|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
1-380 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 528.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 1 MISDHALSLAQALVRMNTVSHRSNLELIDFVRTELARLGVKCRLTHDASKTKANLFATLGEGKPAGIILSGHTDTVPWDG 80
Cdd:PRK07522 1 MASMSSLDILERLVAFDTVSRDSNLALIEWVRDYLAAHGVESELIPDPEGDKANLFATIGPADRGGIVLSGHTDVVPVDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 81 QDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRDAGVRPLAC 160
Cdd:PRK07522 81 QAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARLPERGVKPAGC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 161 IVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFEREEARFDGFDVPFSTASVGQF 240
Cdd:PRK07522 161 IVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFDALFDPPYSTLQTGTI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 241 HGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARS-LEPAMQAVSPRAGFTFEPICEIPSFLGSAGDPVTRLAQR 319
Cdd:PRK07522 241 QGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAeLLPEMRAVHPEAAIEFEPLSAYPGLDTAEDAAAARLVRA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 320 LAGEAGTTLVAFGTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGLAD 380
Cdd:PRK07522 321 LTGDNDLRKVAYGTEAGLFQRAGIPTVVCGPGSIEQAHKPDEFVELAQLAACEAFLRRLLA 381
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
12-380 |
2.44e-170 |
|
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: 480.17 E-value: 2.44e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 12 ALVRMNTVSHRSNLELIDFVRTELARLGVKCRLTHDASKTKANLFATLGEGKPAGIILSGHTDTVPWDGQDWSVDPLSST 91
Cdd:cd03894 5 RLVAFDTVSRNSNLALIEYVADYLAALGVKSRRVPVPEGGKANLLATLGPGGEGGLLLSGHTDVVPVDGQKWSSDPFTLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 92 VRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRDAGVRPLACIVGEPTNMVPA 171
Cdd:cd03894 85 ERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAARGGRPDAAIVGEPTSLQPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 172 IAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFEREEARfDGFDVPFSTASVGQFHGGIADNVVPR 251
Cdd:cd03894 165 VAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRD-PPFDPPYPTLNVGLIHGGNAVNIVPA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 252 DAEFRYEFRDLPTADAARMQAEVVAYARSLEpamqaVSPRAGFTFEPICEIPSFLGSAGDPVTRLAQRLAGEAGTTLVAF 331
Cdd:cd03894 244 ECEFEFEFRPLPGEDPEAIDARLRDYAEALL-----EFPEAGIEVEPLFEVPGLETDEDAPLVRLAAALAGDNKVRTVAY 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1421773316 332 GTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGLAD 380
Cdd:cd03894 319 GTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
12-378 |
2.49e-108 |
|
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: 322.54 E-value: 2.49e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 12 ALVRMNTVSHRSNLELIDFVRTELARLGVKC-RLTHDASKTKANLFATLGEGKPAGIILSGHTDTVPWDGQDWSVDPLSS 90
Cdd:TIGR01892 5 KLVAFDSTSFRPNVDLIDWAQAYLEALGFSVeVQPFPDGAEKSNLVAVIGPSGAGGLALSGHTDVVPYDDAAWTRDPFRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 91 TVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIAdlRDAGvRPLACIVGEPTNMVP 170
Cdd:TIGR01892 85 TEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIE--AGAG-RPRHAIIGEPTRLIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 171 AIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFEREEArFDGFDVPFSTASVGQFHGGIADNVVP 250
Cdd:TIGR01892 162 VRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDL-DEGFTPPYTTLNIGVIQGGKAVNIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 251 RDAEFRYEFRDLPTADAARMQAEVvayaRSLEPAMQAVSPRAGFTFEPICEIPSFLGSAGDPVTRLAQRLAGEAgTTLVA 330
Cdd:TIGR01892 241 GACEFVFEWRPIPGMDPEELLQLL----ETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNA-PEVVS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1421773316 331 FGTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGL 378
Cdd:TIGR01892 316 YGTEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARL 363
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
4-380 |
5.45e-101 |
|
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: 304.50 E-value: 5.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 4 DHALSLAQALVRMNTVSHrSNLELIDFVRTELARLGVKCRLtHDASKTKANLFATL-GEGKPAGIILSGHTDTVPWDGQD 82
Cdd:COG0624 12 DEALELLRELVRIPSVSG-EEAAAAELLAELLEALGFEVER-LEVPPGRPNLVARRpGDGGGPTLLLYGHLDVVPPGDLE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 83 -WSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDA--PFAIHYAFSYDEEVGCFGARELIADLRDaGVRPLA 159
Cdd:COG0624 90 lWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLrlPGNVTLLFTGDEEVGSPGARALVEELAE-GLKADA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 160 CIVGEPTN-MVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFEREEArfdgfdVPFSTASVG 238
Cdd:COG0624 169 AIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRADPL------FGRTTLNVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 239 QFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYarslepaMQAVSPRAGFTFEPI-CEIPSFLGSAGDPVTRLA 317
Cdd:COG0624 243 GIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRAL-------LAAAAPGVEVEVEVLgDGRPPFETPPDSPLVAAA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1421773316 318 QRLAGEAG-----TTLVAFGTEAGLFKN-AGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGLAD 380
Cdd:COG0624 316 RAAIREVTgkepvLSGVGGGTDARFFAEaLGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLE 384
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
23-378 |
1.04e-76 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 242.04 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 23 SNLELIDFVRTELARLGVKCRLTH-DASKTKANLFATLGEGkPAGIILSGHTDTVPWDGQDWSVDPLSSTVRDGRLYGRG 101
Cdd:PRK05111 30 SNRAVIDLLAGWFEDLGFNVEIQPvPGTRGKFNLLASLGSG-EGGLLLAGHTDTVPFDEGRWTRDPFTLTEHDGKLYGLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 102 SADMKAFIAIALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIAdlrDAGVRPLACIVGEPTNMVPAIAHKGVYRYR 181
Cdd:PRK05111 109 TADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAE---ATAIRPDCAIIGEPTSLKPVRAHKGHMSEA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 182 CCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFeREEARFDGFDVPFSTASVGQFHGGIADNVVPRDAEFRYEFRD 261
Cdd:PRK05111 186 IRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDEL-QERYHNPAFTVPYPTLNLGHIHGGDAPNRICGCCELHFDIRP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 262 LPTADAARMQAEVvayARSLEPAMQAVSPRAGFT--FEPiceIPSFLGSAGDPVTRLAQRLAGEAGTTlVAFGTEAGLFK 339
Cdd:PRK05111 265 LPGMTLEDLRGLL---REALAPVSERWPGRITVAplHPP---IPGYECPADHQLVRVVEKLLGHKAEV-VNYCTEAPFIQ 337
|
330 340 350
....*....|....*....|....*....|....*....
gi 1421773316 340 NAGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGL 378
Cdd:PRK05111 338 QLGCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQL 376
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
8-379 |
2.78e-74 |
|
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: 234.89 E-value: 2.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 8 SLAQALVRMNTVShRSNLELIDFVRTELARLGVKCRLTHDasKTKANLFATLGEGKPAGIILSGHTDTVP-WDGQDWSVD 86
Cdd:cd08659 1 SLLQDLVQIPSVN-PPEAEVAEYLAELLAKRGYGIESTIV--EGRGNLVATVGGGDGPVLLLNGHIDTVPpGDGDKWSFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 87 PLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFA--IHYAFSYDEEVGCFGARELIADLRDAgvRPLACIVGE 164
Cdd:cd08659 78 PFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGgrVALLATVDEEVGSDGARALLEAGYAD--RLDALIVGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 165 PTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDmaegFEREEARFDgfDVPFSTASVGQFHGGI 244
Cdd:cd08659 156 PTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRT----LFEELPAHP--LLGPPTLNVGVINGGT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 245 ADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEpamqavsprAGFTFEPICEIPSFLGSAGD-PVTRLAQRLAGE 323
Cdd:cd08659 230 QVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHE---------AKLTVEVSLDGDPPFFTDPDhPLVQALQAAARA 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 324 AGTTLVAFG----TEAGLF-KNAGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGLA 379
Cdd:cd08659 301 LGGDPVVRPftgtTDASYFaKDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
68-379 |
7.62e-55 |
|
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: 183.32 E-value: 7.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 68 ILSGHTDTVPwDGQDWSVdPLSSTVrDGRLYGRGSADMKAFIAIALSQAQRFLESDA-PFAIHYAFSYDEEVGCFGAREL 146
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGW-PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLkKGTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 147 IADLRDAGVRPLACI---VGEPTNMV------PAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAeg 217
Cdd:pfam01546 78 IEDGLLEREKVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIV-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 218 fEREEARFDGfdVPFSTASVGQFHGGIadNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMqavspRAGFTFE 297
Cdd:pfam01546 156 -SRNVDPLDP--AVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAY-----GVKVEVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 298 PICEIPSFLgSAGDPVTRLAQRLAGEAG-------TTLVAFGTEAGLFKNAGISTVV-CGPGSiQQAHQPDEYVSLEQLA 369
Cdd:pfam01546 226 YVEGGAPPL-VNDSPLVAALREAAKELFglkveliVSGSMGGTDAAFFLLGVPPTVVfFGPGS-GLAHSPNEYVDLDDLE 303
|
330
....*....|
gi 1421773316 370 RCEAFMRGLA 379
Cdd:pfam01546 304 KGAKVLARLL 313
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-368 |
9.96e-52 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 177.49 E-value: 9.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 1 MISDHALSLAQALVRMNTV-SHRSNL-ELIDFVRTELARLGVKCRLtHDASKTKAN--------LFATLGEGKPAgIILS 70
Cdd:PRK08651 3 AMMFDIVEFLKDLIKIPTVnPPGENYeEIAEFLRDTLEELGFSTEI-IEVPNEYVKkhdgprpnLIARRGSGNPH-LHFN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 71 GHTDTVPWDGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLE-SDAPFAIhyAFSYDEEVGCFGARELiad 149
Cdd:PRK08651 81 GHYDVVPPGEGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPaGDGNIEL--AIVPDEETGGTGTGYL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 150 LRDAGVRPLACIVGEPTNMV-PAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGR----VRDMAEGFEREEAR 224
Cdd:PRK08651 156 VEEGKVTPDYVIVGEPSGLDnICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERlkssLSTIKSKYEYDDER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 225 FDGFDVPFSTASVgqfHGGIADNVVPRDAEFRYEFRDLP--TADAARmqaevvayaRSLEPAMQAVSPRAGFTFEpICEI 302
Cdd:PRK08651 236 GAKPTVTLGGPTV---EGGTKTNIVPGYCAFSIDRRLIPeeTAEEVR---------DELEALLDEVAPELGIEVE-FEIT 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421773316 303 PSFLGSAGDPVTRLAQRLA--------GEAGTTLVAFGTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQL 368
