|
Name |
Accession |
Description |
Interval |
E-value |
| amidase_AmiC |
NF038267 |
N-acetylmuramoyl-L-alanine amidase AmiC; |
2-400 |
7.66e-118 |
|
N-acetylmuramoyl-L-alanine amidase AmiC;
Pssm-ID: 468440 [Multi-domain] Cd Length: 407 Bit Score: 351.66 E-value: 7.66e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 2 RIRALVAVVGLLLTAVT-VDALAVTQVKSMRLWRAPDNTRLVFDLSGPVQHSVFTLTAPDRLVIDINGATLGAPLN---- 76
Cdd:NF038267 10 RRRLLQGAAATWLLSVSrVGFAASSQVIAVRIWPSSTYTRVTLESNVPLKYKQFALSNPERIVVDIEGVHLNSVLKgmge 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 77 -VSTSNTPITSVRSAQRTPTDLRVVVDLKKAVSPKSFVLAPNAQYGNRLVVDLY-----DQEADAVAA----SNPTPppt 146
Cdd:NF038267 90 qVRSDDPYIKSARVGQFDPNTVRLVLELKQNVSPHLFTLAPVAEFKHRLVLDLYpangaDDEDDPLLAlledYNKGD--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 147 pqppattpavpVTPAQPAIKLPPAPAGK-RDIVVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSEKGYRAEL 225
Cdd:NF038267 167 -----------LERSLPAEAPKPGKAGRdRPIVIMLDPGHGGEDPGAIGKYKTREKDVVLQIARRLKALIDKEPNMKAYM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 226 TRTGDYFIPLRKRTEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGATSETARWLADTENRSDLIGGagnVSLDDk 305
Cdd:NF038267 236 TRNEDVFIPLKVRVAKARKQRADLFVSIHADAFTSRAARGSSVFALSTKGATSTAARFLAQTQNESDLIGG---VSKSG- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 306 DRMLAGVLLDLSMTATLSSSLNVGQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQ 385
Cdd:NF038267 312 DRYLDHTMFDLVQTATINDSLKFGKEVLKRMGKVNKLHKNRVDQAGFAVLKAPDIPSILVETAFISNLEEERKLRTARFQ 391
|
410
....*....|....*
gi 914746497 386 QALARSIHTGVRQFF 400
Cdd:NF038267 392 QQVAESILAGIKAYF 406
|
|
| PRK10319 |
PRK10319 |
N-acetylmuramoyl-L-alanine amidase AmiA; |
157-406 |
8.34e-80 |
|
N-acetylmuramoyl-L-alanine amidase AmiA;
Pssm-ID: 182376 [Multi-domain] Cd Length: 287 Bit Score: 249.69 E-value: 8.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 157 PVTPAQPAIKLPPAPAGKRDIVVaIDAGHGGEDPGASGSRGQHEKDIVLDIAKELqRQINSEKGYRAELTRTGDYFIPLR 236
Cdd:PRK10319 38 PLKTSNGHSKPKAKKSGGKRVVM-LDPGHGGIDTGAIGRNGSKEKHVVLAIAKNV-RSILRNHGIDARLTRSGDTFIPLY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 237 KRTEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGATSETARWLADTENRSDLIGGagnVSLDDKDRMLAGVLLDL 316
Cdd:PRK10319 116 DRVEIAHKHGADLFMSIHADGFTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVAG---KKATDKDHLLQQVLFDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 317 SMTATLSSSLNVGQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:PRK10319 193 VQTDTIKNSLTLGSHILKKIKPVHKLHSRNTEQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQKIATAIAEGI 272
|
250
....*....|....*
gi 914746497 397 RQFF-----QQNPPP 406
Cdd:PRK10319 273 ISYFhwfdnQKAHSK 287
|
|
| AmiC |
COG0860 |
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis]; |
157-402 |
5.63e-76 |
|
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440621 Cd Length: 204 Bit Score: 236.70 E-value: 5.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 157 PVTPAQPAIKLPPAPAGKRDIVVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSeKGYRAELTRTGDYFIPLR 236
Cdd:COG0860 5 ASLALAAAPAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEA-PGAKVVLTRDDDTFVSLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 237 KRTEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGaTSETARWLAdtenrsdliggagnvslddkdrmlagvlldl 316
Cdd:COG0860 84 ERVAIANKAKADLFISIHANAAPNPSARGAEVYYYSGSQ-TSAESKKLA------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 317 smtatlssslnvgQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:COG0860 132 -------------EAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGI 198
|
....*.
