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Conserved domains on  [gi|223005864|ref|NP_937791|]
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inactive carboxypeptidase-like protein X2 precursor [Homo sapiens]

Protein Classification

carboxypeptidase X family protein( domain architecture ID 10044218)

carboxypeptidase X (CPX) family protein is an M14 family zinc carboxypeptidase that relies on its substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell; it contains an extra C-terminal domain which may assist in folding of the carboxypeptidase domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes

CATH:  3.40.630.10
EC:  3.4.17.-
Gene Ontology:  GO:0006508|GO:0004181|GO:0008270
MEROPS:  M14
PubMed:  7674922|10493853

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
318-639 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing.


:

Pssm-ID: 349441  Cd Length: 322  Bit Score: 691.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd03869    1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSELGGWSLGRWTHDGIDINNNFPDLNTLLWEAEDRQNVPRKVP 477
Cdd:cd03869   81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 NHYIAIPEWFLSENATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWKTQEHTPTPDDHVFRWLAYSYAS 557
Cdd:cd03869  161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTPWKTQEYTPTPDDHVFRWLAYSYAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 558 THRLMTDARRRVCHTEDFQKEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIVFM 637
Cdd:cd03869  241 THRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHESELPEEWENNRESLLVFM 320

                 ..
gi 223005864 638 EQ 639
Cdd:cd03869  321 EQ 322
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
137-292 2.17e-58

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 194.49  E-value: 2.17e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 137 PPLGLETLKiTDFQLHASTVKRYGLGAHRGRLNiqaginendfYDGAWCAGRNDLQQWIEVDARRLTRFTGVITQGRNSL 216
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSGWEASRARLN----------SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864 217 WLSDWVTSYKVMVSNDSHTWVTVKNGSGDMIFEGNSEKEIPVLNELPVPMVARYIRINPQSWfdNGSICMRMEILG 292
Cdd:cd00057   70 GSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTW--NGNISLRLELYG 143
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
643-718 1.34e-38

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


:

Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 137.27  E-value: 1.34e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864 643 GIKGLVRDSHGKGIPNAIISVEGINHDIRTANDGDYWRLLNPGEYVVTAKAEGFTASTKNCMVGYDMGATRCDFTL 718
Cdd:cd11308    1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
PHA03247 super family cl33720
large tegument protein UL36; Provisional
48-103 2.09e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864   48 ARPEPELETFSPPLPAGPGEewerRPQEPRPPKRATKPKKAPKREKSAPEPPPPGK 103
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPE----RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
 
Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
318-639 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing.


Pssm-ID: 349441  Cd Length: 322  Bit Score: 691.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd03869    1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSELGGWSLGRWTHDGIDINNNFPDLNTLLWEAEDRQNVPRKVP 477
Cdd:cd03869   81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 NHYIAIPEWFLSENATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWKTQEHTPTPDDHVFRWLAYSYAS 557
Cdd:cd03869  161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTPWKTQEYTPTPDDHVFRWLAYSYAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 558 THRLMTDARRRVCHTEDFQKEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIVFM 637
Cdd:cd03869  241 THRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHESELPEEWENNRESLLVFM 320

                 ..
gi 223005864 638 EQ 639
Cdd:cd03869  321 EQ 322
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
324-632 5.24e-76

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 247.21  E-value: 5.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  324 MRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVCQEYlAR 403
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNY-GR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  404 NARIVHLVEETRIHVLPSLNPDGYEKAYEGgseLGGWSLGRWTHD-----GIDINNNFPDLNTLLWEAEDRQNVPRKVPN 478
Cdd:pfam00246  80 DPEITELLDDTDIYILPVVNPDGYEYTHTT---DRLWRKNRSNANgssciGVDLNRNFPDHWNEVGASSNPCSETYRGPA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  479 HYiaipewflSEnatvaAETRAVIAWM-EKIPFVLGGNLQGGELVVAYPYDLVRSpwktqehTPTPDDHVFRWLAYSYAS 557
Cdd:pfam00246 157 PF--------SE-----PETRAVADFIrSKKPFVLYISLHSYSQVLLYPYGYTRD-------EPPPDDEELKSLARAAAK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  558 THRLMTDARRrvchtedfqKEEGTVNGASWHTVAGSLNDFSYLHTNC-FELSIYVGCDK----YPHESQLPEEWENNRES 632
Cdd:pfam00246 217 ALQKMVRGTS---------YTYGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGrygfLLPASQIIPTAEETWEA 287
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
137-292 2.17e-58

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 194.49  E-value: 2.17e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 137 PPLGLETLKiTDFQLHASTVKRYGLGAHRGRLNiqaginendfYDGAWCAGRNDLQQWIEVDARRLTRFTGVITQGRNSL 216
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSGWEASRARLN----------SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864 217 WLSDWVTSYKVMVSNDSHTWVTVKNGSGDMIFEGNSEKEIPVLNELPVPMVARYIRINPQSWfdNGSICMRMEILG 292
Cdd:cd00057   70 GSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTW--NGNISLRLELYG 143
Zn_pept smart00631
Zn_pept domain;
318-623 1.42e-56

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 194.48  E-value: 1.42e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEhevGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGSH---DKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   398 QEYlARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGselGGWSLGRWTHD---GIDINNNFPDlntlLWEAEDRQnvpr 474
Cdd:smart00631  78 ENY-GRDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGD---RLWRKNRSPNSncrGVDLNRNFPF----HWGETGNP---- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   475 kvpnhyiaIPEWFLSENATVAAETRAVIAWM-EKIPFVLGGNLQGGELVVAYPYDlvrspWKTQEHTPTPDDH--VFRWL 551
Cdd:smart00631 146 --------CSETYAGPSPFSEPETKAVRDFIrSNRRFKLYIDLHSYSQLILYPYG-----YTKNDLPPNVDDLdaVAKAL 212
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223005864   552 AYSYASTHrlmtdarrrvCHTEDFqkeeGTVNGASWHtVAGSLNDFSYLHTN-CFELSIYVGCD-----KYPHESQLP 623
Cdd:smart00631 213 AKALASVH----------GTRYTY----GISNGAIYP-ASGGSDDWAYGVLGiPFSFTLELRDDgrygfLLPPSQIIP 275
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
138-293 1.69e-40