Cdd:PRK08651 303 PFSEAFVTDPDSELVKALReairevlgVEPKKTISLGGTDARFFGAKGIPTVVYGPGELELAHAPDEYVEVKDV 376
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
7-368 |
1.27e-48 |
|
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: 168.73 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 7 LSLAQALVRMNTVSH--RSNLELIDFVRTELARLGVKCRLTH----DASKTKANLFATLGEGKPAGIILSGHTDTVP-WD 79
Cdd:TIGR01910 1 VELLKDLISIPSVNPpgGNEETIANYIKDLLREFGFSTDVIEitddRLKVLGKVVVKEPGNGNEKSLIFNGHYDVVPaGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 80 GQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAP--FAIHYAFSYDEEVGCFGARELIAdlRDAGVRP 157
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKpnGNIILQSVVDEESGEAGTLYLLQ--RGYFKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 158 LACIVGEPTN-MVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEG-FEREEARFDGFDVPFSTA 235
Cdd:TIGR01910 159 DGVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHiYARNSYGFIPGPITFNPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 236 SVgqfHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPamqavSPRAGFTFEPICEI--PSFLGSAGDPV 313
Cdd:TIGR01910 239 VI---KGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSK-----SDGWLYENEPVVKWsgPNETPPDSRLV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1421773316 314 TRL---AQRLAGEAGTTLV-AFGTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQL 368
Cdd:TIGR01910 311 KALeaiIKKVRGIEPEVLVsTGGTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNL 369
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-372 |
4.04e-44 |
|
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: 156.39 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 7 LSLAQALVRMNTVS--HRSNLELIDFVRTELARLGVKCRLtHDASKTKANLFATLGEGKPAG-IILSGHTDTVP-WDGQD 82
Cdd:cd08011 1 VKLLQELVQIPSPNppGDNTSAIAAYIKLLLEDLGYPVEL-HEPPEEIYGVVSNIVGGRKGKrLLFNGHYDVVPaGDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 83 WSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFA--IHYAFSYDEE-VGCFGARELIADLRdagVRPLA 159
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDlpVVLTFVPDEEtGGRAGTKYLLEKVR---IKPND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 160 CIVGEPTNM-VPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDmaegferEEArfdgfdvpfsTASVG 238
Cdd:cd08011 157 VLIGEPSGSdNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYE-------LEK----------TVNPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 239 QFHGGIADNVVPRDAEFRYEFRDLPTADAarmqAEVVAYARSLEPAMQAVSPRagftfepICEIPSFLGSAGD-PVTRLA 317
Cdd:cd08011 220 VIKGGVKVNLVPDYCEFSVDIRLPPGIST----DEVLSRIIDHLDSIEEVSFE-------IKSFYSPTVSNPDsEIVKKT 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 318 QRLAGE-----AGTTLVAFGTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLARCE 372
Cdd:cd08011 289 EEAITEvlgirPKEVISVGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVI 348
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-366 |
4.95e-37 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 137.71 E-value: 4.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTVShRSNLELIDFVRTELARLGVKCRLtHDASKTKANLFATLGEGKPAgIILSGHTDTV-PWDGQDWS 84
Cdd:PRK08588 4 KIQILADIVKINSVN-DNEIEVANYLQDLFAKHGIESKI-VKVNDGRANLVAEIGSGSPV-LALSGHMDVVaAGDVDKWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 85 VDPLSSTVRDGRLYGRGSADMK---AFIAIALSQAQrflESDAPFAIHYAF--SYDEEVGCFGAREL----IADLRDagv 155
Cdd:PRK08588 81 YDPFELTEKDGKLYGRGATDMKsglAALVIAMIELK---EQGQLLNGTIRLlaTAGEEVGELGAKQLtekgYADDLD--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 156 rplACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFEREEARFDGFdvpfsTA 235
Cdd:PRK08588 155 ---ALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNPYLGGL-----TH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 236 SVGQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAmqavsPRAGFTFEPICEIPSFLGSAGDPVTR 315
Cdd:PRK08588 227 VVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQN-----GAAQLSLDIYSNHRPVASDKDSKLVQ 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1421773316 316 LAQRLA-GEAGTTLVAFG----TEAGLF--KNAGISTVVCGPGSIQQAHQPDEYVSLE 366
Cdd:PRK08588 302 LAKDVAkSYVGQDIPLSAipgaTDASSFlkKKPDFPVIIFGPGNNLTAHQVDEYVEKD 359
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
4-384 |
1.53e-35 |
|
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: 133.76 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 4 DHALSLAQALVRMNTvshrSN-----------LELIDFVRTELARLGVKcrlTH--DASKTKANLFATL-GEGKPAGIIL 69
Cdd:cd08013 1 DDPVSLTQTLVRINS----SNpslsatggageAEIATYVAAWLAHRGIE---AHriEGTPGRPSVVGVVrGTGGGKSLML 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 70 SGHTDTVPWDGqdWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIAd 149
Cdd:cd08013 74 NGHIDTVTLDG--YDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 150 lrdAGVRPLACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFEREEArfdgfD 229
Cdd:cd08013 151 ---AGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPERPV-----D 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 230 VPFSTASV--GQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAY---ARSLEPAMQAVSPRAgfTFEPiceiPS 304
Cdd:cd08013 223 PLLGRASVhaSLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAIlgeLAQTVPNFSYREPRI--TLSR----PP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 305 FLGSAGDPVTRL----AQRLAGEAGTTL-VAFGTEAGLFKNAGISTVVCGPgSIQQAHQPDEYVSLEQLARCEAFMRGLa 379
Cdd:cd08013 297 FEVPKEHPFVQLvaahAAKVLGEAPQIRsETFWTDAALLAEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAV- 374
|
....*
gi 1421773316 380 dTRDF 384
Cdd:cd08013 375 -VREF 378
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
11-381 |
2.00e-35 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 133.40 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 11 QALVRMNTVSHRSNLE---LIDFVRTELARLGVKcrlTHDASKTKANLFATLGEGKpagIILSGHTDTVPwDGQDWSVDP 87
Cdd:PRK08737 13 QALVSFDTRNPPRAITtggIFDYLRAQLPGFQVE---VIDHGAGAVSLYAVRGTPK---YLFNVHLDTVP-DSPHWSADP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 88 LSSTVRDGRLYGRGSADMKAFIAIALSQAQrflESDAPFAihYAFSYDEEvgcFGARELIADLRDAGVRPLACIVGEPTN 167
Cdd:PRK08737 86 HVMRRTDDRVIGLGVCDIKGAAAALLAAAN---AGDGDAA--FLFSSDEE---ANDPRCVAAFLARGIPYEAVLVAEPTM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 168 MVPAIAHKGVYRYRCCVRGKEAHSSLTPH-SVNAIEMAARVVGRVRDMAEGfeREEARFDGfdVPFSTASVGQFHGGIAD 246
Cdd:PRK08737 158 SEAVLAHRGISSVLMRFAGRAGHASGKQDpSASALHQAMRWGGQALDHVES--LAHARFGG--LTGLRFNIGRVEGGIKA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 247 NVVPRDAEFRYEFRDLPTADAARMQAEVVAYArslEPAMQavspragfTFEPICEIPSFlgSAGDPVTRLAQRLA----- 321
Cdd:PRK08737 234 NMIAPAAELRFGFRPLPSMDVDGLLATFAGFA---EPAAA--------TFEETFRGPSL--PSGDIARAEERRLAardva 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1421773316 322 -------GEAgttlVAFGTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLAR-CEAFMRGLADT 381
Cdd:PRK08737 301 daldlpiGNA----VDFWTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQLQRyAESVHRIINDS 364
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
7-370 |
2.35e-33 |
|
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: 127.71 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 7 LSLAQALVRMNTVSHrsNLELIDFV----RTELARLGVKCRLtHDASKTKANLFATLGEGKPAGIILSGHTDTVPWDGqd 82
Cdd:cd03885 2 LDLLERLVNIESGTY--DKEGVDRVaellAEELEALGFTVER-RPLGEFGDHLIATFKGTGGKRVLLIGHMDTVFPEG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 83 wSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESD--APFAIHYAFSYDEEVGCFGARELIADL-RDAGvrplA 159
Cdd:cd03885 77 -TLAFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGgrDYLPITVLLNSDEEIGSPGSRELIEEEaKGAD----Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 160 CIVGEPT----NMVpaIAHKGVYRYRCCVRGKEAHSSLTPHS-VNAIEMAARVVGRVRDMAegfereeARFDGfdvpfST 234
Cdd:cd03885 152 VLVFEPAradgNLV--TARKGIGRFRLTVKGRAAHAGNAPEKgRSAIYELAHQVLALHALT-------DPEKG-----TT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 235 ASVGQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMQAVSPRAGFTFEPICEipsflGSAGDPVT 314
Cdd:cd03885 218 VNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELTGGLNRPPMEE-----TPASRRLL 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 315 RLAQRLAGEAGTTL----VAFGTEAGLFKNAGIsTVVCGPGSI-QQAHQPDEYVSLEQLAR 370
Cdd:cd03885 293 ARAQEIAAELGLTLdweaTGGGSDANFTAALGV-PTLDGLGPVgGGAHTEDEYLELDSLVP 352
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
7-368 |
3.06e-33 |
|
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: 127.24 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 7 LSLAQALVRMNTVSHRSNlELIDFVRTELARLGVKCRLtHDASKTKaNLFATLGEGKPAgIILSGHTDTVP-WDGQDWSV 85
Cdd:cd03891 1 LELAKELIRRPSVTPDDA-GAQDLIAERLKALGFTCER-LEFGGVK-NLWARRGTGGPH-LCFAGHTDVVPpGDLEGWSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 86 DPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAF--SYDEE-VGCFGARELIADLRDAGVRPLACIV 162
Cdd:cd03891 77 DPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFliTSDEEgPAIDGTKKVLEWLKARGEKIDYCIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 163 GEPTN------MVpAIAHKGVYRYRCCVRGKEAHSSLtPH-SVNAIEMAARVVGRV--RDMAEGFEreearfdgfDVPFS 233
Cdd:cd03891 157 GEPTSekklgdTI-KIGRRGSLNGKLTIKGKQGHVAY-PHlADNPIHLLAPILAELtaTVLDEGNE---------FFPPS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 234 TASVGQFHGGI-ADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAmqavspragFTFEPICEIPSFLGSAGDP 312
Cdd:cd03891 226 SLQITNIDVGNgATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLD---------YDLEWKLSGEPFLTKPGKL 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 313 VTRLAQRLAGEAGTTLV---AFGT-EAGLFKNAGISTVVCGPGSiQQAHQPDEYVSLEQL 368
Cdd:cd03891 297 VDAVSAAIKEVTGITPElstSGGTsDARFIASYGCPVVEFGLVN-ATIHKVNERVSVADL 355
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
54-368 |
9.05e-33 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 126.65 E-value: 9.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATLGEGKPAG--IILSGHTDTVPWDGQD-WSVDPLSSTVRDGRLYGRGSADMKAFIA---IALSQAQRF-LESDAPf 126
Cdd:cd03895 62 NVVGTHRPRGETGrsLILNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAanlFALDALRAAgLQPAAD- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 127 aIHYAFSYDEEVGCFGAreLIADLRdaGVRPLACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAAR 206
Cdd:cd03895 141 -VHFQSVVEEECTGNGA--LAALMR--GYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 207 VVGRVRDMAEGFEREEAR---FDGFDVPFsTASVGQFHGGIADNVVPRDAEF--RYEFrdLPTADAARMQAEV---VAYA 278
Cdd:cd03895 216 LIQALQELEREWNARKKShphFSDHPHPI-NFNIGKIEGGDWPSSVPAWCVLdcRIGI--YPGESPEEARREIeecVADA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 279 RSLEPAMQAVSPRA---GFTFEPiCEIPsflgSAGDPVTRLA---QRLAGEAGT-TLVAFGTEAGLFKNAG-ISTVVCGP 350
Cdd:cd03895 293 AATDPWLSNHPPEVewnGFQAEG-YVLE----PGSDAEQVLAaahQAVFGTPPVqSAMTATTDGRFFVLYGdIPALCYGP 367
|
330
....*....|....*...