gi 914746497 397 RQFFQQ 402
Cdd:COG0860 199 LRYFGK 204
|
|
| MurNAc-LAA |
cd02696 |
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ... |
178-396 |
5.44e-63 |
|
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
Pssm-ID: 119407 [Multi-domain] Cd Length: 172 Bit Score: 202.00 E-value: 5.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 178 VVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSeKGYRAELTRTGDYFIPLRKRTEIARKKGADLFVSIHADA 257
Cdd:cd02696 1 TIVIDPGHGGKDPGAVGNDGLKEKDINLAIALKLAKLLEA-AGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHANA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 258 APSKAAFGASVFALSDRGATSetarwladtenrsdliggagnvslddkdRMLAgvlldlsmtatlssslnvgQKVLGNMG 337
Cdd:cd02696 80 APNSSARGAEVYYYSGSSEES----------------------------KRLA-------------------EAIQKELV 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 914746497 338 RVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:cd02696 113 KALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPEYQDKIAEAIAEGI 171
|
|
| Amidase_3 |
pfam01520 |
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ... |
179-396 |
2.91e-51 |
|
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
Pssm-ID: 426303 Cd Length: 174 Bit Score: 171.66 E-value: 2.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 179 VAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSeKGYRAELTRTGDYFIPLRKRTEIARKKGADLFVSIHADAA 258
Cdd:pfam01520 1 IVIDPGHGGKDPGAVGPNGILEKDINLKIALKLRKLLEA-KGAEVILTRDSDETVSLEERANIANSNGADLFVSIHANAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 259 PSKAAFGASVFALSDRGATSEtarwladtenrsdliggagnvslddkdrmlagvlldlsmtatlssSLNVGQKVLGNMGR 338
Cdd:pfam01520 80 PNSSASGVEVYYLAKRKSSAE---------------------------------------------SKRLAQSIQKELVK 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 914746497 339 VTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:pfam01520 115 VLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPAYQQKIAEAIADGI 172
|
|
| Ami_3 |
smart00646 |
Ami_3 domain; |
239-396 |
5.97e-32 |
|
Ami_3 domain;
Pssm-ID: 214762 Cd Length: 113 Bit Score: 118.16 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 239 TEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGAtsetarwladtenrsdliggagnvslddkdrmlagvlldlsm 318
Cdd:smart00646 1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGA------------------------------------------ 38
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914746497 319 tatLSSSLNVGQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:smart00646 39 ---IRESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMPAVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
|
|
| spore_cwlD |
TIGR02883 |
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of ... |
178-396 |
1.22e-31 |
|
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
Pssm-ID: 274337 Cd Length: 189 Bit Score: 119.73 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 178 VVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQInSEKGYRAELTRTGDYFIP--------------LRKRTEIAR 243
Cdd:TIGR02883 2 IIVIDPGHGGIDGGAVGKDGTLEKDITLEIALKLKDYL-QEQGALVVMTREDDSDLAsegtkgysrrkiedLRKRVKLIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 244 KKGADLFVSIHADAAPSKAAFGASVFALSDRGATSETARWLADTENRsdliggagnvSLDDKDRmlagvlldlsmtatls 323
Cdd:TIGR02883 81 ESEADLFISIHLNAFPSSKYSGAQTFYYGNSEENKRLAKFIQDELRR----------NLDNTNR---------------- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914746497 324 sslnvgqkvlgnmgRVTPLHkqrveqaGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:TIGR02883 135 --------------RAKKIN-------DYYLLRNAEVPGVIVECGFLSNPEEAELLKDEDYQQKIAAAIYKGV 186
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
354-470 |
2.40e-14 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 70.51 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 354 VLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGVRQFFQQNPPPGTYIAwLRDSGKIAQGPREHTVRPGET 433
Cdd:COG1388 41 LAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIA-RRYGAAAAPSPVTYTVKKGDT 119
|
90 100 110
....*....|....*....|....*....|....*..