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 145.34  E-value: 1.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   138 PLGLETlkitDFQLHASTVkryGLGAHRGRLNIQAginendfyDGAWCAGRNDLQQWIEVDARRLTRFTGVITQGRnslW 217
Cdd:smart00231   5 PLGLES----DSQITASSS---YWAAKIARLNGGS--------DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRR---H 66
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864   218 LSDWVTSYKVMVSNDSHTWVTVKNGsGDMIFEGNSEKEIPVLNELPVPMVARYIRINPQSWfdNGSICMRMEILGC 293
Cdd:smart00231  67 GNGDWVTYKLEYSDDGVNWTTYKDG-NSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGW--NGNIILRVELLGC 139
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
643-718 1.34e-38

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 137.27  E-value: 1.34e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864 643 GIKGLVRDSHGKGIPNAIISVEGINHDIRTANDGDYWRLLNPGEYVVTAKAEGFTASTKNCMVGYDMGATRCDFTL 718
Cdd:cd11308    1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
180-290 1.60e-32

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 122.17  E-value: 1.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  180 YDGAWCAGRNDLQQWIEVDARRLTRFTGVITQGRNSLWlSDWVTSYKVMVSNDSHTWVTVKngsgDMIFEGNSEKEIPVL 259
Cdd:pfam00754  22 PNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGS-NGYVTSYKIEYSLDGENWTTVK----DEKIPGNNDNNTPVT 96
                          90       100       110
                  ....*....|....*....|....*....|.
gi 223005864  260 NELPVPMVARYIRINPQSWFDNGSICMRMEI 290
Cdd:pfam00754  97 NTFDPPIKARYVRIVPTSWNGGNGIALRAEL 127
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
319-550 5.88e-21

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 94.76  E-value: 5.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 319 HNYKEMRQLMKVVNEMcPNITRIYNIGKSHQGLKLYAVEISDHPGehevGEPEFHYIAGAHGNEVLGRELLLLLVQFVCQ 398
Cdd:COG2866   20 YTYEELLALLAKLAAA-SPLVELESIGKSVEGRPIYLLKIGDPAE----GKPKVLLNAQQHGNEWTGTEALLGLLEDLLD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 399 EYlarNARIVHLVEETRIHVLPSLNPDGYEKayeggselgGWslgRWTHDGIDINNNFPDLntllweaedrqnvprkvpn 478
Cdd:COG2866   95 NY---DPLIRALLDNVTLYIVPMLNPDGAER---------NT---RTNANGVDLNRDWPAP------------------- 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223005864 479 hyiaipewFLSEnatvaAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWktQEHTPTPDDHVFRW 550
Cdd:COG2866  141 --------WLSE-----PETRALRDLLDEHDPDFVLDLHGQGELFYWFVGTTEPTG--SFLAPSYDEEREAF 197
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
643-718 8.42e-13

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 64.22  E-value: 8.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  643 GIKGLVRDSHGKGIPNAIISVE----GINHDIRTANDGDYW-RLLNPGEYVVTAKAEGFTASTKNCMVGYDMGATRCDFT 717
Cdd:pfam13620   1 TISGTVTDPSGAPVPGATVTVTntdtGTVRTTTTDADGRYRfPGLPPGTYTVTVSAPGFKTATRTGVTVTAGQTTTLDVT 80

                  .
gi 223005864  718 L 718
Cdd:pfam13620  81 L 81
PHA03247 PHA03247
large tegument protein UL36; Provisional
48-103 2.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864   48 ARPEPELETFSPPLPAGPGEewerRPQEPRPPKRATKPKKAPKREKSAPEPPPPGK 103
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPE----RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
 
Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
318-639 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing.


Pssm-ID: 349441  Cd Length: 322  Bit Score: 691.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd03869    1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSELGGWSLGRWTHDGIDINNNFPDLNTLLWEAEDRQNVPRKVP 477
Cdd:cd03869   81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 NHYIAIPEWFLSENATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWKTQEHTPTPDDHVFRWLAYSYAS 557
Cdd:cd03869  161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTPWKTQEYTPTPDDHVFRWLAYSYAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 558 THRLMTDARRRVCHTEDFQKEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIVFM 637
Cdd:cd03869  241 THRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHESELPEEWENNRESLLVFM 320

                 ..
gi 223005864 638 EQ 639
Cdd:cd03869  321 EQ 322
M14_CP_N-E_like cd03858
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of ...
318-639 4.73e-159

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.


Pssm-ID: 349431 [Multi-domain]  Cd Length: 292  Bit Score: 462.12  E-value: 4.73e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd03858    1 HHNYEELEEFLKQVAKRYPNITRLYSIGKSVEGRELWVLEISDNPGVHEPGEPEFKYVANMHGNEVVGRELLLLLAEYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYLaRNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSelgGWSLGRWTHDGIDINNNFPDLNTLLWeaedrqnvprkvp 477
Cdd:cd03858   81 ENYG-KDPRVTQLVNSTRIHIMPSMNPDGYEKAQEGDC---GGLIGRNNANGVDLNRNFPDQFFQVY------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 nhyiaipewflSENATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPwKTQEHTPTPDDHVFRWLAYSYAS 557
Cdd:cd03858  144 -----------SDNNPRQPETKAVMNWLESIPFVLSANLHGGALVANYPYDDTRSG-KSTEYSPSPDDAVFRMLARSYSD 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 558 THRLMTDARRRVCHtEDFQKEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIVFM 637
Cdd:cd03858  212 AHPTMSMGKPCCCD-DDENFPNGITNGAAWYSVSGGMQDFNYLHTNCFEITLELGCCKYPPASELPKYWEDNKRSLLNFL 290

                 ..
gi 223005864 638 EQ 639
Cdd:cd03858  291 EQ 292
M14_CPZ cd03867
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase ...
318-638 1.46e-109

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase M14-like domain of carboxypeptidase (CP) Z (CPZ), CPZ belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPZ is a secreted Zn-dependent enzyme whose biological function is largely unknown. Unlike other members of the N/E subfamily, CPZ has a bipartite structure, which consists of an N-terminal cysteine-rich domain (CRD) whose sequence is similar to Wnt-binding proteins, and a C-terminal CP catalytic domain that removes C-terminal Arg residues from substrates. CPZ is enriched in the extracellular matrix and is widely distributed during early embryogenesis. That the CRD of CPZ can bind to Wnt4 suggests that CPZ plays a role in Wnt signaling.