gi 1421773316 351 GSiQQAHQPDEYVSLEQL 368
Cdd:cd03895 368 GS-RDAHGFDESVDLESL 384
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
1.35e-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. 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: 125.11 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTVS---HRSNLELIDFVRTELARLGVKcrlthdasktKANLFATLG---EGKPAgIILSGHTDTVPwD 79
Cdd:cd05651 2 AIELLKSLIATPSFSreeHKTADLIENYLEQKGIPFKRK----------GNNVWAENGhfdEGKPT-LLLNSHHDTVK-P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 80 GQDWSVDPLSSTVRDGRLYGRGSADMKAFIAiALSQAQRFL--ESDAPFAIHYAFSYDEEVGCF-GARELIADLRdagvr 156
Cdd:cd05651 70 NAGWTKDPFEPVEKGGKLYGLGSNDAGASVV-SLLATFLHLysEGPLNYNLIYAASAEEEISGKnGIESLLPHLP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 157 PLAC-IVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSlTPHSVNAIEMAARVVGRVRDMaegfereeaRFDGFDvPF--- 232
Cdd:cd05651 144 PLDLaIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAA-RNEGDNAIYKALDDIQWLRDF---------RFDKVS-PLlgp 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 233 STASVGQFHGGIADNVVPRDAEFryeFRDLPTADAARmQAEVVAYARS-LEPAMQAVSPRAgftfepiceIPSFLgSAGD 311
Cdd:cd05651 213 VKMTVTQINAGTQHNVVPDSCTF---VVDIRTTEAYT-NEEIFEIIRGnLKSEIKPRSFRL---------NSSAI-PPDH 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421773316 312 PVTRLAQRLAGEagttlvAFGT-----EAGLfknaGISTVVCGPGSIQQAHQPDEYVSLEQLAR 370
Cdd:cd05651 279 PIVQAAIAAGRT------PFGSptlsdQALM----PFPSVKIGPGDSSRSHTADEFIELSEIEE 332
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
15-371 |
1.37e-32 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 125.55 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 15 RMNTVSHRSN--LELIDFVRTELARLGVKCRLthDASktkANLFATL----GEGKPAgIILSGHTDTVPwdgqDWSVDPL 88
Cdd:COG2195 11 EYVKIPTPSDheEALADYLVEELKELGLEVEE--DEA---GNVIATLpatpGYNVPT-IGLQAHMDTVP----QFPGDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 89 SSTVRDGRLYGRGS----ADMKAFIAIALSQAQRFLESDAPF-AIHYAFSYDEEVGCFGAREL-IADLR-------DAGV 155
Cdd:COG2195 81 KPQIDGGLITADGTttlgADDKAGVAAILAALEYLKEPEIPHgPIEVLFTPDEEIGLRGAKALdVSKLGadfaytlDGGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 156 rplaciVGEPTNMVPAIAhkgvyRYRCCVRGKEAHSSLTPHS-VNAIEMAARVVgrvRDMAEGFEREEarfdgfdvpfST 234
Cdd:COG2195 161 ------EGELEYECAGAA-----DAKITIKGKGGHSGDAKEKmINAIKLAARFL---AALPLGRIPEE----------TE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 235 ASVGQFHGGIADNVVPRDAEFRYEFRDLptaDAARMQAEVVAYARSLEpAMQAVSPRAGFTFEPICEIPSFLGSAGDPVT 314
Cdd:COG2195 217 GNEGFIHGGSATNAIPREAEAVYIIRDH---DREKLEARKAELEEAFE-EENAKYGVGVVEVEIEDQYPNWKPEPDSPIV 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 315 RLAQRLAGEAGTT--LVAF--GTEAGLFKNAGISTVVCGPGsIQQAHQPDEYVSLEQLARC 371
Cdd:COG2195 293 DLAKEAYEELGIEpkIKPIrgGLDGGILSFKGLPTPNLGPG-GHNFHSPDERVSIESMEKA 352
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-368 |
4.39e-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. 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: 123.54 E-value: 4.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTVSHrSNLELIDFVRTELARLGVKCRLTHDASKTKANLFATLGEGKPAGIILSGHTDTVP--Wdgqdw 83
Cdd:cd05652 1 LLSLHKSLVEIPSISG-NEAAVGDFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPRVLLTSHIDTVPpfI----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 84 svdPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESD--APFAIHYAFSYDEEVGCFGARElIADLRDAGVRplACI 161
Cdd:cd05652 75 ---PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGevPEGDLGLLFVVGEETGGDGMKA-FNDLGLNTWD--AVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 162 VGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEGFEREEARfdgfdvpfSTASVGQFH 241
Cdd:cd05652 149 FGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGP--------TTLNIGRIS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 242 GGIADNVVPRDAEFRYEFRdlPTADAARMQAEVVAYARSLEPAMQAVSPRAGFTFEPI---CEIPSFlgsagdpvtrlaq 318
Cdd:cd05652 221 GGVAANVVPAAAEASVAIR--LAAGPPEVKDIVKEAVAGILTDTEDIEVTFTSGYGPVdldCDVDGF------------- 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1421773316 319 rlageaGTTLVAFGTEAGLFKnAGISTVVCGPGSIQQAHQPDEYVSLEQL 368
Cdd:cd05652 286 ------ETDVVAYGTDIPYLK-GDHKRYLYGPGSILVAHGPDEAITVSEL 328
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
54-379 |
5.92e-31 |
|
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: 121.37 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATLGEGKPAgIILSGHTDTVPWDGQD-WSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLE---SDAPFAIH 129
Cdd:cd05649 43 NVIGYIGGGKKK-ILFDGHIDTVGIGNIDnWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDlglRDFAYTIL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 130 YAFSYDEEVgCFG--ARELIadlRDAGVRPLACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARV 207
Cdd:cd05649 122 VAGTVQEED-CDGvcWQYIS---KADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 208 VGRVRDMAEGFerEEARFDGfdvpFSTASVGQ-FHGGIADNVVPRDAEFRY---------------EFRDLPTADAARmQ 271
Cdd:cd05649 198 IQDIRQLNPNF--PEAPFLG----RGTLTVTDiFSTSPSRCAVPDSCRISIdrrltvgetwegcleEIRALPAVKKYG-D 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 272 AEVVAYARSLEPAMqavsprAGFTFEPICEIPSFLGSAGDPVTRLA----QRLAGEA-GTTLVAFGTE----AGlfkNAG 342
Cdd:cd05649 271 DVAVSMYNYDRPSY------TGEVYESERYFPTWLLPEDHELVKALleayKALFGARpLIDKWTFSTNgvsiMG---RAG 341
|
330 340 350
....*....|....*....|....*....|....*..
gi 1421773316 343 ISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGLA 379
Cdd:cd05649 342 IPCIGFGPGAENQAHAPNEYTWKEDLVRCAAGYAAIP 378
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
54-376 |
2.43e-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: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATLGEGKPAGIILSGHTDTVPwdgqdwSVDPLSSTVR-DGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAF 132
Cdd:cd05647 43 TVVARTERGLASRVILAGHLDTVP------VAGNLPSRVEeDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 133 SYDEEVGCF--GARELIADLRDAGVRPLAcIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGR 210
Cdd:cd05647 117 YDCEEVAAElnGLGRLAEEHPEWLAADFA-VLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 211 VrdmaEGFEREEARFDGFDVPFSTASVgQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVayarslepamqAVSP 290
Cdd:cd05647 196 L----AAYEPRTVNIDGLTYREGLNAV-FISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVR-----------EVFE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 291 RAGFTFEPICEIPSFLGSAGDPVTRLAQRLAGeaGTTLVAFG-TEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLA 369
Cdd:cd05647 260 GLGYEIEVTDLSPGALPGLDHPVARDLIEAVG--GKVRAKYGwTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQIT 337
|
....*..
gi 1421773316 370 RCEAFMR 376
Cdd:cd05647 338 ACAAILR 344
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-378 |
2.59e-29 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 116.40 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTVSHRSNlELIDFVRTELARLGVKCRLTHDasKTKANLFAtlgEGKPAgIILSGHTDTVPWDGQDwsv 85
Cdd:PRK08652 4 AKELLKQLVKIPSPSGQED-EIALHIMEFLESLGYDVHIESD--GEVINIVV---NSKAE-LFVEVHYDTVPVRAEF--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 86 dplssTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRdagvrPLACIVGEP 165
Cdd:PRK08652 74 -----FVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFAERYR-----PKMAIVLEP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 166 TNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRdmaegfEREEARFDGFDVPFstaSVGQFHGGIA 245
Cdd:PRK08652 144 TDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLK------ELLKALGKYFDPHI---GIQEIIGGSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 246 DNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMQAVSPRAGFTFEPICEIpsflgsagdpvTRLAQRLAGEAG 325
Cdd:PRK08652 215 EYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGFELDEDEEI-----------VQLLEKAMKEVG 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1421773316 326 TTlVAFG-----TEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGL 378
Cdd:PRK08652 284 LE-PEFTvmrswTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLKAL 340
|
|
| PRK06915 |
PRK06915 |
peptidase; |
54-371 |
4.62e-29 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 116.71 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATL---GEGKpaGIILSGHTDTVP-WDGQDWSVDPLSSTVRDGRLYGRGSADMK-----AFIAI-ALSQAQRFLESD 123
Cdd:PRK06915 82 NIVATLkgsGGGK--SMILNGHIDVVPeGDVNQWDHHPYSGEVIGGRIYGRGTTDMKggnvaLLLAMeALIESGIELKGD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 124 apfaIHYAFSYDEEVGcfGARELIADLRdaGVRPLACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEM 203
Cdd:PRK06915 160 ----VIFQSVIEEESG--GAGTLAAILR--GYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEK 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 204 AARVVGRVRdmaegfEREEAR--------FDGFDVPFSTaSVGQFHGG-----IADNVV------------PRDA--EFR 256
Cdd:PRK06915 232 SMFVIDHLR------KLEEKRndritdplYKGIPIPIPI-NIGKIEGGswpssVPDSVIlegrcgiapnetIEAAkeEFE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 257 YEFRDLPTADA--ARMQAEVVAY-ARSLEPAMQAVSPragftfepiceIPSFLGSAGDPVTrlAQRLAGEAGttlvAFGT 333
Cdd:PRK06915 305 NWIAELNDVDEwfVEHPVEVEWFgARWVPGELEENHP-----------LMTTLEHNFVEIE--GNKPIIEAS----PWGT 367
|
330 340 350
....*....|....*....|....*....|....*....
gi 1421773316 334 EAGLFKNAG-ISTVVCGPGSIQQAHQPDEYVSLEQLARC 371
Cdd:PRK06915 368 DGGLLTQIAgVPTIVFGPGETKVAHYPNEYIEVDKMIAA 406
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
6-371 |
8.56e-29 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 115.20 E-value: 8.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTVSHRSnLELIDFVRTELARLGVKCRLTHDASKTkaNLFATLGEGKPAgIILSGHTDTVP-WDGQDWS 84
Cdd:TIGR01246 1 VTELAKELISRPSVTPND-AGCQDIIAERLEKLGFEIEWMHFGDTK--NLWATRGTGEPV-LAFAGHTDVVPaGPEEQWS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 85 VDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPF--AIHYAFSYDEEvGCF--GARELIADLRDAGVRPLAC 160
Cdd:TIGR01246 77 SPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHkgSISLLITSDEE-GTAidGTKKVVETLMARDELIDYC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 161 IVGEPTNM-----VPAIAHKGVYRYRCCVRGKEAHSSLtPH-SVNAIEMAARVVGRV--RDMAEGFEreearfdgfDVPF 232
Cdd:TIGR01246 156 IVGEPSSVkklgdVIKNGRRGSITGNLTIKGIQGHVAY-PHlANNPIHKAAPALAELtaIKWDEGNE---------FFPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 233 STASVGQFHGGI-ADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARslepamqavSPRAGFTFEPICEIPSFLGSAG- 310
Cdd:TIGR01246 226 TSLQITNIHAGTgANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILD---------QHGLDYDLEWSLSGEPFLTNDGk 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421773316 311 --DPVTRLAQRLAGEAGTTLVAFGTEAGLF-KNAGISTVVCGPGSiQQAHQPDEYVSLEQLARC 371
Cdd:TIGR01246 297 liDKAREAIEETNGIKPELSTGGGTSDGRFiALMGAEVVEFGPVN-ATIHKVNECVSIEDLEKL 359
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
7-368 |
9.78e-29 |
|
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: 115.92 E-value: 9.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 7 LSLAQALVRMNTVSHRSNL----ELIDFVRTELARLGVKCRLTHDASKT-KANLFATLGEGKPA--GIILSGHTDTVPWD 79
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTgsetRAAEVLAARLAEAGIQTEIFVVESHPgRANLVARIGGTDPSagPLLLLGHIDVVPAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 80 GQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESD--APFAIHYAFSYDEEV-GCFGARELIADLRDAGVR 156
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGfkPKRDLVFAFVADEEAgGENGAKWLVDNHPELFDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 157 PLACI---------VGEPTNMVP-AIAHKGVYRYRCCVRGKEAHSSlTPHSVNAIEMAARVVGRVRDMAE--------GF 218
Cdd:cd05675 161 ATFALneggggslpVGKGRRLYPiQVAEKGIAWMKLTVRGRAGHGS-RPTDDNAITRLAEALRRLGAHNFpvrltdetAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 219 EREEARFDGF--------DVPFS--------------------TASVGQFHGGIADNVVPRDAEFRYEFRDLP------- 263
Cdd:cd05675 240 FAQMAELAGGeggalmltAVPVLdpalaklgpsapllnamlrnTASPTMLDAGYATNVLPGRATAEVDCRILPgqseeev 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 264 --TADAARMQAEVVAYARSLEPAMqaVSPRAGFTFEPICEipsflgsagdpvtrLAQRLAGEAGTT--LVAFGTEAGLFK 339
Cdd:cd05675 320 ldTLDKLLGDPDVSVEAVHLEPAT--ESPLDSPLVDAMEA--------------AVQAVDPGAPVVpyMSPGGTDAKYFR 383
|
410 420 430
....*....|....*....|....*....|....*.