gi 914746497 434 LAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIPTT 470
Cdd:COG1388 120 LWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
426-468 |
2.19e-11 |
|
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: 58.56 E-value: 2.19e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 914746497 426 HTVRPGETLAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIP 468
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
424-467 |
5.35e-09 |
|
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: 51.72 E-value: 5.35e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 914746497 424 REHTVRPGETLAMIAVRYQVSVASLRSSNSLKTDE-LKVGQHLDI 467
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
425-467 |
4.33e-08 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 48.98 E-value: 4.33e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 914746497 425 EHTVRPGETLAMIAVRYQVSVASLRSSN-SLKTDELKVGQHLDI 467
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNnILDPDNLQVGQKLKI 44
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
406-476 |
8.37e-08 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 54.36 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 406 PGTYIAWLRDS---GKIA------------QGPREHTVRPGETLAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIPTT 470
Cdd:PRK10783 311 PKKHADQLRESlasGEIAavqstlvadntpLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAG 390
|
....*.
gi 914746497 471 ALASQQ 476
Cdd:PRK10783 391 SSAQRL 396
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| amidase_AmiC |
NF038267 |
N-acetylmuramoyl-L-alanine amidase AmiC; |
2-400 |
7.66e-118 |
|
N-acetylmuramoyl-L-alanine amidase AmiC;
Pssm-ID: 468440 [Multi-domain] Cd Length: 407 Bit Score: 351.66 E-value: 7.66e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 2 RIRALVAVVGLLLTAVT-VDALAVTQVKSMRLWRAPDNTRLVFDLSGPVQHSVFTLTAPDRLVIDINGATLGAPLN---- 76
Cdd:NF038267 10 RRRLLQGAAATWLLSVSrVGFAASSQVIAVRIWPSSTYTRVTLESNVPLKYKQFALSNPERIVVDIEGVHLNSVLKgmge 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 77 -VSTSNTPITSVRSAQRTPTDLRVVVDLKKAVSPKSFVLAPNAQYGNRLVVDLY-----DQEADAVAA----SNPTPppt 146
Cdd:NF038267 90 qVRSDDPYIKSARVGQFDPNTVRLVLELKQNVSPHLFTLAPVAEFKHRLVLDLYpangaDDEDDPLLAlledYNKGD--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 147 pqppattpavpVTPAQPAIKLPPAPAGK-RDIVVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSEKGYRAEL 225
Cdd:NF038267 167 -----------LERSLPAEAPKPGKAGRdRPIVIMLDPGHGGEDPGAIGKYKTREKDVVLQIARRLKALIDKEPNMKAYM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 226 TRTGDYFIPLRKRTEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGATSETARWLADTENRSDLIGGagnVSLDDk 305
Cdd:NF038267 236 TRNEDVFIPLKVRVAKARKQRADLFVSIHADAFTSRAARGSSVFALSTKGATSTAARFLAQTQNESDLIGG---VSKSG- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 306 DRMLAGVLLDLSMTATLSSSLNVGQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQ 385
Cdd:NF038267 312 DRYLDHTMFDLVQTATINDSLKFGKEVLKRMGKVNKLHKNRVDQAGFAVLKAPDIPSILVETAFISNLEEERKLRTARFQ 391
|
410
....*....|....*
gi 914746497 386 QALARSIHTGVRQFF 400
Cdd:NF038267 392 QQVAESILAGIKAYF 406
|
|
| PRK10319 |
PRK10319 |
N-acetylmuramoyl-L-alanine amidase AmiA; |
157-406 |
8.34e-80 |
|
N-acetylmuramoyl-L-alanine amidase AmiA;
Pssm-ID: 182376 [Multi-domain] Cd Length: 287 Bit Score: 249.69 E-value: 8.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 157 PVTPAQPAIKLPPAPAGKRDIVVaIDAGHGGEDPGASGSRGQHEKDIVLDIAKELqRQINSEKGYRAELTRTGDYFIPLR 236