Pssm-ID: 349439  Cd Length: 315  Bit Score: 336.09  E-value: 1.46e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd03867    1 HHSYSQMVRVLKKTAARCAHIARTYSIGRSFEGKDLLVIEFSSNPGQHELLEPEVKYIGNMHGNEVVGREMLIYLAQYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSELGGWSLGRWTHDGIDINNNFPDLNTllwEAEDRQNVPRKVP 477
Cdd:cd03867   81 SEYLLGNPRIQTLINTTRIHLLPSMNPDGYEVAAEEGAGYNGWTSGRQNAQNLDLNRNFPDLTS---EAYRLARTRGARL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 NHyIAIPE--WFlsenATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWKTQEHTPTPDDHVFRWLAYSY 555
Cdd:cd03867  158 DH-IPIPQsyWW----GKVAPETKAVMKWMRSIPFVLSASLHGGDLVVSYPYDFSKHPLEEKMFSPTPDEKMFKLLAKAY 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 556 ASTHRLMTDARRRVChTEDFQKEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIV 635
Cdd:cd03867  233 ADAHPMMSDRSENRC-GGNFLKRGGIINGAEWYSFTGGMADFNYLHTNCFEVTVELGCEKFPPEEELYTIWQENKEALLN 311

                 ...
gi 223005864 636 FME 638
Cdd:cd03867  312 FME 314
M14_CPE cd03865
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 ...
318-639 6.80e-107

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 Carboxypeptidase (CP) E (CPE, also known as carboxypeptidase H, and enkephalin convertase; EC 3.4.17.10) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPE is an important enzyme responsible for the proteolytic processing of prohormone intermediates (such as pro-insulin, pro-opiomelanocortin, or pro-gonadotropin-releasing hormone) by specifically removing C-terminal basic residues. In addition, it has been proposed that the regulated secretory pathway (RSP) of the nervous and endocrine systems utilizes membrane-bound CPE as a sorting receptor. A naturally occurring point mutation in CPE reduces the stability of the enzyme and causes its degradation, leading to an accumulation of numerous neuroendocrine peptides that result in obesity and hyperglycemia. Reduced CPE enzyme and receptor activity could underlie abnormal placental phenotypes from the observation that CPE is down-regulated in enlarged placentas of interspecific hybrid (interspecies hybrid placental dysplasia, IHPD) and cloned mice.


Pssm-ID: 349437 [Multi-domain]  Cd Length: 319  Bit Score: 329.25  E-value: 6.80e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd03865    1 YHRYPELREALVSVWLQCPAISRIYTVGRSFEGRELLVIEVSDNPGEHEPGEPEFKYVGNMHGNEAVGRELLIFLAQYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSELGGWSLGRWTHDGIDINNNFPDLNTLLWEAEdRQNVPRkvp 477
Cdd:cd03865   81 NEYQKGNETIINLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNE-KEGGPN--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 NHYIAIPEWFLSENATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPwKTQEHTPTPDDHVFRWLAYSYAS 557
Cdd:cd03865  157 NHLLKNMKKAVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSG-SAHEYSSCPDDAIFQSLARAYSS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 558 THRLMTDARRRVCHTEDFQKE--EGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIV 635
Cdd:cd03865  236 LNPAMSDPNRPPCRKNDDDSSfvDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKGYWEDNKNSLIN 315

                 ....
gi 223005864 636 FMEQ 639
Cdd:cd03865  316 YIEQ 319
M14_CPN cd03864
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 ...
318-639 8.36e-107

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 Carboxypeptidase N (CPN, also known as kininase I, creatine kinase conversion factor, plasma carboxypeptidase B, arginine carboxypeptidase, and protaminase; EC 3.4.17.3) is an extracellular glycoprotein synthesized in the liver and released into the blood, where it is present in high concentrations. CPN belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. It specifically removes C-terminal basic residues. As CPN can cleave lysine more avidly than arginine residues it is also called lysine carboxypeptidase. CPN substrates include peptides found in the bloodstream, such as kinins (e.g. bradykinin, kalinin, met-lys-bradykinin), complement anaphylatoxins and creatine kinase MM (CK-MM). By removing just one amino acid, CPN can alter peptide activity and receptor binding. For example Bradykinin, a nine-residue peptide released from kiningen in response to tissue injury which is inactivated by CPN, anaphylatoxins which are regulated by CPN by the cleaving and removal of their C-terminal arginines resulting in a reduction in their biological activities of 10-100-fold, and creatine kinase MM, a cytosolic enzyme that catalyzes the reversible transfer of a phosphate group from ATP to creatine, and is regulated by CPN by the cleavage of C-terminal lysines. Like the other N/E subfamily members, two surface loops surrounding the active-site groove restrict access to the catalytic center, thus restricting larger protein carboxypeptidase inhibitors from inhibiting CPN.


Pssm-ID: 349436 [Multi-domain]  Cd Length: 313  Bit Score: 328.82  E-value: 8.36e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEM-RQLMKVVNEmCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFV 396
Cdd:cd03864    1 HHRYDDLvRALYAVQNE-CPYITRIYSIGRSVEGRHLYVLEFSDNPGIHEPLEPEFKYVGNMHGNEVLGRELLIQLSEFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 397 CQEYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSELGGWSLGRWTHDGIDINNNFPDLNTLLWEAEDRQNvprkv 476
Cdd:cd03864   80 CEEYRNGNERITRLIQDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRNNANGVDLNRNFPDLNTLMYYNEKYGG----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 477 PNHYIAIPEWFLSEnatVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYD-----LVRSPWKTQeHTPTPDDHVFRWL 551
Cdd:cd03864  155 PNHHLPLPDNWKSQ---VEPETLAVIQWMQNYNFVLSANLHGGAVVANYPYDksrepRVRGFRRTA-YSPTPDDKLFQKL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 552 AYSYASTHRLMtdarRRVCHTEDFqKEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRE 631
Cdd:cd03864  231 AKTYSYAHGWM----HKGWNCGDY-FDEGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELEREWLGNRE 305

                 ....*...
gi 223005864 632 SLIVFMEQ 639
Cdd:cd03864  306 ALISYMEQ 313
M14_CPD_I cd03868
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The ...
319-639 5.37e-96

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The first carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain I. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. This Domain I family contains two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus regulating intracellular trafficking. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop. In D. melanogaster, the CPD variant 1B short (DmCPD1Bs) is necessary and sufficient for viability of the fruit fly.