gi 1421773316 340 NAGISTVVCGP-------GSIQQAHQPDEYVSLEQL 368
Cdd:cd05675 384 RLGIPGYGFAPlflppelDYTGLFHGVDERVPVESL 419
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
54-378 |
1.73e-28 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 115.04 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATLGEGKPAgIILSGHTDTVPWDGQD-WSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFA--IHY 130
Cdd:PRK13004 60 NVLGYIGHGKKL-IAFDAHIDTVGIGDIKnWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEytLYV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 131 AFSYDEEVgCFG--ARELIadlRDAGVRPLACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSlTPH-SVNAIEMAARV 207
Cdd:PRK13004 139 TGTVQEED-CDGlcWRYII---EEDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGS-APErGDNAIYKMAPI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 208 VGRVRDMAEGFerEEARFDG------FDVPFSTASVgqfhggiadNVVPRDAEFRY---------------EFRDLPTAD 266
Cdd:PRK13004 214 LNELEELNPNL--KEDPFLGkgtltvSDIFSTSPSR---------CAVPDSCAISIdrrltvgetwesvlaEIRALPAVK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 267 AARmqaEVVAYARSLEPAMqavsprAGFTFEPICEIPSFLGSAGDPVTRLA----QRLAGEA-GTTLVAFGTE----AGl 337
Cdd:PRK13004 283 KAN---AKVSMYNYDRPSY------TGLVYPTECYFPTWLYPEDHEFVKAAveayKGLFGKApEVDKWTFSTNgvsiAG- 352
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1421773316 338 fkNAGISTVVCGPGSIQQAHQPDEYVSLEQLARCEAFMRGL 378
Cdd:PRK13004 353 --RAGIPTIGFGPGKEPLAHAPNEYTWKEQLVKAAAMYAAI 391
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
6-370 |
3.12e-28 |
|
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: 113.22 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTVSHRSNlELIDFVRTELARLGVkcrlthDASKTKA-NLFATLGEGKPaGIILSGHTDTVPwdgqdws 84
Cdd:cd05653 3 AVELLLDLLSIYSPSGEEA-RAAKFLEEIMKELGL------EAWVDEAgNAVGGAGSGPP-DVLLLGHIDTVP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 85 vDPLSSTVRDGRLYGRGSADMKA-FIAIALSQAQrfLESDAPFAIHYAFSYDEEVGCFGARELIADlrdaGVRPLACIVG 163
Cdd:cd05653 68 -GEIPVRVEGGVLYGRGAVDAKGpLAAMILAASA--LNEELGARVVVAGLVDEEGSSKGARELVRR----GPRPDYIIIG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 164 EPTNMVP-AIAHKGVY--RYRCcvRGKEAHSSLtpHSVNAIEMAARVVGRVRDMAEGFEREearfdgfDVPFSTASVGQF 240
Cdd:cd05653 141 EPSGWDGiTLGYRGSLlvKIRC--EGRSGHSSS--PERNAAEDLIKKWLEVKKWAEGYNVG-------GRDFDSVVPTLI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 241 HGGIADNVVPRDAEFRYEFRdLPTADaarmqaevvayaRSLEPAMQAVSPRAGFTFEPICEIPSFLGSAGDPVTRLAQRL 320
Cdd:cd05653 210 KGGESSNGLPQRAEATIDLR-LPPRL------------SPEEAIALATALLPTCELEFIDDTEPVKVSKNNPLARAFRRA 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1421773316 321 AGEAG---TTLVAFGTEAG--LFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLAR 370
Cdd:cd05653 277 IRKQGgkpRLKRKTGTSDMnvLAPLWTVPIVAYGPGDSTLDHTPNEHIELAEIER 331
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
4-368 |
3.83e-27 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 111.39 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 4 DHALSLAQALVRMNTVS--HRSNLELIDFVRTELARLGVKCRLT-------HDASKTKANLFATLGEGKPAGII-LSGHT 73
Cdd:PRK13013 14 DDLVALTQDLIRIPTLNppGRAYREICEFLAARLAPRGFEVELIraegapgDSETYPRWNLVARRQGARDGDCVhFNSHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 74 DTVPwDGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFA--IHYAFSYDEEVGCFGARELIADL- 150
Cdd:PRK13013 94 DVVE-VGHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAgsIEISGTADEESGGFGGVAYLAEQg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 151 RDAGVRPLACIVGEPTNM-VPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDmaEGFEREEARFDgfD 229
Cdd:PRK13013 173 RFSPDRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEE--RLFPLLATRRT--A 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 230 VPF-------STASVGQFHGGIADN----------VVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAmqavspRA 292
Cdd:PRK13013 249 MPVvpegarqSTLNINSIHGGEPEQdpdytglpapCVADRCRIVIDRRFLIEEDLDEVKAEITALLERLKRA------RP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 293 GFTFEpICEIPSFLGSAGD---PVTRLA----QRLAGEAGTTLVAFGT-------EAGLFKNAgistVVCGPGSIQQAHQ 358
Cdd:PRK13013 323 GFAYE-IRDLFEVLPTMTDrdaPVVRSVaaaiERVLGRQADYVVSPGTydqkhidRIGKLKNC----IAYGPGILDLAHQ 397
|
410
....*....|
gi 1421773316 359 PDEYVSLEQL 368
Cdd:PRK13013 398 PDEWVGIADM 407
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-378 |
2.14e-25 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 105.94 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTVSHRSN--LELIDfvrTELARLGVKCRlTHDASKTKaNLFATLGEGKPAgIILSGHTDTVP-WDGQD 82
Cdd:PRK13009 4 VLELAQDLIRRPSVTPDDAgcQDLLA---ERLEALGFTCE-RMDFGDVK-NLWARRGTEGPH-LCFAGHTDVVPpGDLEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 83 WSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHYAF---SyDEE-VGCFGARELIADLRDAGVRPL 158
Cdd:PRK13009 78 WTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFlitS-DEEgPAINGTVKVLEWLKARGEKID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 159 ACIVGEPTN------MVpAIAHKGVYRYRCCVRGKEAHSSLtPH-SVNAIEMAARVVGRVRDMA--EGFEreearfdgfD 229
Cdd:PRK13009 157 YCIVGEPTSterlgdVI-KNGRRGSLTGKLTVKGVQGHVAY-PHlADNPIHLAAPALAELAATEwdEGNE---------F 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 230 VPFSTASVGQFHGGI-ADNVVPRDAEFRYEFR--DLPTADAarMQAEVVAYARslepamqavspRAGFTFEPICEIPS-- 304
Cdd:PRK13009 226 FPPTSLQITNIDAGTgATNVIPGELEAQFNFRfsTEHTAES--LKARVEAILD-----------KHGLDYTLEWTLSGep 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 305 FLGSAGDPVTRLAQRLAGEAGTT---LVAFGTEAGLF-KNAGISTVVCGPGSiQQAHQPDEYVS---LEQLARC-EAFMR 376
Cdd:PRK13009 293 FLTPPGKLVDAVVAAIEAVTGITpelSTSGGTSDARFiADYGAQVVEFGPVN-ATIHKVNECVSvadLEKLTRIyERILE 371
|
..
gi 1421773316 377 GL 378
Cdd:PRK13009 372 RL 373
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
60-380 |
9.43e-25 |
|
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: 104.17 E-value: 9.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 60 GEGkPAGIILSGHTDTVPwDGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAiALSQAQRFLES-DAPF--AIHYAFSYDE 136
Cdd:cd02697 70 GDG-GRTVALNAHGDVVP-PGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFA-SFTFAVRALESlGAPLrgAVELHFTYDE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 137 EV-GCFGARELiadLRDAGVRP-LACIVGEPTNMVpaIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDM 214
Cdd:cd02697 147 EFgGELGPGWL---LRQGLTKPdLLIAAGFSYEVV--TAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYAL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 215 AEGFEREEARFDGFDVPFstASVGQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAE---VVAYARSLEPAMqAVSPR 291
Cdd:cd02697 222 NAQYRQVSSQVEGITHPY--LNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEirrVIADAAASMPGI-SVDIR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 292 AGFTFEPICEIPsflGSAG--DPVTRLAQRLAGEAGTTL-VAFGTEAGLFKNAGISTVVCGPGSI----QQAHQPDEYVS 364
Cdd:cd02697 299 RLLLANSMRPLP---GNAPlvEAIQTHGEAVFGEPVPAMgTPLYTDVRLYAEAGIPGVIYGAGPRtvleSHAKRADERLQ 375
|
330
....*....|....*..
gi 1421773316 365 LEQLARC-EAFMRGLAD 380
Cdd:cd02697 376 LEDLRRAtKVIARSLRD 392
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
44-370 |
5.87e-24 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 102.39 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 44 LTHDASKTKaNLFATLGEGKPAG--IILSGHTDTVPWDGQD-WSVDPLSSTVRDGRLYGRGSADMKAFIAIALS-----Q 115
Cdd:PRK06837 76 VEIDYSGAP-NVVGTYRPAGKTGrsLILQGHIDVVPEGPLDlWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFaldalR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 116 AQRFlesdAPFA-IHYAFSYDEEvgCFGARELIADLRdaGVRPLACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLT 194
Cdd:PRK06837 155 AAGL----APAArVHFQSVIEEE--STGNGALSTLQR--GYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 195 PHSVNAIEMAARVVGRVRDMAEGFEREEAR---FDGFDVPFSTaSVGQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQ 271
Cdd:PRK06837 227 GTGANAIDAAYHLIQALRELEAEWNARKASdphFEDVPHPINF-NVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 272 AEV---VAYARSLEPAMQAVSPRA---GFTFEpiceiPSFLGSAGDPVTRLAQRLAGEAGTTLVAFGTEA-------GLf 338
Cdd:PRK06837 306 AEIeacLAAAARDDRFLSNNPPEVvwsGFLAE-----GYVLEPGSEAEAALARAHAAVFGGPLRSFVTTAytdtrfyGL- 379
|
330 340 350
....*....|....*....|....*....|..
gi 1421773316 339 kNAGISTVVCGPGSiQQAHQPDEYVSLEQLAR 370
Cdd:PRK06837 380 -YYGIPALCYGPSG-EGIHGFDERVDLESVRK 409
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
13-369 |
3.16e-23 |
|
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: 99.45 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 13 LVRMNTVSHRSNlELIDFVRTELARLGVKCRLTHDASKTK---ANLFATL---GEGKPAgIILSGHTDTV-PWDGqdwsV 85
Cdd:cd05683 12 LVQIDSETLHEK-EISKVLKKKFENLGLSVIEDDAGKTTGggaGNLICTLkadKEEVPK-ILFTSHMDTVtPGIN----V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 86 DPLSstVRDGRLYGRGS----ADMKAFIAIALSQAQRFLESDAPFA-IHYAFSYDEEVGCFGARELIADLRDA------- 153
Cdd:cd05683 86 KPPQ--IADGYIYSDGTtilgADDKAGIAAILEAIRVIKEKNIPHGqIQFVITVGEESGLVGAKALDPELIDAdygyald 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 154 -GVRPLACIVGEPTNMvpaiahkgvyRYRCCVRGKEAHSSLTPHS-VNAIEMAARVVGRvrdMAEGfereeaRFDgfdvP 231
Cdd:cd05683 164 sEGDVGTIIVGAPTQD----------KINAKIYGKTAHAGTSPEKgISAINIAAKAISN---MKLG------RID----E 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 232 FSTASVGQFHGGIADNVVPRDAEFRYEFRDLptaDAARMQAEVVAYARSLEPAMQAVSPRAGFTFEPIceIPSFLGSAGD 311
Cdd:cd05683 221 ETTANIGKFQGGTATNIVTDEVNIEAEARSL---DEEKLDAQVKHMKETFETTAKEKGAHAEVEVETS--YPGFKINEDE 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1421773316 312 PVTRLAQRLAGEAGTTLVAF----GTEAGLFKNAGISTVVCGPGsIQQAHQPDEYVSLEQLA 369
Cdd:cd05683 296 EVVKLAKRAANNLGLEINTTysggGSDANIINGLGIPTVNLGIG-YENIHTTNERIPIEDLY 356
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
4-368 |
4.23e-23 |
|
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: 99.45 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 4 DHALSLAQALVRMNTVSHRSN----LELIDFVRTELARLGV----KCRLTHDASKTKANLFATLGEGKPAGIILSGHTDT 75
Cdd:cd05650 1 EEIIELERDLIRIPAVNPESGgegeKEKADYLEKKLREYGFytleRYDAPDERGIIRPNIVAKIPGGNDKTLWIISHLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 76 VP-WDGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLES--DAPFAIHYAFSYDEEVGC-FG------ARE 145
Cdd:cd05650 81 VPpGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNgiTPKYNFGLLFVADEEDGSeYGiqyllnKFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 146 LIADlRDAGVRPLAcivGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAegFEREEARF 225
Cdd:cd05650 161 LFKK-DDLIIVPDF---GTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELL--HEKFDEKD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 226 DGFDVPFSTasvgqFHGGIAD------NVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMQavsprAGFTFEPI 299
Cdd:cd05650 235 DLFNPPYST-----FEPTKKEanvpnvNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYG-----AGITYEIV 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1421773316 300 CEIPSFLGSAGDP--VTRLAQRLAGEAGTTL----VAFGTEAGLFKNAGISTVVCGPGsIQQAHQPDEYVSLEQL 368
Cdd:cd05650 305 QKEQAPPATPEDSeiVVRLSKAIKKVRGREAkligIGGGTVAAFLRKKGYPAVVWSTL-DETAHQPNEYIRISHI 378
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
1-368 |
6.55e-20 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 90.29 E-value: 6.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 1 MISDHALSLAQALVRMNTVSHRSN----LELIDFVRTELARLGVKCRLTHDA------SKTKANLFATL-GEGKPAGIIL 69
Cdd:PRK13983 2 ELRDEMIELLSELIAIPAVNPDFGgegeKEKAEYLESLLKEYGFDEVERYDApdprviEGVRPNIVAKIpGGDGKRTLWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 70 SGHTDTVP-WDGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDA--PFAIHYAFSYDEEVGC-FGARE 145
Cdd:PRK13983 82 ISHMDVVPpGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIrpKYNLGLAFVSDEETGSkYGIQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 146 LIADLRDaGVRPLACIV----GEPTNMVPAIAHKGVYRYRCCVRGKEAHSSlTPHS-VNAIEMAArvvgrvrDMAEGFER 220
Cdd:PRK13983 162 LLKKHPE-LFKKDDLILvpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHAS-TPENgINAHRAAA-------DFALELDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 221 E-EARFDG----FDVPFSTasvgqF----HGGIADNV--VPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEpamqaVS 289
Cdd:PRK13983 233 AlHEKFNAkdplFDPPYST-----FeptkKEANVDNIntIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFE-----EE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 290 PRAGFTFEPI------------CEIPSFLGSAGDPVTRLAQRLAGEAGTTLVAFgteaglFKNAGISTVVCGPGsIQQAH 357
Cdd:PRK13983 303 YGVKIEVEIVqreqappptppdSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAF------LRKKGYPAVVWSTL-DETAH 375
|
410
....*....|.
