|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06915 |
PRK06915 |
peptidase; |
4-421 |
0e+00 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 735.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 4 ERLKQQIRQWLFENKSDGIKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDVWEPDGVELINHPYFVSPRGKFQGSP 83
Cdd:PRK06915 2 EQLKKQICDYIESHEEEAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFKKLKDHPYFVSPRTSFSDSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 84 NVVGIKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVY 163
Cdd:PRK06915 82 NIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 164 FQSVIEEESGGSGTLAAILRGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQE 243
Cdd:PRK06915 162 FQSVIEEESGGAGTLAAILRGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 244 LEKKRNERIIDPLYKSVPIPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFVEHP 323
Cdd:PRK06915 242 LEEKRNDRITDPLYKGIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDVDEWFVEHP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 324 TIVEWFGARWLPGAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAETPTIVFGPGVTEKAHHPNEYIEID 403
Cdd:PRK06915 322 VEVEWFGARWVPGELEENHPLMTTLEHNFVEIEGNKPIIEASPWGTDGGLLTQIAGVPTIVFGPGETKVAHYPNEYIEVD 401
|
410
....*....|....*...
gi 516364722 404 KVFQAAEIIALTIIDWCG 421
Cdd:PRK06915 402 KMIAAAKIIALTLLDWCE 419
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
23-421 |
2.43e-167 |
|
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: 475.26 E-value: 2.43e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 23 KLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDVWEPDGVELINHPYFVSPRGKFQGSPNVVGIKKG-NGEGRSLILN 101
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIDVEKLKHHPGFSPVAVDYAGAPNVVGTHRPrGETGRSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 102 GHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGGSGTLAAI 181
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 182 LRGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERII-DPLYKSV 260
Cdd:cd03895 161 MRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARKKsHPHFSDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 261 PIPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFVEHPTIVEWFGARWLPGAIDT 340
Cdd:cd03895 241 PHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPWLSNHPPEVEWNGFQAEGYVLEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 341 KHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAETPTIVFGPGvTEKAHHPNEYIEIDKVFQAAEIIALTIIDWC 420
Cdd:cd03895 321 GSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDIPALCYGPG-SRDAHGFDESVDLESLRKITKTIALFIAEWC 399
|
.
gi 516364722 421 G 421
Cdd:cd03895 400 G 400
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
1-421 |
9.77e-119 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 352.38 E-value: 9.77e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 1 MKDERLKQQIRQWLFENKSDGIKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDVWEPDGVELINHPYFVSPRGKFQ 80
Cdd:PRK06837 2 MLTPDLTQRILAAVDAGFDAQVAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSIDPDDLKSHPGAGPVEIDYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 81 GSPNVVGIKKGNGE-GRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLK 159
Cdd:PRK06837 82 GAPNVVGTYRPAGKtGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 160 GDVYFQSVIEEESGGSGTLAAILRGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIE 239
Cdd:PRK06837 162 ARVHFQSVIEEESTGNGALSTLQRGYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 240 HIQELEKKRNERII-DPLYKSVPIPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPW 318
Cdd:PRK06837 242 ALRELEAEWNARKAsDPHFEDVPHPINFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARDDRF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 319 FVEHPTIVEWFGARWLPGAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAETPTIVFGPgVTEKAHHPNE 398
Cdd:PRK06837 322 LSNNPPEVVWSGFLAEGYVLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTRFYGLYYGIPALCYGP-SGEGIHGFDE 400
|
410 420
....*....|....*....|...
gi 516364722 399 YIEIDKVFQAAEIIALTIIDWCG 421
Cdd:PRK06837 401 RVDLESVRKVTKTIALFVAEWCG 423
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
22-402 |
3.67e-114 |
|
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: 338.99 E-value: 3.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADS---TQGNEQTAQDIVIATLQNIGLEVDVWEPDGVELINHPyfvsprgkfqgspNVVGIKKGNGEGRSL 98
Cdd:TIGR01910 1 VELLKDLISIPSvnpPGGNEETIANYIKDLLREFGFSTDVIEITDDRLKVLG-------------KVVVKEPGNGNEKSL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 99 ILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGGSGTL 178
Cdd:TIGR01910 68 IFNGHYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 179 AAILRGYK--ADAAIIPEPTN-MKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERIidp 255
Cdd:TIGR01910 148 YLLQRGYFkdADGVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARN--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 256 LYKSVPIPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFVEHPTIVEWFGarwlP 335
Cdd:TIGR01910 225 SYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSG----P 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516364722 336 GAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKvAETPTIVFGPGVTEKAHHPNEYIEI 402
Cdd:TIGR01910 301 NETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRK-AGIPSIVYGPGDLETAHQVNEYISI 366
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
8-421 |
5.85e-108 |
|
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: 323.76 E-value: 5.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 8 QQIRQWLFENKSDGIKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDVWEPDGvelinhpyfvsprgkfqGSPNVVG 87
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPP-----------------GRPNLVA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 88 IKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSV 167
Cdd:COG0624 64 RRPGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 168 IEEESGGSGT---LAAILRGYKADAAIIPEPTN-MKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQE 243
Cdd:COG0624 144 GDEEVGSPGAralVEELAEGLKADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 244 LEkkrNERIIDPLYKsvpiPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLAclKQVDPWFVEhp 323
Cdd:COG0624 224 LE---FDGRADPLFG----RTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLA--AAAPGVEVE-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 324 tiVEWFGARWLPGAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAETPTIVFGPGVTEKAHHPNEYIEID 403
Cdd:COG0624 293 --VEVLGDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEALGIPTVVFGPGDGAGAHAPDEYVELD 370
|
410
....*....|....*...
gi 516364722 404 KVFQAAEIIALTIIDWCG 421
Cdd:COG0624 371 DLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
23-416 |
6.25e-82 |
|
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: 256.07 E-value: 6.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 23 KLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVdvwEPDGVElinhpyfvsprgkfqGSPNVVGiKKGNGEGRSLILNG 102
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGI---ESTIVE---------------GRGNLVA-TVGGGDGPVLLLNG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 103 HIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGGSGTLAAIL 182
Cdd:cd08659 62 HIDTVPPGDGDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 183 RGY--KADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERiiDPLYKSV 260
Cdd:cd08659 142 AGYadRLDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAH--PLLGPPT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 261 pipipINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLAclkqvdpwFVEHPTIVEWFGARWLPGAIDT 340
Cdd:cd08659 220 -----LNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILE--------EHEAKLTVEVSLDGDPPFFTDP 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516364722 341 KHEFVNKLINNYEHVLGTPPVVEASPWgTDGGLLTKVAETPTIVFGPGVTEKAHHPNEYIEIDKVFQAAEIIALTI 416
Cdd:cd08659 287 DHPLVQALQAAARALGGDPVVRPFTGT-TDASYFAKDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
16-420 |
1.14e-73 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 236.47 E-value: 1.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 16 ENKSDGIKLLQQLV--QADSTQG-NEQTAQDIVIATLQNIGLEVDVWEpdgvelinhpyfVSPrgkfqGSPNVVGIKKG- 91
Cdd:PRK08596 10 LRKDELLELLKTLVrfETPAPPArNTNEAQEFIAEFLRKLGFSVDKWD------------VYP-----NDPNVVGVKKGt 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 92 -NGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEE 170
Cdd:PRK08596 73 eSDAYKSLIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 171 ESGGSGTLAAILRGYKADAAIIPEPTNMKIFpKQQGSIWFKIHIKGRAA-HGGTRYE---------GVSAIEKALIAIEH 240
Cdd:PRK08596 153 EVGEAGTLQCCERGYDADFAVVVDTSDLHMQ-GQGGVITGWITVKSPQTfHDGTRRQmihaggglfGASAIEKMMKIIQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 241 IQELEkkRNERIIdplyKSVPIPIP----INIGKIEGGNWPSSVADyvciEGRIGVA----PEETIEAAKLEVENWLACL 312
Cdd:PRK08596 232 LQELE--RHWAVM----KSYPGFPPgtntINPAVIEGGRHAAFIAD----ECRLWITvhfyPNETYEQVIKEIEEYIGKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 313 KQVDPWFVEHPTIVEWFGARWL-------PG-AIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKvAETPTIV 384
Cdd:PRK08596 302 AAADPWLRENPPQFKWGGESMIedrgeifPSlEIDSEHPAVKTLSSAHESVLSKNAILDMSTTVTDGGWFAE-FGIPAVI 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 516364722 385 FGPGVTEKAHHPNEYIEIDKVFQAAEIIALTIIDWC 420
Cdd:PRK08596 381 YGPGTLEEAHSVNEKVEIEQLIEYTKVITAFIYEWC 416
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-420 |
2.11e-69 |
|
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: 224.28 E-value: 2.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 20 DGIKLLQQLVQADS---TQGNEQTAQDIVIAT-----LQNIGLEVDVWEpdgvelinhpyfVSPrgkfqGSPNVVGIKKG 91
Cdd:cd08013 2 DPVSLTQTLVRINSsnpSLSATGGAGEAEIATyvaawLAHRGIEAHRIE------------GTP-----GRPSVVGVVRG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 92 NGEGRSLILNGHIDVVpagDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQnlKVSLKGDVYFQSVIEEE 171
Cdd:cd08013 65 TGGGKSLMLNGHIDTV---TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAK--EAGLRGDVILAAVADEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 172 SGGSGTLAAILRGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKA---LIAIEhiqELEKKR 248
Cdd:cd08013 140 DASLGTQEVLAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAgyfLVALE---EYQQEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 249 NERIIDPLYKsvpiPIPINIGKIEGGNWPSSvadY-----VCIEGRigVAPEETIEAAKLEVENWLACLKQVDPWF-VEH 322
Cdd:cd08013 217 PERPVDPLLG----RASVHASLIKGGEEPSS---YparctLTIERR--TIPGETDESVLAELTAILGELAQTVPNFsYRE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 323 PTIVEWFGarwlPGAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKvAETPTIVFGPGVTeKAHHPNEYIEI 402
Cdd:cd08013 288 PRITLSRP----PFEVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAE-AGIPSVVFGPSGA-GLHAKEEWVDV 361
|
410
....*....|....*...
