|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
1-448 |
0e+00 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 773.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 1 MKEQIKEKVnslQDEMISSIQESVKIPSVISEATENCPFGENVDKALRGILDLCKSLGFKT-VYKDGYYGYAEIGQGEKM 79
Cdd:PRK07205 1 MKSYITEKV---QDACVAAIKTLVSYPSVLNEGENGTPFGQAIQDVLEATLDLCQGLGFKTyLDPKGYYGYAEIGQGEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 80 IGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRCI 159
Cdd:PRK07205 78 LAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEETLWRCM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 160 NKYKENnEEIPNYGFTPDSRFPITNAEKGLLQVHLTCDSKSDIELSVGKALNAVPGKAIYIGKYSDKLKKELDKLNFEYT 239
Cdd:PRK07205 158 NRYNEV-EEQATMGFAPDSSFPLTYAEKGLLQAKLVGPGSDQLELEVGQAFNVVPAKASYQGPKLEAVKKELDKLGFEYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 240 VEGNKICIIGKSVHSAASDTGINAVARLCIALNNIGiDSNIIKFLAEVIGEDANGNNIIPNCKDDVSGKLTVNIGRVTID 319
Cdd:PRK07205 237 VKENEVTVLGKSVHAKDAPQGINAVIRLAKALVVLE-PHPALDFLANVIGEDATGLNIFGDIEDEPSGKLSFNIAGLTIT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 320 NEKEFAGIDVRIPVTYKKDDFVKELKKMTDKYNLNYEEYDFLDSIYVPEDTLLVKTLRKVYEEETGLDGTPLSSGGATYA 399
Cdd:PRK07205 316 KEKSEIRIDIRIPVLADKEKLVQQLSQKAQEYGLTYEEFDYLAPLYVPLDSELVSTLMSVYQEKTGDDSPAQSSGGATFA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489530539 400 RALDNCVAFGAIFPGKPETEHQANEYLIVEDIIKATQIYALSIYELLKI 448
Cdd:PRK07205 396 RTMPNCVAFGALFPGAPQTEHQANEHIVLEDLYRAMDIYAEAIYRLTTD 444
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
7-445 |
0e+00 |
|
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: 588.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 7 EKVNSLQDEMISSIQESVKIPSVISEATENCPFGENVDKALRGILDLCKSLGFKTVYKDGYYGYAEIGQGEKMIGILGHV 86
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVRDEATEGAPFGEGPRKALDKFLDLAKRLGFKTKNIDNYAGYAEYGEGEEVLGILGHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 87 DVVPEGdlESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRCINKYKENn 166
Cdd:cd03888 81 DVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGWKCIEHYFEH- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 167 EEIPNYGFTPDSRFPITNAEKGLLQVHLTCDSKSD-----IELSVGKALNAVPGKAIYIGKYSDKLKKELD-----KLNF 236
Cdd:cd03888 158 EEYPDFGFTPDAEFPVINGEKGIVTVDLTFKIDDDkgyrlISIKGGEATNMVPDKAEAVIPGKDKEELALSaatdlKGNI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 237 EYTVEGNKICIIGKSVHSAASDTGINAVARLCIALNNI---GIDSNIIKFLAEVIGEDANGNNIIPNCKDDVSGKLTVNI 313
Cdd:cd03888 238 EIDDGGVELTVTGKSAHASAPEKGVNAITLLAKFLAELnkdGNDKDFIKFLAKNLHEDYNGKKLGINFEDEVMGELTLNP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 314 GRVTIDNEKEFAGIDVRIPVTYKKDDFVKELKKMTDKYNLNYEEYDFLDSIYVPEDTLLVKTLRKVYEEETGLDGTPLSS 393
Cdd:cd03888 318 GIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGHKHQKPLYVPKDSPLVKTLLKVYEEQTGKEGEPVAI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489530539 394 GGATYARALDNCVAFGAIFPGKPETEHQANEYLIVEDIIKATQIYALSIYEL 445
Cdd:cd03888 398 GGGTYARELPNGVAFGPEFPGQKDTMHQANEFIPIDDLIKALAIYAEAIYEL 449
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
1-447 |
2.67e-159 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 458.15 E-value: 2.67e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 1 MKEQIKEKVNSLQDEMISSIQESVKIPSVISE--ATENCPFGENVDKALRGILDLCKSLGFKTVYKDGYYGYAEIGQGEK 78
Cdd:PRK07318 1 MTIDWKKEVEKRKDDLIEDLQELLRINSVRDDskAKEGAPFGPGPVKALEKFLEIAERDGFKTKNVDNYAGHIEYGEGEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 79 MIGILGHVDVVPEGDleSWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRC 158
Cdd:PRK07318 81 VLGILGHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEESGWKC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 159 INKYKENnEEIPNYGFTPDSRFPITNAEKG---LLQVHLTCDSKSDIEL---SVGKALNAVPG--KAIYIGKYSDKLKKE 230
Cdd:PRK07318 159 MDYYFEH-EEAPDFGFSPDAEFPIINGEKGittFDLVHFEGENEGDYVLvsfKSGLRENMVPDsaEAVITGDDLDDLIAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 231 LD------KLNFEYTVEGN--KICIIGKSVHSAASDTGINAVARLCIALNNIGIDS---NIIKFLAEVIGEDANGNNIIP 299
Cdd:PRK07318 238 FEaflaenGLKGELEEEGGklVLTVIGKSAHGSTPEKGVNAATYLAKFLNQLNLDGdakAFLDFAAEYLHEDTRGEKLGI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 300 NCKDDVSGKLTVNIGRVTIDNEKEFA-GIDVRIPVTYKKDDFVKELKKMTDKYNLNYEEYDFLDSIYVPEDTLLVKTLRK 378
Cdd:PRK07318 318 AYEDDVMGDLTMNVGVFSFDEEKGGTlGLNFRYPVGTDFEKIKAKLEKLIGVTGVELSEHEHQKPHYVPKDDPLVKTLLK 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489530539 379 VYEEETGLDGTPLSSGGATYARALDNCVAFGAIFPGKPETEHQANEYLIVEDIIKATQIYALSIYELLK 447
Cdd:PRK07318 398 VYEKQTGLKGEEQVIGGGTYARLLKRGVAFGAMFPGSEDTMHQANEYIEIDDLIKAAAIYAEAIYELAK 466
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
13-442 |
1.05e-155 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 448.37 E-value: 1.05e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 13 QDEMISSIQESVKIPSV--ISEATENCPFGENVDKALRGILDLCKSLGFKTVYKDGYYGYAEIGQGEKMIGILGHVDVVP 90
Cdd:TIGR01887 1 KDEILEDLKELIAIDSVedLEKAKEGAPFGEGPRKALDKFLEIAKRDGFTTENVDNYAGYIEYGQGEEVLGILGHLDVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 91 EGDleSWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRCINKYKENnEEIP 170
Cdd:TIGR01887 81 AGD--GWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGWKCIDYYFEH-EEMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 171 NYGFTPDSRFPITNAEKG--LLQVHLTCDSKSDIEL---SVGKALNAVP--GKAIYIGKYS---DKLKKELDK---LNFE 237
Cdd:TIGR01887 158 DIGFTPDAEFPIIYGEKGitTLEIKFKDDTEGDVVLesfKAGEAYNMVPdhATAVISGKKLtevEQLKFVFFIakeLEGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 238 YTVEGN--KICIIGKSVHSAASDTGINAVARLCIALNNI---GIDSNIIKFLAEVIGEDANGNNIIPNCKDDVSGKLTVN 312
Cdd:TIGR01887 238 FEVNDGtlTITLEGKSAHGSAPEKGINAATYLALFLAQLnlaGGAKAFLQFLAEYLHEDHYGEKLGIKFHDDVSGDLTMN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 313 IGRVTIDN-EKEFAGIDVRIPVTYKKDDFVKELkkMTDKYNLNYEEYD-FLDSIYVPEDTLLVKTLRKVYEEETGLDGTP 390
Cdd:TIGR01887 318 VGVIDYENaEAGLIGLNVRYPVGNDPDTMLKNE--LAKESGVVEVTLNgYLKPLYVPKDDPLVQTLMKVYEKQTGDEGEP 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489530539 391 LSSGGATYARALDNCVAFGAIFPGKPETEHQANEYLIVEDIIKATQIYALSI 442
Cdd:TIGR01887 396 VAIGGGTYARLMPNGVAFGALFPGEEDTMHQANEYIMIDDLLLATAIYAEAI 447