gi 1421773316 358 QPDEYVSLEQL 368
Cdd:PRK13983 376 QPNEYAKISNL 386
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
172-283 |
9.56e-19 |
|
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: 80.85 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 172 IAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDmaegfereEARFDGFDVPFSTASVGQFHGGIADNVVPR 251
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPA--------EYGDIGFDFPRTTLNITGIEGGTATNVIPA 72
|
90 100 110
....*....|....*....|....*....|..
gi 1421773316 252 DAEFRYEFRDLPTADAARMQAEVVAYARSLEP 283
Cdd:pfam07687 73 EAEAKFDIRLLPGEDLEELLEEIEAILEKELP 104
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
9-378 |
7.68e-18 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 85.00 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 9 LAQAlVRMNTVSHRSNLE--------LIDFVRTELARLGVKCRLTHDASKTkanLFATLgEGKPAG---IILSGHTDTVP 77
Cdd:PRK08262 50 LSEA-IRFRTISNRDRAEddaaafdaLHAHLEESYPAVHAALEREVVGGHS---LLYTW-KGSDPSlkpIVLMAHQDVVP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 78 WDG---QDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDapF----AIHYAFSYDEEVGCFGARELIADL 150
Cdd:PRK08262 125 VAPgteGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQG--FqprrTIYLAFGHDEEVGGLGARAIAELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 151 RDAGVRPLACI-------------VGEPTNMVpAIAHKGVYRYRCCVRGKEAHSSlTPHSVNAIEMAARVVGRVRD---- 213
Cdd:PRK08262 203 KERGVRLAFVLdeggaitegvlpgVKKPVALI-GVAEKGYATLELTARATGGHSS-MPPRQTAIGRLARALTRLEDnplp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 214 ------MAEGFEREEARFDGFD-VPFS-------------------------TASVGQFHGGIADNVVPRDAEFRYEFRD 261
Cdd:PRK08262 281 mrlrgpVAEMFDTLAPEMSFAQrVVLAnlwlfeplllrvlakspetaamlrtTTAPTMLKGSPKDNVLPQRATATVNFRI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 262 LPtADAarmQAEVVAYARSLEPAMQAVSPRAGFTFEPiCEIPSFLGSAGDPVTRLAQRLAGEAGTT--LVAFGTEAGLFk 339
Cdd:PRK08262 361 LP-GDS---VESVLAHVRRAVADDRVEIEVLGGNSEP-SPVSSTDSAAYKLLAATIREVFPDVVVApyLVVGATDSRHY- 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1421773316 340 nAGISTVVC-------GPGSIQQAHQPDEYVSLEQLARCEAFMRGL 378
Cdd:PRK08262 435 -SGISDNVYrfsplrlSPEDLARFHGTNERISVANYARMIRFYYRL 479
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
60-370 |
1.53e-17 |
|
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: 82.91 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 60 GEGKPAGIILSGHTDTVPWDGQDWSVdplssTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFA---IHYAFSYDE 136
Cdd:cd03896 50 GTGGGPALLFSAHLDTVFPGDTPATV-----RHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKgdvVFAANVGEE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 137 EVG-CFGARELIADLRDagvRPLACIVGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMA 215
Cdd:cd03896 125 GLGdLRGARYLLSAHGA---RLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 216 EGFereearfdgfdVPFSTASVGQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMQAVSPRagft 295
Cdd:cd03896 202 APY-----------VPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAKHLRVKAR---- 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1421773316 296 FEPICEIPSFLGSAGDPVTRLAQRLAGEAGTTLV--AFGTEAGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLAR 370
Cdd:cd03896 267 VKPVGDRPGGEAQGTEPLVNAAVAAHREVGGDPRpgSSSTDANPANSLGIPAVTYGLGRGGNAHRGDEYVLKDDMLK 343
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
63-279 |
2.28e-17 |
|
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: 83.46 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 63 KPagIILSGHTDTVP-----WDGqdWSVDPLSSTVRDGRLYGRGSADMKaFIAIALSQAQRFLESDAPF---AIHYAFSY 134
Cdd:cd05674 70 KP--LLLMAHQDVVPvnpetEDQ--WTHPPFSGHYDGGYIWGRGALDDK-NSLIGILEAVELLLKRGFKprrTIILAFGH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 135 DEEV-GCFGARELIADLRD-AGVRPLACIV--------GEPTNM---VPAIAHKGVYRYRCCVRGKEAHSSLTP-HSvnA 200
Cdd:cd05674 145 DEEVgGERGAGAIAELLLErYGVDGLAAILdeggavleGVFLGVpfaLPGVAEKGYMDVEITVHTPGGHSSVPPkHT--G 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 201 IEMAARVVGRVRD--MAEGFEREE---------ARFDGFDVPF--------------------------------STASV 237
Cdd:cd05674 223 IGILSEAVAALEAnpFPPKLTPGNpyygmlqclAEHSPLPPRSlksnlwlaspllkallasellstspltrallrTTQAV 302
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1421773316 238 GQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYAR 279
Cdd:cd05674 303 DIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIA 344
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
3-291 |
3.39e-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: 82.53 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 3 SDHALSLAQALVRMNTVSHRSNL-ELIDFVRTELARLGVKCRlTHDASKTKANLFATLGEGKP--AGIILSGHTDTVPWD 79
Cdd:TIGR01880 8 EDIAVTRFREYLRINTVQPNPDYaACVDFLIKQADELGLARK-TIEFVPGKPVVVLTWPGSNPelPSILLNSHTDVVPVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 80 GQDWSVDPLSSTV-RDGRLYGRGSADMKAfIAIALSQAQRFLESDA---PFAIHYAFSYDEEVG------CFGARELIAD 149
Cdd:TIGR01880 87 REHWTHPPFSAFKdEDGNIYARGAQDMKC-VGVQYLEAVRNLKASGfkfKRTIHISFVPDEEIGghdgmeKFAKTDEFKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 150 LR-----DAGvrplaciVGEPTNMVPAI-AHKGVYRYRCCVRGKEAHSS-LTPHSvnAIEMAARVVGRVRDM-AEGFERE 221
Cdd:TIGR01880 166 LNlgfalDEG-------LASPDDVYRVFyAERVPWWVVVTAPGNPGHGSkLMENT--AMEKLEKSVESIRRFrESQFQLL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421773316 222 EARFDGFDVPFSTASVGQFHGGIADNVVPRDAEFRYEFRDLPTADA----ARMQAEVVAYARSLEPAMQAVSPR 291
Cdd:TIGR01880 237 QSNPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFeemeNRLDEWCADAGEGVTYEFSQHSGK 310
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-366 |
4.26e-17 |
|
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: 82.39 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 12 ALVRMNTVSHRSN--LELIDFVRTELARLGVKCRLTHdaSKTKANLFATLGEGKPAGIILSGHTDTVPWDG-QDWSVDPL 88
Cdd:cd05681 7 DLLKIPSVSAQGRgiPETADFLKEFLRRLGAEVEIFE--TDGNPIVYAEFNSGDAKTLLFYNHYDVQPAEPlELWTSDPF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 89 SSTVRDGRLYGRGSADMKAFIAIALSQAQRFLES--DAPFAIHYAFSYDEEVGCFGARELIADLRD-----------AGV 155
Cdd:cd05681 85 ELTIRNGKLYARGVADDKGELMARLAALRALLQHlgELPVNIKFLVEGEEEVGSPNLEKFVAEHADllkadgciwegGGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 156 RPLacivGEPtnmVPAIAHKGVYRYRCCVRG--KEAHSSLTPHSVNAIEMAARVVGRVRDMA-----EGF--------ER 220
Cdd:cd05681 165 NPK----GRP---QISLGVKGIVYVELRVKTadFDLHSSYGAIVENPAWRLVQALNSLRDEDgrvliPGFyddvrplsEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 221 EEARFD--GFDVPFSTASVGQ-----------------------------FHGGIADNVVPRDAEFRYEFRDLPTADAAR 269
Cdd:cd05681 238 ERALIDtyDFDPEELRKTYGLkrplqvegkdplralfteptcningiysgYTGEGSKTILPSEAFAKLDFRLVPDQDPAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 270 MQAEVVAYarsLEpamqavspRAGFTFEPICE---IPSFLGSAGDPVTRLAQRLAGEA-GTTLVAFGTEAG------LFK 339
Cdd:cd05681 318 ILSLLRKH---LD--------KNGFDDIEIHDllgEKPFRTDPDAPFVQAVIESAKEVyGQDPIVLPNSAGtgpmypFYD 386
|
410 420
....*....|....*....|....*...
gi 1421773316 340 NAGISTVVCGPGSIQ-QAHQPDEYVSLE 366
Cdd:cd05681 387 ALEVPVVAIGVGNAGsNAHAPNENIRIA 414
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
9-211 |
9.79e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 81.05 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 9 LAQALVRMNTVSH-----RSNLELIDFVRTELARLGVKCRLtHDASKTKANLFATL-GE--GKPAgIILSGHTDTVPWDG 80
Cdd:PRK07906 4 LCSELIRIDTTNTgdgtgKGEREAAEYVAEKLAEVGLEPTY-LESAPGRANVVARLpGAdpSRPA-LLVHGHLDVVPAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 81 QDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDA--PFAIHYAFSYDEEV-GCFGARELIADLRD--AGV 155
Cdd:PRK07906 82 ADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRrpPRDLVFAFVADEEAgGTYGAHWLVDNHPElfEGV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421773316 156 RPLACIVGEPTNMVP--------AIAHKGVYRYRCCVRGKEAHSSLtPHSVNAIEMAARVVGRV 211
Cdd:PRK07906 162 TEAISEVGGFSLTVPgrdrlyliETAEKGLAWMRLTARGRAGHGSM-VNDDNAVTRLAEAVARI 224
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
11-370 |
1.49e-16 |
|
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: 80.83 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 11 QALVRMNTVS----HRSNLE-LIDFVRTELARLGVKCRLThDASKTKANLFATLG--EGKPAgIILSGHTDTVPWDGQD- 82
Cdd:cd03893 5 AELVAIPSVSaqpdRREELRrAAEWLADLLRRLGFTVEIV-DTSNGAPVVFAEFPgaPGAPT-VLLYGHYDVQPAGDEDg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 83 WSVDPLSSTVRDGRLYGRGSADMKAFIAIALS--QAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRDAGVRPLAC 160
Cdd:cd03893 83 WDSDPFELTERDGRLYGRGAADDKGPILAHLAalRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLVEAHRDLLAADAIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 161 IVGEP--TNMVPAIAH--KGVYRYRCCVRGKEA--HSSLTPHSV-NAIEMAARVVGRVRD-----MAEGF--------ER 220
Cdd:cd03893 163 ISDSTwvGQEQPTLTYglRGNANFDVEVKGLDHdlHSGLYGGVVpDPMTALAQLLASLRDetgriLVPGLydavrelpEE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 221 EEARFDGF--DVPFSTASVGQ-------------------FHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYAR 279
Cdd:cd03893 243 EFRLDAGVleEVEIIGGTTGSvaerlwtrpaltvlgidggFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 280 SLEPamqavsPRAGFTFEPICEIPSFLGSAGDPVTRLAQRLAGEAGTTLVAFGTEAGLFKNA-------GISTVVCGPGS 352
Cdd:cd03893 323 KHAP------SGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGGSIPFIsvlqefpQAPVLLIGVGD 396
|
410
....*....|....*....
