|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
1-470 |
0e+00 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 667.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 1 MKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVtevNEVAKTEK 80
Cdd:PRK13914 3 MKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV---NEVAAAEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 81 QEKSVSATWLNVRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKVASTPVTTTQEVKKEAT 160
Cdd:PRK13914 80 TEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKVTSTPVAPTQEVKKETT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 161 TEQAAPAAETKTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 240
Cdd:PRK13914 160 TQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 241 KLAIKQTANTATPKAEVKTEAPAAEKQAAPAVKENTNTNTATTEKKETTTQQQTAPKAPTEAA----KPAPAPAPSTNTN 316
Cdd:PRK13914 240 KLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAkpapAPSTNTNANKTNT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 317 ANKTNTNNTNTSTPSKNTNTNTNTNANQG--------SSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 388
Cdd:PRK13914 320 NTNTNTNNTNTSTPSKNTNTNTNSNTNTNsntnanqgSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 389 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 468
Cdd:PRK13914 400 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 479
|
..
gi 501577503 469 RV 470
Cdd:PRK13914 480 RV 481
|
|
| NLPC_P60 |
pfam00877 |
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins. |
367-469 |
1.94e-48 |
|
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
Pssm-ID: 395705 [Multi-domain] Cd Length: 105 Bit Score: 161.68 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 367 GKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTR-ISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINA 445
Cdd:pfam00877 1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPRSSGQQYNAGKKtIPKSEPQRGDLVFFGTGKGISHVGIYLGNGQMLHA 80
|
90 100
....*....|....*....|....*
gi 501577503 446 Q-DNGVKYDNIHGSGWGKYLVGFGR 469
Cdd:pfam00877 81 StGGGVSISSLNGGYWQKRLVGVRR 105
|
|
| NlpC |
COG0791 |
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis]; |
257-470 |
1.63e-47 |
|
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440554 [Multi-domain] Cd Length: 218 Bit Score: 163.33 E-value: 1.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 257 VKTEAPAAEKQAAPAVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPAPSTNTNANKTNTNNTNTSTPSKNTNT 336
Cdd:COG0791 2 SVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSAGAAAAAAAAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 337 NTNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQA 416
Cdd:COG0791 82 GSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPRTSADQAAAGTPVSRSEL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501577503 417 KPGDLVFFD-YGSGISHVGIYVGNGQMINAQD--NGVKYDNIHGSGWGKYLVGFGRV 470
Cdd:COG0791 162 QPGDLVFFRtGGGGISHVGIYLGNGKFIHASSsgKGVRISSLDSPYWKSRYVGARRV 218
|
|
| wall_hydro_RipC |
NF038345 |
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as ... |
358-450 |
3.52e-22 |
|
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as Mycobacterium tuberculosis, that is activated by conformation change sent as a signal by the cell division-regulating transporter-like complex FtsEX. Members of this family are distinguished from more distant homologs by a Pro/Gly-rich region.
Pssm-ID: 468486 [Multi-domain] Cd Length: 361 Bit Score: 97.50 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 358 IIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFdYgSGISHVGIYV 437
Cdd:NF038345 253 VVQAALTRIGSPYSWGGSGPNAFDCSGLVMWAFQQAGISLPHSSQALARGGQPVSLDDLQPGDVVTF-Y-SDASHAGIYI 330
|
90
....*....|...
gi 501577503 438 GNGQMINAQDNGV 450
Cdd:NF038345 331 GDGMMVHASTYGT 343
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
201-244 |
1.78e-14 |
|
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: 67.13 E-value: 1.78e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 501577503 201 TTHTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
202-244 |
1.24e-13 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 64.77 E-value: 1.24e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 501577503 202 THTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
89-179 |
8.41e-11 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 61.18 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 89 WLNVRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDkvasTPVTTTQ--EVKKEATTEQAAP 166
Cdd:TIGR04211 7 FVYMRSGPGNQYRILGSLKSGTPVTVLERSEDGYSRVRTPKGREGWVLSRYLSD----TPSARERlpELQQELAELQEEL 82
|
90
....*....|...