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
3-447 |
9.68e-57 |
|
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: 192.02 E-value: 9.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 3 EQIKEKVNSLQDEMISSIQESVKIPSViseatencPFGEnvDKALRGILDLCKSLGFKTVYKDGYYG----YAEI--GQG 76
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSV--------SGEE--AAAAELLAELLEALGFEVERLEVPPGrpnlVARRpgDGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 77 EKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE--- 153
Cdd:COG0624 71 GPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEvgs 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 154 -NLWRCINKYKEnneeipnyGFTPD-------SRFP-ITNAEKGLLQVHLTcdsksdielsvgkalnavpgkaiyigkys 224
Cdd:COG0624 151 pGARALVEELAE--------GLKADaaivgepTGVPtIVTGHKGSLRFELT----------------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 225 dklkkeldklnfeytvegnkicIIGKSVHSAASDTGINAVARLCialnnigidsniiKFLAEVIGEDANGNniipncKDD 304
Cdd:COG0624 194 ----------------------VRGKAAHSSRPELGVNAIEALA-------------RALAALRDLEFDGR------ADP 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 305 VSGKLTVNIGRV---TIDN---EKEFAGIDVRIPVTYKKDDFVKELKKMTDKYNLNYE-EYDFLDSIY----VPEDTLLV 373
Cdd:COG0624 233 LFGRTTLNVTGIeggTAVNvipDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEvEVEVLGDGRppfeTPPDSPLV 312
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489530539 374 KTLRKVYEEETGLDGTPLSSGGAT----YARALD-NCVAFGaifPGKPETEHQANEYLIVEDIIKATQIYALSIYELLK 447
Cdd:COG0624 313 AAARAAIREVTGKEPVLSGVGGGTdarfFAEALGiPTVVFG---PGDGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
13-438 |
4.13e-52 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 183.25 E-value: 4.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 13 QDEMISSIQESVKIPSViseATENCPFGENvdKALRGILDLCKSL--GFKTVYKDGYYGYAEI---GQGEKMIGILGHVD 87
Cdd:PRK06156 45 GAAAIESLRELVAFPTV---RVEGVPQHEN--PEFIGFKKLLKSLarDFGLDYRNVDNRVLEIglgGSGSDKVGILTHAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 88 VVPeGDLESWNYP-----PFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRCINKY 162
Cdd:PRK06156 120 VVP-ANPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEETDGDPLKYY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 163 KENNeEIPNYGFTPDSRFPITNAEKGLLQVHLT-CDSKSD------IELSVGKALNAVPGKAIYI--------------G 221
Cdd:PRK06156 199 LERY-TPPDYNITLDAEYPVVTAEKGWGTIMATfPKRAADgkgaeiVAMTGGAFANQIPQTAVATlsggdpaalaaalqA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 222 KYSDKLKKELDKLNFEYTVEGN--KICIIGKSVHSAASDTGINAVARLCIALNNIGID------SNIIKFLAEVIGEDAN 293
Cdd:PRK06156 278 AAAAQVKRHGGGFSIDFKRDGKdvTITVTGKSAHSSTPESGVNPVTRLALFLQSLDGDlphnhaADAARYINDLVGLDYL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 294 GNNIIPNCKDDVSGKLTVNIGRVTIDNEKEFAGIDVRIPVTYKKDDFVKE----LKKMTDKYNLNYE-EYDFLDSIYVPE 368
Cdd:PRK06156 358 GEKFGVAYKDDFMGPLTLSPTVVGQDDKGTEVTVNLRRPVGKTPELLKGEiadaLAAWQAKHQVALDiDYYWGEPMVRDP 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 369 DTLLVKTLRKVYEEETGLDGTPLSSGGATYARALDNCVAFGAIFPGKPETEHQANEYLIVEDIIKATQIY 438
Cdd:PRK06156 438 KGPWLKTLLDVFGHFTGLDAKPVAIAGSTNAKLFPNAVSFGPAMPGVKYTGHTENEFKTVEQFMLDLQMY 507
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-439 |
1.21e-40 |
|
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: 148.60 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 21 QESVKIPSViseateNCPFGENVDKalrgILDLCKSLGFK---TVYKDGYYGYAEIGQG-EKMIGILGHVDVVPEGDLES 96
Cdd:cd08659 4 QDLVQIPSV------NPPEAEVAEY----LAELLAKRGYGiesTIVEGRGNLVATVGGGdGPVLLLNGHIDTVPPGDGDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 97 WNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRCINKYKEnneeipnYGFTP 176
Cdd:cd08659 74 WSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLE-------AGYAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 177 D---------SRFPITNAEKGllQVHLTCDSKsdielsvgkalnavpgkaiyigkysdklkkeldklnfeytvegnkici 247
Cdd:cd08659 147 RldalivgepTGLDVVYAHKG--SLWLRVTVH------------------------------------------------ 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 248 iGKSVHSAASDTGINAVARLcialnnigidsniIKFLAEVIGEDANgnniIPncKDDVSGKLTVNIGRV-------TIDN 320
Cdd:cd08659 177 -GKAAHSSMPELGVNAIYAL-------------ADFLAELRTLFEE----LP--AHPLLGPPTLNVGVInggtqvnSIPD 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 321 EKEFAgIDVRIPVTYKKDDFVKELKKMTDKYNLNYE-EYDF--LDSIYVPEDTLLVKTLRKVYEEETGlDGTPLSSGGAT 397
Cdd:cd08659 237 EATLR-VDIRLVPGETNEGVIARLEAILEEHEAKLTvEVSLdgDPPFFTDPDHPLVQALQAAARALGG-DPVVRPFTGTT 314
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489530539 398 ----YARALD-NCVAFGaifPGKPETEHQANEYLIVEDIIKATQIYA 439
Cdd:cd08659 315 dasyFAKDLGfPVVVYG---PGDLALAHQPDEYVSLEDLLRAAEIYK 358
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
29-437 |
8.56e-38 |
|
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: 141.38 E-value: 8.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 29 VISEATENCPfGENVDKALRGILDLCKSLGFKT----VYKD-----GYYGYAEIGQG-EKMIGILGHVDVVPEGDLESWN 98
Cdd:TIGR01910 7 LISIPSVNPP-GGNEETIANYIKDLLREFGFSTdvieITDDrlkvlGKVVVKEPGNGnEKSLIFNGHYDVVPAGDLELWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 99 YPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEEN-----LWRCINKYKENneeiPNYG 173
Cdd:TIGR01910 86 TDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESgeagtLYLLQRGYFKD----ADGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 174 FTPD-SRFP-ITNAEKGLLQVHLTcdsksdielsvgkalnavpgkaiyigkysdklkkeldklnfeytvegnkicIIGKS 251
Cdd:TIGR01910 162 LIPEpSGGDnIVIGHKGSIWFKLR---------------------------------------------------VKGKQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 252 VHSAASDTGINAV---ARLCIALNNIGIDSNIIKfLAEVIGEDANGNNIIPNCKDDVSgkltvnigrvTIDNEKEFAgID 328
Cdd:TIGR01910 191 AHASFPQFGVNAImklAKLITELNELEEHIYARN-SYGFIPGPITFNPGVIKGGDWVN----------SVPDYCEFS-ID 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 329 VRIPVTYKKDDFVKELKKMTDKYN----LNYE---EYDFLDSIYVPEDTLLVKTLRKVYEEETGLDGTPLSSGGATYARA 401
Cdd:TIGR01910 259 VRIIPEENLDEVKQIIEDVVKALSksdgWLYEnepVVKWSGPNETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARF 338
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 489530539 402 LDN----CVAFGaifPGKPETEHQANEYLIVEDIIKATQI 437