gi 516364722 403 DKVFQAAEIIALTIIDWC 420
Cdd:cd08013 362 ESIRQLREVLSAVVREFC 379
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
20-416 |
1.41e-63 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 209.46 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 20 DGIKLLQQLVQADSTQGNEQTAQDIV---IATLQNIGLEVDVWEPDGVElinhpyfvsPRGKFQGSPNVVGiKKGNGEGR 96
Cdd:PRK08651 7 DIVEFLKDLIKIPTVNPPGENYEEIAeflRDTLEELGFSTEIIEVPNEY---------VKKHDGPRPNLIA-RRGSGNPH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 97 sLILNGHIDVVPAGDIEQwEHDPFSGEIIDGKLFGRGATDMKGGNVsllLALSALQNLKVSLKGDVYFQSVIEEESGGSG 176
Cdd:PRK08651 77 -LHFNGHYDVVPPGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIA---ALLAAFERLDPAGDGNIELAIVPDEETGGTG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 177 TLAAILRGY-KADAAIIPEPTN-MKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKR--NERI 252
Cdd:PRK08651 152 TGYLVEEGKvTPDYVIVGEPSGlDNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIksKYEY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 253 IDPLYKsvpiPIPINIG--KIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFVEHPtiVEWFG 330
Cdd:PRK08651 232 DDERGA----KPTVTLGgpTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFE--ITPFS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 331 ArwlPGAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAEtPTIVFGPGVTEKAHHPNEYIEIDKVFQAAE 410
Cdd:PRK08651 306 E---AFVTDPDSELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGI-PTVVYGPGELELAHAPDEYVEVKDVEKAAK 381
|
....*.
gi 516364722 411 IIALTI 416
Cdd:PRK08651 382 VYEEVL 387
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-416 |
3.09e-59 |
|
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: 196.84 E-value: 3.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQ---GNEQTAQDIVIATLQNIGLEVDVWEPDgvelinhpyfvsprgkfQGSPNVVGIKKGNGEGRSL 98
Cdd:cd08011 1 VKLLQELVQIPSPNppgDNTSAIAAYIKLLLEDLGYPVELHEPP-----------------EEIYGVVSNIVGGRKGKRL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 99 ILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGG-SGT 177
Cdd:cd08011 64 LFNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGrAGT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 178 LAAILRGYKA-DAAIIPEPTNMK-IFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKrneriidp 255
Cdd:cd08011 144 KYLLEKVRIKpNDVLIGEPSGSDnIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEKT-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 256 lyksvpipipINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFVEHPTivewfgarwlP 335
Cdd:cd08011 216 ----------VNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEEVSFEIKSFYS----------P 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 336 GAIDTKHEFVNKLINNYEHVLGTPPVVEASpWGTDGGLLTKVAETPTIVFGPGVTEKAHHPNEYIEIDKVFQAAEIIALT 415
Cdd:cd08011 276 TVSNPDSEIVKKTEEAITEVLGIRPKEVIS-VGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALV 354
|
.
gi 516364722 416 I 416
Cdd:cd08011 355 A 355
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
16-422 |
1.96e-47 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 167.04 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 16 ENKSDGIKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLevDVWEPDGvelinhpyfvsprgkfQGspNVVGIKKGngeG 95
Cdd:PRK13004 12 KYKADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGF--DKVEIDP----------------MG--NVLGYIGH---G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 96 RSLIL-NGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVY-FQSVIEEESG 173
Cdd:PRK13004 69 KKLIAfDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYvTGTVQEEDCD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 174 GsgtLAA--IL--RGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRN 249
Cdd:PRK13004 149 G---LCWryIIeeDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 250 EriiDPLY----------KSVPipipinigkieggnwPS--SVADYVCIegrigvapeeTIEAAKLEVENWLACLKQVD- 316
Cdd:PRK13004 226 E---DPFLgkgtltvsdiFSTS---------------PSrcAVPDSCAI----------SIDRRLTVGETWESVLAEIRa 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 317 -PWFVEHPTIVE--------WFGA-----RWLPG-AIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAETP 381
Cdd:PRK13004 278 lPAVKKANAKVSmynydrpsYTGLvypteCYFPTwLYPEDHEFVKAAVEAYKGLFGKAPEVDKWTFSTNGVSIAGRAGIP 357
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 516364722 382 TIVFGPGVTEKAHHPNEYIEIDKVFQAAEIIALTIIDWCGE 422
Cdd:PRK13004 358 TIGFGPGKEPLAHAPNEYTWKEQLVKAAAMYAAIPKSLLKK 398
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
99-418 |
1.27e-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: 162.90 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 99 ILNGHIDVVPAGDIEQWehdPFSGEIiDGKLFGRGATDMKGGNVSLLLALSALQNLKVsLKGDVYFQSVIEEESGGSGTL 178
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGL-KKGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 179 AAI----LRGYKADAAI---IPEPTNM------KIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELE 245
Cdd:pfam01546 76 ALIedglLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 246 kkrnERIIDPLYKSVpIPIpINIGKIEGGnwPSSVADYVCIEGRIGVAPEETIEAAKLEVENWlacLKQVDPWFVEHPTI 325
Cdd:pfam01546 156 ----SRNVDPLDPAV-VTV-GNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREI---LEAIAAAYGVKVEV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 326 VEWFGARwlPGAIDTkHEFVNKLINNYEHVLGTPPVVEASPW--GTDGGLLTKVAETPTIVFGPGvTEKAHHPNEYIEID 403
Cdd:pfam01546 225 EYVEGGA--PPLVND-SPLVAALREAAKELFGLKVELIVSGSmgGTDAAFFLLGVPPTVVFFGPG-SGLAHSPNEYVDLD 300
|
330
....*....|....*
gi 516364722 404 KVFQAAEIIALTIID 418
Cdd:pfam01546 301 DLEKGAKVLARLLLK 315
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
18-403 |
2.03e-45 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 161.20 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 18 KSDGIKLLQQLVQADSTQGNEQTaqdiVIATLQ------NIGLEVDVWEPDGVELinhpyfVSPRGkfQGSPnVVGIkkg 91
Cdd:PRK08588 1 EEEKIQILADIVKINSVNDNEIE----VANYLQdlfakhGIESKIVKVNDGRANL------VAEIG--SGSP-VLAL--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 92 ngegrslilNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEE 171
Cdd:PRK08588 65 ---------SGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 172 SGGSGtlAAILR--GY--KADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQEL--E 245
Cdd:PRK08588 136 VGELG--AKQLTekGYadDLDALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYfdS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 246 KKRNERIIDPLYKSVPIpipinigkIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFVEHPTI 325
Cdd:PRK08588 214 IKKHNPYLGGLTHVVTI--------INGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGAAQLSLDIY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 326 VEWFgarwlPGAIDTKHEFVnKLINNY-EHVLGTPPVVEASPWGTDGGLLTKVAET-PTIVFGPGVTEKAHHPNEYIEID 403
Cdd:PRK08588 286 SNHR-----PVASDKDSKLV-QLAKDVaKSYVGQDIPLSAIPGATDASSFLKKKPDfPVIIFGPGNNLTAHQVDEYVEKD 359
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
84-418 |
3.46e-43 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 156.46 E-value: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 84 NVVGIKKGNGEGRSLILNGHIDVVPAGDieQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVY 163
Cdd:PRK13013 73 NLVARRQGARDGDCVHFNSHHDVVEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 164 FQSVIEEESGGSGTLAAIL-RGY----KADAAIIPEPTNM-KIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIA 237
Cdd:PRK13013 151 ISGTADEESGGFGGVAYLAeQGRfspdRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 238 IEHIqelekkrnERIIDPLYKSVPIPIP----------INIGKIEGGNwPSSVADYV-----CIEGRIGVA------PEE 296
Cdd:PRK13013 231 LAEI--------EERLFPLLATRRTAMPvvpegarqstLNINSIHGGE-PEQDPDYTglpapCVADRCRIVidrrflIEE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 297 TIEAAKLEVENWLACLKQVDPWFveHPTIVEWFGArwLPGAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTK 376
Cdd:PRK13013 302 DLDEVKAEITALLERLKRARPGF--AYEIRDLFEV--LPTMTDRDAPVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDR 377
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 516364722 377 VAETPT-IVFGPGVTEKAHHPNEYIEIDKVFQAAEIIALTIID 418
Cdd:PRK13013 378 IGKLKNcIAYGPGILDLAHQPDEWVGIADMVDSAKVMALVLAD 420
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
24-413 |
3.03e-42 |
|
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: 152.36 E-value: 3.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 24 LLQQLVQADSTQGNEQTAqdiVIATLQNI--GLEVDVwepdgvELINHPyfvsPRGKFqgspNVVgIKKGNGEGRSLILN 101
Cdd:cd03894 2 LLARLVAFDTVSRNSNLA---LIEYVADYlaALGVKS------RRVPVP----EGGKA----NLL-ATLGPGGEGGLLLS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 102 GHIDVVPAgDIEQWEHDPFSGEIIDGKLFGRGATDMKGGnvSLLLALSALQNLKVSLKGDVYFQSVIEEESG--GSGTLA 179
Cdd:cd03894 64 GHTDVVPV-DGQKWSSDPFTLTERDGRLYGRGTCDMKGF--LAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGclGVRHLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 180 AILRGY--KADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERIIDPLY 257
Cdd:cd03894 141 AALAARggRPDAAIVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 258 kSVPIPIpINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFVEHPTIVEWFGarwLPGA 337
Cdd:cd03894 221 -DPPYPT-LNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPG---LETD 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516364722 338 IDtkHEFVNKLinnyEHVLGTPPvVEASPWGTDGGLLTKvAETPTIVFGPGVTEKAHHPNEYIEIDKVFQAAEIIA 413
Cdd:cd03894 296 ED--APLVRLA----AALAGDNK-VRTVAYGTEAGLFQR-AGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLR 363
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-413 |
3.20e-40 |
|
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: 147.57 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLevDVWEPDGvelinhpyfvsprgkfQGspNVVGIKKGngeGRSLIL- 100
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGF--DEVEIDP----------------MG--NVIGYIGG---GKKKILf 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 101 NGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNL-KVSLKGDVYFQSVIEEE--SGGSGT 177
Cdd:cd05649 58 DGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLgLRDFAYTILVAGTVQEEdcDGVCWQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 178 LAAILRGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNER------ 251
Cdd:cd05649 138 YISKADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPEApflgrg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 252 ---IIDPLYKSVPIpipinigkieggnwpSSVADY--VCIEGRIGVApeETIEAAKLEVENWLACLK-----QVDPWFVE 321
Cdd:cd05649 218 tltVTDIFSTSPSR---------------CAVPDScrISIDRRLTVG--ETWEGCLEEIRALPAVKKygddvAVSMYNYD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 322 HPTiveWFGA-----RWLPG-AIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAETPTIVFGPGVTEKAHH 395
Cdd:cd05649 281 RPS---YTGEvyeseRYFPTwLLPEDHELVKALLEAYKALFGARPLIDKWTFSTNGVSIMGRAGIPCIGFGPGAENQAHA 357
|
410
....*....|....*...