Pssm-ID: 349440  Cd Length: 294  Bit Score: 299.93  E-value: 5.37e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 319 HNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVCQ 398
Cdd:cd03868    2 HNYDELTDLLHKLAETYPNIAKLHSIGKSVQGRELWVLEISDNVNRREPGKPMFKYVANMHGDETVGRQLLIYLAQYLLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 399 EYlARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSELGGWSLGRWTHDGIDINNNFPDlntlLWEAEDRQNVPRKVPn 478
Cdd:cd03868   82 NY-GKDERVTRLVNSTDIHLMPSMNPDGFENSKEGDCSGDPGYGGRENANNVDLNRNFPD----QFEDSDDRLLEGRQP- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 479 hyiaipewflsenatvaaETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWKTQEHTPTPDDHVFRWLAYSYAST 558
Cdd:cd03868  156 ------------------ETLAMMKWIVENPFVLSANLHGGSVVASYPFDDSPSHIECGVYSKSPDDAVFRHLAHTYADN 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 559 HRLMtdARRRVCHTEDFqkEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIVFME 638
Cdd:cd03868  218 HPTM--HKGNNCCEDSF--KDGITNGAEWYDVPGGMQDFNYVHSNCFEITLELSCCKYPPASELPKEWDNNKEALLSYME 293

                 .
gi 223005864 639 Q 639
Cdd:cd03868  294 Q 294
M14_CPD_II cd03863
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The ...
315-639 1.20e-86

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The second carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain II. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, while the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop.


Pssm-ID: 349435 [Multi-domain]  Cd Length: 296  Bit Score: 275.67  E-value: 1.20e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 315 DFKHHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQ 394
Cdd:cd03863    5 DFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 395 FVCQEYlARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSElggWSLGRWTHDGIDINNNFPDLntllweaedrqnvpr 474
Cdd:cd03863   85 YLCKNF-GTDPEVTDLVQNTRIHIMPSMNPDGYEKSQEGDRG---GTVGRNNSNNYDLNRNFPDQ--------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 475 kvpnhyiaipewFLSENATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWKTqeHTPTPDDHVFRWLAYS 554
Cdd:cd03863  146 ------------FFQITDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGLAT--YSKSPDDAVFQQLALS 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 555 YASTHRLMTDAR--RRVCHTEDFQkeEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRES 632
Cdd:cd03863  212 YSKENSKMYQGSpcKELYPNEYFP--HGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRS 289

                 ....*..
gi 223005864 633 LIVFMEQ 639
Cdd:cd03863  290 LLQFIKQ 296
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
324-632 5.24e-76

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 247.21  E-value: 5.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  324 MRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVCQEYlAR 403
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNY-GR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  404 NARIVHLVEETRIHVLPSLNPDGYEKAYEGgseLGGWSLGRWTHD-----GIDINNNFPDLNTLLWEAEDRQNVPRKVPN 478
Cdd:pfam00246  80 DPEITELLDDTDIYILPVVNPDGYEYTHTT---DRLWRKNRSNANgssciGVDLNRNFPDHWNEVGASSNPCSETYRGPA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  479 HYiaipewflSEnatvaAETRAVIAWM-EKIPFVLGGNLQGGELVVAYPYDLVRSpwktqehTPTPDDHVFRWLAYSYAS 557
Cdd:pfam00246 157 PF--------SE-----PETRAVADFIrSKKPFVLYISLHSYSQVLLYPYGYTRD-------EPPPDDEELKSLARAAAK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  558 THRLMTDARRrvchtedfqKEEGTVNGASWHTVAGSLNDFSYLHTNC-FELSIYVGCDK----YPHESQLPEEWENNRES 632
Cdd:pfam00246 217 ALQKMVRGTS---------YTYGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGrygfLLPASQIIPTAEETWEA 287
M14_CPM cd03866
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 ...
318-639 2.40e-73

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 Carboxypeptidase (CP) M (CPM) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPM is an extracellular glycoprotein, bound to cell membranes via a glycosyl-phosphatidylinositol on the C-terminus of the protein. It specifically removes C-terminal basic residues such as lysine and arginine from peptides and proteins. The highest levels of CPM have been found in human lung and placenta, but significant amounts are present in kidney, blood vessels, intestine, brain, and peripheral nerves. CPM has also been found in soluble form in various body fluids, including amniotic fluid, seminal plasma and urine. Due to its wide distribution in a variety of tissues, it is believed that it plays an important role in the control of peptide hormones and growth factor activity on the cell surface and in the membrane-localized degradation of extracellular proteins, for example it hydrolyses the C-terminal arginine of epidermal growth factor (EGF) resulting in des-Arg-EGF which binds to the EGF receptor (EGFR) with an equal or greater affinity than native EGF. CPM is a required processing enzyme that generates specific agonists for the B1 receptor.


Pssm-ID: 349438  Cd Length: 289  Bit Score: 240.08  E-value: 2.40e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd03866    1 YHNQEQMETYLKDVNKNYPSITHLHSIGKSVEGRDLWVLVLGRFPTKHRIGIPEFKYVANMHGDEVVGRELLLHLIEFLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYlARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSElggWSLGRWTHDGIDINNNFPDlntllweAEDRQNVPRKvp 477
Cdd:cd03866   81 TSY-GSDPVITRLINSTRIHIMPSMNPDGFEATKKPDCY---YTKGRYNKNGYDLNRNFPD-------AFEENNVQRQ-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 nhyiaipewflsenatvaAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRS-PWKTQEHTPTPDDHVFRWLAYSYA 556
Cdd:cd03866  148 ------------------PETRAVMDWIKNETFVLSANLHGGALVASYPFDNGNSgTGQLGYYSVSPDDDVFIYLAKTYS 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 557 STHRLMTdaRRRVCHT-EDFQkeEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIV 635
Cdd:cd03866  210 YNHTNMY--KGIECSNsQSFP--GGITNGYQWYPLQGGMQDYNYVWGQCFEITLELSCCKYPPEETLPQFWNDNRVALIE 285

                 ....
gi 223005864 636 FMEQ 639
Cdd:cd03866  286 YIKQ 289
M14_CPD_III cd06245
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; ...
318-639 1.99e-60

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; The third carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain III. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop.