Cdd:PRK10319 38 PLKTSNGHSKPKAKKSGGKRVVM-LDPGHGGIDTGAIGRNGSKEKHVVLAIAKNV-RSILRNHGIDARLTRSGDTFIPLY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 237 KRTEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGATSETARWLADTENRSDLIGGagnVSLDDKDRMLAGVLLDL 316
Cdd:PRK10319 116 DRVEIAHKHGADLFMSIHADGFTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVAG---KKATDKDHLLQQVLFDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 317 SMTATLSSSLNVGQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:PRK10319 193 VQTDTIKNSLTLGSHILKKIKPVHKLHSRNTEQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQKIATAIAEGI 272
|
250
....*....|....*
gi 914746497 397 RQFF-----QQNPPP 406
Cdd:PRK10319 273 ISYFhwfdnQKAHSK 287
|
|
| PRK10431 |
PRK10431 |
N-acetylmuramoyl-l-alanine amidase II; Provisional |
2-408 |
2.59e-77 |
|
N-acetylmuramoyl-l-alanine amidase II; Provisional
Pssm-ID: 236692 [Multi-domain] Cd Length: 445 Bit Score: 248.62 E-value: 2.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 2 RIR-ALVAVVGLLLTAVTVDALAVTQVKSmrlwrAPDNTRLVFDLSGPVQHSvFTLTAPDRLVIDI--NGATLGAPLNVS 78
Cdd:PRK10431 4 RIRnWLVATLLLLCAQAGAATLSDIQVSN-----GNQQARITLSFIGDPDYA-FSHQSKRTVALDIkqTGVIQGLPLLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 79 TSNTpITSVRSAqrTPTD---LRVVVDLKKavspKSFVLAPNAQYGNRLVVdLYDQEADAVAASnPTPPPTPQPPATTPA 155
Cdd:PRK10431 78 GNNL-VKAIRSG--TPKDaqtLRLVVDLTE----NGKTEAVKRQNGSNYTV-VFTINADVPPPP-PPPPVVAKRVETPAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 156 VPVTPAQPA-------------------IKLPPA---PAGKRDIVVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQR 213
Cdd:PRK10431 149 VAPRVSEPArnpfktesnrttgvissntVTRPAAratANTGDKVIIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 214 QINSEKGYRAELTRTGDYFIPLRKRTEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGATSETARWLADTENRSDL 293
Cdd:PRK10431 229 LLNDDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLEQHEKQSEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 294 IGGAGNVSLDDK-DRMLAGVLLDLSMTATLSSSLNVGQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISN 372
Cdd:PRK10431 309 LGGAGDVLANSQsDPYLSQAVLDLQFGHSQRVGYDVATSVLSQLQRIGELHKRRPEHASLGVLRSPDIPSVLVETGFISN 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 914746497 373 ANEAAKLATRSHQQALARSIHTGVRQFFQQNP----PPGT 408
Cdd:PRK10431 389 NSEERLLASDDYQQQIAEAIYKGLRNYFLAHPmqsaPQGA 428
|
|
| AmiC |
COG0860 |
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis]; |
157-402 |
5.63e-76 |
|
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440621 Cd Length: 204 Bit Score: 236.70 E-value: 5.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 157 PVTPAQPAIKLPPAPAGKRDIVVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSeKGYRAELTRTGDYFIPLR 236
Cdd:COG0860 5 ASLALAAAPAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEA-PGAKVVLTRDDDTFVSLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 237 KRTEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGaTSETARWLAdtenrsdliggagnvslddkdrmlagvlldl 316
Cdd:COG0860 84 ERVAIANKAKADLFISIHANAAPNPSARGAEVYYYSGSQ-TSAESKKLA------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 317 smtatlssslnvgQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:COG0860 132 -------------EAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGI 198
|
....*.
