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Conserved domains on  [gi|557786117|ref|NP_001273599|]
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beta-alanine-activating enzyme isoform 4 [Homo sapiens]

Protein Classification

PQQ-binding-like beta-propeller repeat protein( domain architecture ID 29103)

PQQ (pyrroloquinoline quinone)-binding-like beta-propeller repeat protein

Gene Ontology:  GO:0070968
PubMed:  16232604|11831471

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PQQ_DH_like super family cl11493
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
 265-606 7.61e-13

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


The actual alignment was detected with superfamily member TIGR03300:

Pssm-ID: 472205 [Multi-domain]  Cd Length: 377  Bit Score: 70.35  E-value: 7.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  265 TQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILGDRIesSACVSKCGNFIVV 344
Cdd:TIGR03300  35 QPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGK--VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  345 GCYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTT--GLIYIGSHDQHAYALDIYRKKCVWkskcggtVFSS--PCLN 420
Cdd:TIGR03300 111 GTEKGEVIALDAEDGKELW----RAKLSSEVLSPPLVanGLVVVRTNDGRLTALDAATGERLW-------TYSRvtPPLT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  421 L--------IPHHLYFATLGGLLLAVNPATGNVIWKHSCGKP-----------LFSSPqccsqyicigCVDGNLLCFTHF 481
Cdd:TIGR03300 180 LrgsaspviADGGVLVGFAGGKLVALDLQTGQPLWEQRVALPkgrtelerlvdVDGDP----------VVDGGQVYAVSY 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  482 GEQVWQFSTSGpifsspctspseqkiffgshdcfiyccnmkGHLQWKFETTSrvYATPFAFHNYngsnemlLAAASTDGK 561
Cdd:TIGR03300 250 QGRVAALDLRS------------------------------GRVLWKRDASS--YQGPAVDDNR-------LYVTDADGV 290

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 557786117  562 VWILESQSGQ-LQSVYELPGEVFSSPVVLESMLIIGCRDNYVYCLD 606
Cdd:TIGR03300 291 VVALDRRSGSeLWKNDELKYRQLTAPAVLGGYLVVGDFEGYLHWLD 336
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 5-48 5.22e-10

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd17654:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 449  Bit Score: 62.10  E-value: 5.22e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 557786117   5 DASVKEYIFKELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd17654  405 GESSSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PRK05691 super family cl35369
peptide synthase; Validated
 6-112 1.34e-06

peptide synthase; Validated


The actual alignment was detected with superfamily member PRK05691:

Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 51.71  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117    6 ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNkiyLNYINLKSENKLSGKEDLWEKLQYLWKSTLNLP 85
Cdd:PRK05691 2649 AALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APDPELNRQAYQAPRSELEQQLAQIWREVLNVE 2725

                          90       100
                  ....*....|....*....|....*..
gi 557786117   86 edllRVPDESLFLNSGGDSLKSIRLLS 112
Cdd:PRK05691 2726 ----RVGLGDNFFELGGDSILSIQVVS 2748
 
Name Accession Description Interval E-value
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 265-606 7.61e-13

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 70.35  E-value: 7.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  265 TQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILGDRIesSACVSKCGNFIVV 344
Cdd:TIGR03300  35 QPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGK--VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  345 GCYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTT--GLIYIGSHDQHAYALDIYRKKCVWkskcggtVFSS--PCLN 420
Cdd:TIGR03300 111 GTEKGEVIALDAEDGKELW----RAKLSSEVLSPPLVanGLVVVRTNDGRLTALDAATGERLW-------TYSRvtPPLT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  421 L--------IPHHLYFATLGGLLLAVNPATGNVIWKHSCGKP-----------LFSSPqccsqyicigCVDGNLLCFTHF 481
Cdd:TIGR03300 180 LrgsaspviADGGVLVGFAGGKLVALDLQTGQPLWEQRVALPkgrtelerlvdVDGDP----------VVDGGQVYAVSY 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  482 GEQVWQFSTSGpifsspctspseqkiffgshdcfiyccnmkGHLQWKFETTSrvYATPFAFHNYngsnemlLAAASTDGK 561
Cdd:TIGR03300 250 QGRVAALDLRS------------------------------GRVLWKRDASS--YQGPAVDDNR-------LYVTDADGV 290

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 557786117  562 VWILESQSGQ-LQSVYELPGEVFSSPVVLESMLIIGCRDNYVYCLD 606
Cdd:TIGR03300 291 VVALDRRSGSeLWKNDELKYRQLTAPAVLGGYLVVGDFEGYLHWLD 336
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
 382-606 1.77e-12