Cdd:TIGR01910 339 LRKagipSIVYG---PGDLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
11-447 |
2.39e-37 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 140.51 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 11 SLQDEMISSIQESVKIPSVIseatencPFGENVDKALRGILDLCKSLGFKT-------VYKDGYYGY-----AEIGQGEK 78
Cdd:PRK08651 3 AMMFDIVEFLKDLIKIPTVN-------PPGENYEEIAEFLRDTLEELGFSTeiievpnEYVKKHDGPrpnliARRGSGNP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 79 MIGILGHVDVVPEGDLESwNYPPFEAVLEDGKLYGRGTQDDKGPtISAIYAvkALMDLNVDFNKRIRFIFGADEENLwrc 158
Cdd:PRK08651 76 HLHFNGHYDVVPPGEGWS-VNVPFEPKVKDGKVYGRGASDMKGG-IAALLA--AFERLDPAGDGNIELAIVPDEETG--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 159 inkykenneeipnygftpdsrfpitnaEKGLLQVHLTCDSKSDIelsvgkALNAVPG--KAIYIGKysdklkkeldKLNF 236
Cdd:PRK08651 149 ---------------------------GTGTGYLVEEGKVTPDY------VIVGEPSglDNICIGH----------RGLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 237 EYTVEgnkicIIGKSVHSAASDTGINAVARLcialnnigidSNIIKFLAEVIGEDANGNNIIpnckDDVSGKLTVNIGRV 316
Cdd:PRK08651 186 WGVVK-----VYGKQAHASTPWLGINAFEAA----------AKIAERLKSSLSTIKSKYEYD----DERGAKPTVTLGGP 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 317 TI-----DN----EKEFaGIDVRIPVTYKKDDFVKELKK------MTDKYNLNYEEYDFLDSIYVPEDTLLVKTLRKVYE 381
Cdd:PRK08651 247 TVeggtkTNivpgYCAF-SIDRRLIPEETAEEVRDELEAlldevaPELGIEVEFEITPFSEAFVTDPDSELVKALREAIR 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 382 EETGLDGTPLSSGGATYARALDN----CVAFGaifPGKPETEHQANEYLIVEDIIKATQIYALSIYELLK 447
Cdd:PRK08651 326 EVLGVEPKKTISLGGTDARFFGAkgipTVVYG---PGELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-442 |
3.73e-36 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 136.36 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 21 QESVKIPSViseatenCPFGENVDKALRGILDLCKSLGFKTVY----KDGYYGYAEI--GQGEKMIGILGHVDVVPEGDL 94
Cdd:cd08011 5 QELVQIPSP-------NPPGDNTSAIAAYIKLLLEDLGYPVELheppEEIYGVVSNIvgGRKGKRLLFNGHYDVVPAGDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 95 ESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRCINKY-KENNEEIPNYG 173
Cdd:cd08011 78 EGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYlLEKVRIKPNDV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 174 -FTPDSRFP-ITNAEKGLLQVhltcdsksdielsvgkalnavpgkaiyigkysdklkkeldklnfeytvegnKICIIGKS 251
Cdd:cd08011 158 lIGEPSGSDnIRIGEKGLVWV---------------------------------------------------IIEITGKP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 252 VHSAASDTGINAVARLcialnnigidSNIIKFLAEVIGEDANGNniipnckddVSGKLTVNigrvTIDNEKEFAgIDVRI 331
Cdd:cd08011 187 AHGSLPHRGESAVKAA----------MKLIERLYELEKTVNPGV---------IKGGVKVN----LVPDYCEFS-VDIRL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 332 PVTYKKDDFVKELKKMTDKY-NLNYEEYDFLDSIYVPEDTLLVKTLRKVYEEETGLDGTPLSSGGATYARALDN----CV 406
Cdd:cd08011 243 PPGISTDEVLSRIIDHLDSIeEVSFEIKSFYSPTVSNPDSEIVKKTEEAITEVLGIRPKEVISVGASDARFYRNagipAI 322
|
410 420 430
....*....|....*....|....*....|....*.
gi 489530539 407 AFGaifPGKPETEHQANEYLIVEDIIKATQIYALSI 442
Cdd:cd08011 323 VYG---PGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
11-444 |
1.84e-35 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 135.36 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 11 SLQDEMISSIQESVKIPSViseATENCPFGEnVDKALRgILDLCKSLGFKTVY------KDGYYGY-----AEI--GQGE 77
Cdd:PRK13983 2 ELRDEMIELLSELIAIPAV---NPDFGGEGE-KEKAEY-LESLLKEYGFDEVErydapdPRVIEGVrpnivAKIpgGDGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 78 KMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLwr 157
Cdd:PRK13983 77 RTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 158 ciNKYK-----ENNEEI---------PNYGfTPDSRFpITNAEKGLLQVhltcdsksdielsvgkalnavpgkaiyigky 223
Cdd:PRK13983 155 --SKYGiqyllKKHPELfkkddlilvPDAG-NPDGSF-IEIAEKSILWL------------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 224 sdklkkeldklnfeytvegnKICIIGKSVHSAASDTGINAvarlCIALNNIGIdsNIIKFLAEVIGEdangnniipncKD 303
Cdd:PRK13983 200 --------------------KFTVKGKQCHASTPENGINA----HRAAADFAL--ELDEALHEKFNA-----------KD 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 304 D-----VS----GKLTVNIGRV-TIDNEKEFAgIDVRIPVTYKKDDFVKELKKMTDKYNLNYE---EYDFLD----SIYV 366
Cdd:PRK13983 243 PlfdppYStfepTKKEANVDNInTIPGRDVFY-FDCRVLPDYDLDEVLKDIKEIADEFEEEYGvkiEVEIVQreqaPPPT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 367 PEDTLLVKTLRKVYEEETGLDGTPLSSGGATYARALD----NCVAFGAIfpgkPETEHQANEYLIVEDIIKATQIYALSI 442
Cdd:PRK13983 322 PPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRkkgyPAVVWSTL----DETAHQPNEYAKISNLIEDAKVFALLL 397
|
..
gi 489530539 443 YE 444
Cdd:PRK13983 398 LE 399
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
1-447 |
1.20e-32 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 127.75 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 1 MKEQIKEKVNSLQDEMISSIQESVKIPSVIseatencpfGENVDKALRgILDLCKSLGFKTVYKDGY---YGYaeIGQGE 77
Cdd:PRK13004 2 PFKLILMLAEKYKADMTRFLRDLIRIPSES---------GDEKRVVKR-IKEEMEKVGFDKVEIDPMgnvLGY--IGHGK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 78 KMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIrFIFGA-DEENL- 155
Cdd:PRK13004 70 KLIAFDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTL-YVTGTvQEEDCd 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 156 ---WRCINKYKenneeipnyGFTPDSrfpitnaekgllqVHLTCDSKsdielsvgkaLNavpgkaIYIGKysdKLKKELd 232
Cdd:PRK13004 149 glcWRYIIEED---------KIKPDF-------------VVITEPTD----------LN------IYRGQ---RGRMEI- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 233 klnfeytvegnKICIIGKSVHSAASDTGINAVARLCIALNNIgidsniikflaevigEDANgnniiPNCKDD-VSGK--L 309
Cdd:PRK13004 187 -----------RVETKGVSCHGSAPERGDNAIYKMAPILNEL---------------EELN-----PNLKEDpFLGKgtL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 310 TVN-I-----GRVTIDNEKEfAGIDVRIPVTYKKDDFVKELKKMTD--KYNLNYEEYDFLDSIY---------------V 366
Cdd:PRK13004 236 TVSdIfstspSRCAVPDSCA-ISIDRRLTVGETWESVLAEIRALPAvkKANAKVSMYNYDRPSYtglvyptecyfptwlY 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 367 PEDTLLVKT----LRKVYEEETGLDGTPLSSGGATYA-RALDNCVAFGaifPGKPETEHQANEYLIVEDIIKATQIYALS 441
Cdd:PRK13004 315 PEDHEFVKAaveaYKGLFGKAPEVDKWTFSTNGVSIAgRAGIPTIGFG---PGKEPLAHAPNEYTWKEQLVKAAAMYAAI 391
|
....*.