Pssm-ID: 349464 [Multi-domain]  Cd Length: 283  Bit Score: 205.37  E-value: 1.99e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd06245    1 YHSYKQLSKFLRGLNSNYPTITNLTSLGQSVEKRDIWVLEIGNKPNESEPSEPKILFVGGIHGNAPVGTELLLLLAHFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYlARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSElggWSLGRWTHDGIDINNNFPdlNTLLWEAEDRQnvprkvp 477
Cdd:cd06245   81 HNY-KKDSAITKLLNRTRIHIVPSLNPDGAEKAEEKKCT---SKIGEKNANGVDLDTDFE--SNANNRSGAAQ------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 nhyiaipewflsenatvaAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDlvrSPWKTQEhtptpDDHVFRWLAYSYAS 557
Cdd:cd06245  148 ------------------PETKAIMDWLKEKDFTLSVALDGGSLVVTYPYD---KPVQTVE-----NKETLKHLAKVYAN 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 558 THRLMTDARRRVCHTEDFQKEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIVFM 637
Cdd:cd06245  202 NHPTMHAGDPGCCSNSDENFTNGVIRASEWHSHKGSMLDFSYKFGSCPEITVYTSCCYFPPAEELLTLWAEHKKSLLSMI 281

                 ..
gi 223005864 638 EQ 639
Cdd:cd06245  282 VE 283
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
319-639 4.13e-60

bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial carboxypeptidase (CP) members of the M14 family of metallocarboxypeptidases (MCPs), mostly of which have yet to be characterized. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.


Pssm-ID: 349483 [Multi-domain]  Cd Length: 281  Bit Score: 204.35  E-value: 4.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 319 HNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVgEPEFHYIAGAHGNEVLGRELLLLLVQFVCQ 398
Cdd:cd18173    5 PTYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKISDNVNTEEA-EPEFKYTSTMHGDETTGYELMLRLIDYLLT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 399 EYlARNARIVHLVEETRIHVLPSLNPDGYekaYEGG--SELGGWslgRWTHDGIDINNNFPDlntllweaedRQNVPRKV 476
Cdd:cd18173   84 NY-GTDPRITNLVDNTEIWINPLANPDGT---YAGGnnTVSGAT---RYNANGVDLNRNFPD----------PVDGDHPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 477 PNHYiaipewflsenatvAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDlvrspwkTQEhTPTPDDHVFRWLAYSYA 556
Cdd:cd18173  147 GNGW--------------QPETQAMMNFADEHNFVLSANFHGGAEVVNYPWD-------TWY-SRHPDDDWFQDISREYA 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 557 STHRLMTDARRrvchTEDFqkEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLIVF 636
Cdd:cd18173  205 DTNQANSPPMY----MSEF--NNGITNGYDWYEVYGGRQDYMYYWHGCREVTIELSNTKWPPASQLPTYWNYNRESLLNY 278

                 ...
gi 223005864 637 MEQ 639
Cdd:cd18173  279 IEQ 281
M14_CP_plant cd18172
Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes ...
318-634 1.19e-59

Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes only plant members of the carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). It includes Arabidopsis thaliana SOL1 carboxypeptidase D which is known to possess enzymatic activity to remove the C-terminal arginine residue of CLE19 proprotein in vitro, and SOL1-dependent cleavage of the C-terminal arginine residue is necessary for CLE19 activity in vivo. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.


Pssm-ID: 349482 [Multi-domain]  Cd Length: 276  Bit Score: 203.03  E-value: 1.19e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEvGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:cd18172    1 YHSNAELEDALKAFTRRCGAISRLIVIGSSVNGFPLWALEISDGPGEDE-TEPAFKFVGNMHGDEPVGRELLLRLADWLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 398 QEYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSelggwslgrwthDGIDINNNFPDlntllweaedrQNVPRKVP 477
Cdd:cd18172   80 ANYKAKDPLAAKIVENAHLHLVPTMNPDGFARRRRNNA------------NNVDLNRDFPD-----------QFFPKNLR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 478 NHyiaipewflseNATVAAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDlvRSPWKTQEHTPTPDDHVFRWLAYSYAS 557
Cdd:cd18172  137 ND-----------LAARQPETLAVMNWSRSVRFTASANLHEGALVANYPWD--GNADGRTKYSASPDDATFRRLASVYAQ 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223005864 558 THRLMTDARrrvchteDFqkEEGTVNGASWHTVAGSLNDFSYLHTNCFELSIYVGCDKYPHESQLPEEWENNRESLI 634
Cdd:cd18172  204 AHPNMAKSK-------EF--PGGITNGAQWYPLYGGMQDWNYLHTGCMDLTLEVNDNKWPPEDRLVQIWAEHRKAML 271
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
137-292 2.17e-58

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 194.49  E-value: 2.17e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 137 PPLGLETLKiTDFQLHASTVKRYGLGAHRGRLNiqaginendfYDGAWCAGRNDLQQWIEVDARRLTRFTGVITQGRNSL 216
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSGWEASRARLN----------SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864 217 WLSDWVTSYKVMVSNDSHTWVTVKNGSGDMIFEGNSEKEIPVLNELPVPMVARYIRINPQSWfdNGSICMRMEILG 292
Cdd:cd00057   70 GSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTW--NGNISLRLELYG 143
Zn_pept smart00631
Zn_pept domain;
318-623 1.42e-56

