|
Name |
Accession |
Description |
Interval |
E-value |
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-349 |
0e+00 |
|
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: 601.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 9 NAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKKNNVWAFNRHYDPAKPTILLNSHHDTVKPNGAYTRDPFAA 88
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKGNNVWAENGHFDEGKPTLLLNSHHDTVKPNAGWTKDPFEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 89 TVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKDLKYNLCVAITAEEENSGHDGLECVIPELGPLEFAIVGEPTLMQLAI 168
Cdd:cd05651 81 VEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLIYAASAEEEISGKNGIESLLPHLPPLDLAIVGEPTEMQPAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 169 AERGLMVIDCTAHGKAGHAAREEGDNAIYKAMQDIEWFRTYRFPKVSDLFGAVKMSVTIISAGTQHNVVPAECRFTVDIR 248
Cdd:cd05651 161 AEKGLLVLDCTARGKAGHAARNEGDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGTQHNVVPDSCTFVVDIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 249 VTDRYTNEEVLEIIKEHVSCEVKARSTRLRPSSIRPDHPIVQAGLALGRTTYGSPTTSDQALLDIPSLKLGVGDSARSHS 328
Cdd:cd05651 241 TTEAYTNEEIFEIIRGNLKSEIKPRSFRLNSSAIPPDHPIVQAAIAAGRTPFGSPTLSDQALMPFPSVKIGPGDSSRSHT 320
|
330 340
....*....|....*....|.
gi 1772516668 329 ADEFVHLSEIREGIELYIKML 349
Cdd:cd05651 321 ADEFIELSEIEEGIDIYIELL 341
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
4-353 |
7.80e-107 |
|
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: 317.98 E-value: 7.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 4 EQLYENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHR-----KKNNVWAFnRHYDPAKPTILLNSHHDTVKPN 78
Cdd:COG0624 8 DAHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERlevppGRPNLVAR-RPGDGGGPTLLLYGHLDVVPPG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 79 G--AYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRK-DLKYNLCVAITAEEEnSGHDGLECVIPELGPLE- 154
Cdd:COG0624 87 DleLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGlRLPGNVTLLFTGDEE-VGSPGARALVEELAEGLk 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 155 --FAIVGEPT-LMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFP-KVSDLFGAVKMSVTIIS 229
Cdd:COG0624 166 adAAIVGEPTgVPTIVTGHKGSLRFELTVRGKAAHSSRpELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGIE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 230 AGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEH-------VSCEVKARSTRLRPSSIRPDHPIVQAGLALGRTTYG- 301
Cdd:COG0624 246 GGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALlaaaapgVEVEVEVLGDGRPPFETPPDSPLVAAARAAIREVTGk 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1772516668 302 ------SPTTSD----QALLDIPSLKLGVGDSARSHSADEFVHLSEIREGIELYIKMLSAIL 353
Cdd:COG0624 326 epvlsgVGGGTDarffAEALGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
12-349 |
2.69e-85 |
|
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: 262.24 E-value: 2.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 12 ALLRQMIQTPSFSKEEAGTAGLLAEFLQERG--VEVHRKKN--NVWAfnRHYDPAKPTILLNSHHDTVKPNGAY--TRDP 85
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGygIESTIVEGrgNLVA--TVGGGDGPVLLLNGHIDTVPPGDGDkwSFPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 86 FAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKD-LKYNLCVAITAEEEnSGHDGLECVIPEL--GPLEFAIVGEPT 162
Cdd:cd08659 79 FSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGAlLGGRVALLATVDEE-VGSDGARALLEAGyaDRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 163 LMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPK-VSDLFGAVKMSVTIISAGTQHNVVPAE 240
Cdd:cd08659 158 GLDVVYAHKGSLWLRVTVHGKAAHSSMpELGVNAIYALADFLAELRTLFEELpAHPLLGPPTLNVGVINGGTQVNSIPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 241 CRFTVDIRVTDRYTNEEVLEIIKEHV-----SCEVKARSTRLRPSSIRPDHPIVQAGLALGRTTYGSP------TTSDQA 309
Cdd:cd08659 238 ATLRVDIRLVPGETNEGVIARLEAILeeheaKLTVEVSLDGDPPFFTDPDHPLVQALQAAARALGGDPvvrpftGTTDAS 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1772516668 310 LL----DIPSLKLGVGDSARSHSADEFVHLSEIREGIELYIKML 349
Cdd:cd08659 318 YFakdlGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
12-349 |
4.25e-54 |
|
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: 181.64 E-value: 4.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 12 ALLRQMIQTPSFSKE-EAGTAGLLAEFLQERGVEVHR------KKNNVWAfnRHYDPAKPTILLNSHHDTVKPNG-AYTR 83
Cdd:cd03894 1 ELLARLVAFDTVSRNsNLALIEYVADYLAALGVKSRRvpvpegGKANLLA--TLGPGGEGGLLLSGHTDVVPVDGqKWSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 84 DPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFyDRKDLKYNLCVAITAEEEnSGHDG----LECVIPELGPLEFAIVG 159
Cdd:cd03894 79 DPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRL-LAAKLRKPLHLAFSYDEE-VGCLGvrhlIAALAARGGRPDAAIVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 160 EPTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFR----TYRFPKVSDLF--GAVKMSVTIISAGT 232
Cdd:cd03894 157 EPTSLQPVVAHKGIASYRIRVRGRAAHSSLpPLGVNAIEAAARLIGKLReladRLAPGLRDPPFdpPYPTLNVGLIHGGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 233 QHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVSCEVKARSTRLR--------PSSIRPDHPIVQAGLALGR--TTYGS 302
Cdd:cd03894 237 AVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEveplfevpGLETDEDAPLVRLAAALAGdnKVRTV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1772516668 303 PTTSDQALLD---IPSLKLGVGDSARSHSADEFVHLSEIREGIELYIKML 349
Cdd:cd03894 317 AYGTEAGLFQragIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLI 366
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
4-352 |
1.12e-53 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 181.34 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 4 EQLYENAVALLRQMIQTPSF-----SKEEAgtAGLLAEFLQERG--VEVHR------KKNNVWAFNRHY--DPAKPTILL 68
Cdd:PRK08651 2 EAMMFDIVEFLKDLIKIPTVnppgeNYEEI--AEFLRDTLEELGfsTEIIEvpneyvKKHDGPRPNLIArrGSGNPHLHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 69 NSHHDTVKP-NGAYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKDlkYNLCVAITAEEEnSGHDGLECVI 147
Cdd:PRK08651 80 NGHYDVVPPgEGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGD--GNIELAIVPDEE-TGGTGTGYLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 148 PELG-PLEFAIVGEPT-LMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPKVSDLFG----A 220
Cdd:PRK08651 157 EEGKvTPDYVIVGEPSgLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKSSLSTIKSKYEYdderG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 221 VKMSVTI----ISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHV---SCEVKARSTR-----LRPSSIRPDHPI 288
Cdd:PRK08651 237 AKPTVTLggptVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLdevAPELGIEVEFeitpfSEAFVTDPDSEL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1772516668 289 VQAGLALGRTTYGS---PTTSDQAL-------LDIPSLKLGVGDSARSHSADEFVHLSEIREGIELYIKMLSAI 352
Cdd:PRK08651 317 VKALREAIREVLGVepkKTISLGGTdarffgaKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVLKRL 390
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
67-349 |
3.59e-47 |
|
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: 162.13 E-value: 3.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 67 LLNSHHDTVkPNGAYTRDPFAATVEGdRLYGLGSNDAGASGVSLLAAFLHFYDRKDLKYNLCVAITAEEEnSGHDG---- 142
Cdd:pfam01546 1 LLRGHMDVV-PDEETWGWPFKSTEDG-KLYGRGHDDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEE-GGMGGaral 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 143 LECVIPELGPLEFAI---VGEPTLMQ------LAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFP 212
Cdd:pfam01546 78 IEDGLLEREKVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTpHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 213 KVSDLFGAVK--MSVTIISAGTqhNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVS-------CEVKARSTRLRPSSIR 283
Cdd:pfam01546 158 NVDPLDPAVVtvGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEaiaaaygVKVEVEYVEGGAPPLV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1772516668 284 PDHPIVQA---------GLALGRTTYGSPTTSDQA--LLDIPSLKLGVG-DSARSHSADEFVHLSEIREGIELYIKML 349
Cdd:pfam01546 236 NDSPLVAAlreaakelfGLKVELIVSGSMGGTDAAffLLGVPPTVVFFGpGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
1-345 |
6.34e-41 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 147.78 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 1 METEQLYENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGV-EVHRKKN-NVWAFNRHydpAKPTILLNSHHDTVKPN 78
Cdd:PRK13004 8 MLAEKYKADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFdKVEIDPMgNVLGYIGH---GKKLIAFDAHIDTVGIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 79 GA--YTRDPFAATVEGDRLYGLGSND---AGASGVSLLAAFLHfyDRKDLKYNLCVAITAEEENSghDGL--ECVIPELG 151
Cdd:PRK13004 85 DIknWDFDPFEGEEDDGRIYGRGTSDqkgGMASMVYAAKIIKD--LGLDDEYTLYVTGTVQEEDC--DGLcwRYIIEEDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 152 --PlEFAIVGEPTLMQLAIAERGLMVIDCTAHGKAGH-AAREEGDNAIYKAMQDIEWFRTYRFPKVSDLF-GAVKMSVT- 226
Cdd:PRK13004 161 ikP-DFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHgSAPERGDNAIYKMAPILNELEELNPNLKEDPFlGKGTLTVSd 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 227 IISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVSCE------------------VKARSTRLRPSSIRP-DHP 287
Cdd:PRK13004 240 IFSTSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALPAVKkanakvsmynydrpsytgLVYPTECYFPTWLYPeDHE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1772516668 288 IVQAGLALGRTTYGSPTTSDQALL-----------DIPSLKLGVGDSARSHSADEFVHLSEIREGIELY 345
Cdd:PRK13004 320 FVKAAVEAYKGLFGKAPEVDKWTFstngvsiagraGIPTIGFGPGKEPLAHAPNEYTWKEQLVKAAAMY 388
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
11-345 |
6.50e-37 |
|
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: 136.36 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFSKEEAGT---AGLLAEFLQERG--VEVH---RKKNNVWAfNRHYDPAKPTILLNSHHDTVkPNGA-- 80
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNTsaiAAYIKLLLEDLGypVELHeppEEIYGVVS-NIVGGRKGKRLLFNGHYDVV-PAGDge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 81 -YTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKDlKYNLCVAITA--EEENSGHDG----LECVIPELGpl 153
Cdd:cd08011 79 gWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKA-PWDLPVVLTFvpDEETGGRAGtkylLEKVRIKPN-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 154 eFAIVGEPT-LMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWfrtyrfpkvsdLFGAVKM-SVTIISA 230
Cdd:cd08011 156 -DVLIGEPSgSDNIRIGEKGLVWVIIEITGKPAHGSLpHRGESAVKAAMKLIER-----------LYELEKTvNPGVIKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 231 GTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEH------VSCEVKARSTrlrPSSIRPDHPIVQAGLALGRTTYG--- 301
Cdd:cd08011 224 GVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHldsieeVSFEIKSFYS---PTVSNPDSEIVKKTEEAITEVLGirp 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1772516668 302 ----SPTTSDQALL---DIPSLKLGVGDSARSHSADEFVHLSEIREGIELY 345
Cdd:cd08011 301 keviSVGASDARFYrnaGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVH 351
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
11-350 |
2.73e-35 |
|
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: 131.94 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFSKEEAG---TAGLLAEFLQERGVEVHRKKNNVWA---FNRHYDPAKPTILLNSHHDTVKPNGAYTRD 84
Cdd:cd03885 2 LDLLERLVNIESGTYDKEGvdrVAELLAEELEALGFTVERRPLGEFGdhlIATFKGTGGKRVLLIGHMDTVFPEGTLAFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 85 PFaaTVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKDLKY-NLCVAITAEEENSGHDGLEcVIPELGPL-EFAIVGEPT 162
