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Conserved domains on  [gi|516409375|ref|WP_017798773|]
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MULTISPECIES: serine hydrolase [Oceanobacillus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
strep_PBP3 super family cl45725
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ...
16-419 6.81e-125

streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.


The actual alignment was detected with superfamily member NF038273:

Pssm-ID: 468443 [Multi-domain]  Cd Length: 407  Bit Score: 368.43  E-value: 6.81e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  16 ILVFTSMLTATTTVQANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDY 95
Cdd:NF038273   6 LLLLLLAFFLATTVSADDFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  96 PYSISANNSFSGVGLkQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNE 175
Cdd:NF038273  86 PYELTTNYEISNVPL-DARKYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 176 DLGDN-YPeGTNPNDTNLLSARSAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHegenlASYYYEGVDGLK 254
Cdd:NF038273 165 YLGDHiYP-GSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADFAGTTIYSYNYMLKG-----MPYYREGVDGLK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 255 TGFTDLAGYSFTGTAERNGQRLITVVMKT----GSETERFEETAKLLDYGFSNFENTELFSAGyQEEGNETVPVAKGKED 330
Cdd:NF038273 239 TGTTEKAGASFVATSVENGMRVITVVLNAdnadEDEYARFTATNQLLDYIYQNFEKVTLVKKG-QAYKDSKLPVIDGKKK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 331 QVSISLQDSVSVPIKADEKDLYHLEYNIDQDrlnedgELIAPIEANEAIGTAKLVyDGETEDYGYISDAGSntgeFTLVT 410
Cdd:NF038273 318 TVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK------ELTAPIKKGQVVGKATFK-DKDLIGKGYLGEPPS----VELVA 386

                 ....*....
gi 516409375 411 NEAVEKSNW 419
Cdd:NF038273 387 KKDVKKSFF 395
 
Name Accession Description Interval E-value
strep_PBP3 NF038273
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ...
16-419 6.81e-125

streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.


Pssm-ID: 468443 [Multi-domain]  Cd Length: 407  Bit Score: 368.43  E-value: 6.81e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  16 ILVFTSMLTATTTVQANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDY 95
Cdd:NF038273   6 LLLLLLAFFLATTVSADDFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  96 PYSISANNSFSGVGLkQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNE 175
Cdd:NF038273  86 PYELTTNYEISNVPL-DARKYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 176 DLGDN-YPeGTNPNDTNLLSARSAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHegenlASYYYEGVDGLK 254
Cdd:NF038273 165 YLGDHiYP-GSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADFAGTTIYSYNYMLKG-----MPYYREGVDGLK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 255 TGFTDLAGYSFTGTAERNGQRLITVVMKT----GSETERFEETAKLLDYGFSNFENTELFSAGyQEEGNETVPVAKGKED 330
Cdd:NF038273 239 TGTTEKAGASFVATSVENGMRVITVVLNAdnadEDEYARFTATNQLLDYIYQNFEKVTLVKKG-QAYKDSKLPVIDGKKK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 331 QVSISLQDSVSVPIKADEKDLYHLEYNIDQDrlnedgELIAPIEANEAIGTAKLVyDGETEDYGYISDAGSntgeFTLVT 410
Cdd:NF038273 318 TVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK------ELTAPIKKGQVVGKATFK-DKDLIGKGYLGEPPS----VELVA 386

                 ....*....
gi 516409375 411 NEAVEKSNW 419
Cdd:NF038273 387 KKDVKKSFF 395
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
1-421 3.93e-111