gi 501577503 167 aAETKTEVKQTTQ 179
Cdd:TIGR04211 83 -AELQEQLAELRQ 94
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
18-271 |
1.70e-04 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 44.00 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 18 AAPTIASASTVVVeaGDTLwGIAQSKGTTVDAIKKANNLTTDKIVPGQ------KLQVTEVNEVAKTEKQEKSVSATWLN 91
Cdd:NF040676 17 AFTTTATAETIVT--ADVL-NVREKPTTESKVVEKVKNGQELKVINTEdgwskiELNGKEVFVSSEFTKDVYHVTANLLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 92 VRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNdGKTGFVNGKYLTDKvASTPVTTTQEVKKEATTEQAAPAA-ET 170
Cdd:NF040676 94 VRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYK-GKTAYANVSFLSST-APTEKKADEKTKQVAKVQKSVKAKeEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 171 KTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIwaLSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKqTANT 250
Cdd:NF040676 172 KTQKVAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEI--VKPKEEVKVQEEVKPKEEEKVQEIVKPKEEAK-VQEE 248
|
250 260
....*....|....*....|.
gi 501577503 251 ATPKAEVKTEAPAAEKQAAPA 271
Cdd:NF040676 249 VKVKEEAKVQEIAKAKEEAKA 269
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
90-264 |
4.25e-03 |
|
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: 38.95 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 90 LNVRTGAGVDNSIITSIKGGTKVTVETTE-----------SNGWHKItyndGKTGFVNGKYltdkVASTPVTTTqevkke 158
Cdd:NF038016 1 LNVRSGPATDSAVVGTLANGAKVTVVCKVrgeqirgtvrtTSQWDRL----GSGRYVSHAY----VRWSPSLPT------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 159 atteQAAPAAETKTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIWalsvkyGVSVQDIMSWNNLSS----S 234
Cdd:NF038016 67 ----CPWCAPKAATVATVTTGGGALNVRAAAGTGAARVGTVANGATVTVECQVW------GQEVDGTGVWYRLGDgryvS 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 501577503 235 SIYV--------GQKLAikqTANTATPKAEVKTEAPAA 264
Cdd:NF038016 137 AAYVrrpwlpwcGQDPP---TVPRGTPAQFIAAVAPPA 171
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
1-470 |
0e+00 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 667.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 1 MKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVtevNEVAKTEK 80
Cdd:PRK13914 3 MKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV---NEVAAAEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 81 QEKSVSATWLNVRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKVASTPVTTTQEVKKEAT 160
Cdd:PRK13914 80 TEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKVTSTPVAPTQEVKKETT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 161 TEQAAPAAETKTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 240
Cdd:PRK13914 160 TQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 241 KLAIKQTANTATPKAEVKTEAPAAEKQAAPAVKENTNTNTATTEKKETTTQQQTAPKAPTEAA----KPAPAPAPSTNTN 316
Cdd:PRK13914 240 KLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAkpapAPSTNTNANKTNT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 317 ANKTNTNNTNTSTPSKNTNTNTNTNANQG--------SSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 388
Cdd:PRK13914 320 NTNTNTNNTNTSTPSKNTNTNTNSNTNTNsntnanqgSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 389 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 468
Cdd:PRK13914 400 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 479
|
..
gi 501577503 469 RV 470
Cdd:PRK13914 480 RV 481
|
|
| NLPC_P60 |
pfam00877 |
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins. |
367-469 |
1.94e-48 |
|
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
Pssm-ID: 395705 [Multi-domain] Cd Length: 105 Bit Score: 161.68 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 367 GKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTR-ISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINA 445
Cdd:pfam00877 1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPRSSGQQYNAGKKtIPKSEPQRGDLVFFGTGKGISHVGIYLGNGQMLHA 80
|
90 100
....*....|....*....|....*
gi 501577503 446 Q-DNGVKYDNIHGSGWGKYLVGFGR 469
Cdd:pfam00877 81 StGGGVSISSLNGGYWQKRLVGVRR 105
|
|
| NlpC |
COG0791 |
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis]; |
257-470 |
1.63e-47 |
|
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440554 [Multi-domain] Cd Length: 218 Bit Score: 163.33 E-value: 1.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 257 VKTEAPAAEKQAAPAVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPAPSTNTNANKTNTNNTNTSTPSKNTNT 336
Cdd:COG0791 2 SVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSAGAAAAAAAAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 337 NTNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQA 416
Cdd:COG0791 82 GSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPRTSADQAAAGTPVSRSEL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501577503 417 KPGDLVFFD-YGSGISHVGIYVGNGQMINAQD--NGVKYDNIHGSGWGKYLVGFGRV 470
Cdd:COG0791 162 QPGDLVFFRtGGGGISHVGIYLGNGKFIHASSsgKGVRISSLDSPYWKSRYVGARRV 218
|
|
| wall_hydro_RipC |
NF038345 |
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as ... |
358-450 |
3.52e-22 |
|
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as Mycobacterium tuberculosis, that is activated by conformation change sent as a signal by the cell division-regulating transporter-like complex FtsEX. Members of this family are distinguished from more distant homologs by a Pro/Gly-rich region.