Cdd:cd03885 82 PF--TVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYlPITVLLNSDEEIGSPGSRE-LIEEEAKGaDYVLVFEPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 163 LM--QLAIAERGLMVIDCTAHGKAGHAAR--EEGDNAIYKAMQDIEwfrtyRFPKVSDLFGAVKMSVTIISAGTQHNVVP 238
Cdd:cd03885 159 RAdgNLVTARKGIGRFRLTVKGRAAHAGNapEKGRSAIYELAHQVL-----ALHALTDPEKGTTVNVGVISGGTRVNVVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 239 AECRFTVDIRVTDRYTNEEVLEIIKEHVSC------EVKARSTRLRP-----SSIRPDHPIVQA-GLALGRTTYGSPTT- 305
Cdd:cd03885 234 DHAEAQVDVRFATAEEADRVEEALRAIVATtlvpgtSVELTGGLNRPpmeetPASRRLLARAQEiAAELGLTLDWEATGg 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1772516668 306 -SDQ---ALLDIPSLK-LG-VGDSArsHSADEFVHLSEIREGIELYIKMLS 350
Cdd:cd03885 314 gSDAnftAALGVPTLDgLGpVGGGA--HTEDEYLELDSLVPRIKLLARLLM 362
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
11-342 |
1.48e-34 |
|
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: 130.21 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFS---KEEAGTAGLLAEFLQERGVEVHR----------KKNNVWAFNRHYDpaKPTILLNSHHDTV-- 75
Cdd:TIGR01910 1 VELLKDLISIPSVNppgGNEETIANYIKDLLREFGFSTDVieitddrlkvLGKVVVKEPGNGN--EKSLIFNGHYDVVpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 76 KPNGAYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRK-DLKYNLCVAITAEEENSGHDGLECVipELG--- 151
Cdd:TIGR01910 79 GDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGiKPNGNIILQSVVDEESGEAGTLYLL--QRGyfk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 152 PLEFAIVGEPTL-MQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDI----EWFRTyRFPKVSDLF--GAVKM 223
Cdd:TIGR01910 157 DADGVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFpQFGVNAIMKLAKLItelnELEEH-IYARNSYGFipGPITF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 224 SVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKehvSCeVKARSTRLR-------------PSSIRPDHPIVQ 290
Cdd:TIGR01910 236 NPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIE---DV-VKALSKSDGwlyenepvvkwsgPNETPPDSRLVK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1772516668 291 AGLALGRT-------TYGSPTTSDQALL---DIPSLKLGVGDSARSHSADEFVHLSEIREGI 342
Cdd:TIGR01910 312 ALEAIIKKvrgiepeVLVSTGGTDARFLrkaGIPSIVYGPGDLETAHQVNEYISIKNLVEST 373
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
11-351 |
2.30e-34 |
|
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: 129.85 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFSKEEAGTAGLLAEFLQERGV-EVHRKK-NNVWAFNRHydpAKPTILLNSHHDTVKPNGA--YTRDPF 86
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdEVEIDPmGNVIGYIGG---GKKKILFDGHIDTVGIGNIdnWKFDPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 87 AATVEGDRLYGLGSNDAGASGVSLLAAFLHFYD--RKDLKYNLCVAITAEEENSghDGL--ECVIPELG--PlEFAIVGE 160
Cdd:cd05649 78 EGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDlgLRDFAYTILVAGTVQEEDC--DGVcwQYISKADKikP-DFVVSGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 161 PTLMQLAIAERGLMVIDCTAHGKAGH-AAREEGDNAIYKAMQDIEWFRTYRFPKVSDLF---GAVKMSvTIISAGTQHNV 236
Cdd:cd05649 155 PTDGNIYRGQRGRMEIRVDTKGVSCHgSAPERGDNAVYKMADIIQDIRQLNPNFPEAPFlgrGTLTVT-DIFSTSPSRCA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 237 VPAECRFTVDIRVTDRYTNEEVLEIIKEHVSC------EVKARSTRLRPS---------------SIRPDHPIVQAGLAL 295
Cdd:cd05649 234 VPDSCRISIDRRLTVGETWEGCLEEIRALPAVkkygddVAVSMYNYDRPSytgevyeseryfptwLLPEDHELVKALLEA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1772516668 296 GRTTYGSPTTSDQALLD-----------IPSLKLGVGDSARSHSADEFVHLSEIREGIELYIKMLSA 351
Cdd:cd05649 314 YKALFGARPLIDKWTFStngvsimgragIPCIGFGPGAENQAHAPNEYTWKEDLVRCAAGYAAIPTS 380
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-349 |
3.91e-34 |
|
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: 128.55 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 10 AVALLRQMIQTPSFSKEEAGTAGLLAEFLQERG-----VEVHRK-KNNVWAFNRhyDPAKPTILLNSHHDTVKPNGAYTR 83
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGftvekQPVENKdRFNVYAYPG--SSRQPRVLLTSHIDTVPPFIPYSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 84 DPfaatvEGDRLYGLGSNDAGASGVSLLAAFL-HFYDRKDLKYNLCVAITAEEENsGHDGLECViPELGPLEF--AIVGE 160
Cdd:cd05652 79 SD-----GGDTIYGRGSVDAKGSVAAQIIAVEeLLAEGEVPEGDLGLLFVVGEET-GGDGMKAF-NDLGLNTWdaVIFGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 161 PTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYK------AMQDIEWfrtyrfPKvSDLFGAVKMSVTIISAGTQ 233
Cdd:cd05652 152 PTELKLASGHKGMLGFKLTAKGKAGHSGYpWLGISAIEIlvealvKLIDADL------PS-SELLGPTTLNIGRISGGVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 234 HNVVPAECRFTVDIRVTdrYTNEEVLEIIKEHVS--------CEVKARSTRLrPSSIrpDHPIvqAGLALGRTTYGSptt 305
Cdd:cd05652 225 ANVVPAAAEASVAIRLA--AGPPEVKDIVKEAVAgiltdtedIEVTFTSGYG-PVDL--DCDV--DGFETDVVAYGT--- 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1772516668 306 sdqallDIPSLKL-------GVGDSARSHSADEFVHLSEIREGIELYIKML 349
Cdd:cd05652 295 ------DIPYLKGdhkrylyGPGSILVAHGPDEAITVSELEEAVEGYKKLI 339
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
8-346 |
1.96e-33 |
|
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: 126.70 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 8 ENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKK-NNVWAFNrhyDPAKPTILLNSHHDTVkPNgaytrdPF 86
Cdd:cd05653 1 QDAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEaGNAVGGA---GSGPPDVLLLGHIDTV-PG------EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 87 AATVEGDRLYGLGSNDAGASGVSLLAAFLHFydRKDLKYNLCVAITAEEENSGHDGLECVIPELGPlEFAIVGEPT-LMQ 165
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAASAL--NEELGARVVVAGLVDEEGSSKGARELVRRGPRP-DYIIIGEPSgWDG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 166 LAIAERGLMVIDCTAHGKAGHAAREEgDNAIYKAMQdiEWFRTYRFPKVSDLFGAVKMSV--TIISAGTQHNVVPAECRF 243
Cdd:cd05653 148 ITLGYRGSLLVKIRCEGRSGHSSSPE-RNAAEDLIK--KWLEVKKWAEGYNVGGRDFDSVvpTLIKGGESSNGLPQRAEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 244 TVDIRVTDRYTNEEVLEIIKEHVS-CEVKARStRLRPSSIRPDHPIVQAGLALGRTTYGSPT------TSD----QALLD 312
Cdd:cd05653 225 TIDLRLPPRLSPEEAIALATALLPtCELEFID-DTEPVKVSKNNPLARAFRRAIRKQGGKPRlkrktgTSDmnvlAPLWT 303
|
330 340 350
....*....|....*....|....*....|....
gi 1772516668 313 IPSLKLGVGDSARSHSADEFVHLSEIREGIELYI 346
Cdd:cd05653 304 VPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLK 337
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-340 |
1.29e-32 |
|
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: 125.28 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 8 ENAVALLRQMIQ----TPSFSKE----EAGTAGLLAEFLQERGVEVHRKKNNvwafnrhydPAKPTI------------- 66
Cdd:cd08013 1 DDPVSLTQTLVRinssNPSLSATggagEAEIATYVAAWLAHRGIEAHRIEGT---------PGRPSVvgvvrgtgggksl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 67 LLNSHHDTVKPNGaYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHfYDRKDLKYNLCVAITAEEENSGHdGLECV 146
Cdd:cd08013 72 MLNGHIDTVTLDG-YDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALAD-AKEAGLRGDVILAAVADEEDASL-GTQEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 147 IPELGPLEFAIVGEPTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKA---MQDIEWF-RTYRFPKVSDLFGAV 221
Cdd:cd08013 149 LAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRpDLGVDAILKAgyfLVALEEYqQELPERPVDPLLGRA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 222 KMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVL--------EIIKEHVSCEVKA-RSTRLRPSSIRP-DHPIVQA 291
Cdd:cd08013 229 SVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLaeltailgELAQTVPNFSYREpRITLSRPPFEVPkEHPFVQL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1772516668 292 GLALGRTTYGSPTT-------SDQALLD---IPSLKLGVgDSARSHSADEFVHLSEIRE 340
Cdd:cd08013 309 VAAHAAKVLGEAPQirsetfwTDAALLAeagIPSVVFGP-SGAGLHAKEEWVDVESIRQ 366
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
35-341 |
2.76e-32 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 124.15 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 35 AEFLQERGVEVHR------KKNNVWAfnrHYDPA-KPTILLNSHHDTVKPNG-AYTRDPFAATVEGDRLYGLGSND-AG- 104
Cdd:PRK07522 32 RDYLAAHGVESELipdpegDKANLFA---TIGPAdRGGIVLSGHTDVVPVDGqAWTSDPFRLTERDGRLYGRGTCDmKGf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 105 -ASGVSLLAAFLhfydRKDLKYNLCVAITAEEEnsghdgLECV-----IPELGPL----EFAIVGEPTLMQLAIAERGLM 174
Cdd:PRK07522 109 iAAALAAVPELA----AAPLRRPLHLAFSYDEE------VGCLgvpsmIARLPERgvkpAGCIVGEPTSMRPVVGHKGKA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 175 VIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTyrfpkVSDLFGAVK------------MSVTIISAGTQHNVVPAEC 241
Cdd:PRK07522 179 AYRCTVRGRAAHSSLaPQGVNAIEYAARLIAHLRD-----LADRLAAPGpfdalfdppystLQTGTIQGGTALNIVPAEC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 242 RFTVDIRVTDRYTNEEVLEIIKEHVSCEVKARSTRLRPSS-IR-------------PDHPIVQaglaLGRTTYGSPTTS- 306
Cdd:PRK07522 254 EFDFEFRNLPGDDPEAILARIRAYAEAELLPEMRAVHPEAaIEfeplsaypgldtaEDAAAAR----LVRALTGDNDLRk 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1772516668 307 ----------DQAllDIPSLKLGVGDSARSHSADEFVHLSEIREG 341
Cdd:PRK07522 330 vaygteaglfQRA--GIPTVVCGPGSIEQAHKPDEFVELAQLAAC 372
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
11-339 |
6.20e-32 |
|
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: 123.00 E-value: 6.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKKN----NVWAFnrhYDPAKPTILLNSHHDTVKP--NGAYTRD 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFggvkNLWAR---RGTGGPHLCFAGHTDVVPPgdLEGWSSD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 85 PFAATVEGDRLYGLGSNDAGASgvslLAAFL-----HFYDRKDLKYNLCVAITAEEENSGHDGLECVIPELGP----LEF 155
Cdd:cd03891 78 PFSPTIKDGMLYGRGAADMKGG----IAAFVaaaerFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKArgekIDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 156 AIVGEPTLMQ-----LAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPKVSDLFGAVKMSVTIIS 229
Cdd:cd03891 154 CIVGEPTSEKklgdtIKIGRRGSLNGKLTIKGKQGHVAYpHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 230 AGTQ-HNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHV-SCEVKArSTRLRPSS---IRPDHPIVQAGLA-----LGRT- 298
Cdd:cd03891 234 VGNGaTNVIPGELKAKFNIRFNDEHTGESLKARIEAILdKHGLDY-DLEWKLSGepfLTKPGKLVDAVSAaikevTGITp 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1772516668 299 ---TYGSptTSDQ---ALLDIPSLKLG-VGDSArsHSADEFVHLSEIR 339
Cdd:cd03891 313 elsTSGG--TSDArfiASYGCPVVEFGlVNATI--HKVNERVSVADLE 356
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
13-344 |
1.40e-30 |
|
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: 119.08 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 13 LLRQMIQTPSFSKEEAGTAGLLAEFLQERG-VEVHRKKNNVWAfNRHYDPAKpTILLNSHHDTVkpngaytrdPFAATV- 90
Cdd:cd05647 4 LTAALVDIPSVSGNEKPIADEIEAALRTLPhLEVIRDGNTVVA-RTERGLAS-RVILAGHLDTV---------PVAGNLp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 91 ----EGDRLYGLGSNDAGASgvslLAAFLHFY---DRKDLKYNLC-VAITAEEENSGHDGLECVI---PELGPLEFAIVG 159
Cdd:cd05647 73 srveEDGVLYGCGATDMKAG----DAVQLKLAatlAAATLKHDLTlIFYDCEEVAAELNGLGRLAeehPEWLAADFAVLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 160 EPTLMQLAIAERGLMVIDCTAHGKAGHAARE-EGDNAIYKAMQDIEWFRTYRfPKVSDLFGAV---KMSVTIISAGTQHN 235
Cdd:cd05647 149 EPTDGTIEGGCQGTLRFKVTTHGVRAHSARSwLGENAIHKLAPILARLAAYE-PRTVNIDGLTyreGLNAVFISGGVAGN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 236 VVPAECRFTVDIRVTDRYTNEEVLEIIKEHVSCE-VKARSTRLRPSSiRP--DHPIVQAGL-ALGRTT---YGSPTTSDQ 308
Cdd:cd05647 228 VIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLgYEIEVTDLSPGA-LPglDHPVARDLIeAVGGKVrakYGWTDVARF 306
|
330 340 350
....*....|....*....|....*....|....*.
