|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06915 |
PRK06915 |
peptidase; |
1-423 |
0e+00 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 691.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 1 MTVKNIVRNWIRTHEYKATTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIDLWDIDENpEIKHHPYFHCDRSDFSGN 80
Cdd:PRK06915 2 EQLKKQICDYIESHEEEAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFK-KLKDHPYFVSPRTSFSDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 81 PNLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDI 160
Cdd:PRK06915 81 PNIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 161 IFQSVIEEESGGAGTLATVLRGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIK 240
Cdd:PRK06915 161 IFQSVIEEESGGAGTLAAILRGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 241 ELETTRNQSLLDkPLYRNISIPVPINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNSWFKQ 320
Cdd:PRK06915 241 KLEEKRNDRITD-PLYKGIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDVDEWFVE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 321 KPIEFEWFGARWLPGKMDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGNIPVMVFGPGTTEKAHDCNEYIE 400
Cdd:PRK06915 320 HPVEVEWFGARWVPGELEENHPLMTTLEHNFVEIEGNKPIIEASPWGTDGGLLTQIAGVPTIVFGPGETKVAHYPNEYIE 399
|
410 420
....*....|....*....|...
gi 518071655 401 IASIVKTAEIIACTLIDWCGVDE 423
Cdd:PRK06915 400 VDKMIAAAKIIALTLLDWCEVKK 422
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-420 |
6.64e-160 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 456.38 E-value: 6.64e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIDLWDIDEnPEIKHHPYFHCDRSDFSGNPNLVAVLKGSGE-GKSIILN 99
Cdd:cd03895 2 FLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIDV-EKLKHHPGFSPVAVDYAGAPNVVGTHRPRGEtGRSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 100 GHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGAGTLATV 179
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 180 LRGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELETTRNQSLLDKPLYRNI 259
Cdd:cd03895 161 MRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARKKSHPHFSDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 260 SIPVPINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNSWFKQKPIEFEWFGARWLPGKMDV 339
Cdd:cd03895 241 PHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPWLSNHPPEVEWNGFQAEGYVLEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 340 NHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGNIPVMVFGPGTTEkAHDCNEYIEIASIVKTAEIIACTLIDWC 419
Cdd:cd03895 321 GSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDIPALCYGPGSRD-AHGFDESVDLESLRKITKTIALFIAEWC 399
|
.
gi 518071655 420 G 420
Cdd:cd03895 400 G 400
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
21-410 |
8.87e-112 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 333.21 E-value: 8.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSV---RGNEGKAQAIVVEKCRQLGLEIDLWDIDENpeikhhpyfhcdrsDFSGNPNLVAVLKGSGEGKSII 97
Cdd:TIGR01910 3 LLKDLISIPSVnppGGNEETIANYIKDLLREFGFSTDVIEITDD--------------RLKVLGKVVVKEPGNGNEKSLI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 98 LNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGAGTLA 177
Cdd:TIGR01910 69 FNGHYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 178 TVLRGYK--ADAALIPEPT-SMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELETTRNQslldKP 254
Cdd:TIGR01910 149 LLQRGYFkdADGVLIPEPSgGDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYA----RN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 255 LYRNISIPVPINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNSWFKQKPIEFEWFGARWLP 334
Cdd:TIGR01910 225 SYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGPNETP 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518071655 335 GkmdvNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGnIPVMVFGPGTTEKAHDCNEYIEIASIVKTAEI 410
Cdd:TIGR01910 305 P----DSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAG-IPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
22-424 |
8.34e-103 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 311.94 E-value: 8.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 22 LKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIDLWDIDENpEIKHHPYFHCDRSDFSGNPNLVAVLKGSGE-GKSIILNG 100
Cdd:PRK06837 26 TQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSIDPD-DLKSHPGAGPVEIDYSGAPNVVGTYRPAGKtGRSLILQG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 101 HIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGAGTLATVL 180
Cdd:PRK06837 105 HIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTGNGALSTLQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 181 RGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELETTRNQSLLDKPLYRNIS 260
Cdd:PRK06837 185 RGYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASDPHFEDVP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 261 IPVPINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNSWFKQKPIEFEWFGARWLPGKMDVN 340
Cdd:PRK06837 265 HPINFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARDDRFLSNNPPEVVWSGFLAEGYVLEPG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 341 HPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGNIPVMVFGPgTTEKAHDCNEYIEIASIVKTAEIIACTLIDWCG 420
Cdd:PRK06837 345 SEAEAALARAHAAVFGGPLRSFVTTAYTDTRFYGLYYGIPALCYGP-SGEGIHGFDERVDLESVRKVTKTIALFVAEWCG 423
|
....
gi 518071655 421 VDET 424
Cdd:PRK06837 424 VEPA 427
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
7-420 |
1.80e-102 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 309.51 E-value: 1.80e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 7 VRNWIRTHEYKATTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIDLWDIDEnpeikhhpyfhcdrsdfsGNPNLVAV 86
Cdd:COG0624 3 VLAAIDAHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPP------------------GRPNLVAR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 87 LKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVI 166
Cdd:COG0624 65 RPGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 167 EEESGGAGT---LATVLRGYKADAALIPEPTS-MKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKEL 242
Cdd:COG0624 145 DEEVGSPGAralVEELAEGLKADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 243 ETTRNQSlldkPLYRnisiPVPINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNSwfkqkp 322
Cdd:COG0624 225 EFDGRAD----PLFG----RTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVE------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 323 IEFEWFGARWLPGKMDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGNIPVMVFGPGTTEKAHDCNEYIEIA 402
Cdd:COG0624 291 VEVEVLGDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEALGIPTVVFGPGDGAGAHAPDEYVELD 370
|
410
....*....|....*...
gi 518071655 403 SIVKTAEIIACTLIDWCG 420
Cdd:COG0624 371 DLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-412 |
7.93e-77 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 242.98 E-value: 7.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIDlwdidenpeikhhpyfhcdRSDFSGNPNLVAVLkGSGEGKSIILNG 100
Cdd:cd08659 2 LLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIE-------------------STIVEGRGNLVATV-GGGDGPVLLLNG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 101 HIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGAGTLATVL 180
Cdd:cd08659 62 HIDTVPPGDGDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 181 RGY--KADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLsyfVIEQIKELETtrnqslLDKPLYRN 258
Cdd:cd08659 142 AGYadRLDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYA---LADFLAELRT------LFEELPAH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 259 ISIPVP-INIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRinqtnswfKQKPIEFEWFGARWLPGKM 337
Cdd:cd08659 213 PLLGPPtLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEE--------HEAKLTVEVSLDGDPPFFT 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518071655 338 DVNHPFMQTIlqnYQAIEHKEAVIEASPWG--TDGGILSTVGNIPVMVFGPGTTEKAHDCNEYIEIASIVKTAEIIA 412
Cdd:cd08659 285 DPDHPLVQAL---QAAARALGGDPVVRPFTgtTDASYFAKDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYK 358
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
34-419 |
1.99e-70 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 228.38 E-value: 1.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 34 NEGKAQAIVVEKCRQLGLEIDLWDIdenpeikhhpyfhcdrsdFSGNPNLVAVLKG--SGEGKSIILNGHIDVVPEGNVE 111
Cdd:PRK08596 34 NTNEAQEFIAEFLRKLGFSVDKWDV------------------YPNDPNVVGVKKGteSDAYKSLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 112 DWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGAGTLATVLRGYKADAALIP 191
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVGEAGTLQCCERGYDADFAVVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 192 EPTSMKFfpHQQGSL---WfrLRIKGKQA-HGGTRYE---------GVSSLDLSYFVIEQIKELEttRNQSLLDK----P 254
Cdd:PRK08596 176 DTSDLHM--QGQGGVitgW--ITVKSPQTfHDGTRRQmihaggglfGASAIEKMMKIIQSLQELE--RHWAVMKSypgfP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 255 LYRNIsipvpINIGTCRSGNWPSSVPDltvlEGRYGVS----PYESVEEAMLEMEEIIDRINQTNSWFKQKPIEFEWFGA 330
Cdd:PRK08596 250 PGTNT-----INPAVIEGGRHAAFIAD----ECRLWITvhfyPNETYEQVIKEIEEYIGKVAAADPWLRENPPQFKWGGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 331 RWLPGK--------MDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGnIPVMVFGPGTTEKAHDCNEYIEIA 402
Cdd:PRK08596 321 SMIEDRgeifpsleIDSEHPAVKTLSSAHESVLSKNAILDMSTTVTDGGWFAEFG-IPAVIYGPGTLEEAHSVNEKVEIE 399
|
410
....*....|....*..
gi 518071655 403 SIVKTAEIIACTLIDWC 419
Cdd:PRK08596 400 QLIEYTKVITAFIYEWC 416
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-415 |
7.55e-57 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 190.68 E-value: 7.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVR---GNEGKAQAIVVEKCRQLGLEIDLWDIDEnpeikhhpyfhcdrsdfsGNPNLVAVLKGSGEGKSII 97
Cdd:cd08011 3 LLQELVQIPSPNppgDNTSAIAAYIKLLLEDLGYPVELHEPPE------------------EIYGVVSNIVGGRKGKRLL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 98 LNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGG-AGTL 176
Cdd:cd08011 65 FNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGrAGTK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 177 ATVLRGYKA-DAALIPEPTSMK--FFPHqQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELETTrnqslldk 253
Cdd:cd08011 145 YLLEKVRIKpNDVLIGEPSGSDniRIGE-KGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEKT-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 254 plyrnisipvpINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNSWFKQKPiEFEWfgarwl 333
Cdd:cd08011 216 -----------VNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEEVSFEIKSFY-SPTV------ 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 334 pgkMDVNHPFMQTILQNYQAIEHKEAVIEASpWGTDGGILSTVGNIPVMVFGPGTTEKAHDCNEYIEIASIVKTAEIIAC 413
Cdd:cd08011 278 ---SNPDSEIVKKTEEAITEVLGIRPKEVIS-VGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHAL 353
|
..