gi 516364722 396 PNEYIEIDKVFQAAEIIA 413
Cdd:cd05649 358 PNEYTWKEDLVRCAAGYA 375
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
24-413 |
3.90e-39 |
|
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: 144.19 E-value: 3.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 24 LLQQLVQADSTQGNEQTAQ-DIVIATLQNIGLEVDVWE-PDGVElinhpyfvsprgKFqgspNVVGIKKGNGEGrSLILN 101
Cdd:TIGR01892 2 ILTKLVAFDSTSFRPNVDLiDWAQAYLEALGFSVEVQPfPDGAE------------KS----NLVAVIGPSGAG-GLALS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 102 GHIDVVPAgDIEQWEHDPFSGEIIDGKLFGRGATDMKGgnvSLLLALSALQNLKVS-LKGDVYFQSVIEEESGGSGT--- 177
Cdd:TIGR01892 65 GHTDVVPY-DDAAWTRDPFRLTEKDGRLYGRGTCDMKG---FLACALAAAPDLAAEqLKKPLHLALTADEEVGCTGApkm 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 178 LAAILRgyKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERiidPLY 257
Cdd:TIGR01892 141 IEAGAG--RPRHAIIGEPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLRE---DLD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 258 KSVPIPIP-INIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWFvehptIVEWFGARWLPG 336
Cdd:TIGR01892 216 EGFTPPYTtLNIGVIQGGKAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGF-----EVQIEVVSTDPG 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516364722 337 -AIDTKHEFVNKLinnyEHVLGTPPvvEASPWGTDGGLLTKvAETPTIVFGPGVTEKAHHPNEYIEIDKVFQAAEIIA 413
Cdd:TIGR01892 291 vNTEPDAELVAFL----EELSGNAP--EVVSYGTEAPQFQE-LGAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLA 361
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
91-420 |
4.44e-30 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 119.91 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 91 GNGEGRSLILNGHIDVVPAgDIEQWEHDPFSGEIIDGKLFGRGATDMKG--GNVSLLLALSALQNLK----VSLKGDvyf 164
Cdd:PRK07522 60 GPADRGGIVLSGHTDVVPV-DGQAWTSDPFRLTERDGRLYGRGTCDMKGfiAAALAAVPELAAAPLRrplhLAFSYD--- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 165 qsvieEESG--GSGTLAAIL--RGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKA--LIA- 237
Cdd:PRK07522 136 -----EEVGclGVPSMIARLpeRGVKPAGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAarLIAh 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 238 IEHIQELEKKRNERiiDPLYKsvpipIP---INIGKIEGGNWPSSVADyVC---IEGRI--GVAPEETIEAAKLEVE-NW 308
Cdd:PRK07522 211 LRDLADRLAAPGPF--DALFD-----PPystLQTGTIQGGTALNIVPA-ECefdFEFRNlpGDDPEAILARIRAYAEaEL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 309 LACLKQVDPwfvehPTIVEWfgarwlpgaidtkhefvnKLINNYEhVLGTPPVVEASPW---------------GTDGGL 373
Cdd:PRK07522 283 LPEMRAVHP-----EAAIEF------------------EPLSAYP-GLDTAEDAAAARLvraltgdndlrkvayGTEAGL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 516364722 374 LTKvAETPTIVFGPGVTEKAHHPNEYIEIDKvFQAAEIIALTIIDWC 420
Cdd:PRK07522 339 FQR-AGIPTVVCGPGSIEQAHKPDEFVELAQ-LAACEAFLRRLLASL 383
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-410 |
7.64e-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 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: 118.15 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVdvwepdgvELInhpyFVSPRGKFqgspNVVgIKKGNGEGRSLILN 101
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTV--------EKQ----PVENKDRF----NVY-AYPGSSRQPRVLLT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 102 GHIDVVPAgdieqweHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGGSGTLAA- 180
Cdd:cd05652 65 SHIDTVPP-------FIPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFn 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 181 --ILRGYkaDAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERiidpLYK 258
Cdd:cd05652 138 dlGLNTW--DAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSEL----LGP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 259 SVpipipINIGKIEGGNWPSSVADY--VCIEGRIGVAPEETIEAAKLEVENWLACLKQVDpwfvehptiVEWFGARwLPG 336
Cdd:cd05652 212 TT-----LNIGRISGGVAANVVPAAaeASVAIRLAAGPPEVKDIVKEAVAGILTDTEDIE---------VTFTSGY-GPV 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516364722 337 AIDTKHEFVNKLINNYehvlgtppvveaspwGTDGGLLTKVAETptIVFGPGVTEKAHHPNEYIEIDKVFQAAE 410
Cdd:cd05652 277 DLDCDVDGFETDVVAY---------------GTDIPYLKGDHKR--YLYGPGSILVAHGPDEAITVSELEEAVE 333
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
22-412 |
3.87e-29 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 116.40 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDVwEPDGvELINhpYFVSPRGKfqgspnvvgikkgngegrsLILN 101
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHI-ESDG-EVIN--IVVNSKAE-------------------LFVE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 102 GHIDVVPagdieqwehdPFSGEIIDG-KLFGRGATDMKGGnvSLLLALSALQNLKVSLKGDVYFQSVIEEESGGSGTlAA 180
Cdd:PRK08652 62 VHYDTVP----------VRAEFFVDGvYVYGTGACDAKGG--VAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGS-AL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 181 ILRGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERiIDPlyksv 260
Cdd:PRK08652 129 FAERYRPKMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKY-FDP----- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 261 pipiPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLaclkqvDPWFVEHPTIVEWFGarWlpgAIDT 340
Cdd:PRK08652 203 ----HIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPIL------DEYTVKYEYTEIWDG--F---ELDE 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516364722 341 KHEFVNKLINNYEHVLGTPPVVEASPWgTDGGLLtKVAETPTIVFGPGVTEKAHHPNEYIEIDKVFQAAEII 412
Cdd:PRK08652 268 DEEIVQLLEKAMKEVGLEPEFTVMRSW-TDAINF-RYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFL 337
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
22-220 |
4.67e-29 |
|
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: 116.45 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDvwepdgvelinhpyfvspRGKFQGSPNVVGIKKGNGegRSLILN 101
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCE------------------RLEFGGVKNLWARRGTGG--PHLCFA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 102 GHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGG----NVSLLLALSALQNLKVSLK----GDvyfqsviEEESG 173
Cdd:cd03891 61 GHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGiaafVAAAERFVAKHPNHKGSISflitSD-------EEGPA 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516364722 174 GSGTLAAI--L--RGYKADAAIIPEPTN-------MKIfpKQQGSIWFKIHIKGRAAH 220
Cdd:cd03891 134 IDGTKKVLewLkaRGEKIDYCIVGEPTSekklgdtIKI--GRRGSLNGKLTIKGKQGH 189
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
18-220 |
3.39e-27 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 111.33 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 18 KSDGIKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDvwepdgvelinhpyfvspRGKFQGSPNVVGIKKGngEGRS 97
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCE------------------RMDFGDVKNLWARRGT--EGPH 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 98 LILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGG------NVSLLLALSALQNLKVSL--KGDvyfqsviE 169
Cdd:PRK13009 61 LCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSlaafvvAAERFVAAHPDHKGSIAFliTSD-------E 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516364722 170 EESGGSGT------LAAilRGYKADAAIIPEPTN-------MKIfpKQQGSIWFKIHIKGRAAH 220
Cdd:PRK13009 134 EGPAINGTvkvlewLKA--RGEKIDYCIVGEPTSterlgdvIKN--GRRGSLTGKLTVKGVQGH 193
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-411 |
1.40e-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 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: 106.24 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEV-----DVWepdgveLINHPYFVSPRgkfqgspnvvgikkgngegr 96
Cdd:cd05651 3 IELLKSLIATPSFSREEHKTADLIENYLEQKGIPFkrkgnNVW------AENGHFDEGKP-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 97 SLILNGHIDVVP--AGdieqWEHDPFSGEIIDGKLFGRGATDmKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGG 174
Cdd:cd05651 57 TLLLNSHHDTVKpnAG----WTKDPFEPVEKGGKLYGLGSND-AGASVVSLLATFLHLYSEGPLNYNLIYAASAEEEISG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 175 SGTLAAILRGY-KADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGtRYEGVSAIEKALIAIEHIQELEKKRneriI 253
Cdd:cd05651 132 KNGIESLLPHLpPLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAA-RNEGDNAIYKALDDIQWLRDFRFDK----V 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 254 DPLYKsvpiPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLAClkQVDPwfveHPTivewfgaRW 333
Cdd:cd05651 207 SPLLG----PVKMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKS--EIKP----RSF-------RL 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516364722 334 LPGAIDTKHEFVNKLINnyehvLGTPPVVeaSPWGTDGGLLTkvaeTPTIVFGPGVTEKAHHPNEYIEIDKVFQAAEI 411
Cdd:cd05651 270 NSSAIPPDHPIVQAAIA-----AGRTPFG--SPTLSDQALMP----FPSVKIGPGDSSRSHTADEFIELSEIEEGIDI 336
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
22-420 |
2.91e-25 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 106.06 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADST--------QGNEQtaqdiVIATLQN----IGLEVDVwepdgVELINHPyfvsprGKFqgspNVVGiK 89
Cdd:PRK05111 8 IEMYRALIATPSIsatdpaldQSNRA-----VIDLLAGwfedLGFNVEI-----QPVPGTR------GKF----NLLA-S 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 90 KGNGEGrSLILNGHIDVVPAgDIEQWEHDPFSGEIIDGKLFGRGATDMKG--GNVSLLLALSALQNLKVSLkgdvYFQSV 167
Cdd:PRK05111 67 LGSGEG-GLLLAGHTDTVPF-DEGRWTRDPFTLTEHDGKLYGLGTADMKGffAFILEALRDIDLTKLKKPL----YILAT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 168 IEEESGGSGTLAAILRG-YKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEK 246
Cdd:PRK05111 141 ADEETSMAGARAFAEATaIRPDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 247 KRNERIIDPLYkSVPIPIpINIGKIEGGNWPSsvadyvciegRI--------------GVAPEETIEAakleVENWLACL 312
Cdd:PRK05111 221 ELQERYHNPAF-TVPYPT-LNLGHIHGGDAPN----------RIcgccelhfdirplpGMTLEDLRGL----LREALAPV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 313 KQVDP--WFVE--HPTIvewfgarwlPG-AIDTKHEFVnKLInnyEHVLGTPPvvEASPWGTDGGLLTKVAeTPTIVFGP 387
Cdd:PRK05111 285 SERWPgrITVAplHPPI---------PGyECPADHQLV-RVV---EKLLGHKA--EVVNYCTEAPFIQQLG-CPTLVLGP 348
|
410 420 430
....*....|....*....|....*....|...