gi 1772516668 309 ALLDIPSLKLGVGDSARSHSADEFVHLSEIREGIEL 344
Cdd:cd05647 307 SALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAI 342
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
11-349 |
5.60e-30 |
|
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: 118.62 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQ-----TPSFSKEEAGTAGLLAEFLQERG-------VEVHRKKNNVWAFNRHYDPAKPTILLNSHHDTVKPN 78
Cdd:cd05675 1 VDLLQELIRidttnSGDGTGSETRAAEVLAARLAEAGiqteifvVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVPAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 79 GA-YTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRK-DLKYNLCVAITAEEENSGHDGLECVIPELGPL--- 153
Cdd:cd05675 81 ASdWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGfKPKRDLVFAFVADEEAGGENGAKWLVDNHPELfdg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 154 -EFAI---------VGEPTLMQL-AIAERGLMVIDCTAHGKAGHAAREEGDNAIY------------------------- 197
Cdd:cd05675 161 aTFALneggggslpVGKGRRLYPiQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITrlaealrrlgahnfpvrltdetayf 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 198 KAMQDI----EWFRTYRFPKVSD-----------LFGAV---KMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVL 259
Cdd:cd05675 241 AQMAELaggeGGALMLTAVPVLDpalaklgpsapLLNAMlrnTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEEVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 260 EIIKEHV---SCEVKARStrLRPSSIRP-DHPIVQA-GLALGR-------TTYGSPTTSDQ---ALLDIPS-----LKL- 318
Cdd:cd05675 321 DTLDKLLgdpDVSVEAVH--LEPATESPlDSPLVDAmEAAVQAvdpgapvVPYMSPGGTDAkyfRRLGIPGygfapLFLp 398
|
410 420 430
....*....|....*....|....*....|..
gi 1772516668 319 -GVGDSARSHSADEFVHLSEIREGIELYIKML 349
Cdd:cd05675 399 pELDYTGLFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
8-353 |
1.18e-28 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 114.21 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 8 ENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERG-----VEVHRKKNNVWAFNRHydpAKPTILLNSHHDTVKPN--GA 80
Cdd:PRK08588 2 EEKIQILADIVKINSVNDNEIEVANYLQDLFAKHGieskiVKVNDGRANLVAEIGS---GSPVLALSGHMDVVAAGdvDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 81 YTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKDLKYNlcvAI----TAEEEnSGHDGLEcVIPELG---PL 153
Cdd:PRK08588 79 WTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNG---TIrllaTAGEE-VGELGAK-QLTEKGyadDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 154 EFAIVGEPTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTY--RFPKVSDLFGAVKMSVTIISA 230
Cdd:PRK08588 154 DALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMpELGVNAIDPLLEFYNEQKEYfdSIKKHNPYLGGLTHVVTIING 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 231 GTQHNVVPAECRFTVDIRVTDRYTNEEV---LEIIKEHVSCEVKARSTRLRPSSIRP-----DHPIVQAGLALGRTTY-- 300
Cdd:PRK08588 234 GEQVNSVPDEAELEFNIRTIPEYDNDQVislLQEIINEVNQNGAAQLSLDIYSNHRPvasdkDSKLVQLAKDVAKSYVgq 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1772516668 301 -----GSPTTSDQALL-----DIPSLKLGVGDSARSHSADEFVHLSEIREGIELYIKMLSAIL 353
Cdd:PRK08588 314 diplsAIPGATDASSFlkkkpDFPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQYL 376
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-340 |
3.02e-28 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 113.56 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 12 ALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKKNNVWAFNRH-------------------YDPAKPT---ILLN 69
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIDVEKLKHHpgfspvavdyagapnvvgtHRPRGETgrsLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 70 SHHDTVkPNGA---YTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAF--LHFYDRKdLKYNLCVAITAEEENSGHDGLE 144
Cdd:cd03895 81 GHIDVV-PEGPvelWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALdaLRAAGLQ-PAADVHFQSVVEEECTGNGALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 145 CVipELG-PLEFAIVGEPTLMQLAIAERGLMVIDCTAHGKAGHAA-REEGDNAIYKAMQDIEWFRTY---------RFPK 213
Cdd:cd03895 159 AL--MRGyRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAeASEGVNAIEKAMHLIQALQELerewnarkkSHPH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 214 VSDLFGAVKMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVScEVKARSTRLR--------------P 279
Cdd:cd03895 237 FSDHPHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVA-DAAATDPWLSnhppevewngfqaeG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1772516668 280 SSIRPDHPIVQaglALGRT----------TYGSPTTSDQALL----DIPSLKLGVGdSARSHSADEFVHLSEIRE 340
Cdd:cd03895 316 YVLEPGSDAEQ---VLAAAhqavfgtppvQSAMTATTDGRFFvlygDIPALCYGPG-SRDAHGFDESVDLESLRK 386
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
12-344 |
4.95e-28 |
|
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: 112.22 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 12 ALLRQMIQTPSFS-KEEAGTAGLLAEFLQERGVEVHRKKN-------NVWAFNRHYDPAkpTILLNSHHDTVK-PNGAYT 82
Cdd:TIGR01892 1 EILTKLVAFDSTSfRPNVDLIDWAQAYLEALGFSVEVQPFpdgaeksNLVAVIGPSGAG--GLALSGHTDVVPyDDAAWT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 83 RDPFAATVEGDRLYGLGSNDAGASGVSLLAAfLHFYDRKDLKYNLCVAITAEEEnSGHDGLECVIpELGPLE--FAIVGE 160
Cdd:TIGR01892 79 RDPFRLTEKDGRLYGRGTCDMKGFLACALAA-APDLAAEQLKKPLHLALTADEE-VGCTGAPKMI-EAGAGRprHAIIGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 161 PTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIY---KAMQDIEWFR-TYRFPKVSDLFGAVKMSVTI--ISAGTQ 233
Cdd:TIGR01892 156 PTRLIPVRAHKGYASAEVTVRGRSGHSSYpDSGVNAIFragRFLQRLVHLAdTLLREDLDEGFTPPYTTLNIgvIQGGKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 234 HNVVPAECRFTVDIRVTDRYTNEEVL--------EIIKEHVSCEVKARSTRLRPS-SIRPDHPIVQ-----AGLALGRTT 299
Cdd:TIGR01892 236 VNIIPGACEFVFEWRPIPGMDPEELLqlletiaqALVRDEPGFEVQIEVVSTDPGvNTEPDAELVAfleelSGNAPEVVS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1772516668 300 YGSPTTSDQAlLDIPSLKLGVGDSARSHSADEFVHLSEIREGIEL 344
Cdd:TIGR01892 316 YGTEAPQFQE-LGAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAV 359
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
8-343 |
1.02e-24 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 102.73 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 8 ENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVH-RKKNNVWAFNrhyDPAKPTILLNSHHDTVkPNGAYTRdpf 86
Cdd:PRK04443 6 LEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWvDEAGNARGPA---GDGPPLVLLLGHIDTV-PGDIPVR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 87 aatVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRkdLKYNLCVAITAEEENSGHDGLECVIPELGPlEFAIVGEPTLMQ- 165
Cdd:PRK04443 79 ---VEDGVLWGRGSVDAKGPLAAFAAAAARLEAL--VRARVSFVGAVEEEAPSSGGARLVADRERP-DAVIIGEPSGWDg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 166 LAIAERGLMVIDCTAHGKAGHAAREEgDNAIYKAmqdIEWFRT-----YRFPKVSDLFGAVkmSVTIISAGTQHNVVPAE 240
Cdd:PRK04443 153 ITLGYKGRLLVTYVATSESFHSAGPE-PNAAEDA---IEWWLAveawfEANDGRERVFDQV--TPKLVDFDSSSDGLTVE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 241 CRFTVDIRVTDRYTNEEVLEIIKEHVSCEVKARSTRLRPSSIRPDHPIVQAGLALGRTTYGSPT------TSDQALL--- 311
Cdd:PRK04443 227 AEMTVGLRLPPGLSPEEAREILDALLPTGTVTFTGAVPAYMVSKRTPLARAFRVAIREAGGTPRlkrktgTSDMNVVapa 306
|
330 340 350
....*....|....*....|....*....|...