D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 330.26  E-value: 3.93e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   1 MRNKLnkvlllavasILVFTSMLTATTTVQANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIE 80
Cdd:COG1686    1 MKKLL----------LLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  81 NGNITWDTTTEISDYPYSISAnnsfSGVGLKQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMG 160
Cdd:COG1686   71 AGKISLDDKVTVSEEAARTGG----SKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 161 LQEFKFVNSTGLDNEDlgdnypegtnpndtNLLSARSAALLAYHLVNDYEEALEISSIPQTTF---GGQTINNWNYMLph 237
Cdd:COG1686  147 MTNTHFVNPTGLPDPG--------------HYSTARDLALLARAAIKDYPEFYEIFSTKEFTFpngRGITLRNTNRLL-- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 238 egenlasYYYEGVDGLKTGFTDLAGYSFTGTAERNGQRLITVVMKTGSETERFEETAKLLDYGFSnfentelfsagyqee 317
Cdd:COG1686  211 -------GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGFP--------------- 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 318 gnetvpvaKGKEDQVSISLqdsvsvpikadekdlyhleynidqdrlneDGELIAPIEANEAIGTAKLVYDGETEdygyis 397
Cdd:COG1686  269 --------KGEALKAEVVL-----------------------------DGPLKAPVKKGQVVGTLVVTLDGKTI------ 305
                        410       420
                 ....*....|....*....|....
gi 516409375 398 dagsntGEFTLVTNEAVEKSNWFM 421
Cdd:COG1686  306 ------AEVPLVAAEDVEKAGFFS 323
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
31-281 4.46e-78

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 242.29  E-value: 4.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   31 ANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDYPYSISANNSFSGVgL 110
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGSSNIF-L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  111 KQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNEDlgdnypegtnpndt 190
Cdd:pfam00768  80 KPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHG-------------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  191 NLLSARSAALLAYHLVNDYEEALEISSIPQTTFggQTINNWNYMLPHegeNLASYYYEGVDGLKTGFTDLAGYSFTGTAE 270
Cdd:pfam00768 146 QYSSARDMAILAKALIKDLPEELSITKEKSFTF--RGINKINQRNRN---GLLWDKTWNVDGLKTGYTNEAGYCLVASAT 220
                         250
                  ....*....|.
gi 516409375  271 RNGQRLITVVM 281
Cdd:pfam00768 221 KGGMRLISVVM 231
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
15-360 2.23e-57

penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.


Pssm-ID: 468436 [Multi-domain]  Cd Length: 365  Bit Score: 193.27  E-value: 2.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  15 SILVFTSMLTATTTVQANE--LDLVS-------------ESAILVDgETGKVLYAKNPDVALPPASMTKMMTEYLVWEAI 79
Cdd:NF038258   2 VSLLLLSTIITPPASAAAEtpVEIANqegyqnlseqynpEGAIVTT-QTGQILYDYHGNKKWDPASMTKLMTMYLTLEAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  80 ENGNITWDTTTEISDYPYSISANNSFSGVGLKQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEM 159
Cdd:NF038258  81 KKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 160 GLQEFKFVNSTGLDNEDLGDNYPEGTNPNDTNLLSARSAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHEg 239
Cdd:NF038258 161 GMKHTHFTNPSGADNNLLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQ- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 240 enlaSYYYEGVDGLKTGFTDLaGYSFTGTAERNGQRLITVVMKT------GSETERFEETAKLLDYGFSNFENTELFSAG 313
Cdd:NF038258 240 ----PMSLKGTDGLKTGTSDE-GYNLALTTKRDGLRINQVIMNVgpypseGAKHARNKIANALMERAFKQYEYKKVLSKG 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 516409375 314 YQEegnetvpvAKGKEDQVSISLQDSVSvpikaDEKDLYHLEYNIDQ 360
Cdd:NF038258 315 EHK--------IDGKTYYVKKDLYDVVP-----KDKSKYDLKINKDG 348
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
40-420 4.22e-45

serine-type D-Ala-D-Ala carboxypeptidase DacD;