gi 1421773316 353 IQ-QAHQPDEYVSLEQLAR 370
Cdd:cd03893 397 PDdNAHSPNESLRLGNYKE 415
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
3-370 |
1.58e-14 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 73.84 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 3 SDHALSLAQALVRMNTVSHRSNlELIDFVRTELARLGVKCRLthDASktkANLFATLGEGkPAGIILSGHTDTVPWDgqd 82
Cdd:PRK04443 5 ALEARELLKGLVEIPSPSGEEA-AAAEFLVEFMESHGREAWV--DEA---GNARGPAGDG-PPLVLLLGHIDTVPGD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 83 wsvdpLSSTVRDGRLYGRGSADMK----AFIAialsqAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRdagvRPL 158
Cdd:PRK04443 75 -----IPVRVEDGVLWGRGSVDAKgplaAFAA-----AAARLEALVRARVSFVGAVEEEAPSSGGARLVADRE----RPD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 159 ACIVGEP--TNMVpAIAHKG--VYRYRccVRGKEAHSSltPHSVNAIEMAARVVGRVRDMAEGFEREEARFDGfdVPFST 234
Cdd:PRK04443 141 AVIIGEPsgWDGI-TLGYKGrlLVTYV--ATSESFHSA--GPEPNAAEDAIEWWLAVEAWFEANDGRERVFDQ--VTPKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 235 ASVGQFHGGIADnvvprDAEFRYEFR---DLPTADAARmqaevvayarslepAMQAVSPRAGFTFEPICeiPSFLGSAGD 311
Cdd:PRK04443 214 VDFDSSSDGLTV-----EAEMTVGLRlppGLSPEEARE--------------ILDALLPTGTVTFTGAV--PAYMVSKRT 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1421773316 312 PVTR---LAQRLAGEAGTTLVAFGTE-----AGLFknaGISTVVCGPGSIQQAHQPDEYVSLEQLAR 370
Cdd:PRK04443 273 PLARafrVAIREAGGTPRLKRKTGTSdmnvvAPAW---GCPMVAYGPGDSDLDHTPDEHLPLAEYLR 336
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
6-212 |
3.08e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 73.88 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 6 ALSLAQALVRMNTV-SHRSNLELIDFVRTELARLGVK---CRLThDASKTKANLFATL---GEGKPagIILSGHTDTVPW 78
Cdd:PRK09133 39 ARDLYKELIEINTTaSTGSTTPAAEAMAARLKAAGFAdadIEVT-GPYPRKGNLVARLrgtDPKKP--ILLLAHMDVVEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 79 DGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALS-----QAQRFLES-DapfaIHYAFSYDEEVGCF-GARELIADLR 151
Cdd:PRK09133 116 KREDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVAtlirlKREGFKPKrD----IILALTGDEEGTPMnGVAWLAENHR 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 152 DAgVRPLACI----------VGEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLtPHSVNAIEMAARVVGRVR 212
Cdd:PRK09133 192 DL-IDAEFALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSR-PTKDNAIYRLAAALSRLA 260
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
7-178 |
4.16e-14 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 73.27 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 7 LSLAQALVRMNTVSH-----RSNLELIDFVRTELARLGVKCRLT-HDASKTkanLFATLGEGKPAgIILSGHTDTVPWDG 80
Cdd:PRK08554 4 LELLSSLVSFETVNDpskgiKPSKECPKFIKDTLESWGIESELIeKDGYYA---VYGEIGEGKPK-LLFMAHFDVVPVNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 81 QDWSVDPLSSTVRDGRLYGRGSADMK---AFIAIALSQaqrFLESDAPFAIHYAFSYDEEVGCFGARELIADLRDAGVRP 157
Cdd:PRK08554 80 EEWNTEPFKLTVKGDKAYGRGSADDKgnvASVMLALKE---LSKEPLNGKVIFAFTGDEEIGGAMAMHIAEKLREEGKLP 156
|
170 180
....*....|....*....|.
gi 1421773316 158 LACIVGEPTNMVPAIAHKGVY 178
Cdd:PRK08554 157 KYMINADGIGMKPIIRRRKGF 177
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
54-167 |
4.75e-14 |
|
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: 70.15 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATLGEG-KPAGIILSGHTDTVPWDGQDWSVDPLSS-TVRDGRLYGRGSADMKAFIAIALSQAQRFLESDA--PFAIH 129
Cdd:cd18669 1 NVIARYGGGgGGKRVLLGAHIDVVPAGEGDPRDPPFFVdTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFklKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1421773316 130 YAFSYDEEVGCFGARELIADLRDAGVRPL-ACIVGEPTN 167
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVdYLFVGDATP 119
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
7-370 |
5.35e-14 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 72.76 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 7 LSLAQALVRMNTVS--HRSNLELIDFVRTELARLGVKCRLtHDASKTKANLFATL-GE--GKPAGIILSGHTDTVPWDG- 80
Cdd:PRK08596 16 LELLKTLVRFETPAppARNTNEAQEFIAEFLRKLGFSVDK-WDVYPNDPNVVGVKkGTesDAYKSLIINGHMDVAEVSAd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 81 QDWSVDPLSSTVRDGRLYGRGSADMK-----AFIAIA-LSQAQRFLESDAPF--AIhyafsyDEEVGCFGARE------- 145
Cdd:PRK08596 95 EAWETNPFEPTIKDGWLYGRGAADMKgglagALFAIQlLHEAGIELPGDLIFqsVI------GEEVGEAGTLQccergyd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 146 ----LIADLRD------AGVrplacIVGEPTNMVPAIAHKGvyryrccVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMa 215
Cdd:PRK08596 169 adfaVVVDTSDlhmqgqGGV-----ITGWITVKSPQTFHDG-------TRRQMIHAGGGLFGASAIEKMMKIIQSLQEL- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 216 egfEREEA---RFDGFDVPFSTASVGQFHGGiadnvvpRDAEFryefrdlpTADAARMQAEVVAY--------ARSLEPA 284
Cdd:PRK08596 236 ---ERHWAvmkSYPGFPPGTNTINPAVIEGG-------RHAAF--------IADECRLWITVHFYpnetyeqvIKEIEEY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 285 MQAVS----------PragfTFE--------------PICEIP------SFLGSAGDPVTRlaQRLAGEAGTTLvafgTE 334
Cdd:PRK08596 298 IGKVAaadpwlrenpP----QFKwggesmiedrgeifPSLEIDsehpavKTLSSAHESVLS--KNAILDMSTTV----TD 367
|
410 420 430
....*....|....*....|....*....|....*.
gi 1421773316 335 AGLFKNAGISTVVCGPGSIQQAHQPDEYVSLEQLAR 370
Cdd:PRK08596 368 GGWFAEFGIPAVIYGPGTLEEAHSVNEKVEIEQLIE 403
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
64-274 |
1.24e-13 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 71.53 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 64 PAGIILSGHTDTVpwdgqdWSVDPLSSTVR---DGRLYGRGSADMKAFIAIALSQAQRFLESDAPFAIHY--AFSYDEEV 138
Cdd:PRK07338 92 PRQVLLTGHMDTV------FPADHPFQTLSwldDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLGYdvLINPDEEI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 139 GCFGARELIADLrdaGVRPLACIVGEPtnMVP----AIAHKGVYRYRCCVRGKEAHSSLTPHS-VNAIEMAARVVGRVRD 213
Cdd:PRK07338 166 GSPASAPLLAEL---ARGKHAALTYEP--ALPdgtlAGARKGSGNFTIVVTGRAAHAGRAFDEgRNAIVAAAELALALHA 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 214 MaegfereEARFDGFdvpfsTASVGQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEV 274
Cdd:PRK07338 241 L-------NGQRDGV-----TVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAEL 289
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
29-369 |
1.39e-13 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 71.59 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 29 DFVRTELARLGVKCRLTHDASKTKANLFATL-GEGKpAGIILSGHTDTVPWDG----QDWSVDplsstvrDGRLYGRGSA 103
Cdd:PRK06133 64 ALLAERLKALGAKVERAPTPPSAGDMVVATFkGTGK-RRIMLIAHMDTVYLPGmlakQPFRID-------GDRAYGPGIA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 104 DMKAFIAIALS-----QAQRFLESDApfaIHYAFSYDEEVGCFGARELIADLRDAGVRPLACIVGEPTNMVpAIAHKGVY 178
Cdd:PRK06133 136 DDKGGVAVILHalkilQQLGFKDYGT---LTVLFNPDEETGSPGSRELIAELAAQHDVVFSCEPGRAKDAL-TLATSGIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 179 RYRCCVRGKEAHSSLTPHS-VNA-IEMAARVVgRVRDMAEgfereearfdgfDVPFSTASVGQFHGGIADNVVPRDAefr 256
Cdd:PRK06133 212 TALLEVKGKASHAGAAPELgRNAlYELAHQLL-QLRDLGD------------PAKGTTLNWTVAKAGTNRNVIPASA--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 257 yefrdlpTADaARMQAEVVAYARSLEPAMQAVS-------PRAGFTFE---PiceiPSFLGSAGDPVTRLAQRLAGEAGT 326
Cdd:PRK06133 276 -------SAQ-ADVRYLDPAEFDRLEADLQEKVknklvpdTEVTLRFErgrP----PLEANAASRALAEHAQGIYGELGR 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1421773316 327 TL----VAFG--TEAGLFKNAGISTVVCGPG-SIQQAHQPDEYVSLEQLA 369
Cdd:PRK06133 344 RLepidMGTGggTDAAFAAGSGKAAVLEGFGlVGFGAHSNDEYIELNSIV 393
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
3-280 |
4.39e-13 |
|
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: 69.99 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 3 SDHALSLAQALVRMNTVSHRSNLE-LIDFVRTELARLGVKCRLTHDASKTKANLFATLGEgKP--AGIILSGHTDTVPWD 79
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNPDYDaCVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGS-NPelPSILLNSHTDVVPVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 80 GQDWSVDPLSSTV-RDGRLYGRGSADMKAfIAIALSQAQRFLESDA---PFAIHYAFSYDEEVGCF-GARELIA-----D 149
Cdd:cd05646 80 EEKWTHDPFSAHKdEDGNIYARGAQDMKC-VGIQYLEAIRRLKASGfkpKRTIHLSFVPDEEIGGHdGMEKFVKteefkK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 150 LR-----DAGvrpLACivgePTNMVPAI-AHKGVYRYRCCVRGKEAHSS-LTPHSvnAIEMAARVVGRVRDM-AEGFERE 221
Cdd:cd05646 159 LNvgfalDEG---LAS----PTEEYRVFyGERSPWWVVITAPGTPGHGSkLLENT--AGEKLRKVIESIMEFrESQKQRL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 222 EAR--FDGFDVpfSTASVGQFHGGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARS 280
Cdd:cd05646 230 KSNpnLTLGDV--TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAE 288
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
54-177 |
2.09e-12 |
|
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: 65.52 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATLGEG-KPAGIILSGHTDTVPWDGQDWSVDPLSS-TVRDGRLYGRGSADMKAFIAIALSQAQRFLEsdAPFA---- 127
Cdd:cd03873 1 NLIARLGGGeGGKSVALGAHLDVVPAGEGDNRDPPFAEdTEEEGRLYGRGALDDKGGVAAALEALKRLKE--NGFKpkgt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 128 IHYAFSYDEEVGCFGARELIADLRDAGVRPL-ACIVGEPTNMVpaIAHKGV 177
Cdd:cd03873 79 IVVAFTADEEVGSGGGKGLLSKFLLAEDLKVdAAFVIDATAGP--ILQKGV 127
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
25-152 |
4.52e-11 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 64.16 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 25 LELIDFVRTELARLGVKCRLtHDASKTKAN----------LFATLGE--GKPAGIILsGHTDTVPWDGQD-WSVDPLSST 91
Cdd:cd05676 36 IRMMEWAAERLEKLGFKVEL-VDIGTQTLPdgeelplppvLLGRLGSdpSKKTVLIY-GHLDVQPAKLEDgWDTDPFELT 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1421773316 92 VRDGRLYGRGSADMK----AFI-AIalsQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRD 152
Cdd:cd05676 114 EKDGKLYGRGSTDDKgpvlGWLnAI---EAYQKLGQELPVNLKFCFEGMEESGSEGLDELIEARKD 176
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
60-370 |
9.72e-11 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 63.10 E-value: 9.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 60 GEGKPAgIILSGHTDTVPWDGQD-WSVDPLSSTVRDGRLYGRGSADMK--AFIAIALSQAQRFLESDAPFAIHYAFSYDE 136
Cdd:cd05680 60 APGAPT-VLVYGHYDVQPPDPLElWTSPPFEPVVRDGRLYARGASDDKgqVFIHIKAVEAWLAVEGALPVNVKFLIEGEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 137 EVGCFGARELIADLRDAgvrpLAC--IVGEPTNMV----PAIAH--KGVYRYRCCVRG--KEAHSSLTPHSV-NAIEMAA 205
Cdd:cd05680 139 EIGSPSLPAFLEENAER----LAAdvVLVSDTSMWspdtPTITYglRGLAYLEISVTGpnRDLHSGSYGGAVpNPANALA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 206 RVV-------GRVRdmAEGF----------EREE-ARFdGFD--VPFSTASVGQFHG-------------------GI-- 244
Cdd:cd05680 215 RLLaslhdedGRVA--IPGFyddvrpltdaEREAwAAL-PFDeaAFKASLGVPALGGeagyttlerlwarptldvnGIwg 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 245 ------ADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMQAVSPRAGFTFEPiceipsFLGSAGDPVTRLAQ 318
Cdd:cd05680 292 gyqgegSKTVIPSKAHAKISMRLVPGQDPDAIADLLEAHLRAHAPPGVTLSVKPLHGGRP------YLVPTDHPALQAAE 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1421773316 319 RLAGEagttlvAFGTEAGLFKNAG-------------ISTVVCGPGSIQQA-HQPDEYVSLEQLAR 370
Cdd:cd05680 366 RALEE------AFGKPPVFVREGGsipivalfekvlgIPTVLMGFGLPDDAiHAPNEKFRLECFHK 425
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
56-201 |
6.80e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 60.48 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 56 FATLGEGKPAGIILsGHTDTVP-WDGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIALSQAQRFLESDAPFA--IHYAF 132
Cdd:PRK07205 68 YAEIGQGEELLAIL-CHLDVVPeGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNkrIRFIF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 133 SYDEE-----VGCFGARELIADLrdaGVRP-------------------------LACIVGEPTNMVPAIA-HKGV---- 177
Cdd:PRK07205 147 GTDEEtlwrcMNRYNEVEEQATM---GFAPdssfpltyaekgllqaklvgpgsdqLELEVGQAFNVVPAKAsYQGPklea 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 1421773316 178 ---------YRYRC-----CVRGKEAHSSLTPHSVNAI 201
Cdd:PRK07205 224 vkkeldklgFEYVVkenevTVLGKSVHAKDAPQGINAV 261
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
51-260 |
7.67e-10 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 59.80 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 51 TKANLFaTLGEGKpagIILSGHTDTVPwdGQdwsvdpLSSTVRDGRLYGRGSADMKA-FIAIALSQaqrFLESDAPFAIH 129
Cdd:PRK00466 51 PDSNSF-ILGEGD---ILLASHVDTVP--GY------IEPKIEGEVIYGRGAVDAKGpLISMIIAA---WLLNEKGIKVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 130 YAFSYDEEVGCFGARELIAdlrdAGVRPLACIVGEPTNMVP-AIAHKGVYRYRCCVRGKEAHSSlTPHSvNAIEMAARVV 208
Cdd:PRK00466 116 VSGLADEESTSIGAKELVS----KGFNFKHIIVGEPSNGTDiVVEYRGSIQLDIMCEGTPEHSS-SAKS-NLIVDISKKI 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1421773316 209 GRVRDMAEGFEReearfdgfdvpfSTASVGQFHGGIADNVVPRDAEFRYEFR 260
Cdd:PRK00466 190 IEVYKQPENYDK------------PSIVPTIIRAGESYNVTPAKLYLHFDVR 229
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
62-295 |
2.31e-09 |
|
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: 58.62 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 62 GKPAGIILS---GHTDTVPWDGQDWSVDPLSSTVRDGRLYGRGSADMKAFIAIaLSQAQRFLESDAP------FAIHYAF 132
Cdd:cd08012 73 GTVDGKTVSfvgSHMDVVTANPETWEFDPFSLSIDGDKLYGRGTTDCLGHVAL-VTELFRQLATEKPalkrtvVAVFIAN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 133 SYDEEVGCFGARELIAD--LRDAGVRPLACIvgEPTNMVPAIAHKGVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGR 210
Cdd:cd08012 152 EENSEIPGVGVDALVKSglLDNLKSGPLYWV--DSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 211 V-RDMAEGF--EREEARFdGFDVPfSTASVGQFH---GGIadNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPA 284
Cdd:cd08012 230 IqKRFYIDFppHPKEEVY-GFATP-STMKPTQWSypgGSI--NQIPGECTICGDCRLTPFYDVKEVREKLEEYVDDINAN 305
|
250
....*....|.