gi 914746497 397 RQFFQQ 402
Cdd:COG0860 199 LRYFGK 204
|
|
| MurNAc-LAA |
cd02696 |
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ... |
178-396 |
5.44e-63 |
|
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
Pssm-ID: 119407 [Multi-domain] Cd Length: 172 Bit Score: 202.00 E-value: 5.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 178 VVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSeKGYRAELTRTGDYFIPLRKRTEIARKKGADLFVSIHADA 257
Cdd:cd02696 1 TIVIDPGHGGKDPGAVGNDGLKEKDINLAIALKLAKLLEA-AGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHANA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 258 APSKAAFGASVFALSDRGATSetarwladtenrsdliggagnvslddkdRMLAgvlldlsmtatlssslnvgQKVLGNMG 337
Cdd:cd02696 80 APNSSARGAEVYYYSGSSEES----------------------------KRLA-------------------EAIQKELV 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 914746497 338 RVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:cd02696 113 KALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPEYQDKIAEAIAEGI 171
|
|
| Amidase_3 |
pfam01520 |
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ... |
179-396 |
2.91e-51 |
|
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
Pssm-ID: 426303 Cd Length: 174 Bit Score: 171.66 E-value: 2.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 179 VAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQINSeKGYRAELTRTGDYFIPLRKRTEIARKKGADLFVSIHADAA 258
Cdd:pfam01520 1 IVIDPGHGGKDPGAVGPNGILEKDINLKIALKLRKLLEA-KGAEVILTRDSDETVSLEERANIANSNGADLFVSIHANAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 259 PSKAAFGASVFALSDRGATSEtarwladtenrsdliggagnvslddkdrmlagvlldlsmtatlssSLNVGQKVLGNMGR 338
Cdd:pfam01520 80 PNSSASGVEVYYLAKRKSSAE---------------------------------------------SKRLAQSIQKELVK 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 914746497 339 VTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:pfam01520 115 VLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPAYQQKIAEAIADGI 172
|
|
| Ami_3 |
smart00646 |
Ami_3 domain; |
239-396 |
5.97e-32 |
|
Ami_3 domain;
Pssm-ID: 214762 Cd Length: 113 Bit Score: 118.16 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 239 TEIARKKGADLFVSIHADAAPSKAAFGASVFALSDRGAtsetarwladtenrsdliggagnvslddkdrmlagvlldlsm 318
Cdd:smart00646 1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGA------------------------------------------ 38
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914746497 319 tatLSSSLNVGQKVLGNMGRVTPLHKQRVEQAGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:smart00646 39 ---IRESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMPAVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
|
|
| spore_cwlD |
TIGR02883 |
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of ... |
178-396 |
1.22e-31 |
|
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
Pssm-ID: 274337 Cd Length: 189 Bit Score: 119.73 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 178 VVAIDAGHGGEDPGASGSRGQHEKDIVLDIAKELQRQInSEKGYRAELTRTGDYFIP--------------LRKRTEIAR 243
Cdd:TIGR02883 2 IIVIDPGHGGIDGGAVGKDGTLEKDITLEIALKLKDYL-QEQGALVVMTREDDSDLAsegtkgysrrkiedLRKRVKLIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 244 KKGADLFVSIHADAAPSKAAFGASVFALSDRGATSETARWLADTENRsdliggagnvSLDDKDRmlagvlldlsmtatls 323
Cdd:TIGR02883 81 ESEADLFISIHLNAFPSSKYSGAQTFYYGNSEENKRLAKFIQDELRR----------NLDNTNR---------------- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914746497 324 sslnvgqkvlgnmgRVTPLHkqrveqaGFMVLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGV 396
Cdd:TIGR02883 135 --------------RAKKIN-------DYYLLRNAEVPGVIVECGFLSNPEEAELLKDEDYQQKIAAAIYKGV 186
|
|
| AMIN |
pfam11741 |
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ... |
31-128 |
2.05e-26 |
|
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.