gi 489530539 442 IYELLK 447
Cdd:PRK13004 392 PKSLLK 397
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
81-444 |
5.83e-32 |
|
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: 124.00 E-value: 5.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 81 GILGHVDVVPEGDLESWnypPFEAVlEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDfNKRIRFIFGADEENLWRCIN 160
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKST-EDGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 161 KYkenneeipnygftpdsrfpitnAEKGLLQVHltcDSKSDIELSVGKALNAVPGKAIYIGkysdklkkeldklNFEYTV 240
Cdd:pfam01546 76 AL----------------------IEDGLLERE---KVDAVFGLHIGEPTLLEGGIAIGVV-------------TGHRGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 241 EGNKICIIGKSVHSAASDTGINAV---ARLCIALNNIgIDSNIIKFLAEV-----IGEDANGNNIIPnckddvsgkltvn 312
Cdd:pfam01546 118 LRFRVTVKGKGGHASTPHLGVNAIvaaARLILALQDI-VSRNVDPLDPAVvtvgnITGIPGGVNVIP------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 313 iGRVTidnekefAGIDVRIPVTYKKDDFVKELKKMTDKYNLNYE---EYDFLDSIYVPE--DTLLVKTLRKVYEEETGLD 387
Cdd:pfam01546 184 -GEAE-------LKGDIRLLPGEDLEELEERIREILEAIAAAYGvkvEVEYVEGGAPPLvnDSPLVAALREAAKELFGLK 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530539 388 GTPLSSG--GAT----YARALDNCVA-FGaifPGKpETEHQANEYLIVEDIIKATQIYALSIYE 444
Cdd:pfam01546 256 VELIVSGsmGGTdaafFLLGVPPTVVfFG---PGS-GLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-440 |
7.14e-27 |
|
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: 111.40 E-value: 7.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 14 DEMISSIQESVKIPSVISEATencpfGENVDKALRGILDLCKSLGFKTV----YKDGYYGY-----AEIGQGE-KMIGIL 83
Cdd:cd05650 1 EEIIELERDLIRIPAVNPESG-----GEGEKEKADYLEKKLREYGFYTLerydAPDERGIIrpnivAKIPGGNdKTLWII 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 84 GHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENLWRCINKYK 163
Cdd:cd05650 76 SHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 164 ENNEEI---------PNYGfTPDSRFpITNAEKGLLQVhltcdsksdielsvgkalnavpgkaiyigkysdklkkeldkl 234
Cdd:cd05650 156 LNKFDLfkkddliivPDFG-TEDGEF-IEIAEKSILWI------------------------------------------ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 235 nfeytvegnKICIIGKSVHSAASDTGINAVARLCialnnigidsNIIKFLAEVIGEDANGNNII--PNCKDDVSGKLTVN 312
Cdd:cd05650 192 ---------KVNVKGKQCHASTPENGINAFVAAS----------NFALELDELLHEKFDEKDDLfnPPYSTFEPTKKEAN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 313 IGRV-TIDNEKEFAgIDVRIPVTYKKDDFVKELKKMTDKYNLNYE---EYDFLDS----IYVPEDTLLVKTLRKVYEEET 384
Cdd:cd05650 253 VPNVnTIPGYDVFY-FDCRVLPTYKLDEVLKFVNKIISDFENSYGagiTYEIVQKeqapPATPEDSEIVVRLSKAIKKVR 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 385 GLDGTPLSSGGATYA---RALD-NCVAFGAIfpgkPETEHQANEYLIVEDIIKATQIYAL 440
Cdd:cd05650 332 GREAKLIGIGGGTVAaflRKKGyPAVVWSTL----DETAHQPNEYIRISHIVKDAKVFAE 387
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
71-447 |
2.05e-26 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 109.59 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 71 AEIGQGEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGA 150
Cdd:PRK08588 53 AEIGSGSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 151 DEEnlwrcinkykenNEEIPNYGFTpdsrfpitnaEKGLLQvhltcdsksDIE-LSVGKALNavpGKAIYIGKYSdklkk 229
Cdd:PRK08588 133 GEE------------VGELGAKQLT----------EKGYAD---------DLDaLIIGEPSG---HGIVYAHKGS----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 230 eldkLNFeytvegnKICIIGKSVHSAASDTGINAVarlcialnnigidSNIIKFLAEvigEDANGNNIIPNckDDVSGKL 309
Cdd:PRK08588 174 ----MDY-------KVTSTGKAAHSSMPELGVNAI-------------DPLLEFYNE---QKEYFDSIKKH--NPYLGGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 310 TVNigrVTIDN---------EKEFAGIDVR-IPvTYKKDDFVKELKKMTDKYN------LNYEEYDFLDSIYVPEDTLLV 373
Cdd:PRK08588 225 THV---VTIINggeqvnsvpDEAELEFNIRtIP-EYDNDQVISLLQEIINEVNqngaaqLSLDIYSNHRPVASDKDSKLV 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530539 374 KTLRKVYEEETGLDGTPLSSGGATYARAL---DNCVAFgAIF-PGKPETEHQANEYLIVEDIIKATQIYALSIYELLK 447
Cdd:PRK08588 301 QLAKDVAKSYVGQDIPLSAIPGATDASSFlkkKPDFPV-IIFgPGNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQYLK 377
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-439 |
1.23e-25 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 107.51 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 20 IQESVKIPSviseatENCPFGENVdkalRGILDLCKSLGFKTVYKDGY---YGYaeIGQGEKMIGILGHVDVVPEGDLES 96
Cdd:cd05649 4 LRDLIQIPS------ESGEEKGVV----ERIEEEMEKLGFDEVEIDPMgnvIGY--IGGGKKKILFDGHIDTVGIGNIDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 97 WNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDL-NVDFNKRIRFIFGADEENL----WRCINKYKenneeipn 171
Cdd:cd05649 72 WKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLgLRDFAYTILVAGTVQEEDCdgvcWQYISKAD-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 172 yGFTPDSRFpITNAEKGllqvhltcdsksdielsvgkalnavpgkAIYIGKysdKLKKELdklnfeytvegnKICIIGKS 251
Cdd:cd05649 144 -KIKPDFVV-SGEPTDG----------------------------NIYRGQ---RGRMEI------------RVDTKGVS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 252 VHSAASDTGINAVARlcialnnigidsniikfLAEVIGEDANGNNIIPNckDDVSGKLTVNI--------GRVTIDNEKE 323
Cdd:cd05649 179 CHGSAPERGDNAVYK-----------------MADIIQDIRQLNPNFPE--APFLGRGTLTVtdifstspSRCAVPDSCR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 324 fAGIDVRIPVTYKKDDFVKELKK--MTDKYN----LNYEEYD-------------FLDSIYVPEDTLLVK----TLRKVY 380
Cdd:cd05649 240 -ISIDRRLTVGETWEGCLEEIRAlpAVKKYGddvaVSMYNYDrpsytgevyeserYFPTWLLPEDHELVKalleAYKALF 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 381 EEETGLDGTPLSSGGATYA-RALDNCVAFGaifPGKPETEHQANEYLIVEDIIKATQIYA 439
Cdd:cd05649 319 GARPLIDKWTFSTNGVSIMgRAGIPCIGFG---PGAENQAHAPNEYTWKEDLVRCAAGYA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
50-438 |
1.42e-25 |
|
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: 107.21 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 50 ILDLCKSLGFKTVYKDgyYG-----YAEIGQGEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGpTI 124
Cdd:cd03891 24 IAERLKALGFTCERLE--FGgvknlWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKG-GI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 125 SA-IYAVKALMDLNVDFNKRIRFIFGADEENLWrcINKYKENNEEIPNYGFTPDsrFPITnAEKgllqvhlTCDSKSdie 203
Cdd:cd03891 101 AAfVAAAERFVAKHPNHKGSISFLITSDEEGPA--IDGTKKVLEWLKARGEKID--YCIV-GEP-------TSEKKL--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 204 lsvgkalnavpGKAIYIGKY-SdklkkeldkLNFeytvegnKICIIGKSVHSAASDTGINAVARLCIALNNIgidSNII- 281
Cdd:cd03891 166 -----------GDTIKIGRRgS---------LNG-------KLTIKGKQGHVAYPHLADNPIHLLAPILAEL---TATVl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 282 ----KFLA----EVIGEDANG--NNIIPNckddvSGKLTVNIgrvtidnekefagidvRIPVTYKKDDFVKELKKMTDKY 351
Cdd:cd03891 216 degnEFFPpsslQITNIDVGNgaTNVIPG-----ELKAKFNI----------------RFNDEHTGESLKARIEAILDKH 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 352 NLNYE-EYDFLDSIYVPEDTLLVKTLRKVYEEETGLDGTPLSSGGATYAR--ALDNC--VAFGAIfpgkPETEHQANEYL 426
Cdd:cd03891 275 GLDYDlEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGTSDARfiASYGCpvVEFGLV----NATIHKVNERV 350
|
410
....*....|..