gi 1421773316 285 MQAVSPRAGFT 295
Cdd:cd08012 306 IEELPTRGPVS 316
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
61-366 |
3.99e-09 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 57.83 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 61 EGKPAgIILSGHTDTVPWDGQD-WSVDPLSSTVRDGRLYGRGSADMKA--FIAIALSQAQRFLESDAPFAIHYAFSYDEE 137
Cdd:PRK08201 77 PGKPT-VLIYGHYDVQPVDPLNlWETPPFEPTIRDGKLYARGASDDKGqvFMHLKAVEALLKVEGTLPVNVKFCIEGEEE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 138 VGCFGARELIADLRDAgvrpLAC--IVGEPTNMV----PAIAH--KGVYRYRCCVRGKEA--HSSLTPHSV-NAIEMAAR 206
Cdd:PRK08201 156 IGSPNLDSFVEEEKDK----LAAdvVLISDTTLLgpgkPAICYglRGLAALEIDVRGAKGdlHSGLYGGAVpNALHALVQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 207 VVGRVRD-----MAEGF----------EREEARFDGFDVPFSTASV-----------------------------GQFHG 242
Cdd:PRK08201 232 LLASLHDehgtvAVEGFydgvrpltpeEREEFAALGFDEEKLKRELgvdelfgeegytalertwarptlelngvyGGFQG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 243 GIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMQAVspragfTFEPICEIPSFLGSAGDPVTRLAQRlAG 322
Cdd:PRK08201 312 EGTKTVIPAEAHAKITCRLVPDQDPQEILDLIEAHLQAHTPAGVRV------TIRRFDKGPAFVAPIDHPAIQAAAR-AY 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1421773316 323 EAgttlvAFGTEAGLFKNAGISTVVCGPGSIQQA--------------HQPDEYVSLE 366
Cdd:PRK08201 385 EA-----VYGTEAAFTRMGGSIPVVETFSSQLHIpivlmgfglpsenfHAPNEHFHLE 437
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
13-379 |
7.31e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 57.22 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 13 LVRMNTVSHRSNLE-----LIDFVRTELARLGVKCRLTHDASKTKAnLFATL--GEGKPAgIILSGHTDTVP-WDGQDWS 84
Cdd:PRK07907 27 LVRIPSVAADPFRReevarSAEWVADLLREAGFDDVRVVSADGAPA-VIGTRpaPPGAPT-VLLYAHHDVQPpGDPDAWD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 85 VDPLSSTVRDGRLYGRGSADMKAFIAIALSqAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRDAgVRPLACIVGE 164
Cdd:PRK07907 105 SPPFELTERDGRLYGRGAADDKGGIAMHLA-ALRALGGDLPVGVTVFVEGEEEMGSPSLERLLAEHPDL-LAADVIVIAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 165 PTNM---VPAI--AHKGVYRYRCCVRGKE--AHSSLTPHSV-NAIEMAARVVGRVRD--------------MAEGFEREE 222
Cdd:PRK07907 183 SGNWsvgVPALttSLRGNADVVVTVRTLEhaVHSGQFGGAApDALTALVRLLATLHDedgnvavdgldatePWLGVDYDE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 223 ARF-------DGFDV-------------P------FSTASVGQfhggiADNVVPRDAEFRYEFRDLPTADAARMQAEVVA 276
Cdd:PRK07907 263 ERFradagvlDGVELigtgsvadrlwakPaitvigIDAPPVAG-----ASNALPPSARARLSLRVAPGQDAAEAQDALVA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 277 YARSLEPAMQAVSPRAGFTFEPiceipsFLGSAGDPVTRLAQRLAGEA-GTTLVAFG---------TEAGLFKNAGIS-T 345
Cdd:PRK07907 338 HLEAHAPWGAHVTVERGDAGQP------FAADASGPAYDAARAAMREAwGKDPVDMGmggsipfiaELQEAFPQAEILvT 411
|
410 420 430
....*....|....*....|....*....|....*...
gi 1421773316 346 VVCGPGSiqQAHQPDEYVSLEQLAR---CEA-FMRGLA 379
Cdd:PRK07907 412 GVEDPKT--RAHSPNESVHLGELERaavAEAlLLARLA 447
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
56-368 |
7.81e-09 |
|
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: 56.87 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 56 FATLGEGKPA-GIIlsGHTDTVPwDGQDWSVDPLSSTVRDGRLYGRGSAD-----MKAFIA--------IALSQAQRFL- 120
Cdd:cd03888 64 YAEYGEGEEVlGIL--GHLDVVP-AGEGWTTDPFKPVIKDGKLYGRGTIDdkgptIAALYAlkilkdlgLPLKKKIRLIf 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 121 ----ES---------------------DAPFAIHYAfsydeEVGCFGAReLIADLRDAGVRPLACI-VGEPTNMVP---- 170
Cdd:cd03888 141 gtdeETgwkciehyfeheeypdfgftpDAEFPVING-----EKGIVTVD-LTFKIDDDKGYRLISIkGGEATNMVPdkae 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 171 -----------AIAHKGVYRYRC---------CVRGKEAHSSlTPH-SVNAI----------EMAARVVGRVRDMAEgFE 219
Cdd:cd03888 215 avipgkdkeelALSAATDLKGNIeiddggvelTVTGKSAHAS-APEkGVNAItllakflaelNKDGNDKDFIKFLAK-NL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 220 REEARFDGFDVPFS-------TASVGQFhgGIADNVVprdaEFRYEFRDLPTADAARMQAEvvayarsLEPAMQavspRA 292
Cdd:cd03888 293 HEDYNGKKLGINFEdevmgelTLNPGII--TLDDGKL----ELGLNVRYPVGTSAEDIIKQ-------IEEALE----KY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 293 GFTFEPICEIPSFLGSAGDPV----TRLAQRLAGEAGTTLV-AFGTEAGLFKNAgistVVCG---PGSIQQAHQPDEYVS 364
Cdd:cd03888 356 GVEVEGHKHQKPLYVPKDSPLvktlLKVYEEQTGKEGEPVAiGGGTYARELPNG----VAFGpefPGQKDTMHQANEFIP 431
|
....
gi 1421773316 365 LEQL 368
Cdd:cd03888 432 IDDL 435
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
27-153 |
3.94e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 54.92 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 27 LIDFVRTELARLGVKCRLTHDASKTKAN-LFATLGEGKPAGIILS-GHTDTVPWDGQDWS--VDPLSSTVRDGRLYGRGS 102
Cdd:PRK07079 46 LTDEIAPALAALGFTCRIVDNPVAGGGPfLIAERIEDDALPTVLIyGHGDVVRGYDEQWRegLSPWTLTEEGDRWYGRGT 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1421773316 103 ADMKAFIAI---ALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRDA 153
Cdd:PRK07079 126 ADNKGQHTInlaALEQVLAARGGRLGFNVKLLIEMGEEIGSPGLAEVCRQHREA 179
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
27-153 |
8.49e-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: 349928 [Multi-domain] Cd Length: 448 Bit Score: 53.66 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 27 LIDFVRTELARLGVKCRLTHDASKTKAN-LFATLGEGKPAGIILS-GHTDTVPWDGQDW--SVDPLSSTVRDGRLYGRGS 102
Cdd:cd05679 33 LDQEMRPRFERLGFTVHIHDNPVAGRAPfLIAERIEDPSLPTLLIyGHGDVVPGYEGRWrdGRDPWTVTVWGERWYGRGT 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1421773316 103 ADMKAFIAI---ALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRDA 153
Cdd:cd05679 113 ADNKGQHSInmaALRQVLEARGGKLGFNVKFLIEMGEEMGSPGLRAFCFSHREA 166
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
8-152 |
2.04e-07 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 52.73 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 8 SLAQaLVRMNTVS-HRSNLELID------FVRTELARLGVK-CRLTHDASKTKANLFATLG----EGKPAGIILSGHTDT 75
Cdd:cd05677 4 TLSE-FIAFQTVSqSPTTENAEDsrrcaiFLRQLFKKLGATnCLLLPSGPGTNPIVLATFSgnssDAKRKRILFYGHYDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 76 VPWDGQD-WSVDPLSSTVRDGRLYGRGSADMK-----AFIAIALSQAQRFLESDAPFAIHyafsYDEEVGCFGARELIAD 149
Cdd:cd05677 83 IPAGETDgWDTDPFTLTCENGYLYGRGVSDNKgpllaAIYAVAELFQEGELDNDVVFLIE----GEEESGSPGFKEVLRK 158
|
...