gi 518071655 414 TL 415
Cdd:cd08011 354 VA 355
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
79-419 |
8.55e-56 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 188.84 E-value: 8.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSGEGKSIILNGHIDVVpegNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNdiQLKG 158
Cdd:cd08013 54 GRPSVVGVVRGTGGGKSLMLNGHIDTV---TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEA--GLRG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 159 DIIFQSVIEEESGGAGTLATVLRGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQ 238
Cdd:cd08013 129 DVILAAVADEEDASLGTQEVLAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 239 IKELEttrnQSLLDKPLYRNISiPVPINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNSWF 318
Cdd:cd08013 209 LEEYQ----QELPERPVDPLLG-RASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTVPNF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 319 KQKPIEFEwfgARWLPGKMDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGnIPVMVFGPGTTeKAHDCNEY 398
Cdd:cd08013 284 SYREPRIT---LSRPPFEVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAG-IPSVVFGPSGA-GLHAKEEW 358
|
330 340
....*....|....*....|.
gi 518071655 399 IEIASIVKTAEIIACTLIDWC 419
Cdd:cd08013 359 VDVESIRQLREVLSAVVREFC 379
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
21-415 |
2.52e-52 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 180.19 E-value: 2.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGNEGKAQAIV---VEKCRQLGLEIDLWDIDEnpEIKHHPYFHCdrsdfsgnPNLVAVlKGSGEgKSII 97
Cdd:PRK08651 11 FLKDLIKIPTVNPPGENYEEIAeflRDTLEELGFSTEIIEVPN--EYVKKHDGPR--------PNLIAR-RGSGN-PHLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 98 LNGHIDVVPEGnvEDWDQ-SPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIiknDIQLKGDIIFQSVIEEESGGAGTL 176
Cdd:PRK08651 79 FNGHYDVVPPG--EGWSVnVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEETGGTGTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 177 ATVLRGY-KADAALIPEPTSMKFFPH-QQGSLWFRLRIKGKQAHGGTRYEGVSS-LDLSYFVIEQIKELETTRNQSLLDK 253
Cdd:PRK08651 154 YLVEEGKvTPDYVIVGEPSGLDNICIgHRGLVWGVVKVYGKQAHASTPWLGINAfEAAAKIAERLKSSLSTIKSKYEYDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 254 PLYRnisiPVPINIG--TCRSGNWPSSVPdltvleGRYGVS------PYESVEEAMLEMEEIIDRI-NQTNSWFKQKPIE 324
Cdd:PRK08651 234 ERGA----KPTVTLGgpTVEGGTKTNIVP------GYCAFSidrrliPEETAEEVRDELEALLDEVaPELGIEVEFEITP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 325 FewfgarwLPGKM-DVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGnIPVMVFGPGTTEKAHDCNEYIEIAS 403
Cdd:PRK08651 304 F-------SEAFVtDPDSELVKALREAIREVLGVEPKKTISLGGTDARFFGAKG-IPTVVYGPGELELAHAPDEYVEVKD 375
|
410
....*....|..
gi 518071655 404 IVKTAEIIACTL 415
Cdd:PRK08651 376 VEKAAKVYEEVL 387
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
79-412 |
1.06e-47 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 167.00 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSGEGKsIILNGHIDVVP-EGnvEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDiqLK 157
Cdd:cd03894 44 GKANLLATLGPGGEGG-LLLSGHTDVVPvDG--QKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAK--LR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 158 GDIIFQSVIEEESG--GAGTLATVLRGY--KADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSY 233
Cdd:cd03894 119 KPLHLAFSYDEEVGclGVRHLIAALAARggRPDAAIVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 234 FVIEQIKELETTRNQSLLDKPLyrniSIPVP-INIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEeamlEMEEIIDRIN 312
Cdd:cd03894 199 RLIGKLRELADRLAPGLRDPPF----DPPYPtLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPE----AIDARLRDYA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 313 QTNSWFKQKPIEFEWFgARWLPGKMDVNHPF---MQTILQNYQAIehkeAVieasPWGTDGGILSTVGnIPVMVFGPGTT 389
Cdd:cd03894 271 EALLEFPEAGIEVEPL-FEVPGLETDEDAPLvrlAAALAGDNKVR----TV----AYGTEAGLFQRAG-IPTVVCGPGSI 340
|
330 340
....*....|....*....|...
gi 518071655 390 EKAHDCNEYIEIASIVKTAEIIA 412
Cdd:cd03894 341 AQAHTPDEFVELEQLDRCEEFLR 363
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
97-417 |
3.21e-46 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 161.75 E-value: 3.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 97 ILNGHIDVVPEGNVEDWdqsPYSGYEkNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQlKGDIIFQSVIEEESGGAGTL 176
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 177 ATV----LRGYKADAAL---IPEPTSM------KFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELE 243
Cdd:pfam01546 76 ALIedglLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 244 tTRNQSLLDkplyrnisiPVPINIGtcRSGNWPSS---VPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNswfkQ 320
Cdd:pfam01546 156 -SRNVDPLD---------PAVVTVG--NITGIPGGvnvIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAY----G 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 321 KPIEFEWFGaRWLPGKMDvNHPFMQTILQNYQAIEHKEAVIEASPW--GTDGGILSTvgNIP--VMVFGPGtTEKAHDCN 396
Cdd:pfam01546 220 VKVEVEYVE-GGAPPLVN-DSPLVAALREAAKELFGLKVELIVSGSmgGTDAAFFLL--GVPptVVFFGPG-SGLAHSPN 294
|
330 340
....*....|....*....|.
gi 518071655 397 EYIEIASIVKTAEIIACTLID 417
Cdd:pfam01546 295 EYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
15-420 |
1.88e-43 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 156.64 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 15 EYKA--TTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLeiDLWDIDENpeikhhpyfhcdrsdfsGNpnlvaVLKGSGE 92
Cdd:PRK13004 12 KYKAdmTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGF--DKVEIDPM-----------------GN-----VLGYIGH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 93 GKSIIL-NGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIeSIIKND-IQLKGDIIFQSVIEEE- 169
Cdd:PRK13004 68 GKKLIAfDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAA-KIIKDLgLDDEYTLYVTGTVQEEd 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 170 -SGGAGTLATVLRGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELettrNQ 248
Cdd:PRK13004 147 cDGLCWRYIIEEDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEEL----NP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 249 SLLDKP-LYRNISIPVPInigTCRSgnwPS--SVPD---------LTVLEGRYGV----SPYESVEEAMLEMEEiidrin 312
Cdd:PRK13004 223 NLKEDPfLGKGTLTVSDI---FSTS---PSrcAVPDscaisidrrLTVGETWESVlaeiRALPAVKKANAKVSM------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 313 qtnSWFKQK-----PIEFEwfgaRWLPG-KMDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGNIPVMVFGP 386
Cdd:PRK13004 291 ---YNYDRPsytglVYPTE----CYFPTwLYPEDHEFVKAAVEAYKGLFGKAPEVDKWTFSTNGVSIAGRAGIPTIGFGP 363
|
410 420 430
....*....|....*....|....*....|....
gi 518071655 387 GTTEKAHDCNEYIEIASIVKTAEIIACTLIDWCG 420
Cdd:PRK13004 364 GKEPLAHAPNEYTWKEQLVKAAAMYAAIPKSLLK 397
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
82-410 |
6.04e-43 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 154.66 E-value: 6.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLkgsGEGKSII-LNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDI 160
Cdd:PRK08588 50 NLVAEI---GSGSPVLaLSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 161 IFQSVIEEESGGAGTLATVLRGY--KADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLD-LSYFVIE 237
Cdd:PRK08588 127 RLLATAGEEVGELGAKQLTEKGYadDLDALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDpLLEFYNE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 238 QIKELET-TRNQSLLDkPLYRNISIpvpINigtcrSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTNS 316
Cdd:PRK08588 207 QKEYFDSiKKHNPYLG-GLTHVVTI---IN-----GGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 317 wfkqKPIEFEwFGARWLPGKMDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVG-NIPVMVFGPGTTEKAHDC 395
Cdd:PRK08588 278 ----AQLSLD-IYSNHRPVASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKpDFPVIIFGPGNNLTAHQV 352
|
330
....*....|....*
gi 518071655 396 NEYIEIASIVKTAEI 410
Cdd:PRK08588 353 DEYVEKDMYLKFIDI 367
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
20-218 |
9.25e-34 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 129.55 E-value: 9.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 20 TLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGleidlwdidenpeikhhpyFHCDRSDFSGNPNLVAVlKGSGeGKSIILN 99
Cdd:cd03891 2 ELAKELIRRPSVTPDDAGAQDLIAERLKALG-------------------FTCERLEFGGVKNLWAR-RGTG-GPHLCFA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 100 GHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFqsVI---EEESGGAGTL 176
Cdd:cd03891 61 GHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISF--LItsdEEGPAIDGTK 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518071655 177 AtVL-----RGYKADAALIPEPTSmkffPHQ---------QGSLWFRLRIKGKQAH 218
Cdd:cd03891 139 K-VLewlkaRGEKIDYCIVGEPTS----EKKlgdtikigrRGSLNGKLTIKGKQGH 189
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
82-417 |
1.60e-33 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 130.26 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLKGSGEGKSIILNGHIDVVPEGNveDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDII 161
Cdd:PRK13013 73 NLVARRQGARDGDCVHFNSHHDVVEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 162 FQSVIEEESGGAGTLATVL-RGY----KADAALIPEPTSM-KFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFV 235
Cdd:PRK13013 151 ISGTADEESGGFGGVAYLAeQGRfspdRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 236 IEQIKElettrnqSLLDKPLYRNISIPV--------PINIGTCRSGNwPSSVPDLT-------------VLEGRYGVSpy 294
Cdd:PRK13013 231 LAEIEE-------RLFPLLATRRTAMPVvpegarqsTLNINSIHGGE-PEQDPDYTglpapcvadrcriVIDRRFLIE-- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 295 ESVEEAMLEMEEIIDRINQTNSWFKQKPIEFEWFgarwLPGKMDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILS 374
Cdd:PRK13013 301 EDLDEVKAEITALLERLKRARPGFAYEIRDLFEV----LPTMTDRDAPVVRSVAAAIERVLGRQADYVVSPGTYDQKHID 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 518071655 375 TVGNIP-VMVFGPGTTEKAHDCNEYIEIASIVKTAEIIACTLID 417
Cdd:PRK13013 377 RIGKLKnCIAYGPGILDLAHQPDEWVGIADMVDSAKVMALVLAD 420
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
82-412 |
1.98e-33 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 128.78 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLKGSGEGkSIILNGHIDVVPEGNvEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIikNDIQLKGDII 161
Cdd:TIGR01892 48 NLVAVIGPSGAG-GLALSGHTDVVPYDD-AAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDL--AAEQLKKPLH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 162 FQSVIEEESG--GAGTLATVLRGyKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQI 239
Cdd:TIGR01892 124 LALTADEEVGctGAPKMIEAGAG-RPRHAIIGEPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 240 KELETTrnqsLLDKPLYRNISIPVP-INIGTCRSGNWPSSVPDLTVLEgrygvspYESVEEAMLEMEEIIDRINQTNSWF 318
Cdd:TIGR01892 203 VHLADT----LLREDLDEGFTPPYTtLNIGVIQGGKAVNIIPGACEFV-------FEWRPIPGMDPEELLQLLETIAQAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 319 KQKPIEFE--WFGARWLPGkmdVNHPfmqtilQNYQAIEHKE----AVIEASPWGTDGGILSTVGnIPVMVFGPGTTEKA 392
Cdd:TIGR01892 272 VRDEPGFEvqIEVVSTDPG---VNTE------PDAELVAFLEelsgNAPEVVSYGTEAPQFQELG-AEAVVCGPGDIRQA 341
|
330 340
....*....|....*....|
gi 518071655 393 HDCNEYIEIASIVKTAEIIA 412
Cdd:TIGR01892 342 HQPDEYVEIEDLVRCRAVLA 361
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
19-412 |
6.28e-33 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 127.54 E-value: 6.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 19 TTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLeiDLWDIDenpeikhhPYfhcdrsdfsGNpnlvaVLKGSGEGKSIIL 98
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGF--DEVEID--------PM---------GN-----VIGYIGGGKKKIL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 99 -NGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIeSIIKND--IQLKGDIIFQSVIEEE--SGGA 173
Cdd:cd05649 57 fDGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAA-KIMKDLglRDFAYTILVAGTVQEEdcDGVC 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 174 GTLATVLRGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELettrNQSLLDK 253
Cdd:cd05649 136 WQYISKADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQL----NPNFPEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 254 PLYRNISIPVPINIGTCRSGnwpSSVPD---------LTVLEGRYGV---------SPYESVEEAMLEMEEiiDRINQTN 315
Cdd:cd05649 212 PFLGRGTLTVTDIFSTSPSR---CAVPDscrisidrrLTVGETWEGCleeiralpaVKKYGDDVAVSMYNY--DRPSYTG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 316 SWFKqkpiefewfGARWLPG-KMDVNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGNIPVMVFGPGTTEKAHD 394
Cdd:cd05649 287 EVYE---------SERYFPTwLLPEDHELVKALLEAYKALFGARPLIDKWTFSTNGVSIMGRAGIPCIGFGPGAENQAHA 357
|
410
....*....|....*...