gi 489530539 427 IVEDIIKATQIY 438
Cdd:cd03891 351 SVADLEKLTDIY 362
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
18-164 |
1.12e-24 |
|
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: 105.49 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 18 SSIQESVKIPSVISEATENcpfgENVDKALRGILDLCKSLGFKTVYKDGYYG----YAEIG--QGEKMIGILGHVDVVPE 91
Cdd:cd03893 2 QTLAELVAIPSVSAQPDRR----EELRRAAEWLADLLRRLGFTVEIVDTSNGapvvFAEFPgaPGAPTVLLYGHYDVQPA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489530539 92 GDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE----NLWRCINKYKE 164
Cdd:cd03893 78 GDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEEsgspSLDQLVEAHRD 154
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
21-445 |
5.20e-24 |
|
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: 102.88 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 21 QESVKIPSVISeatencpfgeNVDKALRGILDLCKSLGFKT---VYKDGYYGYAEIGQGEKMIGILGHVDVVPEGDLESW 97
Cdd:TIGR01246 6 KELISRPSVTP----------NDAGCQDIIAERLEKLGFEIewmHFGDTKNLWATRGTGEPVLAFAGHTDVVPAGPEEQW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 98 NYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEENlwRCINKYKENNEEIPNYGFTPD 177
Cdd:TIGR01246 76 SSPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEG--TAIDGTKKVVETLMARDELID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 178 srFPITNaekgllqvhltcdsksdiELSVGKALnavpGKAIYIGKYSdklkkeldKLNFeytvegnKICIIGKSVHSAAS 257
Cdd:TIGR01246 154 --YCIVG------------------EPSSVKKL----GDVIKNGRRG--------SITG-------NLTIKGIQGHVAYP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 258 DTGINAVARLcialnnigidsniIKFLAEVIGEDAN-GNNIIPNCKDDVSgkltvNIGRVTIDNEKEFAGIDVRIPVTYK 336
Cdd:TIGR01246 195 HLANNPIHKA-------------APALAELTAIKWDeGNEFFPPTSLQIT-----NIHAGTGANNVIPGELYVQFNLRFS 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 337 KDDFVKELK----KMTDKYNLNYE-EYDFLDSIYVPEDTLLVKTLRKVYEEETGLDGTPLSSGGATYARALD----NCVA 407
Cdd:TIGR01246 257 TEVSDEILKqrveAILDQHGLDYDlEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGGTSDGRFIAlmgaEVVE 336
|
410 420 430
....*....|....*....|....*....|....*...
gi 489530539 408 FGAIfpgkPETEHQANEYLIVEDIIKATQIYALSIYEL 445
Cdd:TIGR01246 337 FGPV----NATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-207 |
9.78e-21 |
|
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: 93.94 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 16 MISSIQESVKIPSVISEatencpfGENVDKALRGILDLCKSLGFkTVYKDGYYG----YAEIG-QGEKMIGILGHVDVVP 90
Cdd:cd05681 1 YLEDLRDLLKIPSVSAQ-------GRGIPETADFLKEFLRRLGA-EVEIFETDGnpivYAEFNsGDAKTLLFYNHYDVQP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 91 EGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE----NLWRCINKYKENN 166
Cdd:cd05681 73 AEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEvgspNLEKFVAEHADLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530539 167 EE---IPNYG-FTPDSRFPITNAEKGLLQVHLTCDS-KSDIELSVG 207
Cdd:cd05681 153 KAdgcIWEGGgKNPKGRPQISLGVKGIVYVELRVKTaDFDLHSSYG 198
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
70-153 |
4.39e-20 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 91.30 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 70 YAEIGQGEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGpTISA-IYAVKALMDLNVDFNKRIRFIF 148
Cdd:PRK13009 51 WARRGTEGPHLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKG-SLAAfVVAAERFVAAHPDHKGSIAFLI 129
|
....*
gi 489530539 149 GADEE 153
Cdd:PRK13009 130 TSDEE 134
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
74-178 |
6.22e-20 |
|
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: 87.48 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 74 GQGEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:cd03873 9 GEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEE 88
|
90 100
....*....|....*....|....*....
gi 489530539 154 NLWRCI----NKYKENNEEIPNYGFTPDS 178
Cdd:cd03873 89 VGSGGGkgllSKFLLAEDLKVDAAFVIDA 117
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
7-153 |
2.64e-19 |
|
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: 89.97 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 7 EKVNSLQDEMISSIQESVKIPSVISEATEncpFGEnVDKALRGILDLCKSLGFKTVYKDGYYGYAEIGQ----------- 75
Cdd:cd05676 3 KYIDEHQDEFIERLREAVAIQSVSADPEK---RPE-LIRMMEWAAERLEKLGFKVELVDIGTQTLPDGEelplppvllgr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 76 -----GEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGA 150
Cdd:cd05676 79 lgsdpSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEG 158
|
...
gi 489530539 151 DEE 153
Cdd:cd05676 159 MEE 161
|
|
| PRK06915 |
PRK06915 |
peptidase; |
74-444 |
2.74e-18 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 86.67 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 74 GQGEKMIgILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:PRK06915 91 GGGKSMI-LNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 154 -----NLWRCINKYKENNEEIP---NYGFtpdsrFPItnaEKGLLQVHLTcdsksdielsvgkalnaVPGKAIYIG-KYs 224
Cdd:PRK06915 170 sggagTLAAILRGYKADGAIIPeptNMKF-----FPK---QQGSMWFRLH-----------------VKGKAAHGGtRY- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 225 dklkkeldklnfeytvEGnkICIIGKSVHSAASDTGINAV--ARLCIALNN---IGIDSNIIKFlaevigedaNGNNIIP 299
Cdd:PRK06915 224 ----------------EG--VSAIEKSMFVIDHLRKLEEKrnDRITDPLYKgipIPIPINIGKI---------EGGSWPS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 300 NCKDDVS--GKLTVNIGRVTIDNEKEFAGidvripvtykkddFVKELKKMTDKYNLNYEEYDFLDSIYVP----EDTLLV 373
Cdd:PRK06915 277 SVPDSVIleGRCGIAPNETIEAAKEEFEN-------------WIAELNDVDEWFVEHPVEVEWFGARWVPgeleENHPLM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 374 KTLRKVYEEET-----------GLDGTPLSSGGATYAraldncVAFGaifPGKPETEHQANEYLIVEDIIKATQIYALSI 442
Cdd:PRK06915 344 TTLEHNFVEIEgnkpiieaspwGTDGGLLTQIAGVPT------IVFG---PGETKVAHYPNEYIEVDKMIAAAKIIALTL 414
|
..
gi 489530539 443 YE 444
Cdd:PRK06915 415 LD 416
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
74-178 |
1.26e-17 |
|
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: 80.94 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 74 GQGEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:cd18669 9 GGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEE 88
|
90 100
....*....|....*....|....*....