gi 516364722 388 GVTEKAHHPNEYIEIDKVFQAAEIIALTIIDWC 420
Cdd:PRK05111 349 GSIEQAHQPDEYLELSFIKPTRELLRQLIHHFC 381
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
84-421 |
1.04e-23 |
|
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: 101.40 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 84 NVVGIKKGNGEGRSLILNGHIDVVPAGDieqwehDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVY 163
Cdd:cd03896 43 NVVGRLRGTGGGPALLFSAHLDTVFPGD------TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 164 FQSVIEEESGGSGTLAAIL---RGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEH 240
Cdd:cd03896 117 FAANVGEEGLGDLRGARYLlsaHGARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 241 IQELEkkrneriiDPlykSVPiPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPeetiEAAKLEVENwlACLKQVDPWFV 320
Cdd:cd03896 197 LYEWA--------AP---YVP-KTTFAAIRGGGGTSVNRIANLCSMYLDIRSNP----DAELADVQR--EVEAVVSKLAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 321 EHPTI---VEWFGARwlPGA-IDTKHEFVNKLINNYEHVLGTPpvvEASPWGTDGGLLTKVAeTPTIVFGPGVTEKAHHP 396
Cdd:cd03896 259 KHLRVkarVKPVGDR--PGGeAQGTEPLVNAAVAAHREVGGDP---RPGSSSTDANPANSLG-IPAVTYGLGRGGNAHRG 332
|
330 340
....*....|....*....|....*
gi 516364722 397 NEYIEIDKVFQAAEIIALTIIDWCG 421
Cdd:cd03896 333 DEYVLKDDMLKGAKAYLMLAAALCG 357
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
22-416 |
6.53e-23 |
|
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: 99.20 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGN-EQTAQ--DIVIATLQNIGLEVDVwepdgvelinhpyfvSPRGKFqgSPNVVGIKKGNGeGRSL 98
Cdd:cd03885 2 LDLLERLVNIESGTYDkEGVDRvaELLAEELEALGFTVER---------------RPLGEF--GDHLIATFKGTG-GKRV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 99 ILNGHIDVV-PAGDIEQWehdPFSgeIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGGSGT 177
Cdd:cd03885 64 LLIGHMDTVfPEGTLAFR---PFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 178 LAAILR-GYKADAAIIPEPT----NMKIFPKqqGSIWFKIHIKGRAAHGGTRYE-GVSAIEKA---LIAIEHIQELEKKr 248
Cdd:cd03885 139 RELIEEeAKGADYVLVFEPAradgNLVTARK--GIGRFRLTVKGRAAHAGNAPEkGRSAIYELahqVLALHALTDPEKG- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 249 neriidplyksvpipIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLkqvdpwFVEHPTIVEW 328
Cdd:cd03885 216 ---------------TTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATT------LVPGTSVELT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 329 FGARWLPGAIDTKHEfvnKLINNYEHV---LGTPPVVEASPWGTDGGLLTKVAeTPTI-VFGPgVTEKAHHPNEYIEIDK 404
Cdd:cd03885 275 GGLNRPPMEETPASR---RLLARAQEIaaeLGLTLDWEATGGGSDANFTAALG-VPTLdGLGP-VGGGAHTEDEYLELDS 349
|
410
....*....|..
gi 516364722 405 VFQAAEIIALTI 416
Cdd:cd03885 350 LVPRIKLLARLL 361
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
75-414 |
1.06e-21 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 96.07 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 75 PRGKFQGSPNVVGIKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNL 154
Cdd:PRK13983 56 PRVIEGVRPNIVAKIPGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 155 KVSLKGDVYFQSVIEEESGGSGTLAAILRGY-----KADAAIIP---EPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYE 226
Cdd:PRK13983 136 GIRPKYNLGLAFVSDEETGSKYGIQYLLKKHpelfkKDDLILVPdagNPDGSFIEIAEKSILWLKFTVKGKQCHASTPEN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 227 GVSAIEKALIAIEHIQE-LEKKRNERiiDPLY-------------KSVPipipiNIGKIEGgnwpssvADYVCIEGRIgv 292
Cdd:PRK13983 216 GINAHRAAADFALELDEaLHEKFNAK--DPLFdppystfeptkkeANVD-----NINTIPG-------RDVFYFDCRV-- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 293 APEETIEAAKLEVENWLACLKQVDPWFVEHpTIVEWFGArwlPGAIDTKHEFVNKLINNYEHVLGtppvVEASPWGTDGG 372
Cdd:PRK13983 280 LPDYDLDEVLKDIKEIADEFEEEYGVKIEV-EIVQREQA---PPPTPPDSEIVKKLKRAIKEVRG----IEPKVGGIGGG 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 516364722 373 lltKVA------ETPTIVFGPGVtEKAHHPNEYIEIDKVFQAAEIIAL 414
Cdd:PRK13983 352 ---TVAaflrkkGYPAVVWSTLD-ETAHQPNEYAKISNLIEDAKVFAL 395
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
23-221 |
1.32e-21 |
|
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: 96.27 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 23 KLLQQLVQADST-----QGNEQTAQDIVIATLQNIGLEVDVWEPDGvelinHPyfvsprgkfqGSPNVVG-IKKGNGEGR 96
Cdd:cd05675 2 DLLQELIRIDTTnsgdgTGSETRAAEVLAARLAEAGIQTEIFVVES-----HP----------GRANLVArIGGTDPSAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 97 SLILNGHIDVVPAgDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGGSG 176
Cdd:cd05675 67 PLLLLGHIDVVPA-DASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGEN 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 177 TLAAILRGYK-----ADAAI-------IPEPTNMKIFPKQ---QGSIWFKIHIKGRAAHG 221
Cdd:cd05675 146 GAKWLVDNHPelfdgATFALneggggsLPVGKGRRLYPIQvaeKGIAWMKLTVRGRAGHG 205
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
75-414 |
9.64e-21 |
|
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: 93.29 E-value: 9.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 75 PRGKFQgsPNVVgIKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNL 154
Cdd:cd05650 52 ERGIIR--PNIV-AKIPGGNDKTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 155 KVSLKGDVYFQSVIEEESGGSGTLAAILRGY----KADAAIIPE---PTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEG 227
Cdd:cd05650 129 GITPKYNFGLLFVADEEDGSEYGIQYLLNKFdlfkKDDLIIVPDfgtEDGEFIEIAEKSILWIKVNVKGKQCHASTPENG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 228 VSAIEKALIAIEHIQELE-KKRNERiiDPLY-------------KSVPipipiNIGKIEGgnwpssvADYVCIEGRigVA 293
Cdd:cd05650 209 INAFVAASNFALELDELLhEKFDEK--DDLFnppystfeptkkeANVP-----NVNTIPG-------YDVFYFDCR--VL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 294 PEETIEAAKLEVENWLACLKQVDPWFVEHPTIVewfgARWLPGAIDTKHEFVNKLINNYEHVLGtppvVEASPWGTDGGL 373
Cdd:cd05650 273 PTYKLDEVLKFVNKIISDFENSYGAGITYEIVQ----KEQAPPATPEDSEIVVRLSKAIKKVRG----REAKLIGIGGGT 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 516364722 374 LTKVAET---PTIVFGPGVtEKAHHPNEYIEIDKVFQAAEIIAL 414
Cdd:cd05650 345 VAAFLRKkgyPAVVWSTLD-ETAHQPNEYIRISHIVKDAKVFAE 387
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
20-418 |
1.71e-19 |
|
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: 89.54 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 20 DGIKLLQQLVQ--ADSTQGNEQTAQDIVIATLQNIGLEVDvwepdgveliNHPY---FVSPRGKFQGSPNVVGIKKGNGe 94
Cdd:cd02697 4 EEVRFLQKLVRvpTDTPPGNNAPHAERTAALLQGFGFEAE----------RHPVpeaEVRAYGMESITNLIVRRRYGDG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 95 GRSLILNGHIDVVPAGDieQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESGG 174
Cdd:cd02697 73 GRTVALNAHGDVVPPGD--GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 175 SGTLAAILR-GYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRNERii 253
Cdd:cd02697 151 ELGPGWLLRqGLTKPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQV-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 254 dplYKSVP-IPIP-INIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLKQVDPWF-VEHPTIVEWFG 330
Cdd:cd02697 229 ---SSQVEgITHPyLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAASMPGIsVDIRRLLLANS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 331 ARWLPGAidtkHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKvAETPTIVFGPG---VTEK-AHHPNEYIEIDKVF 406
Cdd:cd02697 306 MRPLPGN----APLVEAIQTHGEAVFGEPVPAMGTPLYTDVRLYAE-AGIPGVIYGAGprtVLEShAKRADERLQLEDLR 380
|
410
....*....|..