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 194.48  E-value: 1.42e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   318 HHNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEhevGEPEFHYIAGAHGNEVLGRELLLLLVQFVC 397
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGSH---DKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   398 QEYlARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGselGGWSLGRWTHD---GIDINNNFPDlntlLWEAEDRQnvpr 474
Cdd:smart00631  78 ENY-GRDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGD---RLWRKNRSPNSncrGVDLNRNFPF----HWGETGNP---- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   475 kvpnhyiaIPEWFLSENATVAAETRAVIAWM-EKIPFVLGGNLQGGELVVAYPYDlvrspWKTQEHTPTPDDH--VFRWL 551
Cdd:smart00631 146 --------CSETYAGPSPFSEPETKAVRDFIrSNRRFKLYIDLHSYSQLILYPYG-----YTKNDLPPNVDDLdaVAKAL 212
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223005864   552 AYSYASTHrlmtdarrrvCHTEDFqkeeGTVNGASWHtVAGSLNDFSYLHTN-CFELSIYVGCD-----KYPHESQLP 623
Cdd:smart00631 213 AKALASVH----------GTRYTY----GISNGAIYP-ASGGSDDWAYGVLGiPFSFTLELRDDgrygfLLPPSQIIP 275
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
138-293 1.69e-40

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 145.34  E-value: 1.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864   138 PLGLETlkitDFQLHASTVkryGLGAHRGRLNIQAginendfyDGAWCAGRNDLQQWIEVDARRLTRFTGVITQGRnslW 217
Cdd:smart00231   5 PLGLES----DSQITASSS---YWAAKIARLNGGS--------DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRR---H 66
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864   218 LSDWVTSYKVMVSNDSHTWVTVKNGsGDMIFEGNSEKEIPVLNELPVPMVARYIRINPQSWfdNGSICMRMEILGC 293
Cdd:smart00231  67 GNGDWVTYKLEYSDDGVNWTTYKDG-NSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGW--NGNIILRVELLGC 139
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
643-718 1.34e-38

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 137.27  E-value: 1.34e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864 643 GIKGLVRDSHGKGIPNAIISVEGINHDIRTANDGDYWRLLNPGEYVVTAKAEGFTASTKNCMVGYDMGATRCDFTL 718
Cdd:cd11308    1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
180-290 1.60e-32

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 122.17  E-value: 1.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  180 YDGAWCAGRNDLQQWIEVDARRLTRFTGVITQGRNSLWlSDWVTSYKVMVSNDSHTWVTVKngsgDMIFEGNSEKEIPVL 259
Cdd:pfam00754  22 PNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGS-NGYVTSYKIEYSLDGENWTTVK----DEKIPGNNDNNTPVT 96
                          90       100       110
                  ....*....|....*....|....*....|.
gi 223005864  260 NELPVPMVARYIRINPQSWFDNGSICMRMEI 290
Cdd:pfam00754  97 NTFDPPIKARYVRIVPTSWNGGNGIALRAEL 127
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
319-633 9.79e-27

Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor.


Pssm-ID: 349432 [Multi-domain]  Cd Length: 292  Bit Score: 110.81  E-value: 9.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 319 HNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEvGEPEFHYIAGAHGNEVLGRELLLLLVQFVCQ 398
Cdd:cd03859    5 HTYAELVAELDQLAAEYPEITKLISIGKSVEGRPIWAVKISDNPDEDE-DEPEVLFMGLHHAREWISLEVALYFADYLLE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 399 EYlARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSElGGW-------SLGRWTHDGIDINNNFPdlntLLWEAEDRQN 471
Cdd:cd03859   84 NY-GTDPRITNLVDNREIWIIPVVNPDGYEYNRETGGG-RLWrknrrpnNGNNPGSDGVDLNRNYG----YHWGGDNGGS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 472 VPRKVPNHYIAiPEWFlSENatvaaETRAVIAWMEKIPFVLGGNLQG-GELVVaypydlvrSPWKTQEHTPTPDDHVFRW 550
Cdd:cd03859  158 SPDPSSETYRG-PAPF-SEP-----ETQAIRDLVESHDFKVAISYHSyGELVL--------YPWGYTSDAPTPDEDVFEE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 551 LAYSYASthrlmtdarrrvchtedfQKEEGTVNGASWH--TVAGSLNDFSYLHTNCFELSIYVG---CDKYPHESQLPEE 625
Cdd:cd03859  223 LAEEMAS------------------YNGGGYTPQQSSDlyPTNGDTDDWMYGEKGIIAFTPELGpefYPFYPPPSQIDPL 284

                 ....*...
gi 223005864 626 WENNRESL 633
Cdd:cd03859  285 AEENLPAA 292
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
319-550 5.88e-21

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 94.76  E-value: 5.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 319 HNYKEMRQLMKVVNEMcPNITRIYNIGKSHQGLKLYAVEISDHPGehevGEPEFHYIAGAHGNEVLGRELLLLLVQFVCQ 398
Cdd:COG2866   20 YTYEELLALLAKLAAA-SPLVELESIGKSVEGRPIYLLKIGDPAE----GKPKVLLNAQQHGNEWTGTEALLGLLEDLLD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 399 EYlarNARIVHLVEETRIHVLPSLNPDGYEKayeggselgGWslgRWTHDGIDINNNFPDLntllweaedrqnvprkvpn 478
Cdd:COG2866   95 NY---DPLIRALLDNVTLYIVPMLNPDGAER---------NT---RTNANGVDLNRDWPAP------------------- 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223005864 479 hyiaipewFLSEnatvaAETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLVRSPWktQEHTPTPDDHVFRW 550
Cdd:COG2866  141 --------WLSE-----PETRALRDLLDEHDPDFVLDLHGQGELFYWFVGTTEPTG--SFLAPSYDEEREAF 197
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
372-633 2.91e-19