Pssm-ID: 468486 [Multi-domain] Cd Length: 361 Bit Score: 97.50 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 358 IIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFdYgSGISHVGIYV 437
Cdd:NF038345 253 VVQAALTRIGSPYSWGGSGPNAFDCSGLVMWAFQQAGISLPHSSQALARGGQPVSLDDLQPGDVVTF-Y-SDASHAGIYI 330
|
90
....*....|...
gi 501577503 438 GNGQMINAQDNGV 450
Cdd:NF038345 331 GDGMMVHASTYGT 343
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
138-247 |
5.27e-18 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 80.91 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 138 KYLTDKVASTPVTTTQEVKKEATTEQAAPAAETKTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIWALSVK 217
Cdd:COG1388 47 SLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARR 126
|
90 100 110
....*....|....*....|....*....|
gi 501577503 218 YGVSVQDIMSWNNLSSSSIYVGQKLAIKQT 247
Cdd:COG1388 127 YGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
23-273 |
1.77e-17 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 85.13 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 23 ASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVTEVNEVAKTEKQEKSVSATWLNVRTGAGVDNSI 102
Cdd:PRK06347 328 SNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKPSTGTSTSKPSTGTSTNAKV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 103 ITSIKGGT--------KVTVETTESngwhkitYNDGKTGFVN-GKYLtdKVASTPVTTTQEVKKEATTEQAAPAAETKTe 173
Cdd:PRK06347 408 YTVVKGDSlwriannnKVTIANLKS-------WNNLKSDFIYpGQKL--KVSAGSTSNTNTSKPSTNTNTSKPSTNTNT- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 174 vkqttqattpapkaaetketpvvdkNATTHTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLaiKQTANTATP 253
Cdd:PRK06347 478 -------------------------NAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKL--KVSAGSTTN 530
|
250 260
....*....|....*....|
gi 501577503 254 KaeVKTEAPAAEKQAAPAVK 273
Cdd:PRK06347 531 N--TNTAKPSTNKPSNSTVK 548
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
203-245 |
2.03e-16 |
|
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: 72.81 E-value: 2.03e-16
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 501577503 203 HTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIK 245
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| spr |
PRK10838 |
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase; |
367-462 |
8.18e-16 |
|
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;
Pssm-ID: 236773 [Multi-domain] Cd Length: 190 Bit Score: 75.57 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 367 GKAYSWGGNGPTTFDCSGYTKYVFAKA-GISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINA 445
Cdd:PRK10838 79 GVRYRLGGSTKKGIDCSAFVQRTFREQfGLELPRSTYEQQEMGKSVSRSKLRTGDLVLFRAGSTGRHVGIYIGNNQFVHA 158
|
90
....*....|....*...
gi 501577503 446 Q-DNGVKYDNIHGSGWGK 462
Cdd:PRK10838 159 StSSGVIISSMNEPYWKK 176
|
|
| YgiM |
COG3103 |
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ... |
78-179 |
4.45e-15 |
|
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];
Pssm-ID: 442337 [Multi-domain] Cd Length: 119 Bit Score: 71.31 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 78 TEKQEKSVSATWLNVRTGAGVDNSIITSIKGGTKVTVeTTESNGWHKITYNDGKTGFVNGKYLTD-KVASTPVTTTQEVK 156
Cdd:COG3103 2 AAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTV-LGRSGGWYKVRYSNGKTGWVSSRYLTVtPSARERLPDELNLR 80
|
90 100
....*....|....*....|...