gi 516364722 407 QAAEIIALTIID 418
Cdd:cd02697 381 RATKVIARSLRD 392
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
25-410 |
2.02e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 89.10 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 25 LQQLVQADSTQGNEQTAQDIVIATLQNiglevdvWEPDG-VELINHPyfvsprgkfQGSPNVVGIKkgnGEGRSLiLNGH 103
Cdd:PRK08737 12 LQALVSFDTRNPPRAITTGGIFDYLRA-------QLPGFqVEVIDHG---------AGAVSLYAVR---GTPKYL-FNVH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 104 IDVVPAGDieQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQnlkvslkGDVYFQSVIEEESGGSGTLAAIL- 182
Cdd:PRK08737 72 LDTVPDSP--HWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGD-------GDAAFLFSSDEEANDPRCVAAFLa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 183 RGYKADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHG-GTRYEGVSAIEKALI----AIEHIQELEKKRNERIIDply 257
Cdd:PRK08737 143 RGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHAsGKQDPSASALHQAMRwggqALDHVESLAHARFGGLTG--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 258 ksvpipIPINIGKIEGGNWPSSVADYVciEGRIGVAPeetieAAKLEVENWLACLKQVDPWFVEHPTivEWFGARWLPGA 337
Cdd:PRK08737 220 ------LRFNIGRVEGGIKANMIAPAA--ELRFGFRP-----LPSMDVDGLLATFAGFAEPAAATFE--ETFRGPSLPSG 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516364722 338 IDTKHEFVNKLINNYEHVLGTpPVVEASPWGTDGGLLTKvAETPTIVFGPGVTEKAHHPNEYIEIDKVFQAAE 410
Cdd:PRK08737 285 DIARAEERRLAARDVADALDL-PIGNAVDFWTEASLFSA-AGYTALVYGPGDIAQAHTADEFVTLDQLQRYAE 355
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
22-412 |
8.70e-18 |
|
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: 84.03 E-value: 8.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLevdvwepdgVELINHPYFVSPRGKFqgspnvvgikkgnGEGRSLILN 101
Cdd:cd05647 2 IELTAALVDIPSVSGNEKPIADEIEAALRTLPH---------LEVIRDGNTVVARTER-------------GLASRVILA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 102 GHIDVVP-AGDI-EQWEHDpfsgeiidGKLFGRGATDMKGGNVSL--LLALSALQNLKVSLKGDVY-FQSVIEEESGgsg 176
Cdd:cd05647 60 GHLDTVPvAGNLpSRVEED--------GVLYGCGATDMKAGDAVQlkLAATLAAATLKHDLTLIFYdCEEVAAELNG--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 177 tLAAILRGYK----ADAAIIPEPTNMKIFPKQQGSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELEKKRneRI 252
Cdd:cd05647 129 -LGRLAEEHPewlaADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPRT--VN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 253 IDPL-YKSVpipipINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENWLACLkQVDPWFVEHPTivewfGA 331
Cdd:cd05647 206 IDGLtYREG-----LNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGL-GYEIEVTDLSP-----GA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 332 RwlPGaidTKHEFVNKLInnyEHVLGTPpvvEASPWGTDGGLLTKVAeTPTIVFGPGVTEKAHHPNEYIEIDKVFQAAEI 411
Cdd:cd05647 275 L--PG---LDHPVARDLI---EAVGGKV---RAKYGWTDVARFSALG-IPAVNFGPGDPLLAHKRDEQVPVEQITACAAI 342
|
.
gi 516364722 412 I 412
Cdd:cd05647 343 L 343
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
22-274 |
1.06e-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: 81.38 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQ--TAQDIVIATLQNIGLEVDVWEPdgvelinhpyfvsprgkFQGSPNVVGIKKG-NGEGRSL 98
Cdd:TIGR01880 12 VTRFREYLRINTVQPNPDyaACVDFLIKQADELGLARKTIEF-----------------VPGKPVVVLTWPGsNPELPSI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 99 ILNGHIDVVPAGDiEQWEHDPFSGEI-IDGKLFGRGATDMKGGNVsllLALSALQNLKVS---LKGDVYFQSVIEEESGG 174
Cdd:TIGR01880 75 LLNSHTDVVPVFR-EHWTHPPFSAFKdEDGNIYARGAQDMKCVGV---QYLEAVRNLKASgfkFKRTIHISFVPDEEIGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 175 ---------SGTLAAILRGYKADAAiIPEPTN-MKIFPKQQGSIWFKIHIKGRAAHGGTRYEGvSAIEKALIAIEHIQEL 244
Cdd:TIGR01880 151 hdgmekfakTDEFKALNLGFALDEG-LASPDDvYRVFYAERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRF 228
|
250 260 270
....*....|....*....|....*....|...
gi 516364722 245 EKKRNERI---IDPLYKSVpipIPINIGKIEGG 274
Cdd:TIGR01880 229 RESQFQLLqsnPDLAIGDV---TSVNLTKLKGG 258
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
20-416 |
1.55e-16 |
|
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: 80.09 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 20 DGIKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVdvwEPDGVElinhpyfvsprgkfqgspNVVGIKkgNGEGRSLI 99
Cdd:cd05653 2 DAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEA---WVDEAG------------------NAVGGA--GSGPPDVL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 100 LNGHIDVVPaGDIEQwehdpfsgEIIDGKLFGRGATDMKGGNVSLLLALSAlqnLKVSLKGDVYFQSVIEEESGGSGTLA 179
Cdd:cd05653 59 LLGHIDTVP-GEIPV--------RVEGGVLYGRGAVDAKGPLAAMILAASA---LNEELGARVVVAGLVDEEGSSKGARE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 180 AILRGYKADAAIIPEPTNMK-IFPKQQGSIWFKIHIKGRAAH--GGTRYEGVSAIEKaliaiehIQELeKKRNERIIDPL 256
Cdd:cd05653 127 LVRRGPRPDYIIIGEPSGWDgITLGYRGSLLVKIRCEGRSGHssSPERNAAEDLIKK-------WLEV-KKWAEGYNVGG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 257 YKSVPIPIPINIGKIEGGNWPSSVADYVCIEGRIGVAPEETIEAAKLEVENwlACLKQVD--PWFVEHPTIvewFGARWL 334
Cdd:cd05653 199 RDFDSVVPTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPT--CELEFIDdtEPVKVSKNN---PLARAF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 335 PGAIDT---KHEFVNKlinnyehvlgtppvveaspWGT-DGGLLTKVAETPTIVFGPGVTEKAHHPNEYIEIDKVFQAAE 410
Cdd:cd05653 274 RRAIRKqggKPRLKRK-------------------TGTsDMNVLAPLWTVPIVAYGPGDSTLDHTPNEHIELAEIERAAA 334
|
....*.
gi 516364722 411 IIALTI 416
Cdd:cd05653 335 VLKGAL 340
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
32-139 |
6.10e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 79.13 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 32 DSTQGNEQTAQDIVIATLQNIGLEVDVWEPdgvelinHPyfvsprgkfqGSPNVVGIKKGNGEGRS-LILNGHIDVVPAg 110
Cdd:PRK07906 18 DGTGKGEREAAEYVAEKLAEVGLEPTYLES-------AP----------GRANVVARLPGADPSRPaLLVHGHLDVVPA- 79
|
90 100
....*....|....*....|....*....
gi 516364722 111 DIEQWEHDPFSGEIIDGKLFGRGATDMKG 139
Cdd:PRK07906 80 EAADWSVHPFSGEIRDGYVWGRGAVDMKD 108
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
96-310 |
6.79e-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: 78.85 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 96 RSLILNGHIDVVPAGDiEQWEHDPFSGEI-IDGKLFGRGATDMKGGNVSLLLALsalQNLKVS---LKGDVYFQSVIEEE 171
Cdd:cd05646 65 PSILLNSHTDVVPVFE-EKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAI---RRLKASgfkPKRTIHLSFVPDEE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 172 SGGSGTLAAILR---------GYKADAAIiPEPTN-MKIFPKQQGSIWFKIHIKGRAAHGGTRYEGvSAIEKALIAIEHI 241
Cdd:cd05646 141 IGGHDGMEKFVKteefkklnvGFALDEGL-ASPTEeYRVFYGERSPWWVVITAPGTPGHGSKLLEN-TAGEKLRKVIESI 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516364722 242 QELEKKRNERIIDPLYKSVPIPIPINIGKIEGG---NWPSSVADyVCIEGRIgvAPEETIEAAKLEVENWLA 310
Cdd:cd05646 219 MEFRESQKQRLKSNPNLTLGDVTTVNLTMLKGGvqmNVVPSEAE-AGFDLRI--PPTVDLEEFEKQIDEWCA 287
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
84-197 |
1.96e-15 |
|
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: 74.39 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 84 NVVGIKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVY 163
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 516364722 164 FQSVIEEESGGSGTLA-----AILRGYKADAAIIPEPTN 197
Cdd:cd18669 81 VAFTPDEEVGSGAGKGllskdALEEDLKVDYLFVGDATP 119
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
84-417 |
4.17e-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: 76.90 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 84 NVVG-IKKGNGEGRSLILnGHIDVVPAGdiEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDV 162
Cdd:cd03888 60 NYAGyAEYGEGEEVLGIL-GHLDVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 163 YFQSVIEEESGGS-----------------------------GTLAAILRGYKADA----------------------AI 191
Cdd:cd03888 137 RLIFGTDEETGWKciehyfeheeypdfgftpdaefpvingekGIVTVDLTFKIDDDkgyrlisikggeatnmvpdkaeAV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 192 IPEPTNMKIFPKQQGSIWF---------KIHIKGRAAHGGTRYEGVSAIEKALIAIEhiqELEKKRNER-IIDPLYKSVP 261
Cdd:cd03888 217 IPGKDKEELALSAATDLKGnieiddggvELTVTGKSAHASAPEKGVNAITLLAKFLA---ELNKDGNDKdFIKFLAKNLH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 262 I-----------------PIPINIGKIEGGNWPSSVAdyvcIEGRIGVA--PEETIEAAKLEVENWlaclkQVDPWFVEH 322
Cdd:cd03888 294 EdyngkklginfedevmgELTLNPGIITLDDGKLELG----LNVRYPVGtsAEDIIKQIEEALEKY-----GVEVEGHKH 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 323 PTivewfgarwlPGAIDTKHEFVNKLINNYEHVLGTppvvEASPWGTDGGllTKVAETPTIV-FG---PGVTEKAHHPNE 398
Cdd:cd03888 365 QK----------PLYVPKDSPLVKTLLKVYEEQTGK----EGEPVAIGGG--TYARELPNGVaFGpefPGQKDTMHQANE 428
|
410
....*....|....*....