Pssm-ID: 463338 Cd Length: 96 Bit Score: 102.38 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 31 RLWRAPDNTRLVFDLSGPVQHSVFTLTAPDRLVIDINGATLGAPLNVSTSNTP-ITSVRSAQRTPTDLRVVVDLKKAVSP 109
Cdd:pfam11741 2 RVWPTDDGTELELETSGGEKYQVFTLSNPNRLVIDIPGAQLGLPLKRIENPSPgIKSVRVGQFDPNTVRVVVDLDGSVLP 81
|
90
....*....|....*....
gi 914746497 110 KSFVlapnAQYGNRLVVDL 128
Cdd:pfam11741 82 QVPV----FKSGEGLVVDL 96
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
354-470 |
2.40e-14 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 70.51 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 354 VLKSPDIPSILVETGFISNANEAAKLATRSHQQALARSIHTGVRQFFQQNPPPGTYIAwLRDSGKIAQGPREHTVRPGET 433
Cdd:COG1388 41 LAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIA-RRYGAAAAPSPVTYTVKKGDT 119
|
90 100 110
....*....|....*....|....*....|....*..
gi 914746497 434 LAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIPTT 470
Cdd:COG1388 120 LWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
426-468 |
2.19e-11 |
|
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: 58.56 E-value: 2.19e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 914746497 426 HTVRPGETLAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIP 468
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
424-467 |
5.35e-09 |
|
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: 51.72 E-value: 5.35e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 914746497 424 REHTVRPGETLAMIAVRYQVSVASLRSSNSLKTDE-LKVGQHLDI 467
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
425-467 |
4.33e-08 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 48.98 E-value: 4.33e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 914746497 425 EHTVRPGETLAMIAVRYQVSVASLRSSN-SLKTDELKVGQHLDI 467
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNnILDPDNLQVGQKLKI 44
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
406-476 |
8.37e-08 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 54.36 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 406 PGTYIAWLRDS---GKIA------------QGPREHTVRPGETLAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIPTT 470
Cdd:PRK10783 311 PKKHADQLRESlasGEIAavqstlvadntpLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAG 390
|
....*.
gi 914746497 471 ALASQQ 476
Cdd:PRK10783 391 SSAQRL 396
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
378-471 |
1.03e-06 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 50.96 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 378 KLATRSHQQALARSIHTGVRQFFQQNPPpGTYIAWLRDSGKIAQGPREHTVRPGETLAMIAVRYQVSVASLRSSNSLKTD 457
Cdd:PRK13914 155 KKETTTQQAAPAAETKTEVKQTTQATTP-APKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSS 233
|
90
....*....|....
gi 914746497 458 ELKVGQHLDIPTTA 471
Cdd:PRK13914 234 SIYVGQKLAIKQTA 247
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
406-475 |
5.41e-05 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 45.84 E-value: 5.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914746497 406 PGTYIAWLRDSGKIAQGPREHTVRPGETLAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIPTTALASQ 475
Cdd:PRK06347 462 PSTNTNTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNN 531
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
426-474 |
2.07e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 43.92 E-value: 2.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 914746497 426 HTVRPGETLAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDIPTTALAS 474
Cdd:PRK06347 333 YTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTS 381
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
406-467 |
2.36e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 43.53 E-value: 2.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914746497 406 PGTYIAWLRDSGKIAQGPREHTVRPGETLAMIAVRYQVSVASLRSSNSLKTDELKVGQHLDI 467
Cdd:PRK06347 388 PSTGTSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV 449
|
|
| |
