPVKVAQTTVT--------NIVAPVVPqsSKPVDFIARSKAENVTSVAVTETKAQPQ 459
Cdd:PRK10811 822 QSPMPltvaCASPEMASGkvwIRYPVVRPQDVQVeeqreaeeVQVQPVVA--EVPVAAAVEPVVSAPVVEAVAEVVEEPV 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 460 VANAEVAAPVVAMTHTTAEPAATNVAEAPkaAILADLTAPSVAANDVAPTPAVESVA-VAPVQEERDDLMALVQSQPAEE 538
Cdd:PRK10811 900 VVAEPQPEEVVVVETTHPEVIAAPVTEQP--QVITESDVAVAQEVAEHAEPVVEPQDeTADIEEAAETAEVVVAEPEVVA 977
|
170 180 190
....*....|....*....|....*....|....*.
gi 1090946631 539 PAATVAEATSEAKQVQTVVTAESARAARIAANTAKQ 574
Cdd:PRK10811 978 QPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEH 1013
|
|
| PRK11619 |
PRK11619 |
lytic murein transglycosylase; Provisional |
122-232 |
1.55e-08 |
|
lytic murein transglycosylase; Provisional
Pssm-ID: 183236 [Multi-domain] Cd Length: 644 Bit Score: 57.76 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 122 ESAFVTKAKSHVGASGLWQFMPATGRH----FGLektPLYDGRHDVyaaTDAALN------YLQYLHGMFG-DWSLALAA 190
Cdd:PRK11619 504 ESAWNPKARSPVGASGLMQIMPGTATHtvkmFSI---PGYSSSSQL---LDPETNinigtsYLEYVYQQFGnNRILASAA 577
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1090946631 191 YNWGEGNVGRAVNRARAQgLEPTYENLRMP-NETRNYVPKLLA 232
Cdd:PRK11619 578 YNAGPGRVRTWLGNSAGR-IDAVAFVESIPfSETRGYVKNVLA 619
|
|
| LysM |
smart00257 |
Lysin motif; |
600-642 |
2.30e-08 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 50.52 E-value: 2.30e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1090946631 600 THRVADGDTLFNISKRYNLSVADLIIANNIKG-NNIKKGQILRV 642
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
|
|
| LT_MltC_MltE |
cd16893 |
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ... |
122-232 |
3.22e-08 |
|
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda
Pssm-ID: 381614 [Multi-domain] Cd Length: 162 Bit Score: 53.33 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 122 ESAFVTKAKSHVGASGLWQFMPATG------RHFGLEKTP----LYDGRHDVYAATdAALNYLQ--YLHGMFGDWSL--- 186
Cdd:cd16893 24 ESSFNPYAVSHSPAYGLMQIVPSTAgrdvyrLLGGKGGLPsksyLFDPENNIDIGT-AYLHILQnrYLKGIKNPKSReyc 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1090946631 187 ALAAYNWGEGNVGRAVNRARAQGLE--------PTYENLR---MPNETRNYVPKLLA 232
Cdd:cd16893 103 AIAAYNGGAGNVLRTFSSDRKKAISkinrlspdEVYQHLTkklPAAETRNYLKKVLK 159
|
|
| PHA00368 |
PHA00368 |
internal virion protein D |
120-233 |
6.47e-08 |
|
internal virion protein D
Pssm-ID: 222785 [Multi-domain] Cd Length: 1315 Bit Score: 56.33 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 120 FIESAFVTKAKSHVGASGLWQFMPATGRHFGLEKTPlyDGRHDVYAATDAALNYLQYLHGMF-GDWSLALAAYNWGEGNV 198
Cdd:PHA00368 34 WDESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDD--DDRLDPELAIDAGARYLADLVGKYdGDELKAALAYNQGEGRL 111
|
90 100 110
....*....|....*....|....*....|....*
gi 1090946631 199 GRAVNRARAQGleptyENLRMPNETRNYVPKLLAV 233
Cdd:PHA00368 112 GAPQLEAYDKG-----DFASISEEGRNYLRNLLDV 141
|
|
| Lyz-like |
cd00442 |
lysozyme-like domains; This family contains several members, including soluble lytic ... |
114-173 |
3.50e-07 |
|
lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.