gi 516364722 399 YIEIDKVFQAAEIIALTII 417
Cdd:cd03888 429 FIPIDDLIKALAIYAEAIY 447
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
204-310 |
3.63e-14 |
|
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: 68.14 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 204 QQGSIWFKIHIKGRAAHGGTRYEGVSAIEkalIAIEHIQELEKKRNERIIDplyksvPIPIPINIGKIEGGNWPSSVADY 283
Cdd:pfam07687 3 HKGLAGGHLTVKGKAGHSGAPGKGVNAIK---LLARLLAELPAEYGDIGFD------FPRTTLNITGIEGGTATNVIPAE 73
|
90 100
....*....|....*....|....*..
gi 516364722 284 VCIEGRIGVAPEETIEAAKLEVENWLA 310
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILE 100
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
27-417 |
3.67e-14 |
|
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: 73.25 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 27 QLVQADSTQGNEQTAQDIVIATLQNIGLEvdVWEPDGVELINHpyfvsprgkfqGSPNVVGIKKGNGEGRSLIL-NGHID 105
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLS--VIEDDAGKTTGG-----------GAGNLICTLKADKEEVPKILfTSHMD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 106 -VVPAGDIEqwehdPFSGEiiDGKLFGRGAT----DMKGGNVSLLLALSALQNLKVSlKGDVYFQSVIEEESGGSGtlAA 180
Cdd:cd05683 78 tVTPGINVK-----PPQIA--DGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKNIP-HGQIQFVITVGEESGLVG--AK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 181 ILR--------GYKADAA------IIPEPTNMKIfpkqqgsiwfKIHIKGRAAHGGTRYE-GVSAIEKALIAIEHIQELE 245
Cdd:cd05683 148 ALDpelidadyGYALDSEgdvgtiIVGAPTQDKI----------NAKIYGKTAHAGTSPEkGISAINIAAKAISNMKLGR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 246 kkrneriIDPLYKSvpipipiNIGKIEGGNWPSSVADYVCIEGrigvapeetiEAAKLEVENWLACLKQVDPWFVehpTI 325
Cdd:cd05683 218 -------IDEETTA-------NIGKFQGGTATNIVTDEVNIEA----------EARSLDEEKLDAQVKHMKETFE---TT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 326 VEWFGA-------RWLPGAIDTKHEFVNKLINNYEHVLGTPPVVEASPWGTDGGLLTKVAeTPTIVFGPGVtEKAHHPNE 398
Cdd:cd05683 271 AKEKGAhaeveveTSYPGFKINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLG-IPTVNLGIGY-ENIHTTNE 348
|
410
....*....|....*....
gi 516364722 399 YIEIDKVFQAAEIIaLTII 417
Cdd:cd05683 349 RIPIEDLYDTAVLV-VEII 366
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
81-414 |
1.45e-13 |
|
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: 71.98 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 81 GSPNVVGIKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKG 160
Cdd:cd03893 49 GAPVVFAEFPGAPGAPTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 161 DVYFqsVIE-EESGGSGTLAAILRGYK----ADAAIIPEPTNMK-----IFPKQQGSIWFKIHIKGRAA--HGGtrYEGV 228
Cdd:cd03893 129 NVKF--IIEgEEESGSPSLDQLVEAHRdllaADAIVISDSTWVGqeqptLTYGLRGNANFDVEVKGLDHdlHSG--LYGG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 229 SAIEKALIAIEHIQELEKKRNERIIDPLYKSVPiPIP---------------------------------INIGKIEGGN 275
Cdd:cd03893 205 VVPDPMTALAQLLASLRDETGRILVPGLYDAVR-ELPeeefrldagvleeveiiggttgsvaerlwtrpaLTVLGIDGGF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 276 WPSSVADYVCIEGR----IGVAPEETIEAAKLEVEnwlACLKQVDPWFVEHPTIVEWFGARWlpgAIDTKHEFVNKLINN 351
Cdd:cd03893 284 PGEGSKTVIPPRARakisIRLVPGQDPEEASRLLE---AHLEKHAPSGAKVTVSYVEGGMPW---RSDPSDPAYQAAKDA 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 352 YEHVLGTPPVVEaspwgTDGG------LLTKVAETPTIVFGPG-VTEKAHHPNEYIEIDKVFQAAEIIAL 414
Cdd:cd03893 358 LRTAYGVEPPLT-----REGGsipfisVLQEFPQAPVLLIGVGdPDDNAHSPNESLRLGNYKEGTQAEAA 422
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
96-188 |
2.39e-13 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 71.51 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 96 RSLILNGHIDVVPA--GDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESG 173
Cdd:PRK08262 112 KPIVLMAHQDVVPVapGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVG 191
|
90
....*....|....*....
gi 516364722 174 GSGT--LAAIL--RGYKAD 188
Cdd:PRK08262 192 GLGAraIAELLkeRGVRLA 210
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
81-197 |
4.51e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 70.32 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 81 GSPNVVGIKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVS-LLLALSALQNLKVSLK 159
Cdd:PRK07907 69 GAPAVIGTRPAPPGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMhLAALRALGGDLPVGVT 148
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516364722 160 gdvyfqSVIE-EESGGSGTLAAILRGYK----ADAAIIPEPTN 197
Cdd:PRK07907 149 ------VFVEgEEEMGSPSLERLLAEHPdllaADVIVIADSGN 185
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
91-139 |
9.83e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 69.34 E-value: 9.83e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 516364722 91 GNGEGRSLILnGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKG 139
Cdd:PRK07205 72 GQGEELLAIL-CHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKG 119
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
84-413 |
1.19e-12 |
|
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: 69.33 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 84 NVVG-IKKGNGEGRSLILnGHIDVVPAGDieQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDV 162
Cdd:TIGR01887 56 NYAGyIEYGQGEEVLGIL-GHLDVVPAGD--GWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 163 YFQSVIEEESgGSGTLAAILRGYKA-DAAIIPEPTnmkiFP---KQQGSIWFKIHIKGRAAH--------GGTRYEGVSA 230
Cdd:TIGR01887 133 RFIFGTDEES-GWKCIDYYFEHEEMpDIGFTPDAE----FPiiyGEKGITTLEIKFKDDTEGdvvlesfkAGEAYNMVPD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 231 IEKALIAIEHIQELEKKRNERIIDplyKSVPIPIPIN--------IGKIEGGNWPSS----------------------- 279
Cdd:TIGR01887 208 HATAVISGKKLTEVEQLKFVFFIA---KELEGDFEVNdgtltitlEGKSAHGSAPEKginaatylalflaqlnlaggaka 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 280 ----VADYVCIEGR-------------------IGVAPEETIEAAKLEVENWLACLKQVDPWFV-----EHPTIVEWFGA 331
Cdd:TIGR01887 285 flqfLAEYLHEDHYgeklgikfhddvsgdltmnVGVIDYENAEAGLIGLNVRYPVGNDPDTMLKnelakESGVVEVTLNG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 332 RWLPGAIDTKHEFVNKLINNYEHVLGTppvvEASPWGTDGGllTKVAETPTIV-FG---PGVTEKAHHPNEYIEIDKVFQ 407
Cdd:TIGR01887 365 YLKPLYVPKDDPLVQTLMKVYEKQTGD----EGEPVAIGGG--TYARLMPNGVaFGalfPGEEDTMHQANEYIMIDDLLL 438
|
....*.