gi 1772516668 312 -DIPSLKLGVGDSARSHSADEFVHLSEIREGIE 343
Cdd:PRK04443 307 wGCPMVAYGPGDSDLDHTPDEHLPLAEYLRAIA 339
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
9-265 |
1.05e-24 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 103.24 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 9 NAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKK----NNVWAfnRHYDPAkPTILLNSHHDTVKP--NGAYT 82
Cdd:PRK13009 3 DVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDfgdvKNLWA--RRGTEG-PHLCFAGHTDVVPPgdLEAWT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 83 RDPFAATVEGDRLYGLGSNDAGASgvslLAAFL-----HFYDRKDLKYNLCVAITAEEENSGHDGLECVIPEL---G-PL 153
Cdd:PRK13009 80 SPPFEPTIRDGMLYGRGAADMKGS----LAAFVvaaerFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLkarGeKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 154 EFAIVGEPT-LMQLA----IAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPKVSDLFGAVKMSVTI 227
Cdd:PRK13009 156 DYCIVGEPTsTERLGdvikNGRRGSLTGKLTVKGVQGHVAYpHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITN 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1772516668 228 ISAGTQ-HNVVPAECRFTVDIRVTDRYTNE----EVLEIIKEH 265
Cdd:PRK13009 236 IDAGTGaTNVIPGELEAQFNFRFSTEHTAEslkaRVEAILDKH 278
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
11-353 |
7.21e-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: 97.94 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKKNNVWAFNRHYDP-AKPTILLNSHHDTVKPNGaytrDPFAAT 89
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLGDVERDGRGNVVGRLRGTgGGPALLFSAHLDTVFPGD----TPATVR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 90 VEGDRLYGLGSNDAGASgVSLLAAFLHFYDRKD--LKYNLCVAITAEEENSGHD-GLECVIPELGP-LEFAIVGEPTLMQ 165
Cdd:cd03896 77 HEGGRIYGPGIGDNKGS-LACLLAMARAMKEAGaaLKGDVVFAANVGEEGLGDLrGARYLLSAHGArLDYFVVAEGTDGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 166 LAIAERGLMVIDCTAHGKAGHAAREEGD-NAIYKAMQDI----EWFRTYRfPKVSdlFGAVKmsvtiISAGTQHNVVPAE 240
Cdd:cd03896 156 PHTGAVGSKRFRITTVGPGGHSYGAFGSpSAIVAMAKLVealyEWAAPYV-PKTT--FAAIR-----GGGGTSVNRIANL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 241 CRFTVDIR--------VTDRYTNEEVLEIIKEHVscEVKARSTRL--RPSS-IRPDHPIVQAGLALGRTTYGSPT----- 304
Cdd:cd03896 228 CSMYLDIRsnpdaelaDVQREVEAVVSKLAAKHL--RVKARVKPVgdRPGGeAQGTEPLVNAAVAAHREVGGDPRpgsss 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1772516668 305 --TSDQALLDIPSLKLGVGDSARSHSADEFVHLSEIREGIELYiKMLSAIL 353
Cdd:cd03896 306 tdANPANSLGIPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKAY-LMLAAAL 355
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
14-344 |
1.05e-22 |
|
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: 98.17 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 14 LRQMIQTPSFSKEEAGTAGL------LAEFLQERGVEVHRKKNN-----VWAfnrHY--DPAKPTILLNSHHDTVKPN-- 78
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELrraaewLADLLRRLGFTVEIVDTSngapvVFA---EFpgAPGAPTVLLYGHYDVQPAGde 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 79 GAYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAF-LHFYDRKDLKYNLCVAITAEEEnSGHDGLECVI---PELGPLE 154
Cdd:cd03893 81 DGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALrALMQQGGDLPVNVKFIIEGEEE-SGSPSLDQLVeahRDLLAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 155 FAIVGEPTLM---QLAI--AERGLMVIDCTA-------H-GKAGHAARE-------------EGDNAI-----YKAMQDI 203
Cdd:cd03893 160 AIVISDSTWVgqeQPTLtyGLRGNANFDVEVkgldhdlHsGLYGGVVPDpmtalaqllaslrDETGRIlvpglYDAVREL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 204 --EWFRTYR-----FPKVSDLFGAVKM------SVTIISAGTQH------NVVPAECRFTVDIRVTDRYTNEEVLEIIKE 264
Cdd:cd03893 240 peEEFRLDAgvleeVEIIGGTTGSVAErlwtrpALTVLGIDGGFpgegskTVIPPRARAKISIRLVPGQDPEEASRLLEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 265 HVS----CEVKARSTRL---RPSSIRPDHPIVQAGLALGRTTYGS-----------PTTSD-QALLDIPSLKLGVGDS-A 324
Cdd:cd03893 320 HLEkhapSGAKVTVSYVeggMPWRSDPSDPAYQAAKDALRTAYGVeppltreggsiPFISVlQEFPQAPVLLIGVGDPdD 399
|
410 420
....*....|....*....|
gi 1772516668 325 RSHSADEFVHLSEIREGIEL 344
Cdd:cd03893 400 NAHSPNESLRLGNYKEGTQA 419
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
1-352 |
1.39e-22 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 96.78 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 1 METEQLYENAVALLRQM--IQTPSfsKEEAGTAGLLAEFLQERGV--EVHRKKNNVWAfnrhydpAKPTILLNSHHDTVk 76
Cdd:PRK00466 3 QEKELVKQKAKELLLDLlsIYTPS--GNETNATKFFEKISNELNLklEILPDSNSFIL-------GEGDILLASHVDTV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 77 pngaYTRDPfaATVEGDRLYGLGSNDAGASGVSLLAAfLHFYDRKDLKynLCVAITAEEENSGHDGLECVIPELGPLeFA 156
Cdd:PRK00466 73 ----PGYIE--PKIEGEVIYGRGAVDAKGPLISMIIA-AWLLNEKGIK--VMVSGLADEESTSIGAKELVSKGFNFK-HI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 157 IVGEPT-LMQLAIAERGLMVIDCTAHGKAGHAAREEgDNAIYKAMQDIewFRTYRFPKVSDLFGAVkmsVTIISAGTQHN 235
Cdd:PRK00466 143 IVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSAK-SNLIVDISKKI--IEVYKQPENYDKPSIV---PTIIRAGESYN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 236 VVPAECRFTVDIRVTDRYTNEEVL-EIIKEHVSCEVKARSTrLRPSSIRPDHPIVQAGLALGRTTYGSPT------TSDQ 308
Cdd:PRK00466 217 VTPAKLYLHFDVRYAINNKRDDLIsEIKDKFQECGLKIVDE-TPPVKVSINNPVVKALMRALLKQNIKPRlvrkagTSDM 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1772516668 309 ALLDIPS---LKLGVGDSARSHSADEFVHLSEIREGIELYIKMLSAI 352
Cdd:PRK00466 296 NILQKITtsiATYGPGNSMLEHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
7-339 |
3.93e-21 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 93.53 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 7 YENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKKNNVWAFNRH-------------------YDPAKPT-- 65
Cdd:PRK06837 19 FDAQVAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSIDPDDLKSHpgagpveidysgapnvvgtYRPAGKTgr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 66 -ILLNSHHDTVK--PNGAYTRDPFAATVEGDRLYGLGSNDAGASgvslLAAFLHFYDR-KDLKYNLCVAIT----AEEEN 137
Cdd:PRK06837 99 sLILQGHIDVVPegPLDLWSRPPFDPVIVDGWMYGRGAADMKAG----LAAMLFALDAlRAAGLAPAARVHfqsvIEEES 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 138 SGHDGLE----------CVIPelgplefaivgEPTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWF 206
Cdd:PRK06837 175 TGNGALStlqrgyradaCLIP-----------EPTGEKLVRAQVGVIWFRLRVRGAPVHVREaGTGANAIDAAYHLIQAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 207 RTYRF----PKVSD-LFGAV----KMSVTIISAGTQHNVVPAECRFTVDIRVtdrYTNEEVLEIIKEHVSCeVKARSTRL 277
Cdd:PRK06837 244 RELEAewnaRKASDpHFEDVphpiNFNVGIIKGGDWASSVPAWCDLDCRIAI---YPGVTAADAQAEIEAC-LAAAARDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 278 RPSSIRPDH--------------PIVQAGLALGRT---TYGSP--TTSDQALLD---------IPSLKLG-VGDSArsHS 328
Cdd:PRK06837 320 RFLSNNPPEvvwsgflaegyvlePGSEAEAALARAhaaVFGGPlrSFVTTAYTDtrfyglyygIPALCYGpSGEGI--HG 397
|
410
....*....|.
gi 1772516668 329 ADEFVHLSEIR 339
Cdd:PRK06837 398 FDERVDLESVR 408
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
8-262 |
5.93e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 92.13 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 8 ENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRKKNNVwAFNRHYDPaKPTILLNSHHDTVKPNgaytRDPFa 87
Cdd:PRK08652 2 ERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGE-VINIVVNS-KAELFVEVHYDTVPVR----AEFF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 88 atVEGDRLYGLGSNDAGASGVSLLAAfLHFYDRKDLKYNLCVAITAEEENSGHdGLECVIPELGPlEFAIVGEPTLMQLA 167
Cdd:PRK08652 75 --VDGVYVYGTGACDAKGGVAAILLA-LEELGKEFEDLNVGIAFVSDEEEGGR-GSALFAERYRP-KMAIVLEPTDLKVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 168 IAERGLMVIDCTAHGKAGHAA-REEGDNAIYKA------MQDIEWFRTYRFPKvsdlfgavKMSVTIISAGTQHNVVPAE 240
Cdd:PRK08652 150 IAHYGNLEAYVEVKGKPSHGAcPESGVNAIEKAfemlekLKELLKALGKYFDP--------HIGIQEIIGGSPEYSIPAL 221
|
250 260
....*....|....*....|..
gi 1772516668 241 CRFTVDIRVTDRYTNEEVLEII 262
Cdd:PRK08652 222 CRLRLDARIPPEVEVEDVLDEI 243
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
63-291 |
1.29e-20 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 91.83 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 63 KPTILLNSHHDTVKPN--GAYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRK-DLKYNLCVAITAEEENSG 139
Cdd:PRK13983 76 KRTLWIISHMDVVPPGdlSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGiRPKYNLGLAFVSDEETGS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 140 HDGLECVI---PEL-GPLEFAIV---GEPTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDI-EWFRT-- 208
Cdd:PRK13983 156 KYGIQYLLkkhPELfKKDDLILVpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHASTpENGINAHRAAADFAlELDEAlh 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 209 YRFPKVSDLFgAVKMSV---TIISAGTQH-NVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVScEVKARST--------- 275
Cdd:PRK13983 236 EKFNAKDPLF-DPPYSTfepTKKEANVDNiNTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIAD-EFEEEYGvkieveivq 313
|
250
....*....|....*..
gi 1772516668 276 RLRPSS-IRPDHPIVQA 291
Cdd:PRK13983 314 REQAPPpTPPDSEIVKK 330
|
|
| PRK06915 |
PRK06915 |
peptidase; |
4-344 |
2.45e-20 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 91.29 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 4 EQLYENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEV--------HRKKNNVWAFNRHYDPAKP----------- 64
Cdd:PRK06915 13 ESHEEEAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwepsfkKLKDHPYFVSPRTSFSDSPnivatlkgsgg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 65 --TILLNSHHDTVkPNG---AYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAF--LHFYDRKdLKYNLCVAITAEEEN 137
Cdd:PRK06915 93 gkSMILNGHIDVV-PEGdvnQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMeaLIESGIE-LKGDVIFQSVIEEES 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 138 SGHDGLECVIPELGPlEFAIVGEPTLMQLAIAERGLMVIDCTAHGKAGHAA-REEGDNAIYKAM---QDIEWFRTYRFPK 213
Cdd:PRK06915 171 GGAGTLAAILRGYKA-DGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGtRYEGVSAIEKSMfviDHLRKLEEKRNDR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 214 VSD-LFGAVKMSVTI----ISAGTQHNVVP----AECRFTVDIRVTDRYTNEEVLEIIKE---------HVSCEVKARST 275
Cdd:PRK06915 250 ITDpLYKGIPIPIPInigkIEGGSWPSSVPdsviLEGRCGIAPNETIEAAKEEFENWIAElndvdewfvEHPVEVEWFGA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 276 RLRPSSIRPDHPIVQAGLALGRTTYG-------SPTTSDQALL----DIPSLKLGVGDSARSHSADEFVHLSEIREGIEL 344
Cdd:PRK06915 330 RWVPGELEENHPLMTTLEHNFVEIEGnkpiieaSPWGTDGGLLtqiaGVPTIVFGPGETKVAHYPNEYIEVDKMIAAAKI 409
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
65-287 |
2.68e-18 |
|
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: 85.20 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 65 TILLNSHHDTVKPNGA--YTRDPFAATVEGDRLYGLGSNDAGASGV-SLLAAFLHFYDRKDLKYNLCVAITAEEENSGHD 141
Cdd:cd05650 71 TLWIISHLDTVPPGDLslWETDPWEPVVKDGKIYGRGVEDNQQGIVsSLLALKAIIKNGITPKYNFGLLFVADEEDGSEY 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 142 GLECVIPE---LGPLEFAIV---GEPTLMQLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKA---MQDIEWFRTYRF 211
Cdd:cd05650 151 GIQYLLNKfdlFKKDDLIIVpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTpENGINAFVAAsnfALELDELLHEKF 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1772516668 212 PKVSDLFG--AVKMSVTIISAGTQH-NVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVSCEVKARSTRLRPSSIRPDHP 287
Cdd:cd05650 231 DEKDDLFNppYSTFEPTKKEANVPNvNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQA 309
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
10-298 |
9.85e-18 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 83.53 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 10 AVALLRQMIQTPSFSKEEAG---TAGLLAEFLQERGVEVHRKK------NNVWAfnRHYDPAKPTILLNSHHDTVKPNGA 80
Cdd:PRK06133 39 YLDTLKELVSIESGSGDAEGlkqVAALLAERLKALGAKVERAPtppsagDMVVA--TFKGTGKRRIMLIAHMDTVYLPGM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 81 YTRDPFaaTVEGDRLYGLGSNDAgASGVsllAAFLHFYD-RKDLKY----NLCVAITAEEEnSGHDGLECVIPELGPLEF 155
Cdd:PRK06133 117 LAKQPF--RIDGDRAYGPGIADD-KGGV---AVILHALKiLQQLGFkdygTLTVLFNPDEE-TGSPGSRELIAELAAQHD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 156 AIVG-EPTLMQ--LAIAERGLMVIDCTAHGKAGHA--AREEGDNAIYKAMQDIEWFRtyrfpKVSDLFGAVKMSVTIISA 230
Cdd:PRK06133 190 VVFScEPGRAKdaLTLATSGIATALLEVKGKASHAgaAPELGRNALYELAHQLLQLR-----DLGDPAKGTTLNWTVAKA 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1772516668 231 GTQHNVVPAECRFTVDIRVTDRYTNEEVL----EIIKEHV--SCEVKARSTRLRPssirpdhPIVQ--AGLALGRT 298
Cdd:PRK06133 265 GTNRNVIPASASAQADVRYLDPAEFDRLEadlqEKVKNKLvpDTEVTLRFERGRP-------PLEAnaASRALAEH 333
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
13-344 |
2.66e-17 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 82.18 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 13 LLRQMIQTPSFSKEEA-------GTAGLLAEFLQERG-------VEVHRKKNNVWAfnrHYDPAKPTILLNSHHDTVkP- 77
Cdd:PRK05111 10 MYRALIATPSISATDPaldqsnrAVIDLLAGWFEDLGfnveiqpVPGTRGKFNLLA---SLGSGEGGLLLAGHTDTV-Pf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 78 -NGAYTRDPFAATVEGDRLYGLGSNDagasgvslLAAFLHF-------YDRKDLKYNLCVAITAEEEnSGHDGLECVIPE 149
Cdd:PRK05111 86 dEGRWTRDPFTLTEHDGKLYGLGTAD--------MKGFFAFilealrdIDLTKLKKPLYILATADEE-TSMAGARAFAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 150 LGPL-EFAIVGEPTLMQLAIAERGLM--VIDCTahGKAGHA---AReeGDNAIyKAMQDI---------EWFRTYRFPkv 214
Cdd:PRK05111 157 TAIRpDCAIIGEPTSLKPVRAHKGHMseAIRIT--GQSGHSsdpAL--GVNAI-ELMHDVigellqlrdELQERYHNP-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 215 sdLFgAV---KMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVScEVKAR-STRLrpsSIRP------ 284
Cdd:PRK05111 230 --AF-TVpypTLNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALA-PVSERwPGRI---TVAPlhppip 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1772516668 285 ------DHPIVQA-----GLALGRTTYGS--PTTSDqalLDIPSLKLGVGDSARSHSADEFVHLSEIREGIEL 344
Cdd:PRK05111 303 gyecpaDHQLVRVvekllGHKAEVVNYCTeaPFIQQ---LGCPTLVLGPGSIEQAHQPDEYLELSFIKPTREL 372
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
168-267 |
3.95e-17 |
|
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: 75.85 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 168 IAERGLMVIDCTAHGKAGHA-AREEGDNAIYKAMQDIEWFRTYRFPKVsDLFGAVKMSVTIISAGTQHNVVPAECRFTVD 246
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSgAPGKGVNAIKLLARLLAELPAEYGDIG-FDFPRTTLNITGIEGGTATNVIPAEAEAKFD 79
|
90 100
....*....|....*....|.