M14 family of metallocarboxypeptidases and related proteins; The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349427 [Multi-domain]  Cd Length: 216  Bit Score: 87.13  E-value: 2.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 372 FHYIAGAHGNEVLGRELLLLLVQFVCQEYLarNARIVHLVEETRIHVLPSLNPDGYEKAYEggselggwSLGRWTHDGID 451
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLLENYG--NDPLKRLLDNVELWIVPLVNPDGFARVID--------SGGRKNANGVD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 452 INNNFPdlnTLLWEAEDRQNVPRKVPNHYiaipewFLSENatvaaETRAVIAWMEKIPFVLGGNLQGGELVVAYPYDLvr 531
Cdd:cd00596   71 LNRNFP---YNWGKDGTSGPSSPTYRGPA------PFSEP-----ETQALRDLAKSHRFDLAVSYHSSSEAILYPYGY-- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 532 spwktqEHTPTPDDHVFRWLAYSYASTHRLMTDARRRVCHtedfqkeegtvngasWHTVAGSLNDFSYLHTNCFELSIYV 611
Cdd:cd00596  135 ------TNEPPPDFSEFQELAAGLARALGAGEYGYGYSYT---------------WYSTTGTADDWLYGELGILAFTVEL 193
                        250       260
                 ....*....|....*....|...
gi 223005864 612 GCDKYPHESQLPE-EWENNRESL 633
Cdd:cd00596  194 GTADYPLPGTLLDrRLERNLAAL 216
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
314-429 8.84e-16

Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349476 [Multi-domain]  Cd Length: 359  Bit Score: 79.58  E-value: 8.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 314 LDFKH-HNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHEVGEPEFHYIAGAHGNEVLGRELLLLL 392
Cdd:cd06905    1 LAFDRyYTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTITNGETGPADEKPALWVDGNIHGNEVTGSEVALYL 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 223005864 393 VQFVCQEYlARNARIVHLVEETRIHVLPSLNPDGYEK 429
Cdd:cd06905   81 AEYLLTNY-GKDPEITRLLDTRTFYILPRLNPDGAEA 116
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
643-718 8.42e-13

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 64.22  E-value: 8.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864  643 GIKGLVRDSHGKGIPNAIISVE----GINHDIRTANDGDYW-RLLNPGEYVVTAKAEGFTASTKNCMVGYDMGATRCDFT 717
Cdd:pfam13620   1 TISGTVTDPSGAPVPGATVTVTntdtGTVRTTTTDADGRYRfPGLPPGTYTVTVSAPGFKTATRTGVTVTAGQTTTLDVT 80

                  .
gi 223005864  718 L 718
Cdd:pfam13620  81 L 81
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
319-457 1.90e-12

Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.


Pssm-ID: 349433 [Multi-domain]  Cd Length: 300  Bit Score: 68.71  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 319 HNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDHPGEHevGEPEFHYIAGAHgnevlGRELLLLLVqfvcQ 398
Cdd:cd03860    2 HPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWGSGGKG--GKPAIVIHGGQH-----AREWISTST----V 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 399 EYLA--------RNARIVHLVEETRIHVLPSLNPDGYEkayeggselggWSlgrWTHD----------------GIDINN 454
Cdd:cd03860   71 EYLAhqllsgygSDATITALLDKFDFYIIPVVNPDGYV-----------YT---WTTDrlwrknrqptggsscvGIDLNR 136

                 ...
gi 223005864 455 NFP 457
Cdd:cd03860  137 NWG 139
M14_Endopeptidase_I cd06229
Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like ...
373-512 6.62e-09

Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like domain of Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (also known as Gamma-D-glutamyl-meso-diaminopimelate peptidase I, and Endopeptidase I (ENP1); EC 3.4.19.11). ENP1 is a member of the M14 family of metallocarboxypeptidases (MCPs), and is classified as belonging to subfamily C. However it has an exceptional type of activity of hydrolyzing the gamma-D-Glu-(L)meso-diaminopimelic acid (gamma-D-Glu-Dap) bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. ENP1 has a different substrate specificity and cellular role than MpaA (MpaA does not belong to this group). ENP1 hydrolyzes the gamma-D-Glu-Dap bond of MurNAc-tripeptide and MurNAc-tetrapeptide, as well as the amide bond of free tripeptide and tetrapeptide. ENP1 is active on spore cortex peptidoglycan, and is produced at stage IV of sporulation in forespore and spore integuments.


Pssm-ID: 349448 [Multi-domain]  Cd Length: 238  Bit Score: 56.96  E-value: 6.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 373 HYIAGAHGNEVLGRELLLLLVQFVCQEY----LARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGS-------ELGGWS 441
Cdd:cd06229    2 LYNASFHAREYITTLLLMKFIEDYAKAYvnksYIRGKDVGELLNKVTLHIVPMVNPDGVEISQNGSNainpyylRLVAWN 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223005864 442 LGRWTHD-------GIDINNNFPdlntLLWEAEDRQNVPRKVPNHYIAI-PewfLSENatvaaETRAVIAWMEKIPFVL 512
Cdd:cd06229   82 KKGTDFTgwkanirGVDLNRNFP----AGWEKEKRLGPKAPGPRDYPGKeP---LSEP-----ETKAMAALTRQNDFDL 148
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
344-509 8.83e-07

Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A (MpaA) and related proteins. MpaA is a member of the M14 family of metallocarboxypeptidases (MCPs), however it has an exceptional type of activity, it hydrolyzes the gamma-D-glutamyl-meso-diaminopimelic acid (gamma-D-Glu-Dap) bond in murein peptides. MpaA is specific for cleavage of the gamma-D-Glu-Dap bond of free murein tripeptide; it may also cleave murein tetrapeptide. MpaA has a different substrate specificity and cellular role than endopeptidase I, ENP1 (ENP1 does not belong to this group). MpaA works on free murein peptide in the recycling pathway.


Pssm-ID: 349475 [Multi-domain]  Cd Length: 214  Bit Score: 50.35  E-value: 8.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 344 IGKSHQGLKLYAVEISDHPGehevgePEFHYIAGAHGNEVLGrelllllVQFVcqEYLARNARIVHLVEETRIHVLPSLN 423
Cdd:cd06904    4 YGTSVKGRPILAYKFGPGSR------ARILIIGGIHGDEPEG-------VSLV--EHLLRWLKNHPASGDFHIVVVPCLN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 424 PDGYEKAYeggselggwslgRWTHDGIDINNNFPdlnTLLWEAEDRQNV-PRKVPNHYIAipewflSEnatvaAETRAVI 502
Cdd:cd06904   69 PDGLAAGT------------RTNANGVDLNRNFP---TKNWEPDARKPKdPRYYPGPKPA------SE-----PETRALV 122

                 ....*..
gi 223005864 503 AWMEKIP 509
Cdd:cd06904  123 ELIERFK 129
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
319-610 2.29e-05

Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 carboxypeptidases found specifically in insects, including B-type carboxypeptidase of H. zea (CPBHz, insect gut carboxypeptidase-3) that is insensitive to potato carboxypeptidase inhibitor (PCI) in corn earworm, and midgut procarboxypeptidase A (PCPAHa, insect gut carboxypeptidase-1) from Helicoverpa armigera larva, a devastating pest of crops. PCPAHa preferentially cleaves aliphatic and aromatic residues. The peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.