gi 518071655 395 CNEYIEIASIVKTAEIIA 412
Cdd:cd05649 358 PNEYTWKEDLVRCAAGYA 375
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
20-218 |
1.45e-32 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 126.35 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 20 TLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGleidlwdidenpeikhhpyFHCDRSDFSGNPNLVAVLKGsgEGKSIILN 99
Cdd:PRK13009 6 ELAQDLIRRPSVTPDDAGCQDLLAERLEALG-------------------FTCERMDFGDVKNLWARRGT--EGPHLCFA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 100 GHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFqsVI---EEESGGAGTL 176
Cdd:PRK13009 65 GHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAF--LItsdEEGPAINGTV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518071655 177 AtVL-----RGYKADAALIPEPTSmkffPHQ---------QGSLWFRLRIKGKQAH 218
Cdd:PRK13009 143 K-VLewlkaRGEKIDYCIVGEPTS----TERlgdvikngrRGSLTGKLTVKGVQGH 193
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-410 |
6.77e-30 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 118.57 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 17 KATTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLeidlwdideNPEIKHHpyfhcdrsdfsgnpNLVAVLKGSGEGK-S 95
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGI---------PFKRKGN--------------NVWAENGHFDEGKpT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 96 IILNGHIDVVPEGNveDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDiQLKGDIIFQSVIEEESGGAGT 175
Cdd:cd05651 58 LLLNSHHDTVKPNA--GWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG-PLNYNLIYAASAEEEISGKNG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 176 LATVLRGY-KADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGtRYEGVSSLDLSYFVIEQIKELETTRNQSLLDKP 254
Cdd:cd05651 135 IESLLPHLpPLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAA-RNEGDNAIYKALDDIQWLRDFRFDKVSPLLGPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 255 lyrNISIPVpINIGTCRsgnwpSSVPDLT--VLEGRygvspyesVEEAMlEMEEIIDRI-NQTNSwfKQKPIEFewfgaR 331
Cdd:cd05651 214 ---KMTVTQ-INAGTQH-----NVVPDSCtfVVDIR--------TTEAY-TNEEIFEIIrGNLKS--EIKPRSF-----R 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518071655 332 WLPGKMDVNHPFMQTIlqnyQAIEHKeavIEASPWGTDGGILStvgnIPVMVFGPGTTEKAHDCNEYIEIASIVKTAEI 410
Cdd:cd05651 269 LNSSAIPPDHPIVQAA----IAAGRT---PFGSPTLSDQALMP----FPSVKIGPGDSSRSHTADEFIELSEIEEGIDI 336
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
17-411 |
9.58e-30 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 118.32 E-value: 9.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 17 KATTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEidlWDIDENPEIKhhpyfhcdrsdfsgnpNLVavLKGSGEgksI 96
Cdd:PRK08652 3 RAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYD---VHIESDGEVI----------------NIV--VNSKAE---L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 97 ILNGHIDVVPEgnvedwdQSPYSgyEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSviEEESGGAGTl 176
Cdd:PRK08652 59 FVEVHYDTVPV-------RAEFF--VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVS--DEEEGGRGS- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 177 ATVLRGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELEttrnqslldkPLY 256
Cdd:PRK08652 127 ALFAERYRPKMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELL----------KAL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 257 RNISIPvPINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINqtnswFKQKPIEFewfgarWLPGK 336
Cdd:PRK08652 197 GKYFDP-HIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYT-----VKYEYTEI------WDGFE 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518071655 337 MDVNHPFMQTILQNYQAIEHKEAVIEASPWgTDGGILSTVGnIPVMVFGPGTTEKAHDCNEYIEIASIVKTAEII 411
Cdd:PRK08652 265 LDEDEEIVQLLEKAMKEVGLEPEFTVMRSW-TDAINFRYNG-TKTVVWGPGELDLCHTKFERIDVREVEKAKEFL 337
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
81-412 |
4.12e-28 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 114.48 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 81 PNLVAVLKGsGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDI 160
Cdd:cd05650 58 PNIVAKIPG-GNDKTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 161 IFQSVIEEESGGAGTLATVLRGY----KADAALIPE---PTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSY 233
Cdd:cd05650 137 GLLFVADEEDGSEYGIQYLLNKFdlfkKDDLIIVPDfgtEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAAS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 234 FVIEQIKELE---TTRNQSLLDKPLyrniSIPVPinigTCRSGNWP--SSVP--DLTVLEGRygVSPYESVEEAMLEMEE 306
Cdd:cd05650 217 NFALELDELLhekFDEKDDLFNPPY----STFEP----TKKEANVPnvNTIPgyDVFYFDCR--VLPTYKLDEVLKFVNK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 307 IIDRINQTNswfkQKPIEFEWF----GARWLPGKMDVNHPFMQTIlqnyqaieHKEAVIEASPWGTDGGilsTVG----- 377
Cdd:cd05650 287 IISDFENSY----GAGITYEIVqkeqAPPATPEDSEIVVRLSKAI--------KKVRGREAKLIGIGGG---TVAaflrk 351
|
330 340 350
....*....|....*....|....*....|....*.
gi 518071655 378 -NIPVMVFGPGtTEKAHDCNEYIEIASIVKTAEIIA 412
Cdd:cd05650 352 kGYPAVVWSTL-DETAHQPNEYIRISHIVKDAKVFA 386
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
81-412 |
1.59e-27 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 113.02 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 81 PNLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDI 160
Cdd:PRK13983 64 PNIVAKIPGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 161 IFQSVIEEESG---GAGTLATVLRGY--KADAALIP---EPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDL- 231
Cdd:PRK13983 144 GLAFVSDEETGskyGIQYLLKKHPELfkKDDLILVPdagNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAa 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 232 SYFVIEQIKELETTRNQ--SLLDKPLyrniSIPVPinigTCRSGNWPS--SVP--DLTVLEGRygVSPYESVEEAMLEME 305
Cdd:PRK13983 224 ADFALELDEALHEKFNAkdPLFDPPY----STFEP----TKKEANVDNinTIPgrDVFYFDCR--VLPDYDLDEVLKDIK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 306 EIIDRINQTnswfKQKPIEFEWFGARWLPGKMDVNHPFMQTiLQNyqAIEhKEAVIEASPWGTDGGilsTVG------NI 379
Cdd:PRK13983 294 EIADEFEEE----YGVKIEVEIVQREQAPPPTPPDSEIVKK-LKR--AIK-EVRGIEPKVGGIGGG---TVAaflrkkGY 362
|
330 340 350
....*....|....*....|....*....|...