gi 1421773316 150 LRD 152
Cdd:cd05677 159 NKE 161
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
54-221 |
2.97e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 52.16 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 54 NLFATL-GEGK-PAGIILSGHTDTV------PWdgQDWSVDP-----------LSSTVRD----GR-LYGRGSADMKAFI 109
Cdd:COG4187 67 NVTALVkGKGEsKKTVILISHFDVVdvedygSL--KPLAFDPeeltealkeikLPEDVRKdlesGEwLFGRGTMDMKAGL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 110 AIALSQAQRFLESDApFAIHYAFSY--DEEV---GCFGARELIADLRDA-GVRPLACIVGEPT-NMVPAIAHKGVYR--- 179
Cdd:COG4187 145 ALHLALLEEASENEE-FPGNLLLLAvpDEEVnsaGMRAAVPLLAELKEKyGLEYKLAINSEPSfPKYPGDETRYIYTgsi 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1421773316 180 -------YrccVRGKEAHSSLTPHSVNAIEMAARVVGRVR---DMAEGFERE 221
Cdd:COG4187 224 gklmpgfY---CYGKETHVGEPFSGLNANLLASELTRELElnpDFCEEVGGE 272
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
61-378 |
5.39e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 50.94 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 61 EGKPaGIILSGHTDTVPWDGqdwSVDPLSSTVRDGRLYGRGSADMKAFIAIALsQAQRFLESDA---PFAIHYAFSYDEE 137
Cdd:PRK07473 73 QGEP-GILIAGHMDTVHPVG---TLEKLPWRREGNKCYGPGILDMKGGNYLAL-EAIRQLARAGittPLPITVLFTPDEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 138 VGCFGARELIADLRDAGVRPLACIVGEPTNMVpAIAHKGVYRYRCCVRGKEAHSSLTPHS-VNAIEMAARVVGRVRDMAe 216
Cdd:PRK07473 148 VGTPSTRDLIEAEAARNKYVLVPEPGRPDNGV-VTGRYAIARFNLEATGRPSHAGATLSEgRSAIREMARQILAIDAMT- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 217 gfereearfdGFDVPFstaSVGQFHGGIADNVVPRDAefryefrdlpTADA---ARMQAEV-VAYARSLepAMQAVSPRA 292
Cdd:PRK07473 226 ----------TEDCTF---SVGIVHGGQWVNCVATTC----------TGEAlsmAKRQADLdRGVARML--ALSGTEDDV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 293 GFTFEPICEIPSFLGSAGD-PVTRLAQRLAGEAGTTL---VAFGTEAGLFKNA-GISTV----VCGPGsiqqAHQPDEYV 363
Cdd:PRK07473 281 TFTVTRGVTRPVWEPDAGTmALYEKARAIAGQLGLSLphgSAGGGSDGNFTGAmGIPTLdglgVRGAD----YHTLNEHI 356
|
330
....*....|....*
gi 1421773316 364 SLEQLARCEAFMRGL 378
Cdd:PRK07473 357 EVDSLAERGRLMAGL 371
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
57-106 |
7.32e-07 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 50.99 E-value: 7.32e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 57 ATLGEGKPA-GIIlsGHTDTVPwDGQDWSVDPLSSTVRDGRLYGRGSADMK 106
Cdd:PRK07318 73 IEYGEGEEVlGIL--GHLDVVP-AGDGWDTDPYEPVIKDGKIYARGTSDDK 120
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
30-152 |
1.32e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 50.14 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 30 FVRTELARLGVKCRLThdasKTKAN--LFATLGEGKPAGIILSGHTDTVPWDGQD-WSVDPLSSTVRDGRLYGRGSADMK 106
Cdd:PRK06446 30 YLKDTMEKLGIKANIE----RTKGHpvVYGEINVGAKKTLLIYNHYDVQPVDPLSeWKRDPFSATIENGRIYARGASDNK 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1421773316 107 A-FIAIALSQAQRFLESDAPFAIHYAFSYDEEVGCFGARELIADLRD 152
Cdd:PRK06446 106 GtLMARLFAIKHLIDKHKLNVNVKFLYEGEEEIGSPNLEDFIEKNKN 152
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
4-221 |
1.27e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 46.95 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 4 DHALSLAQALVRMNTVSH-RSNLELIDFVRTELARLG--------VKCRLTHDASKTKaNLFAtLGEGKPAG---IILSG 71
Cdd:cd05654 1 ERLEQLLKSLVSWPSVTGtEGERSFADFLKEILKELPyfkenpshVWQLLPPDDLGRR-NVTA-LVKGKKPSkrtIILIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 72 HTDTVPWDG----QDWSVDP--LSSTV------------RDGR----LYGRGSADMKAFIAIALSQAQRFLES-DAPFAI 128
Cdd:cd05654 79 HFDTVGIEDygelKDIAFDPdeLTKAFseyveeldeevrEDLLsgewLFGRGTMDMKSGLAVHLALLEQASEDeDFDGNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 129 HYAFSYDEEVGCFGARELIADL----RDAGVRPLACIVGEP-TNMVPAIAHKGVY-----RYRCC--VRGKEAHSSLTPH 196
Cdd:cd05654 159 LLMAVPDEEVNSRGMRAAVPALlelkKKHDLEYKLAINSEPiFPQYDGDQTRYIYtgsigKILPGflCYGKETHVGEPFA 238
|
250 260
....*....|....*....|....*...
gi 1421773316 197 SVNAIEMAARVVGRVR---DMAEGFERE 221
Cdd:cd05654 239 GINANLMASEITARLElnaDLCEKVEGE 266
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
184-287 |
1.30e-05 |
|
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: 46.65 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 184 VRGKEAHSSlTPH-SVNAIEMAARVVGRV-----RdmaegfereeaRFDgfdvPFSTA--SVGQFHGGIADNVVPRDAEF 255
Cdd:COG1473 190 IKGKGGHAA-APHlGIDPIVAAAQIVTALqtivsR-----------NVD----PLDPAvvTVGIIHGGTAPNVIPDEAEL 253
|
90 100 110
....*....|....*....|....*....|..
gi 1421773316 256 RYEFRDLPTADAARMQAEVVAYARSLEPAMQA 287
Cdd:COG1473 254 EGTVRTFDPEVRELLEERIERIAEGIAAAYGA 285
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
163-282 |
1.02e-04 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 44.12 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 163 GEPTNMVPAIAhkGVYRYRCCVRGKEAHSSLTPHSV--NAIEMAARVVGRVRDMAEGFEREearfdgfdvpfSTASVGQF 240
Cdd:PRK12890 204 GLPIGVVTAIQ--GIRRQAVTVEGEANHAGTTPMDLrrDALVAAAELVTAMERRARALLHD-----------LVATVGRL 270
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1421773316 241 H-GGIADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLE 282
Cdd:PRK12890 271 DvEPNAINVVPGRVVFTLDLRSPDDAVLEAAEAALLAELEAIA 313
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
29-276 |
1.11e-04 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 43.85 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 29 DFVRTELARLGVKCRltHDASKTkaNLFATLGEGKPAGIILSGHTDTVP-WDGQDWsvdPLSSTVrDGRLYGRGS---AD 104
Cdd:cd08017 23 ALIRRELDALGIPYR--YPVAKT--GIVATIGSGSPPVVALRADMDALPiQELVEW---EHKSKV-DGKMHACGHdahVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 105 MKAFIAIALSQAQRFLesdaPFAIHYAFSYDEEVGCfGARELIadlRDAGVRPLACIVG------EPTNMVPAIA---HK 175
Cdd:cd08017 95 MLLGAAKLLKARKHLL----KGTVRLLFQPAEEGGA-GAKEMI---KEGALDDVEAIFGmhvspaLPTGTIASRPgpfLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 176 GVYRYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEgfeREEARFDGFDVpfstaSVGQFHGGIADNVVPRDAEF 255
Cdd:cd08017 167 GAGRFEVVIRGKGGHAAMPHHTVDPVVAASSAVLALQQLVS---RETDPLDSQVV-----SVTRFNGGHAFNVIPDSVTF 238
|
250 260
....*....|....*....|....
gi 1421773316 256 RYEFRDLPTADAARMQ---AEVVA 276
Cdd:cd08017 239 GGTLRALTTEGFYRLRqriEEVIE 262
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
132-296 |
1.57e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. 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. 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 in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 43.48 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 132 FSYDEEVGCfGARELIAD-LRDAGVRPLAC----IVGEPTNMV---PAIAHKGVYRYRCCVRGKEAHSSlTPH-SVNAIE 202
Cdd:cd05664 129 FQPAEETGG-GAQAMVDDgLYDKIPKPDVVlaqhVMPGPAGTVgtrPGRFLSAADSLDITIFGRGGHGS-MPHlTIDPVV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 203 MAARVVGRVRDMAEgfeREEARFDgfdvpFSTASVGQFHGGIADNVVPRDAEFRYEFRdlpTADAA---RMQAEVVAYAR 279
Cdd:cd05664 207 MAASIVTRLQTIVS---REVDPQE-----FAVVTVGSIQAGSAENIIPDEAELKLNVR---TFDPEvreKVLNAIKRIVR 275
|
170
....*....|....*..
gi 1421773316 280 SlEPAMQAVSPRAGFTF 296
Cdd:cd05664 276 A-ECAASGAPKPPEFTY 291
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
29-279 |
1.59e-04 |
|
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: 43.28 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 29 DFVRTELARLGvkCRLTHDASktkANLFATL-GEGKPAGIILSG-HTDTVP----WDGqdwsvdPLsstvrdGRLYGrgs 102
Cdd:cd03884 33 DLFVEWMEEAG--LSVRVDAV---GNLFGRLeGTDPDAPPVLTGsHLDTVPnggrYDG------IL------GVLAG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 103 admkafIAIALSQAQRFLESDAPFAIhYAFSyDEE-----VGCFGAR--------ELIADLRDA-GV------------- 155
Cdd:cd03884 93 ------LEALRALKEAGIRPRRPIEV-VAFT-NEEgsrfpPSMLGSRafagtldlEELLSLRDAdGVslaealkaigydg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 156 ---------RPLACIV-------------GEPTNMVPAIAhkGVYRYRCCVRGKEAHSSLTPHS--VNAIEMAARVVGRV 211
Cdd:cd03884 165 drpasarrpGDIKAYVelhieqgpvleeeGLPIGVVTGIA--GQRWLEVTVTGEAGHAGTTPMAlrRDALLAAAELILAV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1421773316 212 RDMAEGFEREearfdgfdvpfSTASVGQFH---GGIadNVVPRDAEFRYEFRDLPTADAARMQAEVVAYAR 279
Cdd:cd03884 243 EEIALEHGDD-----------LVATVGRIEvkpNAV--NVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAE 300
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
163-298 |
1.72e-04 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 43.33 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 163 GEPTNMVPAIAhkGVYRYRCCVRGKEAHSSLTP--HSVNAIEMAARVVGRVRDMAegfereeARFDgfdvPFSTASVGQF 240
Cdd:PRK12893 202 GLPIGVVTGIQ--GIRWLEVTVEGQAAHAGTTPmaMRRDALVAAARIILAVERIA-------AALA----PDGVATVGRL 268
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1421773316 241 ---HGGIadNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARSLEPAMQ-AVSPRAGFTFEP 298
Cdd:PRK12893 269 rvePNSR--NVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGvQVTVETVWDFPP 328
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
184-262 |
3.78e-04 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 42.20 E-value: 3.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1421773316 184 VRGKEAHSSLTPHSVNAIEMAARVVGRVRDMaegFEREEARFDGFDVpfstaSVGQFHGGIADNVVPRDAEFRYEFRDL 262
Cdd:cd03886 178 VKGKGGHGASPHLGVDPIVAAAQIVLALQTV---VSRELDPLEPAVV-----TVGKFHAGTAFNVIPDTAVLEGTIRTF 248
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
179-298 |
4.43e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349917 [Multi-domain] Cd Length: 403 Bit Score: 38.95 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 179 RYRCCVRGKEAHSSLTPHSVNAIEMAARVVGRVRDMAEgfereeARFDGFDVPfSTASVGQFHGGIADNVVPRDAEF--- 255
Cdd:cd05667 197 RFRITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTIIS------RRIDLTKEP-AVISIGKINGGTRGNIIPEDAEMvgt 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1421773316 256 --------RYE-FRDLPT-----ADAARMQAEVV------------AYARSLEPAMQAVSPRAGFTFEP 298
Cdd:cd05667 270 irtfdpemREDiFARLKTiaehiAKAYGATAEVEfangypvtyndpALTAKMLPTLQKAVGKADLVVLP 338
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
107-254 |
5.16e-03 |
|
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: 38.79 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 107 AFIAIALSQAQRFLESDAPFA--IHYAFSYDEEVGCFGARELIadlrDAGVRP-------LACIVGEPTNMV---PAIAH 174
Cdd:cd08021 103 GHTAMLLGAAKVLAENKDEIKgtVRFIFQPAEEVPPGGAKPMI----EAGVLEgvdavfgLHLWSTLPTGTIavrPGAIM 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 175 KGVYRYRCCVRGKEAHSSlTPH-SVNAIEMAARVVGRV-----RDMaegfereearfDGFDVPfsTASVGQFHGGIADNV 248
Cdd:cd08021 179 AAPDEFDITIKGKGGHGS-MPHeTVDPIVIAAQIVTALqtivsRRV-----------DPLDPA--VVTIGTFQGGTSFNV 244
|
....*.
gi 1421773316 249 VPRDAE 254
Cdd:cd08021 245 IPDTVE 250
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
66-113 |
8.23e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 38.03 E-value: 8.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1421773316 66 GIILsgHTDTVPWDGQDW-----SVDPLSSTVRDGRLYGRGSADMKAFIAIAL 113
Cdd:PRK06156 113 GILT--HADVVPANPELWvldgtRLDPFKVTLVGDRLYGRGTEDDKGAIVTAL 163
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
163-280 |
9.38e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 37.76 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773316 163 GEPTNMVPAIAhkGVYRYRCCVRGKEAHSSLTPHSV--NAIEMAARVVGRVrdmaegfereEARFDGFDVPfSTASVGQF 240
Cdd:PRK12892 203 GLPVGVVTGIV--GIWQYRITVTGEAGHAGTTPMALrrDAGLAAAEMIAAI----------DEHFPRVCGP-AVVTVGRV 269
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1421773316 241 H---GgiADNVVPRDAEFRYEFRDLPTADAARMQAEVVAYARS 280
Cdd:PRK12892 270 AldpG--SPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCRE 310
|
|
| |