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 161.14  E-value: 4.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  40 SAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDYPYSiSANNSFSGVGL---KQQQEY 116
Cdd:PRK11397  38 SWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWA-KDNPVFVGSSLmflKEGDRV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 117 TVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNedlgdnypegtnPNDTNllSAR 196
Cdd:PRK11397 117 SVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGLDA------------PGQHS--SAY 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 197 SAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHEGENlasyyyegVDGLKTGFTDLAGYSFTGTAERNGQRL 276
Cdd:PRK11397 183 DLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMN--------VDGLKTGHTSGAGFNLIASAVDGQRRL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 277 ITVVMKTGSETERFEETAKLLDYGFSNFENTELFSAGyQEEGNETvpVAKGKEDQVSISLQDSVSVPIKADEKDLYHLEY 356
Cdd:PRK11397 255 IAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRG-KKVGTER--IWYGDKENIALGTEQDFWMVLPKAEIPHIKAKY 331
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516409375 357 NIDQDRLNedgeliAPIEANEAIGTAKLvYDGETEdygyisdagsnTGEFTLVTNEAVEKSNWF 420
Cdd:PRK11397 332 VLDGKELE------APISAHQRVGEIEL-YDRDKQ-----------VAHWPLVTLESVGEGGMF 377
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
304-416 1.94e-13

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 65.70  E-value: 1.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   304 FENTELFSAGyqeEGNETVPVAKGKEDQVSISLQDSVSVPIKADEKDLYHLEYNIDQDrlnedgELIAPIEANEAIGTAK 383
Cdd:smart00936   1 FETVKLYKKG---QVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKP------ELEAPIKKGQVVGTLV 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 516409375   384 LVYDGETEdygyisdagsntGEFTLVTNEAVEK 416
Cdd:smart00936  72 VTLDGKLI------------GEVPLVALEDVEK 92
 
Name Accession Description Interval E-value
strep_PBP3 NF038273
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ...
16-419 6.81e-125

streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.


Pssm-ID: 468443 [Multi-domain]  Cd Length: 407  Bit Score: 368.43  E-value: 6.81e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  16 ILVFTSMLTATTTVQANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDY 95
Cdd:NF038273   6 LLLLLLAFFLATTVSADDFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  96 PYSISANNSFSGVGLkQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNE 175
Cdd:NF038273  86 PYELTTNYEISNVPL-DARKYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 176 DLGDN-YPeGTNPNDTNLLSARSAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHegenlASYYYEGVDGLK 254
Cdd:NF038273 165 YLGDHiYP-GSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADFAGTTIYSYNYMLKG-----MPYYREGVDGLK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 255 TGFTDLAGYSFTGTAERNGQRLITVVMKT----GSETERFEETAKLLDYGFSNFENTELFSAGyQEEGNETVPVAKGKED 330
Cdd:NF038273 239 TGTTEKAGASFVATSVENGMRVITVVLNAdnadEDEYARFTATNQLLDYIYQNFEKVTLVKKG-QAYKDSKLPVIDGKKK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 331 QVSISLQDSVSVPIKADEKDLYHLEYNIDQDrlnedgELIAPIEANEAIGTAKLVyDGETEDYGYISDAGSntgeFTLVT 410
Cdd:NF038273 318 TVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK------ELTAPIKKGQVVGKATFK-DKDLIGKGYLGEPPS----VELVA 386

                 ....*....
gi 516409375 411 NEAVEKSNW 419
Cdd:NF038273 387 KKDVKKSFF 395
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
1-421 3.93e-111