gi 518071655 380 PVMVFGPGtTEKAHDCNEYIEIASIVKTAEIIA 412
Cdd:PRK13983 363 PAVVWSTL-DETAHQPNEYAKISNLIEDAKVFA 394
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
18-218 |
2.38e-27 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 112.12 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 18 ATTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIdlwdidenpEIKHhpyfhcdrsdFSGNPNLVAVlKGSGEgKSII 97
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEI---------EWMH----------FGDTKNLWAT-RGTGE-PVLA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 98 LNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGA-GTL 176
Cdd:TIGR01246 60 FAGHTDVVPAGPEEQWSSPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIdGTK 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518071655 177 ATV----LRGYKADAALIPEPTSMKFFPH-----QQGSLWFRLRIKGKQAH 218
Cdd:TIGR01246 140 KVVetlmARDELIDYCIVGEPSSVKKLGDvikngRRGSITGNLTIKGIQGH 190
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-409 |
1.70e-25 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 106.20 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIDLWDIDENpeikhhpyfhcDRsdfsgnPNLVAVLkGSGEGKSIILNG 100
Cdd:cd05652 4 LHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVENK-----------DR------FNVYAYP-GSSRQPRVLLTS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 101 HIDVVPegnvedwdqsPYSGY---EKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGAGTL- 176
Cdd:cd05652 66 HIDTVP----------PFIPYsisDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 177 ATVLRGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDlsyFVIEQIKELETTrnqSLLDKPLY 256
Cdd:cd05652 136 FNDLGLNTWDAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIE---ILVEALVKLIDA---DLPSSELL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 257 RNISipvpINIGTCRSGNWPSSVPDLTVLEGRYGVSpyESVEEAMLEMEEIIDRINQTNswfkqKPIEFEWFGARwLPGK 336
Cdd:cd05652 210 GPTT----LNIGRISGGVAANVVPAAAEASVAIRLA--AGPPEVKDIVKEAVAGILTDT-----EDIEVTFTSGY-GPVD 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518071655 337 MDVNHPFMQTILQNYqaiehkeavieaspwGTDGGILSTVGNIpvMVFGPGTTEKAHDCNEYIEIASIVKTAE 409
Cdd:cd05652 278 LDCDVDGFETDVVAY---------------GTDIPYLKGDHKR--YLYGPGSILVAHGPDEAITVSELEEAVE 333
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
82-411 |
6.71e-25 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 105.29 E-value: 6.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLkGSGEGkSIILNGHIDVVP--EGNvedWDQSPYSGYEKNGKIYGRGTTDMKGgnvALLLAIESIIKNDI-QLKG 158
Cdd:PRK05111 62 NLLASL-GSGEG-GLLLAGHTDTVPfdEGR---WTRDPFTLTEHDGKLYGLGTADMKG---FFAFILEALRDIDLtKLKK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 159 DIIFQSVIEEESGGAGTLATVLRG-YKADAALIPEPTSMK-FFPHqQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVI 236
Cdd:PRK05111 134 PLYILATADEETSMAGARAFAEATaIRPDCAIIGEPTSLKpVRAH-KGHMSEAIRITGQSGHSSDPALGVNAIELMHDVI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 237 EQIKELettRNQsLLDKplYRN--ISIPVP-INIGTCRSGNWPSSVP-------DLTVLEGrygvspyesveeamLEMEE 306
Cdd:PRK05111 213 GELLQL---RDE-LQER--YHNpaFTVPYPtLNLGHIHGGDAPNRICgccelhfDIRPLPG--------------MTLED 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 307 IIDRINQtnswfKQKPIEfewfgARWlPGKMDVNH------PFMQ----TILQNYQAIEHKEAviEASPWGTDGGILSTV 376
Cdd:PRK05111 273 LRGLLRE-----ALAPVS-----ERW-PGRITVAPlhppipGYECpadhQLVRVVEKLLGHKA--EVVNYCTEAPFIQQL 339
|
330 340 350
....*....|....*....|....*....|....*
gi 518071655 377 GnIPVMVFGPGTTEKAHDCNEYIEIASIVKTAEII 411
Cdd:PRK05111 340 G-CPTLVLGPGSIEQAHQPDEYLELSFIKPTRELL 373
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
70-405 |
2.27e-22 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 97.66 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 70 FHCDRSDFSGN-PNLVAVLKGSGeGKSIILNGHIDVV-PEGNVEDWdqsPYSgyEKNGKIYGRGTTDMKGGNVALLLAIE 147
Cdd:cd03885 37 FTVERRPLGEFgDHLIATFKGTG-GKRVLLIGHMDTVfPEGTLAFR---PFT--VDGDRAYGPGVADMKGGLVVILHALK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 148 SIIKNDIQLKGDIIFQSVIEEESGGAG---TLATVLRGykADAALIPEP--------TSMKffphqqGSLWFRLRIKGKQ 216
Cdd:cd03885 111 ALKAAGGRDYLPITVLLNSDEEIGSPGsreLIEEEAKG--ADYVLVFEParadgnlvTARK------GIGRFRLTVKGRA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 217 AHGGTRYE-GVSSLdlsYFVIEQIKELEttrnqSLLDKPlyRNISipvpINIGTCRSGNWPSSVPDLTVLEG--RYgvsp 293
Cdd:cd03885 183 AHAGNAPEkGRSAI---YELAHQVLALH-----ALTDPE--KGTT----VNVGVISGGTRVNVVPDHAEAQVdvRF---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 294 yeSVEEAMLEMEEIIDRINQTNSWFKQKpIEFEwFGARWLPgkMDVNHPFMQtILQNYQAI---EHKEAVIEASPWGTDG 370
Cdd:cd03885 245 --ATAEEADRVEEALRAIVATTLVPGTS-VELT-GGLNRPP--MEETPASRR-LLARAQEIaaeLGLTLDWEATGGGSDA 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 518071655 371 GILSTVGNIPVMVFGP-GttEKAHDCNEYIEIASIV 405
Cdd:cd03885 318 NFTAALGVPTLDGLGPvG--GGAHTEDEYLELDSLV 351
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
20-420 |
5.03e-22 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 96.40 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 20 TLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEidlwdideNPEIkhhpyfhcdrsdfSGNPNLVAVLKGSGEGKSIILN 99
Cdd:cd03896 2 DTAIELGEIPAPTFREGARADLVAEWMADLGLG--------DVER-------------DGRGNVVGRLRGTGGGPALLFS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 100 GHID-VVPEgnvedwdQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVI-EEESG---GAG 174
Cdd:cd03896 61 AHLDtVFPG-------DTPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVgEEGLGdlrGAR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 175 TLATVLRgYKADAALIPEPTSMKffPHQQ--GSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELETtrnqslld 252
Cdd:cd03896 134 YLLSAHG-ARLDYFVVAEGTDGV--PHTGavGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAA-------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 253 kplyrNISIPVPINIGTCRSGNWPSSVPDLTVLEGRYGVSPyeSVEEAMLEmEEIIDRINQTNSWFKQKPIEFEWFGARw 332
Cdd:cd03896 203 -----PYVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNP--DAELADVQ-REVEAVVSKLAAKHLRVKARVKPVGDR- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 333 lPGKmDVNHpfMQTILQNYQAIeHKEAVIEASP--WGTDGGILSTVGnIPVMVFGPGTTEKAHDCNEYIEIASIVKTAEI 410
Cdd:cd03896 274 -PGG-EAQG--TEPLVNAAVAA-HREVGGDPRPgsSSTDANPANSLG-IPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKA 347
|
410
....*....|
gi 518071655 411 IACTLIDWCG 420
Cdd:cd03896 348 YLMLAAALCG 357
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
82-419 |
2.52e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 94.87 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLkGSGEGKSIILNGHIDVVP-EGnvEDWDQSPYSGYEKNGKIYGRGTTDMKgGNVALLLA-----IESIIKNDIQ 155
Cdd:PRK07522 54 NLFATI-GPADRGGIVLSGHTDVVPvDG--QAWTSDPFRLTERDGRLYGRGTCDMK-GFIAAALAavpelAAAPLRRPLH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 156 LKgdIIFqsviEEESG--GAGTLATVL--RGYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDL 231
Cdd:PRK07522 130 LA--FSY----DEEVGclGVPSMIARLpeRGVKPAGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 232 SYFVIEQIKELettrnQSLLDKPLYRNISIPVP---INIGTCRSGNWPSSVPDLT--VLEGRY--GVSPYESVEEAMLEM 304
Cdd:PRK07522 204 AARLIAHLRDL-----ADRLAAPGPFDALFDPPystLQTGTIQGGTALNIVPAECefDFEFRNlpGDDPEAILARIRAYA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 305 EEIIDRINQTNswFKQKPIEFEWFGArwLPG-KMDVNHPFMQtILQNYQAIEHKEAVieasPWGTDGGILSTVGnIPVMV 383
Cdd:PRK07522 279 EAELLPEMRAV--HPEAAIEFEPLSA--YPGlDTAEDAAAAR-LVRALTGDNDLRKV----AYGTEAGLFQRAG-IPTVV 348
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 518071655 384 FGPGTTEKAHDCNEYIEIasivktAEIIAC-----TLIDWC 419
Cdd:PRK07522 349 CGPGSIEQAHKPDEFVEL------AQLAACeaflrRLLASL 383
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
21-411 |
3.59e-21 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 94.05 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGNEgKAQAIVVEKcrqlgleidlwdidenpEIKHHPYFHCDRSdfsgNPNLVAvLKGSGEGKSIILNG 100
Cdd:cd05647 4 LTAALVDIPSVSGNE-KPIADEIEA-----------------ALRTLPHLEVIRD----GNTVVA-RTERGLASRVILAG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 101 HIDVVP-EGNVEdwdqspySGYEKNGKIYGRGTTDMKGGnVALLLAI-----ESIIKNDIQLkgdiIF---QSVIEEESG 171
Cdd:cd05647 61 HLDTVPvAGNLP-------SRVEEDGVLYGCGATDMKAG-DAVQLKLaatlaAATLKHDLTL----IFydcEEVAAELNG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 172 gagtLATVLRGYK----ADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELETTRn 247
Cdd:cd05647 129 ----LGRLAEEHPewlaADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPRT- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 248 qSLLDKPLYRNIsipvpINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRINQTnswfkqkpIEFEW 327
Cdd:cd05647 204 -VNIDGLTYREG-----LNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYE--------IEVTD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 328 FGARWLPGkmdVNHPFMQTILQNYqaiehKEAVIEASPWgTDGGILSTVGnIPVMVFGPGTTEKAHDCNEYIEIASIVKT 407
Cdd:cd05647 270 LSPGALPG---LDHPVARDLIEAV-----GGKVRAKYGW-TDVARFSALG-IPAVNFGPGDPLLAHKRDEQVPVEQITAC 339
|
....