gi 489530539 154 NLWR----CINKYKENNEEIPNYGFTPDS 178
Cdd:cd18669 89 VGSGagkgLLSKDALEEDLKVDYLFVGDA 117
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
82-138 |
2.46e-17 |
|
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: 83.51 E-value: 2.46e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489530539 82 IL-GHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNV 138
Cdd:cd03895 78 ILnGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGL 135
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
15-153 |
4.64e-17 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 82.90 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 15 EMISSIQ--ESVKIPSVISEATENCPfgenvdKALRGILDlckSLGFKT--VYKDGYYG-YAEIGQGEKMIGILGHVDVV 89
Cdd:PRK08554 5 ELLSSLVsfETVNDPSKGIKPSKECP------KFIKDTLE---SWGIESelIEKDGYYAvYGEIGEGKPKLLFMAHFDVV 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530539 90 PEGdLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMdlNVDFNKRIRFIFGADEE 153
Cdd:PRK08554 76 PVN-PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELS--KEPLNGKVIFAFTGDEE 136
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
14-200 |
6.83e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 82.49 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 14 DEMISSIQESVKIPSVisEATencpfGENVDKALRGILDLCKSLGFKTV---YKDGYYGYAEIGQG-EKMIGILGHVDVV 89
Cdd:PRK06446 2 DEELYTLIEFLKKPSI--SAT-----GEGIEETANYLKDTMEKLGIKANierTKGHPVVYGEINVGaKKTLLIYNHYDVQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 90 PEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNvDFNKRIRFIFGADEENLWRCINKYKENNEEI 169
Cdd:PRK06446 75 PVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYEGEEEIGSPNLEDFIEKNKNK 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530539 170 PN--------YGFTPDSRFPITNAEKGLLQVHLTCDSKS 200
Cdd:PRK06446 154 LKadsvimegAGLDPKGRPQIVLGVKGLLYVELVLRTGT 192
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
82-133 |
9.34e-17 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 81.97 E-value: 9.34e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 489530539 82 IL-GHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKAL 133
Cdd:PRK06837 101 ILqGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDAL 153
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
20-445 |
2.36e-16 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 80.09 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 20 IQESVKIPSVISEATENCPFgenvdkalrgILDLCKSLGFKtVYKDGYYGY-AEIGQGEKMIGILGHVDVVPeGDLEswn 98
Cdd:cd05653 7 LLDLLSIYSPSGEEARAAKF----------LEEIMKELGLE-AWVDEAGNAvGGAGSGPPDVLLLGHIDTVP-GEIP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 99 yppfeAVLEDGKLYGRGTQDDKGPTISAIyavKALMDLNVDFNKRIRFIFGADEENLWRCINKYKENNEEiPNYGFT--P 176
Cdd:cd05653 72 -----VRVEGGVLYGRGAVDAKGPLAAMI---LAASALNEELGARVVVAGLVDEEGSSKGARELVRRGPR-PDYIIIgeP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 177 DSRFPITNAEKGLLQVhltcdsksdielsvgkalnavpgkaiyigkysdklkkeldklNFEYTVEgnkiciigkSVHSAA 256
Cdd:cd05653 143 SGWDGITLGYRGSLLV------------------------------------------KIRCEGR---------SGHSSS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 257 SDTGInavarlcialnnigIDSnIIKFLAEVIGEDANGNniiPNCKDDVSGKLTVNIGRVTIDN--EKEFAGIDVRIPVT 334
Cdd:cd05653 172 PERNA--------------AED-LIKKWLEVKKWAEGYN---VGGRDFDSVVPTLIKGGESSNGlpQRAEATIDLRLPPR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 335 YKKDDFVKELkkMTDKYNLNYEEYDFLDSIYVPEDTLLVKTLRKVYEEetgLDGTP---LSSGGA---TYARALD-NCVA 407
Cdd:cd05653 234 LSPEEAIALA--TALLPTCELEFIDDTEPVKVSKNNPLARAFRRAIRK---QGGKPrlkRKTGTSdmnVLAPLWTvPIVA 308
|
410 420 430
....*....|....*....|....*....|....*...
gi 489530539 408 FGaifPGKPETEHQANEYLIVEDIIKATQIYALSIYEL 445
Cdd:cd05653 309 YG---PGDSTLDHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
3-138 |
9.98e-16 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 78.93 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 3 EQIKEKVNSLQDEMISSIQESVKIPSViseatenCPFGENVDKALRGILDLCKSLGFKTVYKDGYYGYAEI-----GQGE 77
Cdd:PRK08596 2 SQLLEQIELRKDELLELLKTLVRFETP-------APPARNTNEAQEFIAEFLRKLGFSVDKWDVYPNDPNVvgvkkGTES 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530539 78 ---KMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNV 138
Cdd:PRK08596 75 dayKSLIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGI 138
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
1-164 |
2.20e-15 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 77.86 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 1 MKEQIKEKVNSLQDEMISSIQESVKIPSvISEATENcpfGENVDKALRGILDLCKSLGFKTVYKDGYYG----YAEI--G 74
Cdd:PRK08201 1 MMQQVEAYLRERREAHLEELKEFLRIPS-ISALSEH---KEDVRKAAEWLAGALEKAGLEHVEIMETAGhpivYADWlhA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 75 QGEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE- 153
Cdd:PRK08201 77 PGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEi 156
|
170
....*....|....
gi 489530539 154 ---NLWRCINKYKE 164
Cdd:PRK08201 157 gspNLDSFVEEEKD 170
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
1-133 |
2.55e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 77.64 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 1 MKEQIKEKVNSLQDEMISSIQESVKIPSVISEatencPF-GENVDKALRGILDLCKSLGF---KTVYKDG---YYGYAEI 73
Cdd:PRK07907 5 TADDLRARVAELLPRVRADLEELVRIPSVAAD-----PFrREEVARSAEWVADLLREAGFddvRVVSADGapaVIGTRPA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 74 GQGEKMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKAL 133
Cdd:PRK07907 80 PPGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRAL 139
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
22-153 |
4.77e-15 |
|
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: 76.58 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 22 ESVKIPSVISEATencpFGENVDKALRGILDLCKSLGFKTVYKDGYYG----YAE--IGQGEKMIGILGHVDVVPEGDLE 95
Cdd:cd05680 6 ELLRIPSVSADPA----HKGDVRRAAEWLADKLTEAGFEHTEVLPTGGhplvYAEwlGAPGAPTVLVYGHYDVQPPDPLE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489530539 96 SWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:cd05680 82 LWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEE 139
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
78-169 |
1.19e-14 |
|
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: 75.46 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 78 KMIGILGHVDVVPEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALM---DLNVDfnkrIRFIFGADEEN 154
Cdd:cd05677 72 KRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFqegELDND----VVFLIEGEEES 147
|
90
....*....|....*....
gi 489530539 155 ----LWRCINKYKENNEEI 169
Cdd:cd05677 148 gspgFKEVLRKNKELIGDI 166
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
80-153 |
7.49e-14 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 73.44 E-value: 7.49e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489530539 80 IGILGHVDVVP--EGDLESWNYPPFEAVLEDGKLYGRGTQDDKGpTISAIY-AVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:PRK08262 114 IVLMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKG-SLVAILeAAEALLAQGFQPRRTIYLAFGHDEE 189
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
82-195 |
8.29e-14 |
|
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: 72.78 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 82 ILGHVDVVPeGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE-------- 153
Cdd:cd05675 70 LLGHIDVVP-ADASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEaggengak 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489530539 154 ----NLWRCINKYKENNEEIPNYGFT-PDSR--FPITNAEKGLLQVHLT 195
Cdd:cd05675 149 wlvdNHPELFDGATFALNEGGGGSLPvGKGRrlYPIQVAEKGIAWMKLT 197
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
52-439 |
3.69e-13 |
|
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: 70.31 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 52 DLCKSLGFKTVYKDGYYG-----YAEIGQGEKmIGIL--GHVDVVP-EGDLesWNYPPFEAVLEDGKLYGRGTQDDKGpT 123
Cdd:cd03894 26 DYLAALGVKSRRVPVPEGgkanlLATLGPGGE-GGLLlsGHTDVVPvDGQK--WSSDPFTLTERDGRLYGRGTCDMKG-F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 124 ISAIYAVKALMDLnVDFNKRIRFIFGADEENLWRCINKYKennEEIPNYGFTPDSrfpITNAEKGLLQVhltcdsksdie 203
Cdd:cd03894 102 LAAVLAAVPRLLA-AKLRKPLHLAFSYDEEVGCLGVRHLI---AALAARGGRPDA---AIVGEPTSLQP----------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 204 lsvgkaLNAVPGKAIYigkysdklkkeldklnfeytvegnKICIIGKSVHSAASDTGINAV---ARLCIALNNIGidsni 280
Cdd:cd03894 164 ------VVAHKGIASY------------------------RIRVRGRAAHSSLPPLGVNAIeaaARLIGKLRELA----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 281 ikflAEVIGEDANGNNIIPNckddvsgkLTVNIGRV-------TIDNEKEFaGIDVR-IP------VTYKKDDFVKELKK 346
Cdd:cd03894 209 ----DRLAPGLRDPPFDPPY--------PTLNVGLIhggnavnIVPAECEF-EFEFRpLPgedpeaIDARLRDYAEALLE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 347 MTDKYnLNYEEYDFLDSIYVPEDTLLVKTLRKVYEEETGlDGTPLSSGGATYARALDNCVAFGaifPGKPETEHQANEYL 426
Cdd:cd03894 276 FPEAG-IEVEPLFEVPGLETDEDAPLVRLAAALAGDNKV-RTVAYGTEAGLFQRAGIPTVVCG---PGSIAQAHTPDEFV 350
|
410
....*....|...
gi 489530539 427 IVEDIIKATQIYA 439
Cdd:cd03894 351 ELEQLDRCEEFLR 363
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
84-153 |
4.99e-13 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 70.56 E-value: 4.99e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 84 GHVDVVPEGDleSWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:PRK13013 91 SHHDVVEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEE 158
|
|
| dapE-lys-deAc |
TIGR01902 |
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related ... |
52-446 |
7.90e-12 |
|
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related bacterial species contains two characterized enzymes, an deacetylase with specificity for both N-acetyl-ornithine and N-acetyl-lysine from Thermus, which is found within a lysine biosynthesis operon, and a fusion protein with acetyl-glutamate kinase (an enzyme of ornithine biosynthesis) from Lactobacillus. It is possible that all of the sequences within this clade have dual specificity, or that a mix of specificities have evolved within this clade.