D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 330.26  E-value: 3.93e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   1 MRNKLnkvlllavasILVFTSMLTATTTVQANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIE 80
Cdd:COG1686    1 MKKLL----------LLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  81 NGNITWDTTTEISDYPYSISAnnsfSGVGLKQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMG 160
Cdd:COG1686   71 AGKISLDDKVTVSEEAARTGG----SKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 161 LQEFKFVNSTGLDNEDlgdnypegtnpndtNLLSARSAALLAYHLVNDYEEALEISSIPQTTF---GGQTINNWNYMLph 237
Cdd:COG1686  147 MTNTHFVNPTGLPDPG--------------HYSTARDLALLARAAIKDYPEFYEIFSTKEFTFpngRGITLRNTNRLL-- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 238 egenlasYYYEGVDGLKTGFTDLAGYSFTGTAERNGQRLITVVMKTGSETERFEETAKLLDYGFSnfentelfsagyqee 317
Cdd:COG1686  211 -------GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGFP--------------- 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 318 gnetvpvaKGKEDQVSISLqdsvsvpikadekdlyhleynidqdrlneDGELIAPIEANEAIGTAKLVYDGETEdygyis 397
Cdd:COG1686  269 --------KGEALKAEVVL-----------------------------DGPLKAPVKKGQVVGTLVVTLDGKTI------ 305
                        410       420
                 ....*....|....*....|....
gi 516409375 398 dagsntGEFTLVTNEAVEKSNWFM 421
Cdd:COG1686  306 ------AEVPLVAAEDVEKAGFFS 323
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
31-281 4.46e-78

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 242.29  E-value: 4.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   31 ANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDYPYSISANNSFSGVgL 110
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGSSNIF-L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  111 KQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNEDlgdnypegtnpndt 190
Cdd:pfam00768  80 KPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHG-------------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  191 NLLSARSAALLAYHLVNDYEEALEISSIPQTTFggQTINNWNYMLPHegeNLASYYYEGVDGLKTGFTDLAGYSFTGTAE 270
Cdd:pfam00768 146 QYSSARDMAILAKALIKDLPEELSITKEKSFTF--RGINKINQRNRN---GLLWDKTWNVDGLKTGYTNEAGYCLVASAT 220
                         250
                  ....*....|.
gi 516409375  271 RNGQRLITVVM 281
Cdd:pfam00768 221 KGGMRLISVVM 231
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
15-360 2.23e-57

penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.


Pssm-ID: 468436 [Multi-domain]  Cd Length: 365  Bit Score: 193.27  E-value: 2.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  15 SILVFTSMLTATTTVQANE--LDLVS-------------ESAILVDgETGKVLYAKNPDVALPPASMTKMMTEYLVWEAI 79
Cdd:NF038258   2 VSLLLLSTIITPPASAAAEtpVEIANqegyqnlseqynpEGAIVTT-QTGQILYDYHGNKKWDPASMTKLMTMYLTLEAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  80 ENGNITWDTTTEISDYPYSISANNSFSGVGLKQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEM 159
Cdd:NF038258  81 KKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 160 GLQEFKFVNSTGLDNEDLGDNYPEGTNPNDTNLLSARSAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHEg 239
Cdd:NF038258 161 GMKHTHFTNPSGADNNLLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQ- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 240 enlaSYYYEGVDGLKTGFTDLaGYSFTGTAERNGQRLITVVMKT------GSETERFEETAKLLDYGFSNFENTELFSAG 313
Cdd:NF038258 240 ----PMSLKGTDGLKTGTSDE-GYNLALTTKRDGLRINQVIMNVgpypseGAKHARNKIANALMERAFKQYEYKKVLSKG 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 516409375 314 YQEegnetvpvAKGKEDQVSISLQDSVSvpikaDEKDLYHLEYNIDQ 360
Cdd:NF038258 315 EHK--------IDGKTYYVKKDLYDVVP-----KDKSKYDLKINKDG 348
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
40-420 4.22e-45

serine-type D-Ala-D-Ala carboxypeptidase DacD;


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 161.14  E-value: 4.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  40 SAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDYPYSiSANNSFSGVGL---KQQQEY 116
Cdd:PRK11397  38 SWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWA-KDNPVFVGSSLmflKEGDRV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 117 TVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNedlgdnypegtnPNDTNllSAR 196
Cdd:PRK11397 117 SVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGLDA------------PGQHS--SAY 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 197 SAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHEGENlasyyyegVDGLKTGFTDLAGYSFTGTAERNGQRL 276
Cdd:PRK11397 183 DLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMN--------VDGLKTGHTSGAGFNLIASAVDGQRRL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 277 ITVVMKTGSETERFEETAKLLDYGFSNFENTELFSAGyQEEGNETvpVAKGKEDQVSISLQDSVSVPIKADEKDLYHLEY 356
Cdd:PRK11397 255 IAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRG-KKVGTER--IWYGDKENIALGTEQDFWMVLPKAEIPHIKAKY 331
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516409375 357 NIDQDRLNedgeliAPIEANEAIGTAKLvYDGETEdygyisdagsnTGEFTLVTNEAVEKSNWF 420
Cdd:PRK11397 332 VLDGKELE------APISAHQRVGEIEL-YDRDKQ-----------VAHWPLVTLESVGEGGMF 377
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
35-392 7.15e-39