Pssm-ID: 381596 [Multi-domain] Cd Length: 59 Bit Score: 47.40 E-value: 3.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1090946631 114 EIALLPFIESAF--VTKAKSHVGASGLWQFMPATGRHFGLEktpLYDGRHDVYAATDAALNY 173
Cdd:cd00442 1 VLAAIIGQESGGnkPANAGSGSGAAGLFQFMPGTWKAYGKN---SSSDLNDPEASIEAAAKY 59
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
406-519 |
1.08e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 48.88 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 406 ASSVAEPVKVAQTTVTNIVAPV------VPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVaapVVAMTHTTAEP 479
Cdd:PRK10811 903 EPQPEEVVVVETTHPEVIAAPVteqpqvITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEV---VVAEPEVVAQP 979
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1090946631 480 AATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAP 519
Cdd:PRK10811 980 AAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATAP 1019
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
429-559 |
1.34e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 48.56 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 429 PQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMthTTAEPAATNVAEAPKAAIladltAPSVAANDVAP 508
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAA--AASAPAAPPAAAPPAPVA-----APAAAAPAAAP 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1090946631 509 TPAVESVAVAPVQEERD-DLMALVQSQPAEEPAATVAEATSEAKQVQTVVTA 559
Cdd:PRK14951 439 AAAPAAVALAPAPPAQAaPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
399-569 |
3.27e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 47.15 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 399 PAMSPIIASSVAEPVKVAQTTVTNIVAP--VVPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTT 476
Cdd:PRK07003 385 ARAAAAVGASAVPAVTAVTGAAGAALAPkaAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCD 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 477 AEPAATNVAEAPKAAILADltAPSVAANDVAPTPAVESVAVAPVQEERDDLMAlvqSQPAEEPAATvAEATSEAKQVQTV 556
Cdd:PRK07003 465 ERDAQPPADSGSASAPASD--APPDAAFEPAPRAAAPSAATPAAVPDARAPAA---ASREDAPAAA-APPAPEARPPTPA 538
|
170
....*....|...
gi 1090946631 557 VTAESARAARIAA 569
Cdd:PRK07003 539 AAAPAARAGGAAA 551
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
509-646 |
5.26e-05 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 46.33 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 509 TPAVESVAVAPVQEerddlmalVQSQPAEEPAATVAEATSEAKQVQTVVTAESARAARIAANTAKQqqriNARlarvngq 588
Cdd:PRK13914 140 TDKVTSTPVAPTQE--------VKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQ----NAT------- 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1090946631 589 qntqtaalavgTHRVADGDTLFNISKRYNLSVADLIIANNIKGNNIKKGQILRV-----TAAP 646
Cdd:PRK13914 201 -----------THAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIkqtanTATP 252
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
429-587 |
6.57e-05 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 46.42 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 429 PQSSKP--VDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTTAEPAATNVAEAPKAailadlTAPSVAANDV 506
Cdd:PRK12270 22 PNSVDPswREFFADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPK------PAAAAAAAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 507 APTPAVESVAVAPVQEERDDlmalvQSQPAEEPAATVAEATSEAkqvQTVVTAESARA--ARIAANTAKQqqrINARLAR 584
Cdd:PRK12270 96 PAAPPAAAAAAAPAAAAVED-----EVTPLRGAAAAVAKNMDAS---LEVPTATSVRAvpAKLLIDNRIV---INNHLKR 164
|
...
gi 1090946631 585 VNG 587
Cdd:PRK12270 165 TRG 167
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
456-572 |
7.68e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 456 AQPQVANAEVAAPV-VAMTHTTAEPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVA-PVQEERDDLMALVQS 533
Cdd:PRK12323 373 GPATAAAAPVAQPApAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAArQASARGPGGAPAPAP 452
|
90 100 110
....*....|....*....|....*....|....*....