gi 518071655 408 AEII 411
Cdd:cd05647 340 AAIL 343
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
82-195 |
1.22e-20 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 89.41 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDII 161
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 518071655 162 FQSVIEEESGGAGTLATVLRG-----YKADAALIPEPTS 195
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDaleedLKVDYLFVGDATP 119
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
20-219 |
6.47e-20 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 91.27 E-value: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 20 TLLKKMVQQRSVR-----GNEGKAQAIVVEKCRQLGLEIDlwdIDENPEikhHPyfhcdrsdfsGNPNLVAVLKGSGEG- 93
Cdd:cd05675 2 DLLQELIRIDTTNsgdgtGSETRAAEVLAARLAEAGIQTE---IFVVES---HP----------GRANLVARIGGTDPSa 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 94 KSIILNGHIDVVPeGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGGA 173
Cdd:cd05675 66 GPLLLLGHIDVVP-ADASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518071655 174 GTLATVLRGYK-----ADAAL-------IPEPTSMKFFPHQ---QGSLWFRLRIKGKQAHG 219
Cdd:cd05675 145 NGAKWLVDNHPelfdgATFALneggggsLPVGKGRRLYPIQvaeKGIAWMKLTVRGRAGHG 205
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
25-411 |
9.86e-20 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 90.20 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 25 MVQQRSVRGNEGKAQAIVVEKCRQLGLEIDlwdIDENPEIKHHpyfhcdrsdfsGNPNLVAVLKGSGE-GKSIILNGHID 103
Cdd:cd05683 12 LVQIDSETLHEKEISKVLKKKFENLGLSVI---EDDAGKTTGG-----------GAGNLICTLKADKEeVPKILFTSHMD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 104 VVPEGNVEDWDQspysgyEKNGKIYGRGTT----DMKGGNVALLLAIESIIKNDIQlKGDIIFQSVIEEESG--GAGTLA 177
Cdd:cd05683 78 TVTPGINVKPPQ------IADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKNIP-HGQIQFVITVGEESGlvGAKALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 178 TVL----RGYKADAA------LIPEPTSMKFfphqqgslwfRLRIKGKQAHGGTRYE-GVSSLDLSYFVIEQIK----EL 242
Cdd:cd05683 151 PELidadYGYALDSEgdvgtiIVGAPTQDKI----------NAKIYGKTAHAGTSPEkGISAINIAAKAISNMKlgriDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 243 ETTrnqslldkplyrnisipvpINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIIDRInqtnswFKQKP 322
Cdd:cd05683 221 ETT-------------------ANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETT------AKEKG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 323 IEFEWFGARWLPG-KMDVNHPFMQTILQNYQAIEhKEAVIEASPWGTDGGILSTVGnIPVMVFGPGTtEKAHDCNEYIEI 401
Cdd:cd05683 276 AHAEVEVETSYPGfKINEDEEVVKLAKRAANNLG-LEINTTYSGGGSDANIINGLG-IPTVNLGIGY-ENIHTTNERIPI 352
|
410
....*....|
gi 518071655 402 ASIVKTAEII 411
Cdd:cd05683 353 EDLYDTAVLV 362
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
17-415 |
2.14e-19 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 88.56 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 17 KATTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEidLWdIDEnpeikhhpyfhcdrsdfSGNpnlvAVLKGSGEGKSI 96
Cdd:cd05653 2 DAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLE--AW-VDE-----------------AGN----AVGGAGSGPPDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 97 ILNGHIDVVPegnvedwdqspysGY----EKNGKIYGRGTTDMKGGNVALLLAieSIIKNDiQLKGDIIFQSVIEEESGG 172
Cdd:cd05653 58 LLLGHIDTVP-------------GEipvrVEGGVLYGRGAVDAKGPLAAMILA--ASALNE-ELGARVVVAGLVDEEGSS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 173 AGTLATVLRGYKADAALIPEPT-------SMKffphqqGSLWFRLRIKGKQAHggtryegvSSLDLSYFVIEQIKE-LET 244
Cdd:cd05653 122 KGARELVRRGPRPDYIIIGEPSgwdgitlGYR------GSLLVKIRCEGRSGH--------SSSPERNAAEDLIKKwLEV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 245 TRNQSLLDKPLYRNISIPVPINigtcRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMlemeEIIDRinqtnswfKQKPIE 324
Cdd:cd05653 188 KKWAEGYNVGGRDFDSVVPTLI----KGGESSNGLPQRAEATIDLRLPPRLSPEEAI----ALATA--------LLPTCE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 325 FEWFGaRWLPGKMDVNHP----FMQTIL-QNYQ-AIEHKeavieaspWGT-DGGILSTVGNIPVMVFGPGTTEKAHDCNE 397
Cdd:cd05653 252 LEFID-DTEPVKVSKNNPlaraFRRAIRkQGGKpRLKRK--------TGTsDMNVLAPLWTVPIVAYGPGDSTLDHTPNE 322
|
410
....*....|....*...
gi 518071655 398 YIEIASIVKTAEIIACTL 415
Cdd:cd05653 323 HIELAEIERAAAVLKGAL 340
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
82-194 |
2.72e-19 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 85.55 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDII 161
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 518071655 162 FQSVIEEE---SGGAGTLATVL--RGYKADAALIPEPT 194
Cdd:cd03873 81 VAFTADEEvgsGGGKGLLSKFLlaEDLKVDAAFVIDAT 118
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
83-192 |
5.35e-18 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 85.77 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 83 LVAVLKGSGEG-KSIILNGHIDVVP--EGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGD 159
Cdd:cd05674 58 LLYTWEGSDPSlKPLLLMAHQDVVPvnPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRT 137
|
90 100 110
....*....|....*....|....*....|....*....
gi 518071655 160 IIFQSVIEEESGG---AGTLATVL---RGYKADAALIPE 192
Cdd:cd05674 138 IILAFGHDEEVGGergAGAIAELLlerYGVDGLAAILDE 176
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
68-189 |
2.71e-17 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 83.84 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 68 PYFH--CDRSDFsGNPNLVAVLKGSGEG-KSIILNGHIDVVP--EGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVAL 142
Cdd:PRK08262 84 PAVHaaLEREVV-GGHSLLYTWKGSDPSlKPIVLMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAI 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 518071655 143 LLAIESIIKNDIQLKGDIIFQSVIEEESGGAGT--LATVL--RGYKADAAL 189
Cdd:PRK08262 163 LEAAEALLAQGFQPRRTIYLAFGHDEEVGGLGAraIAELLkeRGVRLAFVL 213
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
79-190 |
9.44e-17 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 81.61 E-value: 9.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKG 158
Cdd:cd03893 49 GAPVVFAEFPGAPGAPTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPV 128
|
90 100 110
....*....|....*....|....*....|....*...
gi 518071655 159 DIIFqsVIE--EESGGAGtLATVLRGYK----ADAALI 190
Cdd:cd03893 129 NVKF--IIEgeEESGSPS-LDQLVEAHRdllaADAIVI 163
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
82-189 |
2.17e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 80.82 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLKGSGEGKSIILNGHIDVVpEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGnVALLLAiesiikNDIQLKG--- 158
Cdd:PRK09133 90 NLVARLRGTDPKKPILLLAHMDVV-EAKREDWTRDPFKLVEENGYFYGRGTSDDKAD-AAIWVA------TLIRLKRegf 161
|
90 100 110
....*....|....*....|....*....|....*..
gi 518071655 159 ----DIIFQSVIEEESGGAGTLATVLRGYKA--DAAL 189
Cdd:PRK09133 162 kpkrDIILALTGDEEGTPMNGVAWLAENHRDliDAEF 198
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
78-410 |
2.69e-16 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 80.22 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 78 SGNPNLVAVLKGSG-EGKSIILNGHIDVVPEGNvEDWDQSPYSGY-EKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQ 155
Cdd:TIGR01880 55 PGKPVVVLTWPGSNpELPSILLNSHTDVVPVFR-EHWTHPPFSAFkDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 156 LKGDIIFQSVIEEESGG--------AGTLATVLR-GYKADAALiPEPT-SMKFFPHQQGSLWFRLRIKGKQAHGGTRYEG 225
Cdd:TIGR01880 134 FKRTIHISFVPDEEIGGhdgmekfaKTDEFKALNlGFALDEGL-ASPDdVYRVFYAERVPWWVVVTAPGNPGHGSKLMEN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 226 VSSLDLSYfVIEQIKELETTRNQSLLDKPlyrnisipvPINIGTCRSGNwpssvpdLTVLEG--RYGVSPYESveEA--- 300
Cdd:TIGR01880 213 TAMEKLEK-SVESIRRFRESQFQLLQSNP---------DLAIGDVTSVN-------LTKLKGgvQSNVIPSEA--EAgfd 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 301 -----MLEMEEIIDRINQtnsWFKQK----PIEFEWFGARWLPGKMDVNHPFMqTILQNYQAIEHKEAVIEASPWGTDGG 371
Cdd:TIGR01880 274 irlapSVDFEEMENRLDE---WCADAgegvTYEFSQHSGKPLVTPHDDSNPWW-VAFKDAVKEMGCTFKPEILPGSTDSR 349
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 518071655 372 ILSTVGnIPVMVFGP--GTTEKAHDCNEYIEIASIVKTAEI 410
Cdd:TIGR01880 350 YIRAAG-VPALGFSPmnNTPVLLHDHNEFLNEAVFLRGIEI 389
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
79-399 |
4.34e-16 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 79.24 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSG-EGKSIILNGHIDVVPegnVED--WDQSPYSGYE-KNGKIYGRGTTDMKGGNVALLLAIESIIKNDI 154
Cdd:cd05646 49 GKPVVVLTWEGSNpELPSILLNSHTDVVP---VFEekWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKASGF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 155 QLKGDIIFQSVIEEESGGAGTLATVLR---------GYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEG 225
Cdd:cd05646 126 KPKRTIHLSFVPDEEIGGHDGMEKFVKteefkklnvGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLEN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 226 VSSLDLSYfVIEQIKELETTRNQSLLDKPLyrnisipvpINIGTCRSGNwpssvpdLTVLEGryGVSpYESVEEamlEME 305
Cdd:cd05646 206 TAGEKLRK-VIESIMEFRESQKQRLKSNPN---------LTLGDVTTVN-------LTMLKG--GVQ-MNVVPS---EAE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 306 EIID-RI----------NQTNSWFK----QKPIEFEWFGARWLPGKMDVNHPFMQTILQNYQAiEHKEAVIEASPWGTDG 370
Cdd:cd05646 263 AGFDlRIpptvdleefeKQIDEWCAeagrGVTYEFEQKSPEKDPTSLDDSNPWWAAFKKAVKE-MGLKLKPEIFPAATDS 341
|
330 340 350
....*....|....*....|....*....|.