gi 1772516668 247 IRVTDRYTNEEVLEIIKEHVS 267
Cdd:pfam07687 80 IRLLPGEDLEELLEEIEAILE 100
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
60-352 |
5.34e-17 |
|
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: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 60 DPAKPTILLNSHHDTVkP--NGAYTRDPFAATVEGD-RLYGLGSNDAGASGVSLLAAFLHFYdRKDLKYNLCVAIT--AE 134
Cdd:TIGR01880 68 NPELPSILLNSHTDVV-PvfREHWTHPPFSAFKDEDgNIYARGAQDMKCVGVQYLEAVRNLK-ASGFKFKRTIHISfvPD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 135 EENSGHDGLECVIP--ELGPLEFAIV---GEPT---LMQLAIAERGLMVIDCTAHGKAGHAAREEGDNAIYKAMQDIEWF 206
Cdd:TIGR01880 146 EEIGGHDGMEKFAKtdEFKALNLGFAldeGLASpddVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 207 RTYRFPKVSDL-------FGAV-KMSVTIISAGTQHNVVPAECRFTVDIRVT--------DRYTNEEVLEIIkEHVSCEV 270
Cdd:TIGR01880 226 RRFRESQFQLLqsnpdlaIGDVtSVNLTKLKGGVQSNVIPSEAEAGFDIRLApsvdfeemENRLDEWCADAG-EGVTYEF 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 271 KARSTRLRPSSIRPDHP----IVQAGLALGRT----------------TYGSPTTSDQALLDIPSLklgvgdsarSHSAD 330
Cdd:TIGR01880 305 SQHSGKPLVTPHDDSNPwwvaFKDAVKEMGCTfkpeilpgstdsryirAAGVPALGFSPMNNTPVL---------LHDHN 375
|
330 340
....*....|....*....|..
gi 1772516668 331 EFVHLSEIREGIELYIKMLSAI 352
Cdd:TIGR01880 376 EFLNEAVFLRGIEIYQTLISAL 397
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
60-352 |
6.04e-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: 78.08 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 60 DPAKPTILLNSHHDTVkP--NGAYTRDPFAATVEGD-RLYGLGSNDAGASGVSLLAAFLH-FYDRKDLKYNLCVAITAEE 135
Cdd:cd05646 61 NPELPSILLNSHTDVV-PvfEEKWTHDPFSAHKDEDgNIYARGAQDMKCVGIQYLEAIRRlKASGFKPKRTIHLSFVPDE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 136 ENSGHDGLECVI--PELGPLE--FAI---VGEPT-LMQLAIAERGLMVIDCTAHGKAGHAAREEGDNAIYKAMQDIEWFR 207
Cdd:cd05646 140 EIGGHDGMEKFVktEEFKKLNvgFALdegLASPTeEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 208 TYRFPKVSDL-------FGAV-KMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKE-------HVSCEVKA 272
Cdd:cd05646 220 EFRESQKQRLksnpnltLGDVtTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEwcaeagrGVTYEFEQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 273 RSTRLRPSSIRPDHPIVQA--------GLALGRTTYgsPTTSDQAL---LDIPSLklgvGDSARS------HSADEFVHL 335
Cdd:cd05646 300 KSPEKDPTSLDDSNPWWAAfkkavkemGLKLKPEIF--PAATDSRYiraLGIPAL----GFSPMNntpillHDHNEFLNE 373
|
330
....*....|....*..
gi 1772516668 336 SEIREGIELYIKMLSAI 352
Cdd:cd05646 374 DVFLRGIEIYEKIIPAL 390
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
64-351 |
1.31e-15 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 77.16 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 64 PTILLNSHHDTVKPNGAYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAflhfYDRKDLKYnlCVAITAEEENSGHDGL 143
Cdd:PRK08737 64 PKYLFNVHLDTVPDSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAA----ANAGDGDA--AFLFSSDEEANDPRCV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 144 ECVIPELGPLEFAIVGEPTLMQLAIAERGLMVIDCTAHGKAGHAA--REEGDNAIYKAM----QDIEWFRTYRFPKVSDL 217
Cdd:PRK08737 138 AAFLARGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASgkQDPSASALHQAMrwggQALDHVESLAHARFGGL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 218 FGAvKMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIK-----EHVSCEVKARSTRLRPSSI------RPDH 286
Cdd:PRK08737 218 TGL-RFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAgfaepAAATFEETFRGPSLPSGDIaraeerRLAA 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 287 PIVQAGLALgrtTYGSPTT--SDQALLD---IPSLKLGVGDSARSHSADEFVHLSEIREGIELYIKMLSA 351
Cdd:PRK08737 297 RDVADALDL---PIGNAVDfwTEASLFSaagYTALVYGPGDIAQAHTADEFVTLDQLQRYAESVHRIIND 363
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
10-217 |
4.05e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 76.19 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 10 AVALLRQMIQTPSfsKEEAGTAGLLAEFLQER----G--------VEVHRKKNNVWAFNRHYDPAKPtILLNSHHDTVKP 77
Cdd:PRK09133 39 ARDLYKELIEINT--TASTGSTTPAAEAMAARlkaaGfadadievTGPYPRKGNLVARLRGTDPKKP-ILLLAHMDVVEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 78 NGA-YTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLH-----FYDRKDLKynlcVAITAEEENSGHDGLECVI---P 148
Cdd:PRK09133 116 KREdWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRlkregFKPKRDII----LALTGDEEGTPMNGVAWLAenhR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 149 ELGPLEFAI----------VGEPTLMQLAIAERGLMVIDCTAHGKAGHAAREEGDNAIYKAMQDIEWFRTYRFP-KVSDL 217
Cdd:PRK09133 192 DLIDAEFALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAAYRFPvMLNDV 271
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
14-349 |
1.86e-14 |
|
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: 73.91 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 14 LRQMIQTPSFSKEEAG---TAGLLAEFLQERGVEV---HRKKNN-VWA-FNRHydpAKPTILLNSHHDT--VKPNGAYTR 83
Cdd:cd05681 5 LRDLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVeifETDGNPiVYAeFNSG---DAKTLLFYNHYDVqpAEPLELWTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 84 DPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRK-DLKYNLCVAITAEEEnSGHDGLECVIPELGPL--------E 154
Cdd:cd05681 82 DPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLgELPVNIKFLVEGEEE-VGSPNLEKFVAEHADLlkadgciwE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 155 FAIVGEPTLMQLAIAERGLMVIDCTAHG---------------------KAGHAAREEGDNAIYK---------AMQDIE 204
Cdd:cd05681 161 GGGKNPKGRPQISLGVKGIVYVELRVKTadfdlhssygaivenpawrlvQALNSLRDEDGRVLIPgfyddvrplSEAERA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 205 WFRTYRFP--KVSDLFGAVKM----------------SVTI--ISAGTQ----HNVVPAECRFTVDIRVTDRYTNEEVLE 260
Cdd:cd05681 241 LIDTYDFDpeELRKTYGLKRPlqvegkdplralftepTCNIngIYSGYTgegsKTILPSEAFAKLDFRLVPDQDPAKILS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 261 IIKEHVS----CEVKARSTRL-RPSSIRPDHPIVQAGLALGRTTYGS-----PTTSDQA-------LLDIPSLKLGVG-D 322
Cdd:cd05681 321 LLRKHLDkngfDDIEIHDLLGeKPFRTDPDAPFVQAVIESAKEVYGQdpivlPNSAGTGpmypfydALEVPVVAIGVGnA 400
|
410 420
....*....|....*....|....*..