gi 1090946631 534 QPAEEPAATVAEATSEAKQVQTVVTAESARAARIAANTA 572
Cdd:PRK12323 453 APAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAP 491
|
|
| SpoVID |
COG5846 |
Stage VI sporulation protein SpoVID (LysM domain), required for assembly of the spore coat ... |
428-640 |
9.64e-05 |
|
Stage VI sporulation protein SpoVID (LysM domain), required for assembly of the spore coat [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444548 [Multi-domain] Cd Length: 398 Bit Score: 45.50 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 428 VPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEvaaPVVAMTHTTAEPA-------ATNVAEAPKAAILADLTAPS 500
Cdd:COG5846 145 EPPRQQEEDEPAEEEEEEEEIAAEFEVEAKQESYEEE---ESPSEKEEPEQPAedeptlqLEEVDEEEAQEDEPELESKS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 501 VAANDVAPTPAVESVAVAPVQEERDDL-MALVQSQPAEEPAATVAEATSEAKQVQTvvTAESARAARIAANTAKQQQRIN 579
Cdd:COG5846 222 ESDKVEEEPALVEEQSEQQTEEEPKSQqYAEFFPEEELEEAAQYEVFGEREPEVEE--EPESESVEAEAEESSVEESSEI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 580 ARLARVNGQQNTQTAA----------------LAVGTHR------------VADGDTLFNISKRYNLSVADLIIANNIKG 631
Cdd:COG5846 300 EEVQAVIEEQEEESEAeeeeekerrdenalylTKLFTKNeeeeftklkmciVQEGDTLETIAERYDISVQQLIRVNQLES 379
|
....*....
gi 1090946631 632 NNIKKGQIL 640
Cdd:COG5846 380 DEVSEGQIL 388
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
316-559 |
1.21e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 45.34 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 316 RNANPDTLMSWDIYTSLGNKKLNAIANDTGMSVAelkrlnglSGSAISEGRSILVAKNSATQSQDIINFIDKDNTPDTYQ 395
Cdd:pfam17823 40 QNASGDAVPRADNKSSEQ*NFCAATAAPAPVTLT--------KGTSAAHLNSTEVTAEHTPHGTDLSEPATREGAADGAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 396 SNMPAmspiiASSVAEPVKVAQTTVTNIVAPVVPQSSKPvdfiarskaenVTSVAVTETKAQPQVANAEVAAPVVAMTHT 475
Cdd:pfam17823 112 SRALA-----AAASSSPSSAAQSLPAAIAALPSEAFSAP-----------RAAACRANASAAPRAAIAAASAPHAASPAP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 476 TAEPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQT 555
Cdd:pfam17823 176 RTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALAT 255
|
....
gi 1090946631 556 VVTA 559
Cdd:pfam17823 256 LAAA 259
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
424-576 |
1.51e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 44.86 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 424 VAPVVPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTTAE--------PAATNVAEAPKAAILAD 495
Cdd:PRK07994 367 EPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQllaarqqlQRAQGATKAKKSEPAAA 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 496 LTAPSVAAnDVAPTPAVESVAVAPVQE-ERDDLMALVQSQPAEEPAATVAEATSEAKQVQTVVTAESarAARIAANTAKQ 574
Cdd:PRK07994 447 SRARPVNS-ALERLASVRPAPSALEKApAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPEL--AAKLAAEAIER 523
|
..
gi 1090946631 575 QQ 576
Cdd:PRK07994 524 DP 525
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
456-569 |
1.58e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.09 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 456 AQPQVANAEVAAPVVAMTHTTAEPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQP 535
Cdd:PRK14951 371 EAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPA 450
|
90 100 110
....*....|....*....|....*....|....
gi 1090946631 536 AEEPAAtvAEATSEAKQVQTVVTAESARAARIAA 569
Cdd:PRK14951 451 PPAQAA--PETVAIPVRVAPEPAVASAAPAPAAA 482
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
395-588 |
1.92e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.71 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 395 QSNMPAMSPIIASSVAEPVKVAQTTVTNIVAPVVPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAmth 474
Cdd:PRK14951 367 AAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 475 TTAEPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQ-EERDDLMALVQSQPAEEPAATVAEATseAKQV 553
Cdd:PRK14951 444 AVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPtEEGDVWHATVQQLAAAEAITALAREL--ALQS 521
|
170 180 190
....*....|....*....|....*....|....*...