gi 518071655 371 GILSTVGnIPVMVFGP--GTTEKAHDCNEYI 399
Cdd:cd05646 342 RYIRALG-IPALGFSPmnNTPILLHDHNEFL 371
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
21-405 |
1.76e-15 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 77.75 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGN-EGKAQ--AIVVEKCRQLGLEIDLWDIDEnpeikhhpyfhcdrsdfSGNPNLVAVLKGSGEgKSII 97
Cdd:PRK06133 42 TLKELVSIESGSGDaEGLKQvaALLAERLKALGAKVERAPTPP-----------------SAGDMVVATFKGTGK-RRIM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 98 LNGHIDVV-PEGNVedwDQSPYsgYEKNGKIYGRGTTDMKGGnVALLLAIESIIKnDIQLK--GDIIFQSVIEEESGGAG 174
Cdd:PRK06133 104 LIAHMDTVyLPGML---AKQPF--RIDGDRAYGPGIADDKGG-VAVILHALKILQ-QLGFKdyGTLTVLFNPDEETGSPG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 175 TLATVLR-GYKADAALIPEPTSMK--FFPHQQGSLWFRLRIKGKQAHGGTRYE-GVSSL-DLSYfvieQIKELettrnqs 249
Cdd:PRK06133 177 SRELIAElAAQHDVVFSCEPGRAKdaLTLATSGIATALLEVKGKASHAGAAPElGRNALyELAH----QLLQL------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 250 lldkplyRNISIPVP---INIGTCRSGNWPSSVPDLTVLEG--RYGV-SPYESVEEAmleMEEIIdrinqtnswfkqkpi 323
Cdd:PRK06133 246 -------RDLGDPAKgttLNWTVAKAGTNRNVIPASASAQAdvRYLDpAEFDRLEAD---LQEKV--------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 324 efewfGARWLPG-----KMDVNHPFM-------------QTIlqnYQAIEHK-EAVIEASPWGTDGGILSTVGNIPVM-- 382
Cdd:PRK06133 301 -----KNKLVPDtevtlRFERGRPPLeanaasralaehaQGI---YGELGRRlEPIDMGTGGGTDAAFAAGSGKAAVLeg 372
|
410 420
....*....|....*....|....*
gi 518071655 383 --VFGPGttekAHDCNEYIEIASIV 405
Cdd:PRK06133 373 fgLVGFG----AHSNDEYIELNSIV 393
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
33-411 |
6.10e-15 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 75.86 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 33 GNEGKAQAIVVEKCRQLGLEIDlwdIDENpeikhhpyfhcdrsdfsGNpnLVAVLKGSGE--GKSIILNGHIDVVPEG-- 108
Cdd:COG2195 20 DHEEALADYLVEELKELGLEVE---EDEA-----------------GN--VIATLPATPGynVPTIGLQAHMDTVPQFpg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 109 -NVEdwdqsPysgYEKNGKIYGRGTT----DMKGGNVALLLAIESIIKNDIQlKGDI--IFqsVIEEESGGAGTLATVLR 181
Cdd:COG2195 78 dGIK-----P---QIDGGLITADGTTtlgaDDKAGVAAILAALEYLKEPEIP-HGPIevLF--TPDEEIGLRGAKALDVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 182 GYKADAALI----PEptsmkffphqqGSLW--------FRLRIKGKQAHGGTRYE-GVSSLDLSYFVIEQIKELETTRNq 248
Cdd:COG2195 147 KLGADFAYTldggEE-----------GELEyecagaadAKITIKGKGGHSGDAKEkMINAIKLAARFLAALPLGRIPEE- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 249 slldkplyrnisipVPINIGTCRSGNWPSSVPDLTVLEgrYGVSP--YESVEEAMLEMEEIIDRINQTnswFKQKPIEFE 326
Cdd:COG2195 215 --------------TEGNEGFIHGGSATNAIPREAEAV--YIIRDhdREKLEARKAELEEAFEEENAK---YGVGVVEVE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 327 WFGArwLPG-KMDVNHPFMQTILQNYQAIeHKEAVIEASPWGTDGGILSTVGnIPVMVFGPGtTEKAHDCNEYIEIASIV 405
Cdd:COG2195 276 IEDQ--YPNwKPEPDSPIVDLAKEAYEEL-GIEPKIKPIRGGLDGGILSFKG-LPTPNLGPG-GHNFHSPDERVSIESME 350
|
....*.
gi 518071655 406 KTAEII 411
Cdd:COG2195 351 KAWELL 356
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
91-175 |
9.16e-15 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 75.74 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 91 GEGKSII-LNGHIDVVPEGnvEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDI--IFQSviE 167
Cdd:cd03888 68 GEGEEVLgILGHLDVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIrlIFGT--D 143
|
....*...
gi 518071655 168 EESGGAGT 175
Cdd:cd03888 144 EETGWKCI 151
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
11-174 |
1.02e-14 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 75.72 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 11 IRTHEYKATTLLKKMVQQRSV------RGNEGKAQAIVVEKCRQLGLEIDLWDIDENP----EIKHHPyfhcdrsdfsgn 80
Cdd:cd05676 5 IDEHQDEFIERLREAVAIQSVsadpekRPELIRMMEWAAERLEKLGFKVELVDIGTQTlpdgEELPLP------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 81 PNLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDI 160
Cdd:cd05676 73 PVLLGRLGSDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNL 152
|
170
....*....|....*.
gi 518071655 161 IFqsVIE--EESGGAG 174
Cdd:cd05676 153 KF--CFEgmEESGSEG 166
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
89-162 |
1.82e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 71.65 E-value: 1.82e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518071655 89 GSGEGKSIILnGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIF 162
Cdd:PRK07205 72 GQGEELLAIL-CHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRF 144
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
89-175 |
2.04e-13 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 71.64 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 89 GSGEGKSIILnGHIDVVPEGnvEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEE 168
Cdd:TIGR01887 64 GQGEEVLGIL-GHLDVVPAG--DGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDE 140
|
....*..
gi 518071655 169 ESGGAGT 175
Cdd:TIGR01887 141 ESGWKCI 147
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
82-417 |
2.49e-13 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 71.05 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLKGSGEGKSIILNGHIDVVPEGnvEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDII 161
Cdd:cd02697 62 NLIVRRRYGDGGRTVALNAHGDVVPPG--DGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 162 FQSVIEEESGGAGTLATVLR-GYKADAALIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIK 240
Cdd:cd02697 140 LHFTYDEEFGGELGPGWLLRqGLTKPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 241 ELETTrnqslldkplYRNISIPVP------INIGTCRSGNWPSSVPDLTVLEGRYGVSPYESVEEAMLEMEEIID----- 309
Cdd:cd02697 220 ALNAQ----------YRQVSSQVEgithpyLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIAdaaas 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 310 ---------RINQTNSWfkqkpiefewfgaRWLPGkmdvNHPFMQTILQNYQAIEHKEAVIEASPWGTDGGILSTVGnIP 380
Cdd:cd02697 290 mpgisvdirRLLLANSM-------------RPLPG----NAPLVEAIQTHGEAVFGEPVPAMGTPLYTDVRLYAEAG-IP 351
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 518071655 381 VMVFGPGT----TEKAHDCNEYIEIASIVKTAEIIACTLID 417
Cdd:cd02697 352 GVIYGAGPrtvlESHAKRADERLQLEDLRRATKVIARSLRD 392
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
21-267 |
5.12e-13 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 70.45 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGNEGkaQAIVVEKCRQLGLEIDLWDidENPEIKHHPYFHcdrsDFSGNPNLVAVLKGSGEGK-SIILN 99
Cdd:cd05654 6 LLKSLVSWPSVTGTEG--ERSFADFLKEILKELPYFK--ENPSHVWQLLPP----DDLGRRNVTALVKGKKPSKrTIILI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 100 GHIDVVpegNVEDWD------------QSPYSGYE-----------KNGK-IYGRGTTDMKGGnVALLLA-IESIIKNDi 154
Cdd:cd05654 78 SHFDTV---GIEDYGelkdiafdpdelTKAFSEYVeeldeevredlLSGEwLFGRGTMDMKSG-LAVHLAlLEQASEDE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 155 QLKGDIIFQSVIEEESGGAGTLATV--LRGYKAD------AALIPEPTSMKFFPHQQ--------GSLWFRLRIKGKQAH 218
Cdd:cd05654 153 DFDGNLLLMAVPDEEVNSRGMRAAVpaLLELKKKhdleykLAINSEPIFPQYDGDQTryiytgsiGKILPGFLCYGKETH 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518071655 219 GGTRYEGVSSldlSYFVIEQIKELETtrNQSLLDKplYRNISIPVPINI 267
Cdd:cd05654 233 VGEPFAGINA---NLMASEITARLEL--NADLCEK--VEGEITPPPVCL 274
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
79-184 |
5.37e-13 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 70.07 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSG---EGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDiQ 155
Cdd:cd05677 54 TNPIVLATFSGNSsdaKRKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEG-E 132
|
90 100
....*....|....*....|....*....
gi 518071655 156 LKGDIIFQSVIEEESGGAGtLATVLRGYK 184
Cdd:cd05677 133 LDNDVVFLIEGEEESGSPG-FKEVLRKNK 160
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
21-266 |
1.02e-12 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 69.88 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 21 LLKKMVQQRSVRGNEGKAQaiVVEKCRQLGLEIDLWDidENPE-IKHHPyfhCDRsDFSGNPNLVAVLKGSGEGK-SIIL 98
Cdd:COG4187 13 LLCELVSIPSVTGTEGEKE--VAEFIYEKLSELPYFQ--ENPEhLGLHP---LPD-DPLGRKNVTALVKGKGESKkTVIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 99 NGHIDVVpegNVED---WDQSPYSGYE-----KNGK--------------IYGRGTTDMKGGnVALLLA-IESIIKNDiQ 155
Cdd:COG4187 85 ISHFDVV---DVEDygsLKPLAFDPEEltealKEIKlpedvrkdlesgewLFGRGTMDMKAG-LALHLAlLEEASENE-E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 156 LKGDIIFQSVIEEESGGAGTLATV-----LR---GYKADAALIPEPTS-------------------MKFFphqqgslwf 208
Cdd:COG4187 160 FPGNLLLLAVPDEEVNSAGMRAAVpllaeLKekyGLEYKLAINSEPSFpkypgdetryiytgsigklMPGF--------- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 518071655 209 rlRIKGKQAHGGTRYEGvssLDLSYFVIEQIKELETtrNQSLLDKplYRNISIPVPIN 266
Cdd:COG4187 231 --YCYGKETHVGEPFSG---LNANLLASELTRELEL--NPDFCEE--VGGEVTPPPVS 279
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
22-189 |
5.22e-12 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 66.98 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 22 LKKMVQQRSVrgnegKAQAIVVEKCRQLgLEIDLWDIDENPEIKHHPyfhcdrsdfsGNPNLVAVLKgSGEGKSIILNGH 101
Cdd:cd05681 5 LRDLLKIPSV-----SAQGRGIPETADF-LKEFLRRLGAEVEIFETD----------GNPIVYAEFN-SGDAKTLLFYNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 102 IDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFqsVIE-EESGGAGTLATVL 180
Cdd:cd05681 68 YDVQPAEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKF--LVEgEEEVGSPNLEKFV 145
|
170
....*....|...