Pssm-ID: 130957 [Multi-domain] Cd Length: 336 Bit Score: 66.03 E-value: 7.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 52 DLCKSLGFKTVYKDGYYGYAEIGQGEKMIGILGHVDVVPegdleswNYPPFEavLEDGKLYGRGTQDDKGPTISAIYAVK 131
Cdd:TIGR01902 25 EISKDLGLKLIIDDAGNFILGKGDGHKKILLAGHVDTVP-------GYIPVK--IEGGLLYGRGAVDAKGPLIAMIFATW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 132 ALMDLNVdfnkRIRFIFGADEENLWRCINKYKENNEEIPNYGFTPDSRFPITNAEKGLLQVHLTCDsksdielsvgkaln 211
Cdd:TIGR01902 96 LLNEKGI----KVIVSGLVDEESSSKGAREVIDKNYPFYVIVGEPSGAEGITLGYKGSLQLKIMCE-------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 212 avpgkaiyigkysdklkkeldklnfeytvegnkiciiGKSVHSAASDTGINAvarlcialnnigidsnIIKFLAEVIGED 291
Cdd:TIGR01902 158 -------------------------------------GTPFHSSSAGNAAEL----------------LIDYSKKIIEVY 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 292 ANGNNIIPnckDDVSGKLtVNIGRVTIDNEKE-FAGIDVRIPVTYKKDDFVKELkkmTDKYNLNYEEYDFLDSIYVPEDT 370
Cdd:TIGR01902 185 KQPENYDK---PSIVPTI-IRFGESYNDTPAKlELHFDLRYPPNNKPEEAIKEI---TDKFPICLEIVDETPPYKVSRNN 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 371 LLVKTLRKVYEEETGLDGTPLSSGGA---TYARALD-NCVAFGaifPGKPETEHQANEYLIVEDIIKATQIYALSIYELL 446
Cdd:TIGR01902 258 PLVRAFVRAIRKQGMKPRLKKKTGTSdmnILAPIWTvPMVAYG---PGDSTLDHTPQEKISLAEYLIGIKTLMLAIEELW 334
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
83-153 |
9.26e-12 |
|
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: 66.51 E-value: 9.26e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489530539 83 LGHVDVVP--EGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALmdLNVDFN-KR-IRFIFGADEE 153
Cdd:cd05674 75 MAHQDVVPvnPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELL--LKRGFKpRRtIILAFGHDEE 147
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
85-153 |
2.02e-11 |
|
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: 65.37 E-value: 2.02e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 85 HVDVVPEGDlESWNYPPFEAVL-EDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:cd05646 72 HTDVVPVFE-EKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEE 140
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
14-446 |
4.16e-11 |
|
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: 64.50 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 14 DEMISSIQESVKIPSviseateNCPFGENVDKALRgILDLCKSLGFKT----VYKDGYYGYA-----------EIGQGEK 78
Cdd:cd02697 3 DEEVRFLQKLVRVPT-------DTPPGNNAPHAER-TAALLQGFGFEAerhpVPEAEVRAYGmesitnlivrrRYGDGGR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 79 MIGILGHVDVVPEGDleSWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEEnlwrc 158
Cdd:cd02697 75 TVALNAHGDVVPPGD--GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEE----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 159 inkykenneeipnygftpdsrfpiTNAEKG---LLQVHLTcdsKSDIELSVGKALNAVPGKAiyigkysdklkkelDKLN 235
Cdd:cd02697 148 ------------------------FGGELGpgwLLRQGLT---KPDLLIAAGFSYEVVTAHN--------------GCLQ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 236 FEYTVEgnkiciiGKSVHSAASDTGINAVARLCIALNNI-GIDSNIIKFLAEVIG-----------EDANGNNIIPnckD 303
Cdd:cd02697 187 MEVTVH-------GKQAHAAIPDTGVDALQGAVAILNALyALNAQYRQVSSQVEGithpylnvgriEGGTNTNVVP---G 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 304 DVSGKL-------------TVNIGRVTIDNEKEFAGIDVRIpvtyKKDDFVKELKKmtdkynlnyeeydfldsiyVPEDT 370
Cdd:cd02697 257 KVTFKLdrrmipeenpvevEAEIRRVIADAAASMPGISVDI----RRLLLANSMRP-------------------LPGNA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 371 LLVKTLRK----VYEEETGLDGTPLSSGGATYARALDNCVAFGAifpgKPET-----EHQANEYLIVEDIIKATQIYALS 441
Cdd:cd02697 314 PLVEAIQThgeaVFGEPVPAMGTPLYTDVRLYAEAGIPGVIYGA----GPRTvleshAKRADERLQLEDLRRATKVIARS 389
|
....*
gi 489530539 442 IYELL 446
Cdd:cd02697 390 LRDLL 394
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
70-153 |
1.79e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 62.51 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 70 YAEIGQGEKMiGIL--GHVDVVP-EGdlESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVdfNKRIRF 146
Cdd:PRK07522 56 FATIGPADRG-GIVlsGHTDVVPvDG--QAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPL--RRPLHL 130
|
....*..
gi 489530539 147 IFGADEE 153
Cdd:PRK07522 131 AFSYDEE 137
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
55-442 |
4.28e-10 |
|
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: 61.07 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 55 KSLGFKT----VYKDGYYGYAEI-GQGEKMIGILGHVDVV-PEGDLESWnypPFEavLEDGKLYGRGTQDDKGPTISAIY 128
Cdd:cd03885 33 EALGFTVerrpLGEFGDHLIATFkGTGGKRVLLIGHMDTVfPEGTLAFR---PFT--VDGDRAYGPGVADMKGGLVVILH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 129 AVKALMDLNVDFNKRIRFIFGADEEnlwrcINKykenneeipnygftPDSRFPITNAEKGllqvhltcdskSDIelsvgk 208
Cdd:cd03885 108 ALKALKAAGGRDYLPITVLLNSDEE-----IGS--------------PGSRELIEEEAKG-----------ADY------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 209 ALNAVPGKAiyigkySDKLKKElDKLNFEYTVEgnkicIIGKSVHS-AASDTGINAV---ARLCIALNNIGidsniikfl 284
Cdd:cd03885 152 VLVFEPARA------DGNLVTA-RKGIGRFRLT-----VKGRAAHAgNAPEKGRSAIyelAHQVLALHALT--------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 285 aevigedangnniipnckDDVSGkLTVNIGRV---TIDN---EKEFAGIDVRIPVTYKKDDFVKELKKMTD-KYNLNYE- 356
Cdd:cd03885 211 ------------------DPEKG-TTVNVGVIsggTRVNvvpDHAEAQVDVRFATAEEADRVEEALRAIVAtTLVPGTSv 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 357 EYDFldSIYVP-----EDTL-LVKTLRKVYEEEtGLDGTPLSSGGAT---YARALDNCV--AFGAIfPGKPETEHqanEY 425
Cdd:cd03885 272 ELTG--GLNRPpmeetPASRrLLARAQEIAAEL-GLTLDWEATGGGSdanFTAALGVPTldGLGPV-GGGAHTED---EY 344
|
410
....*....|....*..