D-alanyl-D-alanine carboxypeptidase fraction A; Provisional


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 145.00  E-value: 7.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  35 DLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTTEISDYPYSiSANNSFSGVG---LK 111
Cdd:PRK10793  43 QIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWA-TGNPVFKGSSlmfLK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 112 QQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKFVNSTGLDNEDlgdnypegtnpndtN 191
Cdd:PRK10793 122 PGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADG--------------Q 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 192 LLSARSAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHEGENlasyyyegVDGLKTGFTDLAGYSFTGTAER 271
Cdd:PRK10793 188 YSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLN--------VDGIKTGHTDKAGYNLVASATE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 272 NGQRLITVVMKTGSETERFEETAKLLDYGFSNFENTELFSAGyQEEGNEtvPVAKGKEDQVSISLQDSVSVPI-KADEKD 350
Cdd:PRK10793 260 GQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVG-KEFASE--PVWFGDSDRASLGVDKDVYLTIpRGRMKD 336
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 516409375 351 LyHLEYNIDqdrlneDGELIAPIEANEAIGTAKLVYDGETED 392
Cdd:PRK10793 337 L-KASYVLN------TSELHAPLQKNQVVGTINFQLDGKTIE 371
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
11-390 9.95e-38

serine-type D-Ala-D-Ala carboxypeptidase;


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 141.67  E-value: 9.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  11 LAVASILVFTSMLTATTTVQANELDLVSESA-ILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTT 89
Cdd:PRK10001  11 LAAGSAFLFLFAPTAFAAEQTVEAPSVDARAwILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  90 TEISDYPYSiSANNSFSGVG---LKQQQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEFKF 166
Cdd:PRK10001  91 VTVGKDAWA-TGNPALRGSSvmfLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 167 VNSTGLDNedlgdnypegtnPNDTNllSARSAALLAYHLVNDYEEALEISSIPQTTFGGQTINNWNYMLPHEGENlasyy 246
Cdd:PRK10001 170 QTVHGLDA------------PGQFS--TARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLN----- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 247 yegVDGLKTGFTDLAGYSFTGTAERNGQRLITVVMKTGSETERFEETAKLLDYGFSNFENTELFSAgyqEEGNETVPVAK 326
Cdd:PRK10001 231 ---VDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKP---DATFVTQRVWF 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516409375 327 GKEDQVSISLQDSVSVPIKADEKDLYHLEYNIDQDrlnedgELIAPIEANEAIGTAKLVYDGET 390
Cdd:PRK10001 305 GDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEP------QLTAPLKKGQVVGTIDFQLNGKS 362
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
9-263 1.77e-17

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 82.81  E-value: 1.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   9 LLLAVASILVFTSMLTATTTVQ--ANELDLVSESAILVDGETGKVLYAKNPDVALPPASMTKMMTEYLVWEAiengNITW 86
Cdd:PRK11669  10 LLLLLAGVPFAPQAVAKTAAATtaSQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA----KLPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  87 DT--TTEISDYPysiSANNSFSGVGLKqqQEYTVKELYEAMAINSDNATTIALAELIAGSESEFVKMMNEKGEEMGLQEF 164
Cdd:PRK11669  86 DEklKVDISQTP---EMKGVYSRVRLN--SEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375 165 KFVNSTGLDNEdlgdnypegtnpndtNLLSARSAALL-----AYHLVNdyeealEISSIPQTTFggqTINNWNYMLPHEG 239
Cdd:PRK11669 161 RYVEPTGLSIH---------------NVSTARDLTKLliaskQYPLIG------QLSTTREKTA---TFRKPNYTLPFRN 216
                        250       260
                 ....*....|....*....|....*
gi 516409375 240 ENLASYYYE-GVDGLKTGFTDLAGY 263
Cdd:PRK11669 217 TNHLVYRDNwNIQLTKTGFTNAAGH 241
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
304-416 6.56e-14