gi 518071655 181 RGY----KADAAL 189
Cdd:cd05681 146 AEHadllKADGCI 158
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
91-175 |
1.19e-11 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 66.02 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 91 GEGKSI--ILnGHIDVVPEGnvEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIEsIIKnDIQL----KGDIIFQS 164
Cdd:PRK07318 76 GEGEEVlgIL-GHLDVVPAG--DGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALK-IIK-ELGLplskKVRFIVGT 150
|
90
....*....|.
gi 518071655 165 viEEESGGAGT 175
Cdd:PRK07318 151 --DEESGWKCM 159
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
79-190 |
2.56e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 64.93 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIiknDIQLKG 158
Cdd:PRK07907 69 GAPAVIGTRPAPPGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRAL---GGDLPV 145
|
90 100 110
....*....|....*....|....*....|....*...
gi 518071655 159 DIIFqsVIE--EESGGAGtLATVLRGYK----ADAALI 190
Cdd:PRK07907 146 GVTV--FVEgeEEMGSPS-LERLLAEHPdllaADVIVI 180
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
85-192 |
6.02e-11 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 64.02 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 85 AVLKGSGEGKSIIL-NGHIDVVPEgNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDiqLKGDIIFQ 163
Cdd:PRK08554 54 AVYGEIGEGKPKLLfMAHFDVVPV-NPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEP--LNGKVIFA 130
|
90 100
....*....|....*....|....*....
gi 518071655 164 SVIEEESGGAgtLATVLRGYKADAALIPE 192
Cdd:PRK08554 131 FTGDEEIGGA--MAMHIAEKLREEGKLPK 157
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
18-193 |
1.24e-10 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 62.67 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 18 ATTLLKKMVQQRSVRGNEGKAQAIVVEKCRQLGLEIdlWdIDEnpeikhhpyfhcdrsdfSGNpnlvAVLKGSGEGKSII 97
Cdd:PRK04443 8 ARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREA--W-VDE-----------------AGN----ARGPAGDGPPLVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 98 LNGHIDVVPeGN----VEDwdqspysgyeknGKIYGRGTTDMKGGNVALLLAiesIIKNDIQLKGDIIFQSVIEEE---S 170
Cdd:PRK04443 64 LLGHIDTVP-GDipvrVED------------GVLWGRGSVDAKGPLAAFAAA---AARLEALVRARVSFVGAVEEEapsS 127
|
170 180
....*....|....*....|...
gi 518071655 171 GGAgtlATVLRGYKADAALIPEP 193
Cdd:PRK04443 128 GGA---RLVADRERPDAVIIGEP 147
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
79-219 |
1.45e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 62.56 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSGEGKS-IILNGHIDVVPeGNVEDWDQSPYSGYEKNGKIYGRGTTDMKgGNVALLLA-IESIIKNDIQL 156
Cdd:PRK07906 50 GRANVVARLPGADPSRPaLLVHGHLDVVP-AEAADWSVHPFSGEIRDGYVWGRGAVDMK-DMDAMMLAvVRHLARTGRRP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 157 KGDIIFQSVIEEESGG---------------AG-------------TLATVLRGYKADAAlipeptsmkffphQQGSLWF 208
Cdd:PRK07906 128 PRDLVFAFVADEEAGGtygahwlvdnhpelfEGvteaisevggfslTVPGRDRLYLIETA-------------EKGLAWM 194
|
170
....*....|.
gi 518071655 209 RLRIKGKQAHG 219
Cdd:PRK07906 195 RLTARGRAGHG 205
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
32-196 |
2.35e-10 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 62.07 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 32 RGNEGKAQAIVVEKCRQLGLEidlwdideNPEI---KHHPYFHCDRSDFSGNPnlvavlkgsgegkSIILNGHIDVVPEG 108
Cdd:PRK08201 36 KEDVRKAAEWLAGALEKAGLE--------HVEImetAGHPIVYADWLHAPGKP-------------TVLIYGHYDVQPVD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 109 NVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFqsVIE-EESGGAGTLATVLRGYK--- 184
Cdd:PRK08201 95 PLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKF--CIEgEEEIGSPNLDSFVEEEKdkl 172
|
170
....*....|...
gi 518071655 185 -ADAALIPEpTSM 196
Cdd:PRK08201 173 aADVVLISD-TTL 184
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
202-312 |
4.93e-10 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 56.59 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 202 QQGSLWFRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELETTRNqslldkplyrNISIPVPINIGTCRSGNWPSSVPD 281
Cdd:pfam07687 3 HKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIG----------FDFPRTTLNITGIEGGTATNVIPA 72
|
90 100 110
....*....|....*....|....*....|.
gi 518071655 282 LTVLEGRYGVSPYESVEEAMLEMEEIIDRIN 312
Cdd:pfam07687 73 EAEAKFDIRLLPGEDLEELLEEIEAILEKEL 103
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
37-196 |
6.04e-09 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 57.70 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 37 KAQAIVVEKCRQLGLEidlwdidenpeikhhpyfHCDRSDFSGNPNLVAVLKGSGEGKSIILNGHIDVVPEGNVEDWDQS 116
Cdd:cd05680 25 RAAEWLADKLTEAGFE------------------HTEVLPTGGHPLVYAEWLGAPGAPTVLVYGHYDVQPPDPLELWTSP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 117 PYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFqsVIE-EESGGAGTLATVLRGYK----ADAALIP 191
Cdd:cd05680 87 PFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKF--LIEgEEEIGSPSLPAFLEENAerlaADVVLVS 164
|
....*
gi 518071655 192 EpTSM 196
Cdd:cd05680 165 D-TSM 168
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
96-313 |
8.50e-09 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 56.89 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 96 IILNGHIDVV-PEGN----VEDWDqspysgyekNGKIYGRGTTDMKGGNVALLLAIESIIKNdiQLKGDIIFQSVI--EE 168
Cdd:PRK07338 95 VLLTGHMDTVfPADHpfqtLSWLD---------DGTLNGPGVADMKGGIVVMLAALLAFERS--PLADKLGYDVLInpDE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 169 ESGGAGT---LATVLRGYkaDAALIPEPTsmkfFPH------QQGSLWFRLRIKGKQAHGGTRY-EGVSSLDLSYFVIEQ 238
Cdd:PRK07338 164 EIGSPASaplLAELARGK--HAALTYEPA----LPDgtlagaRKGSGNFTIVVTGRAAHAGRAFdEGRNAIVAAAELALA 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518071655 239 IKELETTRNQslldkplyrnisipVPINIGTCRSGNWPSSVPDLTVLegRYGVSPYESVEEAMLEME--EIIDRINQ 313
Cdd:PRK07338 238 LHALNGQRDG--------------VTVNVAKIDGGGPLNVVPDNAVL--RFNIRPPTPEDAAWAEAElkKLIAQVNQ 298
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
79-311 |
2.63e-08 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 55.42 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSGEGKSIILNGHIDVVPegnVEDWDQSPYSGYEKnGKIYGRGttdmKGGNVALLLAiESIIKNDI--QL 156
Cdd:cd08019 40 GGTGVIATIKGGKAGKTVALRADIDALP---VEECTDLEYKSKNP-GLMHACG----HDGHTAMLLG-AAKILNEIkdTI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 157 KGDI--IFQSViEEESGGAGTLATVLRGYKADAAL-------IPEPT-SMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGV 226
Cdd:cd08019 111 KGTVklIFQPA-EEVGEGAKQMIEEGVLEDVDAVFgihlwsdVPAGKiSVEAGPRMASADIFKIEVKGKGGHGSMPHQGI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 227 SS-LDLSYFVIEqikelettrnqslLDKPLYRNISI--PVPINIGTCRSGNWPSSVPDLTVLEG--RYgvspYEsvEEAM 301
Cdd:cd08019 190 DAvLAAASIVMN-------------LQSIVSREIDPlePVVVTVGKLNSGTRFNVIADEAKIEGtlRT----FN--PETR 250
|
250
....*....|
gi 518071655 302 LEMEEIIDRI 311
Cdd:cd08019 251 EKTPEIIERI 260
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
71-312 |
3.48e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 55.16 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 71 HCDRSDF-SGNPNLVAVLKGSGEGKSIILNG-HIDVVPeGNVEDWDQSPYSGYEKNGKIYGRGTTDMKgGNVALL--LAI 146
Cdd:cd08012 54 VIDHVSYvKGRGNIIVEYPGTVDGKTVSFVGsHMDVVT-ANPETWEFDPFSLSIDGDKLYGRGTTDCL-GHVALVteLFR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 147 EsIIKNDIQLKGDIIFQSVIEEESG---GAGTLATVLRG----------YKADAAlIPEPTSmkffpHQQGSLWFRLRIK 213
Cdd:cd08012 132 Q-LATEKPALKRTVVAVFIANEENSeipGVGVDALVKSGlldnlksgplYWVDSA-DSQPCI-----GTGGMVTWKLTAT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 214 GKQAHGGTRYEGVSSLDLsyfVIEQIKELEttrnqslldKPLYRNISiPVP-------INIGTCRSGNW--PS----SVP 280
Cdd:cd08012 205 GKLFHSGLPHKAINALEL---VMEALAEIQ---------KRFYIDFP-PHPkeevygfATPSTMKPTQWsyPGgsinQIP 271
|
250 260 270
....*....|....*....|....*....|..
gi 518071655 281 DLTVLEGRYGVSPYESVEEAMLEMEEIIDRIN 312
Cdd:cd08012 272 GECTICGDCRLTPFYDVKEVREKLEEYVDDIN 303
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
34-314 |
5.92e-08 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 54.14 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 34 NEGKAQAIVVEKCRQLGLEIdlwdidenpeikhhpyfhcdrSDFSGNPNLVAVLKGSGEGKSIILNGHIDVVP--EGNve 111
Cdd:cd03886 17 EEFRTAARIAEELRELGLEV---------------------RTGVGGTGVVATLKGGGPGPTVALRADMDALPiqEET-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 112 dwDQSPYSGYEkngkiygrGTTDMKG--GNVALLLAIESIIKNDI-QLKGDI--IFQSViEEESGGAGTL--ATVLRGYK 184
Cdd:cd03886 74 --GLPFASKHE--------GVMHACGhdGHTAMLLGAAKLLAERRdPLKGTVrfIFQPA-EEGPGGAKAMieEGVLENPG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 185 ADAALipeptSMKFFPHQQ-GSLW------------FRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELeTTRNQSLL 251
Cdd:cd03886 143 VDAAF-----GLHVWPGLPvGTVGvrsgalmasadeFEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTV-VSRELDPL 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518071655 252 DkplyrnisiPVPINIGTCRSGNWPSSVPDLTVLEG--RygvspyeSVEEAMleMEEIIDRINQT 314
Cdd:cd03886 217 E---------PAVVTVGKFHAGTAFNVIPDTAVLEGtiR-------TFDPEV--REALEARIKRL 263
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
79-189 |
8.72e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 53.99 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKgSGEGKSIILNGHIDVVPEGNVEDWDQSPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDiqlKG 158
Cdd:PRK06446 49 GHPVVYGEIN-VGAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKH---KL 124
|
90 100 110
....*....|....*....|....*....|....*.