gi 501577503 157 KEATTEQAAPAAETKTEVKQTTQ 179
Cdd:COG3103 81 AGPSTSSEVLGLLPKGETVTVLK 103
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
201-244 |
1.78e-14 |
|
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: 67.13 E-value: 1.78e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 501577503 201 TTHTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
202-244 |
1.24e-13 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 64.77 E-value: 1.24e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 501577503 202 THTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
15-69 |
1.71e-12 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 65.12 E-value: 1.71e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 501577503 15 TAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 69
Cdd:COG1388 99 RRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
28-70 |
3.00e-12 |
|
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: 60.87 E-value: 3.00e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 501577503 28 VVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVT 70
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
27-69 |
1.30e-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: 59.04 E-value: 1.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 501577503 27 TVVVEAGDTLWGIAQSKGTTVDAIKKANNLTT-DKIVPGQKLQV 69
Cdd:cd00118 2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
89-179 |
8.41e-11 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 61.18 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 89 WLNVRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDkvasTPVTTTQ--EVKKEATTEQAAP 166
Cdd:TIGR04211 7 FVYMRSGPGNQYRILGSLKSGTPVTVLERSEDGYSRVRTPKGREGWVLSRYLSD----TPSARERlpELQQELAELQEEL 82
|
90
....*....|...
gi 501577503 167 aAETKTEVKQTTQ 179
Cdd:TIGR04211 83 -AELQEQLAELRQ 94
|
|
| SH3b |
smart00287 |
Bacterial SH3 domain homologues; |
80-138 |
1.50e-10 |
|
Bacterial SH3 domain homologues;
Pssm-ID: 214600 [Multi-domain] Cd Length: 63 Bit Score: 56.57 E-value: 1.50e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 501577503 80 KQEKSVSATWLNVRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGK 138
Cdd:smart00287 1 SETAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYGSGQRGYVPGY 59
|
|
| YraI |
COG4991 |
Uncharacterized conserved protein YraI [Function unknown]; |
85-150 |
7.22e-10 |
|
Uncharacterized conserved protein YraI [Function unknown];
Pssm-ID: 444015 [Multi-domain] Cd Length: 92 Bit Score: 55.84 E-value: 7.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501577503 85 VSATWLNVRTGAGVDNSIITSIKGGTKVTV-ETTESNGWHKITYnDGKTGFVNGKYLTDKVASTPVT 150
Cdd:COG4991 26 VATDDLNLRSGPGTGYPVVGTLPAGATVTVlGCTSGGGWCKVSY-GGQRGWVSARYLQVSYDGQPVP 91
|
|
| LysM |
smart00257 |
Lysin motif; |
27-69 |
9.48e-10 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 53.99 E-value: 9.48e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 501577503 27 TVVVEAGDTLWGIAQSKGTTVDAIKKANN-LTTDKIVPGQKLQV 69
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
|
|
| SH3_3 |
pfam08239 |
Bacterial SH3 domain; |
90-141 |
1.12e-09 |
|
Bacterial SH3 domain;
Pssm-ID: 462405 [Multi-domain] Cd Length: 54 Bit Score: 53.79 E-value: 1.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 501577503 90 LNVRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLT 141
Cdd:pfam08239 3 LNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGGWYKVRTYDGYEGWVSSSYLS 54
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
198-244 |
5.23e-08 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 55.13 E-value: 5.23e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 501577503 198 KNATTHTVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAI 244
Cdd:PRK10783 341 LNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
15-95 |
9.54e-07 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 50.89 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 15 TAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVTevNEVAKTEKQEKSVSATWlNVRT 94
Cdd:PRK10783 333 TLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIG--AGSSAQRLANNSDSITY-RVRK 409
|
.
gi 501577503 95 G 95
Cdd:PRK10783 410 G 410
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
145-244 |
1.52e-05 |
|
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: 45.38 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 145 ASTPVTTTQEVKKEATTEQAAPAAETKTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIWALSVKY---GVS 221
Cdd:COG1652 54 PLAAGLAAAVAAAAAAAVLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPAR 133
|
90 100
....*....|....*....|....*.