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 429749 [Multi-domain]  Cd Length: 91  Bit Score: 67.23  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  304 FENTELFSAGYQEEgneTVPVAKGKEDQVSISLQDSVSVPIKADEKDLYHLEYNIDQDrlnedgeLIAPIEANEAIGTAK 383
Cdd:pfam07943   1 FETKKLYKKGDVVK---KVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP-------LEAPIKKGQVVGKLE 70
                          90       100       110
                  ....*....|....*....|....*....|...
gi 516409375  384 LVYDGETedygyisdagsnTGEFTLVTNEAVEK 416
Cdd:pfam07943  71 VYLDGKL------------IGEVPLVAKEDVEE 91
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
304-416 1.94e-13

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 65.70  E-value: 1.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   304 FENTELFSAGyqeEGNETVPVAKGKEDQVSISLQDSVSVPIKADEKDLYHLEYNIDQDrlnedgELIAPIEANEAIGTAK 383
Cdd:smart00936   1 FETVKLYKKG---QVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKP------ELEAPIKKGQVVGTLV 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 516409375   384 LVYDGETEdygyisdagsntGEFTLVTNEAVEK 416
Cdd:smart00936  72 VTLDGKLI------------GEVPLVALEDVEK 92
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
6-208 2.77e-08

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 54.90  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   6 NKVLLLAVASILVFTSMLTATTTVQANELDLVSESAILV-DGETGKVLyAKNPDVALPPASMTKMMTEYLVWEAIENGNI 84
Cdd:COG2367    1 MRLLALLLLAAAAAAPASALEAELAALEAALGGRVGVYVlDLDTGETV-GINADERFPAASTFKLPVLAAVLRQVDAGKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  85 TWDTTTEISDYPYSisannSFSGV--GLKQQQEYTVKELYEAMAINSDNATTIALAELIAGSEsefvkmMNEKGEEMGLQ 162
Cdd:COG2367   80 SLDERVTLTPEDLV-----GGSGIlqKLPDGTGLTLRELAELMITVSDNTATNLLLRLLGPDA------VNAFLRSLGLT 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 516409375 163 EFKFVNSTGLDNEDLGDNypegtnpndTNLLSARSAALLAYHLVND 208
Cdd:COG2367  149 DTRLDRKEPDLNELPGDG---------RNTTTPRDMARLLAALYRG 185
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
43-208 1.22e-07

Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 463854 [Multi-domain]  Cd Length: 215  Bit Score: 52.28  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375   43 LVDGETGKVLyAKNPDVALPPASMTKMMTEYLVWEAIENGNITWDTTteisdYPYSISANNSFSGVGLKQQ--QEYTVKE 120
Cdd:pfam13354   4 VRDLDTGEEL-GINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDER-----LTVTAEDKVGGSGILQYLPdgSQLSLRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516409375  121 LYEAMAINSDNATTIALAELIAGSEsefvkmMNEKGEEMGLQEfkfvnsTGLDNEDLGDNYPEGTNpndTNLLSARSAAL 200
Cdd:pfam13354  78 LLTLMIAVSDNTATNLLIDRLGLEA------VNARLRALGLRD------TRLRRKLPDLRAADKGG---TNTTTARDMAK 142

                  ....*...
gi 516409375  201 LAYHLVND 208
Cdd:pfam13354 143 LLEALYRG 150
 
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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