gi 518071655 159 DIIFQSVIE-EESGGAGTLATVLRGY----KADAAL 189
Cdd:PRK06446 125 NVNVKFLYEgEEEIGSPNLEDFIEKNknklKADSVI 160
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
85-419 |
1.70e-07 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 52.86 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 85 AVLKGSGEgksIILNGHIDVVPeGNVEdwdqspysGYEKNGKIYGRGTTDMKGGNVALLLAieSIIKNDIQLKgdIIFQS 164
Cdd:PRK00466 55 SFILGEGD---ILLASHVDTVP-GYIE--------PKIEGEVIYGRGAVDAKGPLISMIIA--AWLLNEKGIK--VMVSG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 165 VIEEESGGAGTLATVLRGYKADAALIPEPT-SMKFFPHQQGSLWFRLRIKGKQAHGGTRYEGVsSLDLSYFVIEQIKELE 243
Cdd:PRK00466 119 LADEESTSIGAKELVSKGFNFKHIIVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNL-IVDISKKIIEVYKQPE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 244 TtrnqslldkplYRNISIpVPINIgtcRSGNWPSSVPD--LTVLEGRYgvsPYESVEEAMleMEEIIDRINQTNSwfkqK 321
Cdd:PRK00466 198 N-----------YDKPSI-VPTII---RAGESYNVTPAklYLHFDVRY---AINNKRDDL--ISEIKDKFQECGL----K 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 322 PIEfewfgaRWLPGKMDVNHP----FMQTIL-QNYQAIEHKEAvieaspwGT-DGGILSTVGNiPVMVFGPGTTEKAHDC 395
Cdd:PRK00466 254 IVD------ETPPVKVSINNPvvkaLMRALLkQNIKPRLVRKA-------GTsDMNILQKITT-SIATYGPGNSMLEHTN 319
|
330 340
....*....|....*....|....
gi 518071655 396 NEYIEIASIVKTAEIIACTLIDWC 419
Cdd:PRK00466 320 QEKITLDEIYIAVKTYMLAIEELW 343
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
31-287 |
4.86e-06 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 48.49 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 31 VRGNEGKAQAIVVEKCRQLGLEIdlwdidenpeikhhpyfhcdRSDFSGNPNLVAVLKGSGEGKSIILNGHIDVVPEGNV 110
Cdd:TIGR01891 14 LSFEEFKTSSLIAEALESLGIEV--------------------RRGVGGATGVVATIGGGKPGPVVALRADMDALPIQEQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 111 EDWdqsPYSGyEKNGKIYGRGttdmKGGNVALLLAIESIIK-NDIQLKGDI--IFQSVieeESGGAGTLATVlrgykADA 187
Cdd:TIGR01891 74 TDL---PYKS-TNPGVMHACG----HDLHTAILLGTAKLLKkLADLLEGTVrlIFQPA---EEGGGGATKMI-----EDG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 188 AL--IPEPTSMKFFPHQQ-GSLW------------FRLRIKGKQAHGGTRYEGVSSLDLSYFVIEQIKELeTTRNQSLLD 252
Cdd:TIGR01891 138 VLddVDAILGLHPDPSIPaGTVGlrpgtimaaadkFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQI-VSRNVDPSR 216
|
250 260 270
....*....|....*....|....*....|....*
gi 518071655 253 KPLyrnisipvpINIGTCRSGNWPSSVPDLTVLEG 287
Cdd:TIGR01891 217 PAV---------VSVGIIEAGGAPNVIPDKASMSG 242
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
84-287 |
7.25e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349917 [Multi-domain] Cd Length: 403 Bit Score: 47.81 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 84 VAVLKGSGEGKSIILNGHIDVVPegnVEDWDQSPYSGYEKNgKIYGRGTTDMKG----GNVALLLAI-ESIIKNDIQLKG 158
Cdd:cd05667 57 VGILKGGKPGPVIALRADMDALP---VEEKTGLPFASKVKT-TYLGQTVGVMHAcghdAHVAILLGAaEVLAANKDKIKG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 159 DI--IFQSViEE-----ESGGAGTLAT--VLRGYKADAA--------LIPEPTSMKFFPHQQGSLWFRLRIKGKQAHGGT 221
Cdd:cd05667 133 TVmfIFQPA-EEgppegEEGGAKLMLKegAFKDYKPEAIfglhvgsgLPSGQLGYRSGPIMASADRFRITVKGKQTHGSR 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518071655 222 RYEGVsslDLSYFVIEQIKELETTrnqslldkpLYRNISI---PVPINIGTCRSGNWPSSVPDLTVLEG 287
Cdd:cd05667 212 PWDGI---DPIMASAQIIQGLQTI---------ISRRIDLtkePAVISIGKINGGTRGNIIPEDAEMVG 268
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
87-174 |
1.44e-05 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 47.27 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 87 LKGSGEGKSIILNgHIDVVPeGNVEDWDQ-----SPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDII 161
Cdd:PRK06156 104 LGGSGSDKVGILT-HADVVP-ANPELWVLdgtrlDPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIE 181
|
90
....*....|...
gi 518071655 162 FQSVIEEESGGAG 174
Cdd:PRK06156 182 LLVYTTEETDGDP 194
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
79-314 |
2.65e-05 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 46.11 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 79 GNPNLVAVLKGSGEGKSIILNGHIDVVPegnVEDWDQSPYSgyEKNgkiygrgttdmKG--------GNVALLL-AIESI 149
Cdd:cd08021 52 GGTGVVATLKGGKPGKTVALRADMDALP---IEEETDLPFK--SKN-----------PGvmhacghdGHTAMLLgAAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 150 IKNDIQLKGDI--IFQSVIEEESGGAGTL--ATVLRGykADAAL-------IPEPT-SMKFFPHQQGSLWFRLRIKGKQA 217
Cdd:cd08021 116 AENKDEIKGTVrfIFQPAEEVPPGGAKPMieAGVLEG--VDAVFglhlwstLPTGTiAVRPGAIMAAPDEFDITIKGKGG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 218 HGGTRYEGVSSLDLSYFVIEQIKELeTTRNQSLLDKPLyrnisipvpINIGTCRSGNWPSSVPDLTVLEGRYGVSPYESV 297
Cdd:cd08021 194 HGSMPHETVDPIVIAAQIVTALQTI-VSRRVDPLDPAV---------VTIGTFQGGTSFNVIPDTVELKGTVRTFDEEVR 263
|
250
....*....|....*..
gi 518071655 298 EEAMLEMEEIIDRINQT 314
Cdd:cd08021 264 EQVPKRIERIVKGICEA 280
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
78-190 |
4.31e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 45.55 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 78 SGNPNLVAVLKGSGEGKSIILNGHIDVVPEgNVEDWDQ-SPY----------------------SGYEKNGKIYGRGTTD 134
Cdd:cd05678 45 SGLPLLLAEKPISDARKTVLFYMHLDGQPV-DPSKWDQkSPYtpvlkrkdaagnweeinwdaifSNLDPEWRVFARAAAD 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518071655 135 MKGGNVALLLAIESIIKNDIQLKGD--IIFQSviEEESGGAGTLATVLRG---YKADAALI 190
Cdd:cd05678 124 DKGPIMMMLAALDALKAGGIAPKFNvkIILDS--EEEKGSPSLPKAVKEYkelLAADALII 182
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
96-229 |
5.00e-05 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 45.16 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 96 IILNGHIDVV-PEGNVED--WDQspysgyeKNGKIYGRGTTDMKGGNVALLLAIESIIKNDIQLKGDIIFQSVIEEESGG 172
Cdd:PRK07473 78 ILIAGHMDTVhPVGTLEKlpWRR-------EGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGT 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 173 AGTLATVlrgyKADAA-----LIPEP-------TSMKFFPHQqgslwFRLRIKGKQAHGGTRY-EGVSSL 229
Cdd:PRK07473 151 PSTRDLI----EAEAArnkyvLVPEPgrpdngvVTGRYAIAR-----FNLEATGRPSHAGATLsEGRSAI 211
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
82-192 |
2.76e-03 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 38.81 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 82 NLVAVLKGSGEGKSIILNGHIDVVPEGNvedwdqspysgyekngkiygrGTTDmKGGNVALLLAIESIIKNDIQLKGDII 161
Cdd:pfam04389 1 NVIAKLPGKAPDEVVLLSAHYDSVGTGP---------------------GADD-NASGVAALLELARVLAAGQRPKRSVR 58
|
90 100 110
....*....|....*....|....*....|.
gi 518071655 162 FQSVIEEESGgagtlatvLRGYKADAALIPE 192
Cdd:pfam04389 59 FLFFDAEEAG--------LLGSHHFAKSHPP 81
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
94-182 |
4.40e-03 |
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M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 39.04 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518071655 94 KSIILNGHIDVVPEGNVE---DWDQSPYSGYEKNGKIYGRGTT---DmKGGNVALLLAI-ESiikNDIQLkGDIIFQSVI 166
Cdd:cd03890 61 PPVILQGHMDMVCEKNADsehDFEKDPIKLRIDGDWLKATGTTlgaD-NGIGVAYALAIlED---KDIEH-PPLEVLFTV 135
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90
....*....|....*....
gi 518071655 167 EEESG--GAGTL-ATVLRG 182
Cdd:cd03890 136 DEETGmtGALGLdPSLLKG 154
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| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
100-151 |
8.06e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 38.36 E-value: 8.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 518071655 100 GHIDVVPeGNVEDWDQ--SPYSGYEKNGKIYGRGTTDMKGGNVALLLAIESIIK 151
Cdd:PRK07079 92 GHGDVVR-GYDEQWREglSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQVLA 144
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