gi 1090946631 554 QTVVTAESA---RAARIAANTAKQQQRINARLARVNGQ 588
Cdd:PRK14951 522 ELVARDGDQwllRVERESLNQPGARERLRAALEAALGH 559
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
244-370 |
2.18e-04 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 42.39 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 244 GMNISEISNQPYFKSVSIDKPIDNSTIARFANISESELLALNPGFNAPVFIPKNNRRLLLPVSAVSAFEKNYRNANPDTL 323
Cdd:COG1388 1 GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1090946631 324 MSWDIYTSLGNKKLNAIAN------------------DT--------GMSVAELKRLNGLSGSAISEGRSILV 370
Cdd:COG1388 81 AAAARYTVKSGDTLSGIARrygaaaapspvtytvkkgDTlwsiarryGVSVEELKRWNGLSSDTIRPGQKLKI 153
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
443-597 |
2.38e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.32 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 443 AENVTSVAVTETKAQPQV---ANAEVAAPVVAMTHTTAEPAATNVAEAPKAAIL-ADLTAPSVAANDVAPTPAVESVAVA 518
Cdd:PRK14951 369 AAEAAAPAEKKTPARPEAaapAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPpAPVAAPAAAAPAAAPAAAPAAVALA 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 519 PVQEERD-----DLMALVQSQPAE---------EPAATVAEATSE----AKQVQTVVTAESARA-AR--------IAANT 571
Cdd:PRK14951 449 PAPPAQAapetvAIPVRVAPEPAVasaapapaaAPAAARLTPTEEgdvwHATVQQLAAAEAITAlARelalqselVARDG 528
|
170 180
....*....|....*....|....*.
gi 1090946631 572 AKQQQRINARLARVNGQQNTQTAALA 597
Cdd:PRK14951 529 DQWLLRVERESLNQPGARERLRAALE 554
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
479-616 |
2.45e-04 |
|
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];
Pssm-ID: 441258 [Multi-domain] Cd Length: 163 Bit Score: 42.30 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 479 PAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQTVVT 558
Cdd:COG1652 1 VAAAAAAAALAALLPAVSAAAATVLALAAAAALAVVAGLGAAVGAGGALAAALPLAAGLAAAVAAAAAAAVLIAPVAVMR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1090946631 559 AESARAARIAANTAKQQqrinarlarvnGQQNTQTAALAVGTHRVADGDTLFNISKRY 616
Cdd:COG1652 81 AGAAAKLSPAVTVAEEA-----------AAPSAELAPDAPKTYTVKPGDTLWGIAKRF 127
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
403-607 |
8.51e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 403 PIIASSVAEPVKVAQTTVTNIVAPVVPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPV--VAMTHTTAEPA 480
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARgpGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 481 ATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQTVVTAE 560
Cdd:PRK12323 456 AAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPD 535
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1090946631 561 SARAARIAANTAKQQQRINARLARVNGQqnTQTAALAVGTHRVADGD 607
Cdd:PRK12323 536 DAFETLAPAPAAAPAPRAAAATEPVVAP--RPPRASASGLPDMFDGD 580
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
425-604 |
9.54e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.53 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 425 APVVPQSSKPVDFIARSKAENVTSVAVTETKAQPQVAnaevAAPVVAMTHTTAEPAATNVAEAPKAAiladltAPSVAAN 504
Cdd:PRK07003 367 APGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVT----GAAGAALAPKAAAAAAATRAEAPPAA------PAPPATA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 505 DVAPTPAVESVAVAPVQEERDDLMALVQSQPAEePAATVAEATSEAKQVQTVVTAESARAARIAANTAKQQQRINARLAR 584
Cdd:PRK07003 437 DRGDDAADGDAPVPAKANARASADSRCDERDAQ-PPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAA 515
|
170 180
....*....|....*....|
gi 1090946631 585 VngQQNTQTAALAVGTHRVA 604
Cdd:PRK07003 516 A--SREDAPAAAAPPAPEAR 533
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
433-565 |
1.21e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 42.16 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 433 KPVDFIARSKAENVTS--VAVTETKAQPQVANAEVAAPVVAMTHTTAEPAATNVAEAPKAAILADLTAPSVAANDVAPTP 510