gi 1772516668 323 SARSHSADEFVHLSEIREGIELYIKML 349
Cdd:cd05681 401 GSNAHAPNENIRIADYYKGIEHTEELL 427
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
16-352 |
1.94e-14 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 73.55 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 16 QMIQTPSFSKEEAGTAGLLAEFLQERGVEVHR-KKNNVWAF---NRHYDpaKPTILLNSHHDTVKpngAYTRDPFAATVE 91
Cdd:COG2195 11 EYVKIPTPSDHEEALADYLVEELKELGLEVEEdEAGNVIATlpaTPGYN--VPTIGLQAHMDTVP---QFPGDGIKPQID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 92 GDRLYG-----LGSND-AG-ASGVSLLAAFLHfydrKDLKY-NLCVAITAEEEnSGHDGLECVIPELGPLEFAIV--GEp 161
Cdd:COG2195 86 GGLITAdgtttLGADDkAGvAAILAALEYLKE----PEIPHgPIEVLFTPDEE-IGLRGAKALDVSKLGADFAYTldGG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 162 tlmqlaiaERGLMVIDC--------TAHGKAGHA--AREEGDNAIYKAMQDIEWFRTYRFPKVSDLfgavkmSVTIISAG 231
Cdd:COG2195 160 --------EEGELEYECagaadakiTIKGKGGHSgdAKEKMINAIKLAARFLAALPLGRIPEETEG------NEGFIHGG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 232 TQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHV--------SCEVKARSTRLRPS-SIRPDHPIV----QAGLALGRT 298
Cdd:COG2195 226 SATNAIPREAEAVYIIRDHDREKLEARKAELEEAFeeenakygVGVVEVEIEDQYPNwKPEPDSPIVdlakEAYEELGIE 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1772516668 299 tygsPTT------SDQALL---DIPSLKLGVGdsARS-HSADEFVHLSEIREGIELYIKMLSAI 352
Cdd:COG2195 306 ----PKIkpirggLDGGILsfkGLPTPNLGPG--GHNfHSPDERVSIESMEKAWELLVEILKLI 363
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
7-339 |
5.33e-14 |
|
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: 72.59 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 7 YENAVALLRQMIQTPSFSK--EEAGTAGLLAEFLQERGVEVHRK---KNNVWAFN----------RHYDPAKPTILLNSH 71
Cdd:cd02697 2 FDEEVRFLQKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAERHpvpEAEVRAYGmesitnlivrRRYGDGGRTVALNAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 72 HDTVKPNGAYTRDPFAATVEGDRLYGlgsnDAGASGVSLLAAFLhFYDR------KDLKYNLCVAITAEEENSGhdglec 145
Cdd:cd02697 82 GDVVPPGDGWTRDPYGAVVEDGVMYG----RAAAVSKSDFASFT-FAVRaleslgAPLRGAVELHFTYDEEFGG------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 146 vipELGP--LEFAIVGEPTLM-------QLAIAERGLMVIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYR--FPK 213
Cdd:cd02697 151 ---ELGPgwLLRQGLTKPDLLiaagfsyEVVTAHNGCLQMEVTVHGKQAHAAIpDTGVDALQGAVAILNALYALNaqYRQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 214 VSDLFGAVK---MSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIK---EHVSCEVKARSTRLR----PSSIR 283
Cdd:cd02697 228 VSSQVEGIThpyLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRrviADAAASMPGISVDIRrlllANSMR 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1772516668 284 P---DHPIVQA-----GLALGR--TTYGSPTTSDQALL---DIPSLKLGVGD----SARSHSADEFVHLSEIR 339
Cdd:cd02697 308 PlpgNAPLVEAiqthgEAVFGEpvPAMGTPLYTDVRLYaeaGIPGVIYGAGPrtvlESHAKRADERLQLEDLR 380
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
11-333 |
6.68e-13 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 69.40 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFS---KEEAGTAGLLAEFLQERGVEVHR-------------KKNNVWAFNRHYDPAkPTILLNSHHDT 74
Cdd:PRK13013 17 VALTQDLIRIPTLNppgRAYREICEFLAARLAPRGFEVELiraegapgdsetyPRWNLVARRQGARDG-DCVHFNSHHDV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 75 VKPNGAYTRDPFAATVEGDRLYGLGSND-AGASGVSLLA--AFLHFYdrKDLKYNLCVAITAEEENSGHDGLeCVIPELG 151
Cdd:PRK13013 96 VEVGHGWTRDPFGGEVKDGRIYGRGACDmKGGLAASIIAaeAFLAVY--PDFAGSIEISGTADEESGGFGGV-AYLAEQG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 152 -----PLEFAIVGEPTLM-QLAIAERGLMVIDCTAHGKAGHAARE-EGDNAIYK---AMQDIE-------WFRTYRFPKV 214
Cdd:PRK13013 173 rfspdRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMPfLGDSAIRHmgaVLAEIEerlfpllATRRTAMPVV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 215 SDlfGAVKMSVTIIS------------AGTQHNVVPAECRFTVDirvtDRYTNEEVLEIIKEHVScEVKARSTRLRPS-- 280
Cdd:PRK13013 253 PE--GARQSTLNINSihggepeqdpdyTGLPAPCVADRCRIVID----RRFLIEEDLDEVKAEIT-ALLERLKRARPGfa 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1772516668 281 -------SIRP-----DHPIVQAGLA-----LGRTT--YGSPTTSDQALLD-IPSLK----LGVGDSARSHSADEFV 333
Cdd:PRK13013 326 yeirdlfEVLPtmtdrDAPVVRSVAAaiervLGRQAdyVVSPGTYDQKHIDrIGKLKnciaYGPGILDLAHQPDEWV 402
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
4-339 |
1.04e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 68.78 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 4 EQLYENAVALLRQMIQTPS-----FSKEE-AGTAGLLAEFLQERG---VEVHRKkNNVWAFNRHYDPA--KPTILLNSHH 72
Cdd:PRK07907 14 AELLPRVRADLEELVRIPSvaadpFRREEvARSAEWVADLLREAGfddVRVVSA-DGAPAVIGTRPAPpgAPTVLLYAHH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 73 DtVKPNG---AYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDrkDLKYNLCVAITAEEEnSGHDGLECVIPE 149
Cdd:PRK07907 93 D-VQPPGdpdAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGG--DLPVGVTVFVEGEEE-MGSPSLERLLAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 150 lGPLEFAI------------VGEPTlmqLAIAERGlmVIDCTAH----------GKAGHAA---------------REEG 192
Cdd:PRK07907 169 -HPDLLAAdviviadsgnwsVGVPA---LTTSLRG--NADVVVTvrtlehavhsGQFGGAApdaltalvrllatlhDEDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 193 DNAIYKAMQDIEW-FRTY---RFPKVS------DLFGA--------VKMSVTII-----SAGTQHNVVPAECRFTVDIRV 249
Cdd:PRK07907 243 NVAVDGLDATEPWlGVDYdeeRFRADAgvldgvELIGTgsvadrlwAKPAITVIgidapPVAGASNALPPSARARLSLRV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 250 TDRYTNEEVLEIIKEHVSCEVK--ARSTRLR-----PSSIRPDHPIVQAGLALGRTTYGSPTTsDQA----------LLD 312
Cdd:PRK07907 323 APGQDAAEAQDALVAHLEAHAPwgAHVTVERgdagqPFAADASGPAYDAARAAMREAWGKDPV-DMGmggsipfiaeLQE 401
|
410 420 430
....*....|....*....|....*....|..
gi 1772516668 313 I-PSLKL---GVGD-SARSHSADEFVHLSEIR 339
Cdd:PRK07907 402 AfPQAEIlvtGVEDpKTRAHSPNESVHLGELE 433
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
51-162 |
4.21e-12 |
|
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: 64.38 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 51 NVWAFNRHyDPAKPTILLNSHHDTVKPNGAYTRDPFAA--TVEGDRLYGLGSNDAGASGVSLLAAFLHFYD-RKDLKYNL 127
Cdd:cd18669 1 NVIARYGG-GGGGKRVLLGAHIDVVPAGEGDPRDPPFFvdTVEEGRLYGRGALDDKGGVAAALEALKLLKEnGFKLKGTV 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1772516668 128 CVAITAEEENSGHDGLECV----IPELGPLEFAIVGEPT 162
Cdd:cd18669 80 VVAFTPDEEVGSGAGKGLLskdaLEEDLKVDYLFVGDAT 118
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
10-264 |
4.68e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 66.80 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 10 AVALLRQMIQ--TPSF----SKEEAGTAGLLAEFLQERGVEV-----HRKKNNVWAFNRHYDPAKPTILLNSHHDTVKPN 78
Cdd:PRK07906 1 VVDLCSELIRidTTNTgdgtGKGEREAAEYVAEKLAEVGLEPtylesAPGRANVVARLPGADPSRPALLVHGHLDVVPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 79 GA-YTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYD-----RKDLkynlCVAITAEEENSGHDG---------- 142
Cdd:PRK07906 81 AAdWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARtgrrpPRDL----VFAFVADEEAGGTYGahwlvdnhpe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 143 -LECV---IPELGPLEFAIVGEPTLMQLAIAERGLMVIDCTAHGKAGHAAREEGDNAIYKAMQDIEWFRTYRFP------ 212
Cdd:PRK07906 157 lFEGVteaISEVGGFSLTVPGRDRLYLIETAEKGLAWMRLTARGRAGHGSMVNDDNAVTRLAEAVARIGRHRWPlvltpt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 213 ------KVSDLFG-----------------AVKM---------SVTIISAGTQHNVVPAECRFTVDIRVTDRYTnEEVLE 260
Cdd:PRK07906 237 vrafldGVAELTGlefdpddpdallaklgpAARMvgatlrntaNPTMLKAGYKVNVIPGTAEAVVDGRFLPGRE-EEFLA 315
|
....
gi 1772516668 261 IIKE 264
Cdd:PRK07906 316 TVDE 319
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
60-267 |
1.70e-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: 64.97 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 60 DPA-KPtILLNSHHDTV----KPNGAYTRDPFAATVEGDRLYGLGSNDAGASGVSLLAA---------------FLHF-Y 118
Cdd:cd05674 66 DPSlKP-LLLMAHQDVVpvnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAvelllkrgfkprrtiILAFgH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 119 DRKDLKYNLCVAITAEEENS-GHDGLECVIPELGP-LEFAIVGEPTLMqLAIAERGLMVIDCTAHGKAGHAA-------- 188
Cdd:cd05674 145 DEEVGGERGAGAIAELLLERyGVDGLAAILDEGGAvLEGVFLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSvppkhtgi 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 189 -----------------REEGDNAIYKAMQ----------------------DIEWFRTYRFPKVSDLFGAV---KMSVT 226
Cdd:cd05674 224 gilseavaaleanpfppKLTPGNPYYGMLQclaehsplpprslksnlwlaspLLKALLASELLSTSPLTRALlrtTQAVD 303
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1772516668 227 IISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVS 267
Cdd:cd05674 304 IINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIA 344
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
34-349 |
3.90e-11 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 63.81 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 34 LAEFLQERGVEVHR--KKNNVWAFNRHY-----DPAKPTILLNSHHDTV----KPNGAYTRDPFAATVEGDRLYGLGSND 102
Cdd:PRK08262 75 LHAHLEESYPAVHAalEREVVGGHSLLYtwkgsDPSLKPIVLMAHQDVVpvapGTEGDWTHPPFSGVIADGYVWGRGALD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 103 AGASGVSLLAAFLH-----FYDRKDLKYnlcvAITAEEENSGHDG-------------LECVIPELGPL---EFAIVGEP 161
Cdd:PRK08262 155 DKGSLVAILEAAEAllaqgFQPRRTIYL----AFGHDEEVGGLGAraiaellkergvrLAFVLDEGGAItegVLPGVKKP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 162 TLMqLAIAERGLMVIDCTAHGKAGHAAREEGDNAI---YKAMQDIEWFR-TYRF-PKVSDLF--------GAVKMS---- 224
Cdd:PRK08262 231 VAL-IGVAEKGYATLELTARATGGHSSMPPRQTAIgrlARALTRLEDNPlPMRLrGPVAEMFdtlapemsFAQRVVlanl 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 225 --------------------------VTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHV---SCEVKARST 275
Cdd:PRK08262 310 wlfeplllrvlakspetaamlrtttaPTMLKGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRRAVaddRVEIEVLGG 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 276 RLRPS---------------SIRPDHP--IVQAGLALGRT--TYGSPTTSDqaLLDIPSLKLGVGDSARSHSADEFVHLS 336
Cdd:PRK08262 390 NSEPSpvsstdsaaykllaaTIREVFPdvVVAPYLVVGATdsRHYSGISDN--VYRFSPLRLSPEDLARFHGTNERISVA 467
|
410
....*....|...
gi 1772516668 337 EIREGIELYIKML 349
Cdd:PRK08262 468 NYARMIRFYYRLI 480
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
61-350 |
6.77e-11 |
|
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: 63.25 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 61 PAKPTILLNSHHDTVKPN-GAYTRDPFAATVEGDRLYGLGSNDAgASGVSLLAAFLHFY--DRKDLKYNLCVAITAEEEN 137
Cdd:cd08012 76 DGKTVSFVGSHMDVVTANpETWEFDPFSLSIDGDKLYGRGTTDC-LGHVALVTELFRQLatEKPALKRTVVAVFIANEEN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 138 SG----------HDGLECVIPElGPLEFAIVGEPtlmQLAIAERGLMVIDCTAHGKAGHAA-REEGDNAIYKAMQDIEWF 206
Cdd:cd08012 155 SEipgvgvdalvKSGLLDNLKS-GPLYWVDSADS---QPCIGTGGMVTWKLTATGKLFHSGlPHKAINALELVMEALAEI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 207 --RTYR-FP-----KVSDLFGAVKMSVTIIS-AGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVScEVKARSTRL 277
Cdd:cd08012 231 qkRFYIdFPphpkeEVYGFATPSTMKPTQWSyPGGSINQIPGECTICGDCRLTPFYDVKEVREKLEEYVD-DINANIEEL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 278 R---PSS--IRPDHPIV-----------QAGLA----------LGRTT-----YGSPTTSDQALLDIPSLK--------L 318
Cdd:cd08012 310 PtrgPVSkyVLPAEGLRgrvslefdeaaASGVAcnldspgfhaLCKATsevvgYVKPYAITGSLPLIRELQdegfdvqiT 389
|
330 340 350
....*....|....*....|....*....|..