gi 489530539 426 LIVEDIIKATQIYALSI 442
Cdd:cd03885 345 LELDSLVPRIKLLARLL 361
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
85-153 |
6.90e-10 |
|
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: 60.58 E-value: 6.90e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 85 HVDVVPEGDlESWNYPPFEAVL-EDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:TIGR01880 79 HTDVVPVFR-EHWTHPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEE 147
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
16-153 |
9.39e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 57.14 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 16 MISSIQESVKIPSvISeATEncpfgENVDKALRGILDL----CKSLGFKT------VYKDGYYGYAEIGQGEKmiGIL-- 83
Cdd:PRK05111 7 FIEMYRALIATPS-IS-ATD-----PALDQSNRAVIDLlagwFEDLGFNVeiqpvpGTRGKFNLLASLGSGEG--GLLla 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 84 GHVDVVPEgDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKAlMDLNvDFNKRIRFIFGADEE 153
Cdd:PRK05111 78 GHTDTVPF-DEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRD-IDLT-KLKKPLYILATADEE 144
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
74-153 |
5.40e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 55.01 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 74 GQG-EKMIGILGHVDVVpEGDLESWNYPPFEAVLEDGKLYGRGTQDDKGptiSAIYAVKALMDLNVD-FNKR--IRFIFG 149
Cdd:PRK09133 97 GTDpKKPILLLAHMDVV-EAKREDWTRDPFKLVEENGYFYGRGTSDDKA---DAAIWVATLIRLKREgFKPKrdIILALT 172
|
....
gi 489530539 150 ADEE 153
Cdd:PRK09133 173 GDEE 176
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
71-153 |
6.96e-08 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 54.19 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 71 AEIGQGEKMIGILGHVDVVPeGDLeswnypPFEavLEDGKLYGRGTQDDKGPTISAIYAVKALMDLnvdfnKRIRFIF-G 149
Cdd:PRK04443 53 GPAGDGPPLVLLLGHIDTVP-GDI------PVR--VEDGVLWGRGSVDAKGPLAAFAAAAARLEAL-----VRARVSFvG 118
|
....
gi 489530539 150 ADEE 153
Cdd:PRK04443 119 AVEE 122
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
43-153 |
2.13e-07 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 53.11 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 43 VDKALRGILDLCKSLGFK-----TVYKDGY--YGYAEI---GQGEKMIGILGHVDVVPEgdLESW--NYPPFEAVLEDGK 110
Cdd:cd05682 29 LEKAANLIADWVKAQNIKgakveVVELEGRtpLLFVEIpgtEQDDDTVLLYGHMDKQPP--FTGWdeGLGPTKPVIRGDK 106
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489530539 111 LYGRGTQDDKGPTISAIYAVKALMDLNVDfNKRIRFIFGADEE 153
Cdd:cd05682 107 LYGRGGADDGYAIFASLTAIKALQEQGIP-HPRCVVLIEACEE 148
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
84-154 |
4.20e-07 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 52.21 E-value: 4.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489530539 84 GHVDVVPEGDLESWNYPPFEAVLED----GK-LYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEEN 154
Cdd:PRK09104 89 GHYDVQPVDPLDLWESPPFEPRIKEtpdgRKvIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEES 164
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
85-153 |
5.80e-06 |
|
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: 48.07 E-value: 5.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489530539 85 HVDVVPEGdlESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDlNVDFNKRIRFIFGADEE 153
Cdd:cd05651 63 HHDTVKPN--AGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYS-EGPLNYNLIYAASAEEE 128
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
74-153 |
5.99e-06 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 48.47 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 74 GQGEKMIGILGHVDVV-PEGDLESwnyPPFEavLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADE 152
Cdd:PRK06133 96 GTGKRRIMLIAHMDTVyLPGMLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDE 170
|
.
gi 489530539 153 E 153
Cdd:PRK06133 171 E 171
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
84-154 |
8.37e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 47.92 E-value: 8.37e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489530539 84 GHVDVVPeGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEEN 154
Cdd:PRK07906 72 GHLDVVP-AEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEA 141
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
85-154 |
2.72e-05 |
|
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: 46.11 E-value: 2.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 85 HVDVVPEgdleswnYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEEN 154
Cdd:cd05652 66 HIDTVPP-------FIPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEET 128
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
82-121 |
1.15e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 44.52 E-value: 1.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489530539 82 ILGHVDVVPeGDLESWNYP--PFEAVLEDGKLYGRGTQDDKG 121
Cdd:PRK07079 90 IYGHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKG 130
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
75-153 |
1.39e-04 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 44.01 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 75 QGEKMIGILGHVDVV-PEGDLESWnypPFEAvlEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE 153
Cdd:PRK07473 73 QGEPGILIAGHMDTVhPVGTLEKL---PWRR--EGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEE 147
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
16-164 |
1.97e-04 |
|
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: 43.20 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 16 MISSIQESVKIPSVisEATENcPFGENVDKALRGildlCKSLgfkTVYKDGYYGYA--EIGQGEKMIgILGHVDVVPEGD 93
Cdd:cd05647 1 PIELTAALVDIPSV--SGNEK-PIADEIEAALRT----LPHL---EVIRDGNTVVArtERGLASRVI-LAGHLDTVPVAG 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489530539 94 leswNYPPfeAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNkrIRFIF-----GADEEN-LWRCINKYKE 164
Cdd:cd05647 70 ----NLPS--RVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFydceeVAAELNgLGRLAEEHPE 138
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
78-154 |
3.52e-04 |
|
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: 42.83 E-value: 3.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530539 78 KMIGILG-HVDVVPeGDLESWNYPPFEAVLEDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEEN 154
Cdd:cd08012 78 KTVSFVGsHMDVVT-ANPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEEN 154
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
76-445 |
1.34e-03 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 40.54 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 76 GEKMIGILGHVDVVPeGDLEswnyppfeAVLEDGKLYGRGTQDDKGPTISAIYAVKALmdlnvdfNKR---IRFIFGADE 152
Cdd:PRK00466 59 GEGDILLASHVDTVP-GYIE--------PKIEGEVIYGRGAVDAKGPLISMIIAAWLL-------NEKgikVMVSGLADE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 153 EN----LWRCINKYKENNEEIPNygfTPDSRFPITNAEKGLLQVHLTCDsksdielsvgkalnavpgkaiyigkysdklk 228
Cdd:PRK00466 123 EStsigAKELVSKGFNFKHIIVG---EPSNGTDIVVEYRGSIQLDIMCE------------------------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 229 keldklnfeytvegnkiciiGKSVHSAAsdtginavarlciALNNIGIDsnIIKFLAEVIGEdangnniiPNCKDDVSgk 308
Cdd:PRK00466 169 --------------------GTPEHSSS-------------AKSNLIVD--ISKKIIEVYKQ--------PENYDKPS-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 309 LTVNIGR----VTIDNEKEFAGIDVRIPVTYKKDDFVKELKKMTDKYNLnyEEYDFLDSIYVPEDTLLVKTLRKVYEEEt 384
Cdd:PRK00466 204 IVPTIIRagesYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGL--KIVDETPPVKVSINNPVVKALMRALLKQ- 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489530539 385 GLDGTPLSSGGAT----YARALDNCVAFGaifPGKPETEHQANEYLIVEDIIKATQIYALSIYEL 445
Cdd:PRK00466 281 NIKPRLVRKAGTSdmniLQKITTSIATYG---PGNSMLEHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
92-164 |
1.66e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 40.55 E-value: 1.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530539 92 GDLESWNYPPFEAVL-EDGKLYGRGTQDDKGPTISAIYAVKALMDLNVDFNKRIRFIFGADEE----NLWRCINKYKE 164
Cdd:cd05678 96 GNWEEINWDAIFSNLdPEWRVFARAAADDKGPIMMMLAALDALKAGGIAPKFNVKIILDSEEEkgspSLPKAVKEYKE 173
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
82-153 |
1.70e-03 |
|
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: 40.56 E-value: 1.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489530539 82 ILGHVDVVPeGDLESWN--YPPFEAVLEDGKLYGRGTQDDKGP---TISAIYAVKALMDLNVDFNkrIRFIFGADEE 153
Cdd:cd05679 77 IYGHGDVVP-GYEGRWRdgRDPWTVTVWGERWYGRGTADNKGQhsiNMAALRQVLEARGGKLGFN--VKFLIEMGEE 150
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
242-356 |
6.15e-03 |
|
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: 36.17 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530539 242 GNKICIIGKSVHSAASDTGINAVARLCialnnigidsniiKFLAEVIGEDANGNNIIPnckddvsgKLTVNIGRV----- 316
Cdd:pfam07687 8 GGHLTVKGKAGHSGAPGKGVNAIKLLA-------------RLLAELPAEYGDIGFDFP--------RTTLNITGIeggta 66
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489530539 317 -TIDNEKEFAGIDVRIPVTYKKDDFVKELKKMTDKYNLNYE 356
Cdd:pfam07687 67 tNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| |