gi 516364722 408 AAEIIA 413
Cdd:TIGR01887 439 ATAIYA 444
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
84-139 |
1.40e-12 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 69.10 E-value: 1.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 516364722 84 NVVG-IKKGNGEGRSLILnGHIDVVPAGDieQWEHDPFSGEIIDGKLFGRGATDMKG 139
Cdd:PRK07318 68 NYAGhIEYGEGEEVLGIL-GHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKG 121
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
98-220 |
1.47e-11 |
|
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: 65.74 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 98 LILNGHIDVVPA--GDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVslllalSALQNLKVSLKGDvyFQ---SVI---- 168
Cdd:cd05674 72 LLLMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLI------GILEAVELLLKRG--FKprrTIIlafg 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 169 --EEESG--GSGTLAAIL---RGYKADAAIIPE--PTNMKIFPKQQ---------GSIWFKIHIKGRAAH 220
Cdd:cd05674 144 hdEEVGGerGAGAIAELLlerYGVDGLAAILDEggAVLEGVFLGVPfalpgvaekGYMDVEITVHTPGGH 213
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
84-209 |
1.96e-11 |
|
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: 62.83 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 84 NVVGIKKGNGEGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVY 163
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516364722 164 FQSVIEEESG-----GSGTLAAILRGYKADAAIIPEPTNMKIFPKQQGSIW 209
Cdd:cd03873 81 VAFTADEEVGsgggkGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVIRN 131
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
16-139 |
2.29e-11 |
|
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: 65.32 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 16 ENKSDGIKLLQQLV--QADSTQ----GNEQTAQDIVIATLQNIGLEVdvwepdgvELINHPYFVSPRGKFQGSPNVVGIK 89
Cdd:cd05676 7 EHQDEFIERLREAVaiQSVSADpekrPELIRMMEWAAERLEKLGFKV--------ELVDIGTQTLPDGEELPLPPVLLGR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516364722 90 KGNGEG-RSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKG 139
Cdd:cd05676 79 LGSDPSkKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKG 129
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
1-245 |
2.90e-11 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 65.26 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 1 MKDERLKQQIRqwlfenksdgiKLLQQLVQADS---TQGnEQTAQDIVIATLQniglEVDVWE--PDGVELINHPyfvsp 75
Cdd:COG4187 1 MKKWQTKEQLE-----------ELLCELVSIPSvtgTEG-EKEVAEFIYEKLS----ELPYFQenPEHLGLHPLP----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 76 rGKFQGSPNVVGIKKGNGEGR-SLILNGHIDVVPA---GDIEQWEHDP------FSGEIID---------GK-LFGRGAT 135
Cdd:COG4187 60 -DDPLGRKNVTALVKGKGESKkTVILISHFDVVDVedyGSLKPLAFDPeelteaLKEIKLPedvrkdlesGEwLFGRGTM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 136 DMKGGNVslllalSALQNLK-----VSLKGDVYFQSVIEEESGGSGTLAAI-----LR---GYKADAAIIPEPTnmkiFP 202
Cdd:COG4187 139 DMKAGLA------LHLALLEeasenEEFPGNLLLLAVPDEEVNSAGMRAAVpllaeLKekyGLEYKLAINSEPS----FP 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 516364722 203 KQQGSIWFKIH------------IKGRAAHGGTRYEGVSAIekaLIAIEHIQELE 245
Cdd:COG4187 209 KYPGDETRYIYtgsigklmpgfyCYGKETHVGEPFSGLNAN---LLASELTRELE 260
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
16-235 |
3.26e-11 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 64.21 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 16 ENKSDGIKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVdvwEPDGVElinhpyfvsprgkfqgspNVVGIKKGngEG 95
Cdd:PRK04443 3 ISALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREA---WVDEAG------------------NARGPAGD--GP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 96 RSLILNGHIDVVPaGDIeqwehdPFsgEIIDGKLFGRGATDMKG---GNVSLLLALSALQNLKVSLKGdvyfqsVIEEES 172
Cdd:PRK04443 60 PLVLLLGHIDTVP-GDI------PV--RVEDGVLWGRGSVDAKGplaAFAAAAARLEALVRARVSFVG------AVEEEA 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516364722 173 GGSGTLAAILRGYKADAAIIPEPtnmkifpkqqgSIWFKIHI--KGRAA--------HGGTRYEGVSAIEKAL 235
Cdd:PRK04443 125 PSSGGARLVADRERPDAVIIGEP-----------SGWDGITLgyKGRLLvtyvatseSFHSAGPEPNAAEDAI 186
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
21-191 |
5.38e-11 |
|
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: 63.90 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 21 GIKLLQQLVQADST--QGN--EQTAqDIVIATLQNIGLEVDVWEPDGvelinHPyfvsprgkfqgspnVVGIKKGNGEGR 96
Cdd:cd05681 1 YLEDLRDLLKIPSVsaQGRgiPETA-DFLKEFLRRLGAEVEIFETDG-----NP--------------IVYAEFNSGDAK 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 97 SLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKVSLKGDVYFqsVIE-EESGGS 175
Cdd:cd05681 61 TLLFYNHYDVQPAEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKF--LVEgEEEVGS 138
|
170 180
....*....|....*....|
gi 516364722 176 GTLAAILRGY----KADAAI 191
Cdd:cd05681 139 PNLEKFVAEHadllKADGCI 158
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
29-228 |
8.62e-11 |
|
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: 63.48 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 29 VQADST-QGNEQTAQDIVIATLQNIGLE-VDVWEPDGvelinHPYFVSPRGKFQGSPNVvgikkgngegrsLILnGHIDV 106
Cdd:cd05680 13 VSADPAhKGDVRRAAEWLADKLTEAGFEhTEVLPTGG-----HPLVYAEWLGAPGAPTV------------LVY-GHYDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 107 VPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKG----------------GNVSLllalsalqNLKVSLKGdvyfqsviEE 170
Cdd:cd05680 75 QPPDPLELWTSPPFEPVVRDGRLYARGASDDKGqvfihikaveawlaveGALPV--------NVKFLIEG--------EE 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516364722 171 ESgGSGTLAAILRGYK----ADAAIIPEpTNMkiFPKQQGSI--------WFKIHIKG--RAAHGGTrYEGV 228
Cdd:cd05680 139 EI-GSPSLPAFLEENAerlaADVVLVSD-TSM--WSPDTPTItyglrglaYLEISVTGpnRDLHSGS-YGGA 205
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
18-139 |
1.95e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 62.46 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 18 KSDGIKLLQQLVQADST----QGNEQTAQDIViATLQNIGLEVdvwepdgvELINHPyfvsprgkfqGSPNVVGiKKGNG 93
Cdd:PRK06446 1 MDEELYTLIEFLKKPSIsatgEGIEETANYLK-DTMEKLGIKA--------NIERTK----------GHPVVYG-EINVG 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 516364722 94 EGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKG 139
Cdd:PRK06446 61 AKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKG 106
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
60-242 |
5.16e-10 |
|
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: 60.94 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 60 EPDGVELINHPYFVSPRGkfqgspNVVGIKKGNGEGRSLILNG-HIDVVPAgDIEQWEHDPFSgEIIDG-KLFGRGATDM 137
Cdd:cd08012 48 ENGGPLVIDHVSYVKGRG------NIIVEYPGTVDGKTVSFVGsHMDVVTA-NPETWEFDPFS-LSIDGdKLYGRGTTDC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 138 KGGNVSLLLALSALQNLKVSLKGDVYFQSVIEEESG---GSGTLAAILRGykadaaiipEPTNMKIFP--------KQQ- 205
Cdd:cd08012 120 LGHVALVTELFRQLATEKPALKRTVVAVFIANEENSeipGVGVDALVKSG---------LLDNLKSGPlywvdsadSQPc 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516364722 206 ----GSIWFKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQ 242
Cdd:cd08012 191 igtgGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEIQ 231
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
210-412 |
9.82e-10 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 59.68 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 210 FKIHIKGRAAHGGTRYE-GVSAIekaLIAIEHIQELEKKRneriidplyksVPIPIPINIGKIEGGNWPSSVADYVCIEg 288
Cdd:COG2195 174 AKITIKGKGGHSGDAKEkMINAI---KLAARFLAALPLGR-----------IPEETEGNEGFIHGGSATNAIPREAEAV- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 289 riGVAPEETIEAAKLEVENWLACLKQVdpwFVEHP------TIVEWFGArWLPgaiDTKHEFVNKLINNYEHvLGTPPVV 362
Cdd:COG2195 239 --YIIRDHDREKLEARKAELEEAFEEE---NAKYGvgvvevEIEDQYPN-WKP---EPDSPIVDLAKEAYEE-LGIEPKI 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 516364722 363 EASPWGTDGGLLTKvAETPTIVFGPGVtEKAHHPNEYIEIDKVFQAAEII 412
Cdd:COG2195 309 KPIRGGLDGGILSF-KGLPTPNLGPGG-HNFHSPDERVSIESMEKAWELL 356
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
24-140 |
1.72e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 59.24 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 24 LLQQLVQADSTQGNEQTAQ--DIVIATLQNIGlevdvWEPDGVElinhpyFVSPRGKFQgspNVVGIKKGNGEGRSLILN 101
Cdd:PRK09133 42 LYKELIEINTTASTGSTTPaaEAMAARLKAAG-----FADADIE------VTGPYPRKG---NLVARLRGTDPKKPILLL 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 516364722 102 GHIDVVPAgDIEQWEHDPFSGEIIDGKLFGRGATDMKGG 140
Cdd:PRK09133 108 AHMDVVEA-KREDWTRDPFKLVEENGYFYGRGTSDDKAD 145
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
81-245 |
2.97e-09 |
|
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: 58.89 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 81 GSPNVVGIKKGNGEG-RSLILNGHIDVVPAGDIEQWEHDPF-------------------------SGEIidgkLFGRGA 134
Cdd:cd05654 56 GRRNVTALVKGKKPSkRTIILISHFDTVGIEDYGELKDIAFdpdeltkafseyveeldeevredllSGEW----LFGRGT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 135 TDMKGGNVSLLLALSALQNLKvSLKGDVYFQSVIEEESGGSGTLAAI--LRGYKAD------AAIIPEPtnmkIFPKQQG 206
Cdd:cd05654 132 MDMKSGLAVHLALLEQASEDE-DFDGNLLLMAVPDEEVNSRGMRAAVpaLLELKKKhdleykLAINSEP----IFPQYDG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516364722 207 SIWFKIH------------IKGRAAHGGTRYEGVSAiekALIAIEHIQELE 245
Cdd:cd05654 207 DQTRYIYtgsigkilpgflCYGKETHVGEPFAGINA---NLMASEITARLE 254
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
77-186 |
5.03e-09 |
|
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: 57.74 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 77 GKFQGSPNVVGIKKGNG---EGRSLILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKGGNVSLL-LALSALQ 152
Cdd:cd05677 50 SGPGTNPIVLATFSGNSsdaKRKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIyAVAELFQ 129
|
90 100 110
....*....|....*....|....*....|....
gi 516364722 153 NLKvsLKGDVYFQSVIEEESGGSGtLAAILRGYK 186
Cdd:cd05677 130 EGE--LDNDVVFLIEGEEESGSPG-FKEVLRKNK 160
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
96-282 |
7.54e-09 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 57.28 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 96 RSLILNGHIDVV-PAGDieqwehdPFS--GEIIDGKLFGRGATDMKGGNVSLLLALSALQNLKvsLKGDVYFQSVI--EE 170
Cdd:PRK07338 93 RQVLLTGHMDTVfPADH-------PFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAFERSP--LADKLGYDVLInpDE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 171 ESG--GSGTL-AAILRGYkaDAAIIPEPTnmkiFPK------QQGSIWFKIHIKGRAAHGGTRY-EGVSAIEKALIAIEH 240
Cdd:PRK07338 164 EIGspASAPLlAELARGK--HAALTYEPA----LPDgtlagaRKGSGNFTIVVTGRAAHAGRAFdEGRNAIVAAAELALA 237
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 516364722 241 IQELEKKRNEriidplyksvpipIPINIGKIEGGNWPSSVAD 282
Cdd:PRK07338 238 LHALNGQRDG-------------VTVNVAKIDGGGPLNVVPD 266
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
8-139 |
1.90e-08 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 56.29 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 8 QQIRQWLFENKSDGIKLLQQLVQADSTQGNEQTAQDI------VIATLQNIGLE-VDVWEPDGvelinHPYFVSPRGKFQ 80
Cdd:PRK08201 3 QQVEAYLRERREAHLEELKEFLRIPSISALSEHKEDVrkaaewLAGALEKAGLEhVEIMETAG-----HPIVYADWLHAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 516364722 81 GSPNVvgikkgngegrslILNGHIDVVPAGDIEQWEHDPFSGEIIDGKLFGRGATDMKG 139
Cdd:PRK08201 78 GKPTV-------------LIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKG 123
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
20-174 |
2.56e-08 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 55.55 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 20 DGIKLLQQLVQ----ADSTQGNEQT--AQDIVIATLQNIGLEVDVWEPDGVelinhpyfvsprgkfqgsPNVVGIKkgnG 93
Cdd:PRK08554 2 DVLELLSSLVSfetvNDPSKGIKPSkeCPKFIKDTLESWGIESELIEKDGY------------------YAVYGEI---G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 94 EGRSLIL-NGHIDVVPAGDiEQWEHDPFSGEIIDGKLFGRGATDMKgGNVSLLLALSALQNlKVSLKGDVYFQSVIEEES 172
Cdd:PRK08554 61 EGKPKLLfMAHFDVVPVNP-EEWNTEPFKLTVKGDKAYGRGSADDK-GNVASVMLALKELS-KEPLNGKVIFAFTGDEEI 137
|
..