Cdd:PRK07994 360 HPAAPLPEPEVPPQSAapAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAK 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1090946631 511 AVESVAVA---PVQEERDDLMALVQSQPAEEPAATVAEA------TSEAKQVQTVVTAESARAA 565
Cdd:PRK07994 440 KSEPAAASrarPVNSALERLASVRPAPSALEKAPAKKEAyrwkatNPVEVKKEPVATPKALKKA 503
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
399-587 |
1.22e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.17 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 399 PAMSPIIASSVAEPVKVAQTTVTNIVAPVVPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTTAE 478
Cdd:PRK12323 405 APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAA 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 479 PAATNVAEA----PKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQ 554
Cdd:PRK12323 485 PAAAPAPADddppPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPR 564
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1090946631 555 TVVTAES-----------ARAARIAANTAKQQQRINARLARVNG 587
Cdd:PRK12323 565 PPRASASglpdmfdgdwpALAARLPVRGLAQQLARQSELAGVEG 608
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
438-577 |
1.33e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 438 IARSKAEnvtsvavtetKAQPQVANAEVAAPVvaMTHTTAEPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAV 517
Cdd:PRK05035 554 IARAKAK----------KAAQQAANAEAEEEV--DPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI 621
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1090946631 518 APVQEERDDLMALVQSQPAEEP-----AATVAEATSEAKQVQTVVTAES--------ARAARIAANTAKQQQR 577
Cdd:PRK05035 622 ARAKAKKAEQQANAEPEEPVDPrkaavAAAIARAKARKAAQQQANAEPEeaedpkkaAVAAAIARAKAKKAAQ 694
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
399-569 |
1.33e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.14 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 399 PAMSPIIASSVAEPVKVAQTTVTNIVA-PVVPQSSKPVDfIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTTA 477
Cdd:PRK07003 381 PAPGARAAAAVGASAVPAVTAVTGAAGaALAPKAAAAAA-ATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 478 EPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDDLMALVQSQPAEEPAATVAEATSEAkqvqtvv 557
Cdd:PRK07003 460 DSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEA------- 532
|
170
....*....|..
gi 1090946631 558 TAESARAARIAA 569
Cdd:PRK07003 533 RPPTPAAAAPAA 544
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
395-588 |
1.41e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 41.77 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 395 QSNMPAMSPIIASSVAE-PVKVAQTTVTNIVAPVVPQSSKPVdfiARSKAENVTSVavteTKAQPQVANAEVAAPVVAMT 473
Cdd:PRK07994 403 PASAPQQAPAVPLPETTsQLLAARQQLQRAQGATKAKKSEPA---AASRARPVNSA----LERLASVRPAPSALEKAPAK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 474 HTTAEPAATNVAEAPKAAIladlTAPSVAANDVAPTPAVESVA-VAPVQEERDDLMALVQSQPAEEPAATVAE-ATSEAK 551
Cdd:PRK07994 476 KEAYRWKATNPVEVKKEPV----ATPKALKKALEHEKTPELAAkLAAEAIERDPWAALVSQLGLPGLVEQLALnAWKEEH 551
|
170 180 190
....*....|....*....|....*....|....*..
gi 1090946631 552 QVQTVVTAesARAARIAANTAKQQQRINARLARVNGQ 588
Cdd:PRK07994 552 DNGEVCLH--LRPSQRHLNSPRAQQRLAEALSELLGR 586
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
399-535 |
1.42e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.95 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 399 PAMSPIIASSVAEPVKVAQT--TVTNIVA-PVVPQSSKPVDFIARSKAE-NVTSVAVTEtkaQPQV---ANAEVAAPVVA 471
Cdd:PRK10811 868 PVVAEVPVAAAVEPVVSAPVveAVAEVVEePVVVAEPQPEEVVVVETTHpEVIAAPVTE---QPQViteSDVAVAQEVAE 944
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1090946631 472 MTHTTAEPAATNVAEAPKAAILADLTA-PSVAANDVAP----------TPAVESVAVAPVQEERDDLMALVQSQP 535
Cdd:PRK10811 945 HAEPVVEPQDETADIEEAAETAEVVVAePEVVAQPAAPvvaevaaeveTVTAVEPEVAPAQVPEATVEHNHATAP 1019
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
337-370 |
1.80e-03 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 36.61 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|....