gi 1772516668 319 GVGDSARSHSADEFVHLSEIREGIELYIKMLS 350
Cdd:cd08012 390 GYGLMATYHAKNEYCLLSDFQNGFKVLARTIA 421
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
8-136 |
1.67e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 62.08 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 8 ENAVALLRQMIQTPSFSKEEAG---TAGLLAEFLQERGVE--VHRKKNNVWAFNRHYDPAKPTILLNSHHDT--VKPNGA 80
Cdd:PRK06446 2 DEELYTLIEFLKKPSISATGEGieeTANYLKDTMEKLGIKanIERTKGHPVVYGEINVGAKKTLLIYNHYDVqpVDPLSE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1772516668 81 YTRDPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKDLKYNLCVAITAEEE 136
Cdd:PRK06446 82 WKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVNVKFLYEGEEE 137
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
4-353 |
2.74e-10 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 61.21 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 4 EQLYENAVALLRQMIQTPSFSKEEAGTAGL---LAEFLQERGVEVHRKK-----NNVWAFNRHYDPAKP-TILLNSHHD- 73
Cdd:PRK08596 9 ELRKDELLELLKTLVRFETPAPPARNTNEAqefIAEFLRKLGFSVDKWDvypndPNVVGVKKGTESDAYkSLIINGHMDv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 74 -TVKPNGAYTRDPFAATVEGDRLYGLGSND--AGASGVSLLAAFLHFYDRkDLKYNLCV-AITAEEenSGHDG-LECVip 148
Cdd:PRK08596 89 aEVSADEAWETNPFEPTIKDGWLYGRGAADmkGGLAGALFAIQLLHEAGI-ELPGDLIFqSVIGEE--VGEAGtLQCC-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 149 ELGP-LEFAIVGEPTlmqlaiaerglmviDCTAHGKAG-----------------------HA-AREEGDNAIYK----- 198
Cdd:PRK08596 164 ERGYdADFAVVVDTS--------------DLHMQGQGGvitgwitvkspqtfhdgtrrqmiHAgGGLFGASAIEKmmkii 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 199 -AMQDIE--WFRTYRFPKVSDlfGAVKMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVScEVKARST 275
Cdd:PRK08596 230 qSLQELErhWAVMKSYPGFPP--GTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIG-KVAAADP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 276 RLR---------------------PS-SIRPDHPIVQAGLALGRTTYG-------SPTTSDQALL---DIPSLKLGVGDS 323
Cdd:PRK08596 307 WLRenppqfkwggesmiedrgeifPSlEIDSEHPAVKTLSSAHESVLSknaildmSTTVTDGGWFaefGIPAVIYGPGTL 386
|
410 420 430
....*....|....*....|....*....|
gi 1772516668 324 ARSHSADEFVHLSEIREgielYIKMLSAIL 353
Cdd:PRK08596 387 EEAHSVNEKVEIEQLIE----YTKVITAFI 412
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
2-349 |
1.06e-08 |
|
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: 56.48 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 2 ETEQLYENAVALLRQMIQTPSF---SKEEA----GTAGLLAEFLQ---ERGVEVHRKKNNVWAFNrhYDPAKPTILLNSH 71
Cdd:cd03888 2 EIDKYKDEILEDLKELVAIPSVrdeATEGApfgeGPRKALDKFLDlakRLGFKTKNIDNYAGYAE--YGEGEEVLGILGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 72 HDTVKPNGAYTRDPFAATVEGDRLYGLGSND-AGASGVSLLA-------------------------------------- 112
Cdd:cd03888 80 LDVVPAGEGWTTDPFKPVIKDGKLYGRGTIDdKGPTIAALYAlkilkdlglplkkkirlifgtdeetgwkciehyfehee 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 113 ----AF-------------------LHFYDRKDLKYNLCVAITAEEENSGHDGLECVIPELGPLEFAIVGEPTLMQLAIA 169
Cdd:cd03888 160 ypdfGFtpdaefpvingekgivtvdLTFKIDDDKGYRLISIKGGEATNMVPDKAEAVIPGKDKEELALSAATDLKGNIEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 170 ERGLMVIdcTAHGKAGHAAR-EEGDNAI---YKAMQDIE---------------WFRTYRFPKV-----SDLFGAVKMSV 225
Cdd:cd03888 240 DDGGVEL--TVTGKSAHASApEKGVNAItllAKFLAELNkdgndkdfikflaknLHEDYNGKKLginfeDEVMGELTLNP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 226 TIIsagtqhNVVPAECRFTVDIRVTDRYTNEEVLEIIKE-----HVSCEvkaRSTRLRPSSIRPDHPIVQA--------- 291
Cdd:cd03888 318 GII------TLDDGKLELGLNVRYPVGTSAEDIIKQIEEalekyGVEVE---GHKHQKPLYVPKDSPLVKTllkvyeeqt 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 292 -----GLALGRTTYGSpttsdqalldipSLKLGV-------GDSARSHSADEFVHLSEIREGIELYIKML 349
Cdd:cd03888 389 gkegePVAIGGGTYAR------------ELPNGVafgpefpGQKDTMHQANEFIPIDDLIKALAIYAEAI 446
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
11-352 |
1.18e-08 |
|
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: 56.16 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRqmiqTPSFSKEEAGTAGLL--AEFLQERGVEVHRKKNNVWAFNRH--------YDPAKPTILLNSHHDT--VKPN 78
Cdd:cd05680 5 FELLR----IPSVSADPAHKGDVRraAEWLADKLTEAGFEHTEVLPTGGHplvyaewlGAPGAPTVLVYGHYDVqpPDPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 79 GAYTRDPFAATVEGDRLYGLG-SNDAGASGVSLLAAFLHFYDRKDLKYNLCVAITAEEEnSGHDGLECVIPELGPLEFA- 156
Cdd:cd05680 81 ELWTSPPFEPVVRDGRLYARGaSDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEE-IGSPSLPAFLEENAERLAAd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 157 -IVGEPTLM------QLAIAERGLMVIDCTAHG--KAGHAAREEG--DNAIY------KAMQD------IEWF------- 206
Cdd:cd05680 160 vVLVSDTSMwspdtpTITYGLRGLAYLEISVTGpnRDLHSGSYGGavPNPANalarllASLHDedgrvaIPGFyddvrpl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 207 ------RTYRFP----------KVSDLFGAVKMS------------VTIISAGTQ----HNVVPAECRFTVDIRVTDRYT 254
Cdd:cd05680 240 tdaereAWAALPfdeaafkaslGVPALGGEAGYTtlerlwarptldVNGIWGGYQgegsKTVIPSKAHAKISMRLVPGQD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 255 NEEVLEIIKEH--------VSCEVKaRSTRLRPSSIRPDHPIVQ-AGLALGRtTYGSP------------TTSDQALLDI 313
Cdd:cd05680 320 PDAIADLLEAHlrahappgVTLSVK-PLHGGRPYLVPTDHPALQaAERALEE-AFGKPpvfvreggsipiVALFEKVLGI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1772516668 314 PSLKLGVG-DSARSHSADEFVHLSEIREGIELYIKMLSAI 352
Cdd:cd05680 398 PTVLMGFGlPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
16-338 |
2.11e-08 |
|
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: 55.15 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 16 QMIQTPSFSKEEAGTAGLLAEFLQERGVEV----HRKK-----NNVWAFNRHYDPAKPTILLNSHHDTVKPnGAYTRDPf 86
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVieddAGKTtgggaGNLICTLKADKEEVPKILFTSHMDTVTP-GINVKPP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 87 aaTVEGDRLYGLGSNDAGA---SGVSLLAAFLHFYDRKDLKY-NLCVAITAEEEnSGHDGLECVIPELGPLE--FAIVGE 160
Cdd:cd05683 89 --QIADGYIYSDGTTILGAddkAGIAAILEAIRVIKEKNIPHgQIQFVITVGEE-SGLVGAKALDPELIDADygYALDSE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 161 PTLMQLAIAERGLMVIDCTAHGKAGHA--AREEGDNAIYKAMQDIEWFRTYRFPKVSdlfgavKMSVTIISAGTQHNVVP 238
Cdd:cd05683 166 GDVGTIIVGAPTQDKINAKIYGKTAHAgtSPEKGISAINIAAKAISNMKLGRIDEET------TANIGKFQGGTATNIVT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 239 ------AECRFTVDIRVTDRYTN-EEVLE--IIKEHVSCEVKArSTRLRPSSIRPDHPIVQ----AGLALGRT--TYGSP 303
Cdd:cd05683 240 devnieAEARSLDEEKLDAQVKHmKETFEttAKEKGAHAEVEV-ETSYPGFKINEDEEVVKlakrAANNLGLEinTTYSG 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 1772516668 304 TTSDQALLD---IPSLKLGVGdSARSHSADEFVHLSEI 338
Cdd:cd05683 319 GGSDANIINglgIPTVNLGIG-YENIHTTNERIPIEDL 355
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
62-340 |
2.34e-08 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 55.35 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 62 AKPTILLNSHHDTVKPNGAytrdPFAA--TVEGDRLYGLGSNDAGASGVSLLAAFLHFyDRKDLKYNLC--VAITAEEEn 137
Cdd:PRK07338 91 APRQVLLTGHMDTVFPADH----PFQTlsWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSPLADKLGydVLINPDEE- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 138 SGHDGLECVIPELGP-LEFAIVGEPTLMQ--LAIAERGLMVIDCTAHGKAGHAAR--EEGDNAIYKAMQDIEwfrtyRFP 212
Cdd:PRK07338 165 IGSPASAPLLAELARgKHAALTYEPALPDgtLAGARKGSGNFTIVVTGRAAHAGRafDEGRNAIVAAAELAL-----ALH 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 213 KVSDLFGAVKMSVTIISAGTQHNVVPAECRFTVDIRVTD----RYTNEEVLEIIKE-----HVSCEVKARSTR----LRP 279
Cdd:PRK07338 240 ALNGQRDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTpedaAWAEAELKKLIAQvnqrhGVSLHLHGGFGRppkpIDA 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1772516668 280 SSIRPDHPIVQAGLALGRTTYGSPT--TSDQALL---DIPSLK-LGVgDSARSHSADEFVHLSEIRE 340
Cdd:PRK07338 320 AQQRLFEAVQACGAALGLTIDWKDSggVCDGNNLaaaGLPVVDtLGV-RGGNIHSEDEFVILDSLVE 385
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
15-264 |
9.02e-08 |
|
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: 53.12 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 15 RQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHR---KKNNVWAfNRHYDPAKPTILLNSHHDTVkPNGAYTRDPFAATVE 91
Cdd:TIGR01891 6 RHLHEHPELSFEEFKTSSLIAEALESLGIEVRRgvgGATGVVA-TIGGGKPGPVVALRADMDAL-PIQEQTDLPYKSTNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 92 GdRLYGLGSNDAGASGvsLLAAFLhfydRKDLKYNLCVAIT-----AEE---------ENSGHDGLECVIpELGPLEFAI 157
Cdd:TIGR01891 84 G-VMHACGHDLHTAIL--LGTAKL----LKKLADLLEGTVRlifqpAEEggggatkmiEDGVLDDVDAIL-GLHPDPSIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 158 VGeptlmQLAIAERGLM----VIDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPKVSDLFGAVkMSVTIISAGT 232
Cdd:TIGR01891 156 AG-----TVGLRPGTIMaaadKFEVTIHGKGAHAARpHLGRDALDAAAQLVVALQQIVSRNVDPSRPAV-VSVGIIEAGG 229
|
250 260 270
....*....|....*....|....*....|..
gi 1772516668 233 QHNVVPAECRFTVDIRVTDRYTNEEVLEIIKE 264
Cdd:TIGR01891 230 APNVIPDKASMSGTVRSLDPEVRDQIIDRIER 261
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
60-162 |
1.51e-07 |
|
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: 51.27 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 60 DPAKPTILLNSHHDTVKPNGAYTRDPFAA--TVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRK-DLKYNLCVAITAEEE 136
Cdd:cd03873 9 GEGGKSVALGAHLDVVPAGEGDNRDPPFAedTEEEGRLYGRGALDDKGGVAAALEALKRLKENGfKPKGTIVVAFTADEE 88
|
90 100 110
....*....|....*....|....*....|
gi 1772516668 137 NSGHDG----LECVIPELGPLEFAIVGEPT 162
Cdd:cd03873 89 VGSGGGkgllSKFLLAEDLKVDAAFVIDAT 118
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
179-264 |
1.91e-07 |
|
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: 52.22 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 179 TAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYrFPKVSDLFGAVKMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEE 257
Cdd:cd03886 177 TVKGKGGHGASpHLGVDPIVAAAQIVLALQTV-VSRELDPLEPAVVTVGKFHAGTAFNVIPDTAVLEGTIRTFDPEVREA 255
|
....*..
gi 1772516668 258 VLEIIKE 264
Cdd:cd03886 256 LEARIKR 262
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
21-139 |
2.35e-07 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 52.08 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 21 PSFSKEEAGTAGLLAEFLQERGVevhrkknnvWAFNRHYDPAKPTILLNSHHDTVKPN-GAYTRDPFAATVEGDRLYGLG 99
Cdd:PRK08554 30 PKFIKDTLESWGIESELIEKDGY---------YAVYGEIGEGKPKLLFMAHFDVVPVNpEEWNTEPFKLTVKGDKAYGRG 100
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1772516668 100 SNDAGASGVSLLAAfLHFYDRKDLKYNLCVAITAEEENSG 139
Cdd:PRK08554 101 SADDKGNVASVMLA-LKELSKEPLNGKVIFAFTGDEEIGG 139
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
181-266 |
3.05e-07 |
|
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: 51.66 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 181 HGKAGHAAR-EEGDNAIY------KAMQDIewfrtyrfpkVS---DLFGAVKMSVTIISAGTQHNVVPAECRFTVDIRVT 250
Cdd:COG1473 191 KGKGGHAAApHLGIDPIVaaaqivTALQTI----------VSrnvDPLDPAVVTVGIIHGGTAPNVIPDEAELEGTVRTF 260
|
90
....*....|....*.