gi 516364722 173 GG 174
Cdd:PRK08554 138 GG 139
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
18-231 |
3.62e-07 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 51.94 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 18 KSDGIKLLQQLVQADSTQGNEQ---TAQDIVIATLQNIGLEVDVwepdgvelinhpyfVSPRGKfqGSPNVVGIKKGNGE 94
Cdd:PRK06133 36 QPAYLDTLKELVSIESGSGDAEglkQVAALLAERLKALGAKVER--------------APTPPS--AGDMVVATFKGTGK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 95 gRSLILNGHIDVV-PAGDIEQwehDPFsgEIIDGKLFGRGATDMKGGNVSLLLALSALQNLK--------VSLKGDvyfq 165
Cdd:PRK06133 100 -RRIMLIAHMDTVyLPGMLAK---QPF--RIDGDRAYGPGIADDKGGVAVILHALKILQQLGfkdygtltVLFNPD---- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516364722 166 svieEE--SGGSGTLAAILrGYKADAAIIPEPTNmkifPKQQGSIWFK------IHIKGRAAHGGTRYE-GVSAI 231
Cdd:PRK06133 170 ----EEtgSPGSRELIAEL-AAQHDVVFSCEPGR----AKDALTLATSgiatalLEVKGKASHAGAAPElGRNAL 235
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
210-306 |
4.33e-07 |
|
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: 51.58 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 210 FKIHIKGRAAHGGTRYEGVSAIEKALIAIEHIQELekkrNERIIDPLYKSVpipipINIGKIEGGNWPSSVADYVCIEGR 289
Cdd:TIGR01891 173 FEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQI----VSRNVDPSRPAV-----VSVGIIEAGGAPNVIPDKASMSGT 243
|
90
....*....|....*..
gi 516364722 290 IGVAPEETIEAAKLEVE 306
Cdd:TIGR01891 244 VRSLDPEVRDQIIDRIE 260
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
153-288 |
1.53e-06 |
|
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: 50.03 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 153 NLKVSLKGDV--YFQSViEEESGGSGTLAAILRGYKADAAI-------IPEPT-NMKIFPKQQGSIWFKIHIKGRAAHGG 222
Cdd:cd08019 105 EIKDTIKGTVklIFQPA-EEVGEGAKQMIEEGVLEDVDAVFgihlwsdVPAGKiSVEAGPRMASADIFKIEVKGKGGHGS 183
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516364722 223 TRYEGVSAIekaLIAIEHIQELEKKRNeRIIDPLYksvpiPIPINIGKIEGGNWPSSVADYVCIEG 288
Cdd:cd08019 184 MPHQGIDAV---LAAASIVMNLQSIVS-REIDPLE-----PVVVTVGKLNSGTRFNVIADEAKIEG 240
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
3-259 |
4.53e-06 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 48.24 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 3 DERLKQQIRqwlfenksdgiKLLQQLVQADSTQGNEQTAQDIV--IATLQNIGLEVDvwePDGvelinHPYFVsprgkfq 80
Cdd:PRK00466 5 KELVKQKAK-----------ELLLDLLSIYTPSGNETNATKFFekISNELNLKLEIL---PDS-----NSFIL------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 81 gspnvvgikkGNGEGrslILNGHIDVVPaGDIEQWEHdpfsGEIIdgklFGRGATDMKG--GNVSLLLALSALQNLKVSL 158
Cdd:PRK00466 59 ----------GEGDI---LLASHVDTVP-GYIEPKIE----GEVI----YGRGAVDAKGplISMIIAAWLLNEKGIKVMV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 159 KGdvyfqsVIEEESGGSGTLAAILRGYKADAAIIPEPTN-MKIFPKQQGSIWFKIHIKGRAAHGGTRYEG-VSAIEKALI 236
Cdd:PRK00466 117 SG------LADEESTSIGAKELVSKGFNFKHIIVGEPSNgTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNlIVDISKKII 190
|
250 260
....*....|....*....|...
gi 516364722 237 AIehIQELEKKRNERIIDPLYKS 259
Cdd:PRK00466 191 EV--YKQPENYDKPSIVPTIIRA 211
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
210-306 |
6.79e-06 |
|
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: 48.04 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 210 FKIHIKGRAAHGGTRYEGVSAIekaLIAIEHIQELEK--KRNeriIDPLYKSVpipipINIGKIEGGNWPSSVADYVCIE 287
Cdd:cd08021 184 FDITIKGKGGHGSMPHETVDPI---VIAAQIVTALQTivSRR---VDPLDPAV-----VTIGTFQGGTSFNVIPDTVELK 252
|
90
....*....|....*....
gi 516364722 288 GRIGVAPEETIEAAKLEVE 306
Cdd:cd08021 253 GTVRTFDEEVREQVPKRIE 271
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
41-139 |
3.07e-05 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 46.05 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 41 AQDIVIATLQNIGLEVDVWEPDGvelinHPYfvsprgkfqgspnVVGIKKGN-GEGRSLILNGHIDVVPAGDIEQWEHDP 119
Cdd:PRK09104 45 AADWLVADLASLGFEASVRDTPG-----HPM-------------VVAHHEGPtGDAPHVLFYGHYDVQPVDPLDLWESPP 106
|
90 100
....*....|....*....|....*
gi 516364722 120 FSGEIID----GK-LFGRGATDMKG 139
Cdd:PRK09104 107 FEPRIKEtpdgRKvIVARGASDDKG 131
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
210-307 |
1.35e-04 |
|
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: 43.74 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 210 FKIHIKGRAAHGGTRYEGVSAIekaLIAIEHIQELEKKrNERIIDPLYKSVpipipINIGKIEGGNWPSSVADYVCIEGR 289
Cdd:cd03886 174 FEITVKGKGGHGASPHLGVDPI---VAAAQIVLALQTV-VSRELDPLEPAV-----VTVGKFHAGTAFNVIPDTAVLEGT 244
|
90
....*....|....*...
gi 516364722 290 IGVAPEETIEAAKLEVEN 307
Cdd:cd03886 245 IRTFDPEVREALEARIKR 262
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
206-421 |
2.72e-04 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 42.80 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 206 GSIWFKIHIKGRAAHGGTRYEGVSAIekalIAIEHI----QELekkrNERIIDPLYKSVpipipINIGKIEGGNWPSSVA 281
Cdd:COG1473 182 AADSFEITIKGKGGHAAAPHLGIDPI----VAAAQIvtalQTI----VSRNVDPLDPAV-----VTVGIIHGGTAPNVIP 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 282 DYVCIEGRIGVAPEETIEAAKLEVENwlaclkqvdpwFVEHptIVEWFGAR----WLPGAIDTK--HEFVNKLINNYEHV 355
Cdd:COG1473 249 DEAELEGTVRTFDPEVRELLEERIER-----------IAEG--IAAAYGATaeveYLRGYPPTVndPELTELAREAAREV 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516364722 356 LGTPPVVEASP--WGTDGGLLTKvaETPTIVFGPGVTEKA-----HHPN-----EYIEIdkvfqAAEIIALTIIDWCG 421
Cdd:COG1473 316 LGEENVVDAEPsmGSEDFAYYLQ--KVPGAFFFLGAGNPGtvpplHSPKfdfdeKALPI-----GAKALAALALDLLA 386
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
93-239 |
5.15e-04 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 42.08 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 93 GEGRSLILnGHIDVV-PAGDIEQWehdPFSGEiiDGKLFGRGATDMKGGNVSL--LLALSALQNLKVSLKGDVYFQSviE 169
Cdd:PRK07473 74 GEPGILIA-GHMDTVhPVGTLEKL---PWRRE--GNKCYGPGILDMKGGNYLAleAIRQLARAGITTPLPITVLFTP--D 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 170 EESGGSGTLAAIlrgyKADAA-----IIPEP--TNMKIFPKQQGSIWFKIHIKGRAAHGGTRY-EGVSAIE---KALIAI 238
Cdd:PRK07473 146 EEVGTPSTRDLI----EAEAArnkyvLVPEPgrPDNGVVTGRYAIARFNLEATGRPSHAGATLsEGRSAIRemaRQILAI 221
|
.
gi 516364722 239 E 239
Cdd:PRK07473 222 D 222
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
210-362 |
5.98e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized 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: 349936 [Multi-domain] Cd Length: 371 Bit Score: 41.88 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 210 FKIHIKGRAAHGGTRYEGVSAIekaLIAIEHIQELEKkRNERIIDPLYKSVpipipINIGKIEGGNWPSSVADYVCIEGr 289
Cdd:cd08014 173 LEIRIQGEGGHGARPHLTVDLV---WAAAQVVTDLPQ-AISRRIDPRSPVV-----LTWGSIEGGRAPNVIPDSVELSG- 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516364722 290 igvapeeTIEAAKLEVenWlaclKQVDPWfVEHptIVEWFGARWlpGAidtKHEFvnklinnyEHVLGTPPVV 362
Cdd:cd08014 243 -------TVRTLDPDT--W----AQLPDL-VEE--IVAGICAPY--GA---KYEL--------EYRRGVPPVI 286
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
22-105 |
9.36e-04 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 41.27 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516364722 22 IKLLQQLVQADSTQGNEQTAQDIVIATLQNIGLEVDVwepDGvelinhpyfvspRGkfqgspNVVGIKKGNGEGRSLILN 101
Cdd:COG1363 5 LELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVET---DR------------LG------NLIATKKGKGDGPKVMLA 63
|
....
gi 516364722 102 GHID 105
Cdd:COG1363 64 AHMD 67
|
|
| |