gi 1090946631 337 LNAIANDTGMSVAELKRLNGLSGSAISEGRSILV 370
Cdd:pfam01476 9 LSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
446-598 |
1.98e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.56 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 446 VTSVAVTETKAQPQvANAEVAAPVVAmthttaEPAATNVAEAPKAAiladltaPSVAAndvAPTPAVESVAVAPVQEERD 525
Cdd:PRK10811 847 VVRPQDVQVEEQRE-AEEVQVQPVVA------EVPVAAAVEPVVSA-------PVVEA---VAEVVEEPVVVAEPQPEEV 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 526 DlmalvqSQPAEEP---AATVAEATSEAKQVQTVVTAESARAARIAA-----NTAKQQQRINARLARVNGQQNTQTAALA 597
Cdd:PRK10811 910 V------VVETTHPeviAAPVTEQPQVITESDVAVAQEVAEHAEPVVepqdeTADIEEAAETAEVVVAEPEVVAQPAAPV 983
|
.
gi 1090946631 598 V 598
Cdd:PRK10811 984 V 984
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
447-580 |
3.42e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 40.53 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 447 TSVAVTETKAQPQVANAEVAAPVVAMTHTTAEPAATNVAEAPKAAILADLTAPSVAANDVAPTPAVESVAVAPVQEERDD 526
Cdd:PRK14971 379 IKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKI 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1090946631 527 LMALVQS------QPAEEPAatvAEATSEAKQVQTVVTAES------ARAARIAANTAKQQQRINA 580
Cdd:PRK14971 459 PVSKVSSlgpstlRPIQEKA---EQATGNIKEAPTGTQKEIfteedlQYYWQEFAGTRPQEEKALK 521
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
449-609 |
4.04e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 449 VAVTETKAQPQVANAEVAAPVVAMTHTTAEPAATNVAEAPKAAILADltAPSVAAndvAPTPAVESVAVAPVQEERddlm 528
Cdd:PRK07764 387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAP--APAPAP---APPSPAGNAPAGGAPSPP---- 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 529 ALVQSQPAEEPAATVAEATSEAKQVQTVVTAESARAARIAANTAKQQ---------QRINARLARVnGQQNTQTAALAVG 599
Cdd:PRK07764 458 PAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAgaddaatlrERWPEILAAV-PKRSRKTWAILLP 536
|
170
....*....|..
gi 1090946631 600 THRVA--DGDTL 609
Cdd:PRK07764 537 EATVLgvRGDTL 548
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
442-570 |
5.91e-03 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 39.49 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 442 KAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTTAEPAA--TNVAEAPKAAiladlTAPSVAANDVAPTPAVESVAVAP 519
Cdd:TIGR00601 65 KEKDFVVVMVSKPKTGTGKVAPPAATPTSAPTPTPSPPASpaSGMSAAPASA-----VEEKSPSEESATATAPESPSTSV 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1090946631 520 VQEERDDLMALVQSQPAEEPAATVAEATSEAKQVQtvvtaesaRAARIAAN 570
Cdd:TIGR00601 140 PSSGSDAASTLVVGSERETTIEEIMEMGYEREEVE--------RALRAAFN 182
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
410-488 |
6.36e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.02 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090946631 410 AEPVKVAQTTVTNI-----VAPVVPQSSKPVDFIARSKAENVTSVAVTETKAQPQVANAEVAAPVVAMTHTTA----EPA 480
Cdd:PRK10811 946 AEPVVEPQDETADIeeaaeTAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATApmtrAPA 1025
|
....*...
gi 1090946631 481 ATNVAEAP 488
Cdd:PRK10811 1026 PEYVPEAP 1033
|
|
| |