Pssm-ID: 349467 [Multi-domain]  Cd Length: 297  Bit Score: 47.07  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 319 HNYKEMRQLMKVVNEMCPNITRIYNIGKSHQGLKLYAVEISDhPGEHEVGEPEFHYIAGAHGNEVLgrelLLLLVQFVCQ 398
Cdd:cd06248    2 HSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRS-TNSEDTSKPTIMIEGGINPREWI----SPPAALYAIH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 399 EYLARNARIVHLVEETRIHVLPSLNPDGYEKAYEGGSElggWSLGRWTHD--------GIDINNNFpDLNtllWEAEDRQ 470
Cdd:cd06248   77 KLVEDVETQSDLLNNFDWIILPVANPDGYVFTHTNDRE---WTKNRSTNSnplgqicfGVNINRNF-DYQ---WNPVLSS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 471 NVPrkvPNHYIAIPEWFlSEnatvaAETRAVIAWMEK--IPFVLGGNLQGGELVVAYPYDLVRSpwktqehtpTPDDHVF 548
Cdd:cd06248  150 ESP---CSELYAGPSAF-SE-----AESRAIRDILHEhgNRIHLYISFHSGGSFILYPWGYDGS---------TSSNARQ 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223005864 549 RWLAYSYASthrlmtdarrRVCHTEDFQKEEGTVNGASWHTVAGSLNDFSYLHTN---CFELSIY 610
Cdd:cd06248  212 LHLAGVAAA----------AAISSNNGRPYVVGQSSVLLYRAAGTSSDYAMGIAGidyTYELPGY 266
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
374-469 1.69e-04

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349461 [Multi-domain]  Cd Length: 220  Bit Score: 43.83  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 374 YIAGAHGNEVLGRELLLLLVQFVCQEYLARNarivhLVEETRIHVLPSLNPDGYEkAYEggselggwslgRWTHDGIDIN 453
Cdd:cd06242    6 LVGQQHGNEPAGREAALALARDLAFGDDARE-----LLEKVNVLVVPRANPDGRA-ANT-----------RGNANGVDLN 68
                         90
                 ....*....|....*.
gi 223005864 454 NNFpdlnTLLWEAEDR 469
Cdd:cd06242   69 RDH----LLLSTPETR 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
48-103 2.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 223005864   48 ARPEPELETFSPPLPAGPGEewerRPQEPRPPKRATKPKKAPKREKSAPEPPPPGK 103
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPE----RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
374-460 1.47e-03

Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349430 [Multi-domain]  Cd Length: 203  Bit Score: 40.52  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 374 YIAGAHGNEVLGRElllLLVQFVcQEYLARNARIVHLVEETRIHVLPSLNPDGYEK-AYEGGSELGGWSLGRWTHDGIDI 452
Cdd:cd03857    4 LAAQIHGNETTGTE---ALMELI-RDLASESDEAAKLLDNIVILLVPQLNPDGAELfVNFYLDSMNGLPGTRYNANGIDL 79

                 ....*...
gi 223005864 453 NNNFPDLN 460
Cdd:cd03857   80 NRDHVKLT 87
M14-like cd06232
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
344-486 1.62e-03

Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349451  Cd Length: 276  Bit Score: 41.22  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 344 IGKSHQGLKLYAVEI-SDHPGEHEVG------EPEFHYIAGAHGNEVLGRELLLLLVQFV---CQEYLARnariVHLVee 413
Cdd:cd06232    2 EARSYQGRDIWAREFtEPSTSEFVSQaklslyKPTILISARHHANEVSSTNAALRLAELLatdPPEILKK----VNLV-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 414 trihVLPSLNPDGYEKAYEGGSELGGWSL--GRWTHDGIDINNNFPDLNTLLWEAEDRQNVPRK-----------VPNHy 480
Cdd:cd06232   76 ----IIPLENPDGYALHEELQKDNPEHKLhaARYNALGDEYAYEYFNDDPRFPEAEVRPRAWERwlpdihvdlhgYPSH- 150

                 ....*.
gi 223005864 481 iaipEW 486
Cdd:cd06232  151 ----EW 152
PRK10819 PRK10819
transport protein TonB; Provisional
50-120 2.91e-03

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 40.05  E-value: 2.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223005864  50 PEPELETF-SPPLPAG-PGEEWERRPQE-PRP-PKRATKPKKAPKREKSAPEPPPPGKHSNKKVMRTKSSEKAAN 120
Cdd:PRK10819  74 PEPEPEPIpEPPKEAPvVIPKPEPKPKPkPKPkPKPVKKVEEQPKREVKPVEPRPASPFENTAPARPTSSTATAA 148
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
374-456 4.05e-03

Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family includes Francisella tularensis protein rapid encystment phenotype 34 (REP34) which is a zinc-containing monomeric protein demonstrating carboxypeptidase B-like activity. REP34 possesses a novel topology with its substrate binding pocket deviating from the canonical M14 peptidases with a possible catalytic role for a conserved tyrosine and distinct S1' recognition site. Thus, REP34, identified as an active carboxypeptidase and a potential key F. tularensis effector protein, may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 39.60  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005864 374 YI-AGAHGNEVLGrelllllVQFVCQeYLARNARIvhLVEETRIHVLPSLNPDGYEKayegGSelggwslgRWTHDGIDI 452
Cdd:cd06231   46 LIsAGIHGDEPAG-------VEALLR-FLESLAEK--YLRRVNLLVLPCVNPWGFER----NT--------RENADGIDL 103

                 ....
gi 223005864 453 NNNF 456
Cdd:cd06231  104 NRSF 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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