gi 1772516668 251 DRYTNEEVLEIIKEHV 266
Cdd:COG1473 261 DPEVRELLEERIERIA 276
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
21-349 |
2.66e-06 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 48.61 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 21 PSFSKEEAGTAGLLAEFLQERGVEVHRKKN-NVWAFNRHYDPAKPTILLNSHHDTVkPN-GAY----------------- 81
Cdd:PRK09290 30 LALSPEDLQARDLFAEWMEAAGLTVRVDAVgNLFGRLEGRDPDAPAVLTGSHLDTV-PNgGRFdgplgvlagleavrtln 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 82 -----TRDPFAATV----EGDRlYG---LGSndAGASGVSLLAAFLhfyDRKDLKynlcvAITAEE--ENSGHDGLECVI 147
Cdd:PRK09290 109 ergirPRRPIEVVAftneEGSR-FGpamLGS--RVFTGALTPEDAL---ALRDAD-----GVSFAEalAAIGYDGDEAVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 148 PELGP------LEFAIVGEPTL----MQLAIAE--RGLMVIDCTAHGKAGHA---AREEGDNAIY---KAMQDIEwfRTY 209
Cdd:PRK09290 178 AARARrdikafVELHIEQGPVLeaegLPIGVVTgiVGQRRYRVTFTGEANHAgttPMALRRDALLaaaEIILAVE--RIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 210 RfPKVSDLFGAV-KMSVtiiSAGTqHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVSCEVKARSTRL---RPSSIRP- 284
Cdd:PRK09290 256 A-AHGPDLVATVgRLEV---KPNS-VNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVeieLISRRPPv 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 285 --DHPIV----QAGLALGRTTY---------------GSPTtsdqALLDIPSlKLGVgdsarSHSADEFVHLSEIREGIE 343
Cdd:PRK09290 331 pfDPGLVaaleEAAERLGLSYRrlpsgaghdaqilaaVVPT----AMIFVPS-VGGI-----SHNPAEFTSPEDCAAGAN 400
|
....*.
gi 1772516668 344 LYIKML 349
Cdd:PRK09290 401 VLLHAL 406
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-143 |
7.06e-06 |
|
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: 349928 [Multi-domain] Cd Length: 448 Bit Score: 47.49 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 12 ALLRQMIQTPSFSKEEAGTAGL---LAEFLQER----GVEVHRKKNNVWA------FNRHYDPAKPTILLNSHHDTVKPN 78
Cdd:cd05679 8 AELARRVAVPTESQEPARKPELrayLDQEMRPRferlGFTVHIHDNPVAGrapfliAERIEDPSLPTLLIYGHGDVVPGY 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 79 GAYTR---DPFAATVEGDRLYGLGSNDAGASGVSLLAAFLHFYDRKD--LKYNLCVAITAEEEnSGHDGL 143
Cdd:cd05679 88 EGRWRdgrDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEARGgkLGFNVKFLIEMGEE-MGSPGL 156
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
21-81 |
9.63e-06 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 47.21 E-value: 9.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1772516668 21 PSFSKEEAGTAGLLAEFLQERGVEVHRKK-NNVWAFNRHYDPAKPTILLNSHHDTVKPNGAY 81
Cdd:PRK12890 31 LALSDEERAARALLAAWMRAAGLEVRRDAaGNLFGRLPGRDPDLPPLMTGSHLDTVPNGGRY 92
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
14-352 |
2.13e-05 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 45.89 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 14 LRQMIQTPSFS-----KEE-AGTAGLLAEFLQERG---VEVHRKKNN--VWAfNRHYDPAKPTILLNSHHDT--VKPNGA 80
Cdd:PRK08201 20 LKEFLRIPSISalsehKEDvRKAAEWLAGALEKAGlehVEIMETAGHpiVYA-DWLHAPGKPTVLIYGHYDVqpVDPLNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 81 YTRDPFAATVEGDRLYGLG-SNDAGASGVSLLAAFLHFYDRKDLKYNLCVAITAEEENSGHDGLECVIPELGPLEFAIV- 158
Cdd:PRK08201 99 WETPPFEPTIRDGKLYARGaSDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIGSPNLDSFVEEEKDKLAADVVl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 159 ---------GEPTlmqLAIAERGLMVIDCTAHGKAG---------------HAA--------REEGDNAI---YKAMQDI 203
Cdd:PRK08201 179 isdttllgpGKPA---ICYGLRGLAALEIDVRGAKGdlhsglyggavpnalHALvqllaslhDEHGTVAVegfYDGVRPL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 204 -----EWFRTYRFPK--------VSDLFG-----AVK-------MSVTIISAGTQ----HNVVPAECRFTVDIRVTDRYT 254
Cdd:PRK08201 256 tpeerEEFAALGFDEeklkrelgVDELFGeegytALErtwarptLELNGVYGGFQgegtKTVIPAEAHAKITCRLVPDQD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 255 NEEVLEIIKEHVSCEVKA-------RSTRLRPSSIRPDHPIVQAGLALGRTTYGSPT--TSD----------QALLDIPS 315
Cdd:PRK08201 336 PQEILDLIEAHLQAHTPAgvrvtirRFDKGPAFVAPIDHPAIQAAARAYEAVYGTEAafTRMggsipvvetfSSQLHIPI 415
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1772516668 316 LKLGVG-DSARSHSADEFVHLSEIREGIEL---YIKMLSAI 352
Cdd:PRK08201 416 VLMGFGlPSENFHAPNEHFHLENFDKGLRTlveYWHQLAEG 456
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
57-102 |
4.12e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 45.29 E-value: 4.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1772516668 57 RHYDPAKPTILLNSHHDTVkpNGAYTR-----DPFAATVEGDRLYGLGSND 102
Cdd:PRK07079 79 RIEDDALPTVLIYGHGDVV--RGYDEQwreglSPWTLTEEGDRWYGRGTAD 127
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
3-267 |
7.92e-05 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 44.19 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 3 TEQLYENAVALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHR--KKNNVWAFNRHYDPAKpTILLNSHHDTVkPNGA 80
Cdd:cd08021 5 VDQLEDEMIQWRRHIHQYPELSFEEFETAAYIANELKKLGLEVETnvGGTGVVATLKGGKPGK-TVALRADMDAL-PIEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 81 YTRDPFAATVEGdRLYGLGsNDAGASgVSLLAAFLHFYDRKDLKYNlcVAIT---AEEENSGhdGLECVIpELGPLE--- 154
Cdd:cd08021 83 ETDLPFKSKNPG-VMHACG-HDGHTA-MLLGAAKVLAENKDEIKGT--VRFIfqpAEEVPPG--GAKPMI-EAGVLEgvd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 155 --FAI---VGEPTlMQLAIAERGLMV----IDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPKVSDLFGAVkMS 224
Cdd:cd08021 155 avFGLhlwSTLPT-GTIAVRPGAIMAapdeFDITIKGKGGHGSMpHETVDPIVIAAQIVTALQTIVSRRVDPLDPAV-VT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1772516668 225 VTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVS 267
Cdd:cd08021 233 IGTFQGGTSFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVK 275
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
11-264 |
9.89e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; 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).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 43.67 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 11 VALLRQMIQTPSFSKEEAGTAGLLAEFLQERGVEVHRK--KNNVWAFNRHYDPAKpTILLNSHHDTVkPNGAYTRDPFAA 88
Cdd:cd05666 4 TAWRRDLHAHPELGFEEHRTSALVAEKLREWGIEVHRGigGTGVVGVLRGGDGGR-AIGLRADMDAL-PIQEATGLPYAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 89 TVEGdRLYGLGSNDAGASgvsLLAAFLHFYDRKDLKYNLCVAITAEEENSG------HDGL------ECV-----IPELG 151
Cdd:cd05666 82 THPG-KMHACGHDGHTTM---LLGAARYLAETRNFDGTVHFIFQPAEEGGGgakamiEDGLferfpcDAVyglhnMPGLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 152 PLEFAIVGEPtlmQLAIAERglmvIDCTAHGKAGHAAREEGDN-------AIYKAMQDIewfrtyrfpkVS---DLFGAV 221
Cdd:cd05666 158 AGKFAVRPGP---MMASADT----FEITIRGKGGHAAMPHLGVdpivaaaQLVQALQTI----------VSrnvDPLDAA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1772516668 222 KMSVTIISAGTQHNVVPAecrfTVDIRVTDRYTNEEVLEIIKE 264
Cdd:cd05666 221 VVSVTQIHAGDAYNVIPD----TAELRGTVRAFDPEVRDLIEE 259
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
58-242 |
2.73e-04 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 42.46 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 58 HYDPAKPTILLNSHHDTVKPNGAYTRDPFaaTVEGDRLYGLGSNDAGASGVSLLAAFLHFyDRKDLKYNLCVAI--TAEE 135
Cdd:PRK07473 70 HPRQGEPGILIAGHMDTVHPVGTLEKLPW--RREGNKCYGPGILDMKGGNYLALEAIRQL-ARAGITTPLPITVlfTPDE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 136 ENSGHDGLECVIPELGPLEFAIVGEP-------TLMQLAIAERGLmvidcTAHGKAGHA-AR-EEGDNAIyKAMqdiewf 206
Cdd:PRK07473 147 EVGTPSTRDLIEAEAARNKYVLVPEPgrpdngvVTGRYAIARFNL-----EATGRPSHAgATlSEGRSAI-REM------ 214
|
170 180 190
....*....|....*....|....*....|....*..
gi 1772516668 207 rTYRFPKVSDLFGA-VKMSVTIISAGTQHNVVPAECR 242
Cdd:PRK07473 215 -ARQILAIDAMTTEdCTFSVGIVHGGQWVNCVATTCT 250
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
60-164 |
3.10e-04 |
|
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 dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 42.32 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 60 DPAKPTILLNSHHDTVKPNGAYTRD--PFAATVEGDRLYGLGSNDAGASGVSLLAAfLHFYDRKDLKYNLCVAITAEEEN 137
Cdd:cd05682 70 EQDDDTVLLYGHMDKQPPFTGWDEGlgPTKPVIRGDKLYGRGGADDGYAIFASLTA-IKALQEQGIPHPRCVVLIEACEE 148
|
90 100
....*....|....*....|....*..
gi 1772516668 138 SGHDGLECVIPELGPLefaiVGEPTLM 164
Cdd:cd05682 149 SGSADLPFYLDKLKER----IGNVDLV 171
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
21-81 |
3.47e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 38.92 E-value: 3.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1772516668 21 PSFSKEEAGTAGLLAEFLQERGVEVHRKK-NNVWAFNRHYDPaKPTILLNSHHDTVKPNGAY 81
Cdd:PRK12892 32 PTYSDAHVAARRRLAAWCEAAGLAVRIDGiGNVFGRLPGPGP-GPALLVGSHLDSQNLGGRY 92
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
181-260 |
3.59e-03 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. 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 in 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.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 38.81 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 181 HGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPKVSDLFGAVkMSVTIISAGTQHNVVPAECRFTVDIRVTDRYTNEEVL 259
Cdd:cd05669 180 AGKGAHAAKpENGVDPIVAASQIINALQTIVSRNISPLESAV-VSVTRIHAGNTWNVIPDSAELEGTVRTFDAEVRQLVK 258
|
.
gi 1772516668 260 E 260
Cdd:cd05669 259 E 259
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
234-343 |
4.62e-03 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 38.66 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 234 HNVVPAECRFTVDIRVTDRYTNEEVLEIIKEHVS-------CEVKARSTRLRPSSirPDHPIVQAGL--ALGRTTYGSPT 304
Cdd:cd03884 267 VNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEaiaaergVEVEVERLWDSPPV--PFDPELVAALeaAAEALGLSYRR 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1772516668 305 -TS-------------DQALLDIPSlKLGVgdsarSHSADEFVHLSEIREGIE 343
Cdd:cd03884 345 mPSgaghdamfmaricPTAMIFVPS-RDGI-----SHNPAEYTSPEDLAAGVQ 391
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
176-266 |
6.26e-03 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. 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 in 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.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 38.01 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516668 176 IDCTAHGKAGHAAR-EEGDNAIYKAMQDIEWFRTYRFPKVSDLFGAVkmsVTI--ISAGTQHNVVPAECRFTVDIRVTDr 252
Cdd:cd05670 175 LHIDFIGKSGHAAYpHNANDMVVAAANFVTQLQTIVSRNVDPIDGAV---VTIgkIHAGTARNVIAGTAHLEGTIRTLT- 250
|
90
....*....|....
gi 1772516668 253 ytnEEVLEIIKEHV 266
Cdd:cd05670 251 ---QEMMELVKQRV 261
|
|
| |