gi 501577503 222 VQDIMSWN--NLSSSS-IYVGQKLAI 244
Cdd:COG1652 134 WPEIAEANrdQIKNPDlIYPGQVLRI 159
|
|
| PRK14125 |
PRK14125 |
cell division suppressor protein YneA; Provisional |
26-88 |
1.55e-05 |
|
cell division suppressor protein YneA; Provisional
Pssm-ID: 184523 [Multi-domain] Cd Length: 103 Bit Score: 43.87 E-value: 1.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501577503 26 STVVVEAGDTLWGIAQ--------SKGTTVDAIKKANNLTTDKIVPGQKLqvteVNEVAKTeKQEKSVSAT 88
Cdd:PRK14125 37 VEITVQEGDTLWALADqyagkhhmAKNEFIEWVEDVNNLPSGHIKAGDKL----VIPVLKS-KSDSYILAA 102
|
|
| OapA |
COG3061 |
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ... |
159-249 |
4.75e-05 |
|
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442295 [Multi-domain] Cd Length: 425 Bit Score: 45.43 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 159 ATTEQAAPAAETKTEVKQTTQATTPAPKAAETKETPVVDKNatTHTVKSGDTIWALSVKYGVSVQDImswNNLSS----- 233
Cdd:COG3061 30 SPDASASRVSQPLVPLALTAEADAPAAAAPAAPAAPEGEWQ--EYTVQSGDTLSQIFRRLGLSASDL---YALLAaegda 104
|
90
....*....|....*....
gi 501577503 234 ---SSIYVGQKLAIKQTAN 249
Cdd:COG3061 105 kplSRLKPGQELRFQLDAD 123
|
|
| YgiM |
COG3103 |
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ... |
77-135 |
5.87e-05 |
|
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];
Pssm-ID: 442337 [Multi-domain] Cd Length: 119 Bit Score: 42.42 E-value: 5.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 501577503 77 KTEKQEKSVSATWLNVRTGAGVDNSIITSIKGGTKVTVeTTESNGWHKITYNdgKTGFV 135
Cdd:COG3103 64 TVTPSARERLPDELNLRAGPSTSSEVLGLLPKGETVTV-LKKSGGWFKVGYR--GTGWV 119
|
|
| spore_safA |
TIGR02899 |
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ... |
205-244 |
7.38e-05 |
|
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]
Pssm-ID: 131945 [Multi-domain] Cd Length: 44 Bit Score: 40.17 E-value: 7.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 501577503 205 VKSGDTIWALSVKYGVSVQDIMSWN-NLSSSS-IYVGQKLAI 244
Cdd:TIGR02899 1 VQKGDTLWKIAKKYGVDFDELIQANpQLSNPNlIYPGMKIKI 42
|
|
| PRK14125 |
PRK14125 |
cell division suppressor protein YneA; Provisional |
193-244 |
1.02e-04 |
|
cell division suppressor protein YneA; Provisional
Pssm-ID: 184523 [Multi-domain] Cd Length: 103 Bit Score: 41.17 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501577503 193 TPVVDKNA-TTHTVKSGDTIWALSVKY----GVSVQDIMSW----NNLSSSSIYVGQKLAI 244
Cdd:PRK14125 28 TVPVDKNQyVEITVQEGDTLWALADQYagkhHMAKNEFIEWvedvNNLPSGHIKAGDKLVI 88
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
18-271 |
1.70e-04 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 44.00 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 18 AAPTIASASTVVVeaGDTLwGIAQSKGTTVDAIKKANNLTTDKIVPGQ------KLQVTEVNEVAKTEKQEKSVSATWLN 91
Cdd:NF040676 17 AFTTTATAETIVT--ADVL-NVREKPTTESKVVEKVKNGQELKVINTEdgwskiELNGKEVFVSSEFTKDVYHVTANLLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 92 VRTGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNdGKTGFVNGKYLTDKvASTPVTTTQEVKKEATTEQAAPAA-ET 170
Cdd:NF040676 94 VRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYK-GKTAYANVSFLSST-APTEKKADEKTKQVAKVQKSVKAKeEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 171 KTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIwaLSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKqTANT 250
Cdd:NF040676 172 KTQKVAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEI--VKPKEEVKVQEEVKPKEEEKVQEIVKPKEEAK-VQEE 248
|
250 260
....*....|....*....|.
gi 501577503 251 ATPKAEVKTEAPAAEKQAAPA 271
Cdd:NF040676 249 VKVKEEAKVQEIAKAKEEAKA 269
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
23-69 |
2.52e-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: 41.53 E-value: 2.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 501577503 23 ASASTVVVEAGDTLWGIAQS---KGTTVDAIKKANNLT---TDKIVPGQKLQV 69
Cdd:COG1652 107 DAPKTYTVKPGDTLWGIAKRfygDPARWPEIAEANRDQiknPDLIYPGQVLRI 159
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
20-69 |
3.89e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 42.76 E-value: 3.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 501577503 20 PTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 69
Cdd:PRK06347 542 PSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
141-208 |
2.03e-03 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 40.60 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501577503 141 TDKVASTPVTTTQEVKKEATTEQAAPAAETKT-EVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSG 208
Cdd:COG3266 295 QPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKpVVTETAAPAAPAPEAAAAAAAPAAPAVAKKLAADEQ 363
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
16-205 |
2.10e-03 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 40.55 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 16 AFAAPTIASASTVVVEAGDTLWGIAQ---------SKGTTVDAIKKAN-----NLTTDKIVPGQKLQVTEVNEVAKTEKQ 81
Cdd:COG3170 138 AAEAAPAASGEYYPVRPGDTLWSIAArpvrpssgvSLDQMMVALYRANpdafiDGNINRLKAGAVLRVPAAEEVAALSPA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 82 E--KSVSATWLNVRTGAGVDNSIITSIKGGTKVTVETTESNgwhkityNDGKTGFVNGKYLTDKVASTPVTTTQEVKKEA 159
Cdd:COG3170 218 EarQEVQAQSADWAAYRARLAAAVEPAPAAAAPAAPPAAAA-------AAGPVPAAAEDTLSPEVTAAAAAEEADALPEA 290
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501577503 160 TTEQAAPAAETKTEV---KQTTQATTPAPKAAETKetPVVDKNATTHTV 205
Cdd:COG3170 291 AAELAERLAALEAQLaelQRLLALKNPAPAAAVSA--PAAAAAAATVEA 337
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
90-264 |
4.25e-03 |
|
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: 38.95 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 90 LNVRTGAGVDNSIITSIKGGTKVTVETTE-----------SNGWHKItyndGKTGFVNGKYltdkVASTPVTTTqevkke 158
Cdd:NF038016 1 LNVRSGPATDSAVVGTLANGAKVTVVCKVrgeqirgtvrtTSQWDRL----GSGRYVSHAY----VRWSPSLPT------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 159 atteQAAPAAETKTEVKQTTQATTPAPKAAETKETPVVDKNATTHTVKSGDTIWalsvkyGVSVQDIMSWNNLSS----S 234
Cdd:NF038016 67 ----CPWCAPKAATVATVTTGGGALNVRAAAGTGAARVGTVANGATVTVECQVW------GQEVDGTGVWYRLGDgryvS 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 501577503 235 SIYV--------GQKLAikqTANTATPKAEVKTEAPAA 264
Cdd:NF038016 137 AAYVrrpwlpwcGQDPP---TVPRGTPAQFIAAVAPPA 171
|
|
| yfaT |
COG3234 |
Uncharacterized conserved protein YfaT, DUF1175 family [Function unknown]; |
414-440 |
4.81e-03 |
|
Uncharacterized conserved protein YfaT, DUF1175 family [Function unknown];
Pssm-ID: 442466 Cd Length: 231 Bit Score: 38.54 E-value: 4.81e-03
10 20
....*....|....*....|....*....
gi 501577503 414 SQAKPGDLVFFDYGSGIS--HVGIYVGNG 440
Cdd:COG3234 153 NQALPGDLLFFDHPEDDMpyHLMIYMGDG 181
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
111-209 |
5.04e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 39.28 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501577503 111 KVTVE--TTESNGWHKITYNDGKTGFVNGKYLTDKVASTPVTTTQEVKKEATTEQAAP-AAETKTEVKQTTQATTPAPKA 187
Cdd:PTZ00144 85 KVSVDirAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPeKPKAAAPTPEPPAASKPTPPA 164
|
90 100
....*....|....*....|..
gi 501577503 188 AETKETPVVDKNATTHTVKSGD 209
Cdd:PTZ00144 165 AAKPPEPAPAAKPPPTPVARAD 186
|
|
| |