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 68.90  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 382 GLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQC 461
Cdd:cd10276   39 DMVYAADANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSPPT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 462 CSQ-YICIGCVDGNLLCF-THFGEQVWQFSTSGPIFSSPCTSP---SEQKIFFGSHDCFIYCCNMK-GHLQWKFETTSRV 535
Cdd:cd10276  119 YADgKIYVGTGDGRLYYCnAETGKVVWNRTSTAPELSLRGGAApvgAYDVVFVGDGNGTVVALNTGtGVDIWEFSVSEPR 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557786117 536 YATPFA--------FHNYNGSnemlLAAASTDGKVWILESQSGQLQSVYELpGEVFSSPVVLESMLIIGCRDNYVYCLD 606
Cdd:cd10276  199 GRTELPrmidssvtYVVVGGY----LYSTSYQGYLVALDFESGQFLWSRKA-SGGTSTSTDANGRVYVGDGEGSLYCLD 272
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 250-447 2.52e-11

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 65.61  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 250 SCVAKVSEEGKPA---IGTQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILG 326
Cdd:COG1520    9 SGFSSEDDEPPPAplpEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDR--VYAADADGRVAALDAATGKELWRVDLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 327 DRIesSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTT--GLIYIGSHDQHAYALDIYRKKCV 404
Cdd:COG1520   87 EPL--SGGVGADGGLVVVGTEDGEVIALDADDGEELW----RARLSSEVLAAPAVagGRVVVRTGDGRVYALDAATGERL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557786117 405 WkskcggtVFSS--PCLNL--------IPHHLYFATLGGLLLAVNPATGNVIW 447
Cdd:COG1520  161 W-------SYQRpvPALTLrgtsspviVGGAVLVGFANGKLVALDLANGQPLW 206
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 308-528 9.05e-11

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 62.42  E-value: 9.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  308 RMKAVDFYSGKVKWEQILGDRIESSACVSkcGNFIVVGCYNGLVYVLKSNSGEKYWMFTTEDAVKSSATMDptTGLIYIG 387
Cdd:pfam13360   4 VVTALDAATGAELWRVDLETGLGGGVAVD--GGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVA--GGRVFVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  388 SHDQHAYALDIYRKKCVW---KSKCGGTVFSSPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKP---------- 454
Cdd:pfam13360  80 AGDGSLIALDAADGRRLWsyqRSGEPLALRSSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAPrgtnelerlv 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557786117  455 -LFSSPQCCSQYICIGCVDGNLLCF-THFGEQVWQfstsgPIFSSPCT-SPSEQKIFFGSHDCFIYCCNMK-GHLQWK 528
Cdd:pfam13360 160 dITGTPVVAGGRVFASAYQGRLVAFdAATGRRLWT-----REISGPNGpILDGDLLYVVSDDGELYALDRAtGAVVWK 232
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 5-48 5.22e-10

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 62.10  E-value: 5.22e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 557786117   5 DASVKEYIFKELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd17654  405 GESSSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PRK05691 PRK05691
peptide synthase; Validated
 6-112 1.34e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 51.71  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117    6 ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNkiyLNYINLKSENKLSGKEDLWEKLQYLWKSTLNLP 85
Cdd:PRK05691 2649 AALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APDPELNRQAYQAPRSELEQQLAQIWREVLNVE 2725

                          90       100
                  ....*....|....*....|....*..
gi 557786117   86 edllRVPDESLFLNSGGDSLKSIRLLS 112
Cdd:PRK05691 2726 ----RVGLGDNFFELGGDSILSIQVVS 2748
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 67-123 2.97e-05

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 42.53  E-value: 2.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786117  67 KEDLWEKLQYLWKSTLNLPEDLLRvPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:COG0236    3 REELEERLAEIIAEVLGVDPEEIT-PDDSFFEDLGLDSLDAVELIAALEEEFGIELP 58
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
 348-450 3.04e-05

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 46.46  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 348 NGLVYVLKSNSGEKYW---------MFTTEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPC 418
Cdd:PRK11138  78 AGLVKALDADTGKEIWsvdlsekdgWFSKNKSALLSGGVTVAGGKVYIGSEKGQVYALNAEDGEVAWQTKVAGEALSRPV 157

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557786117 419 L--NLIPHHlyfaTLGGLLLAVNPATGNVIWKHS 450
Cdd:PRK11138 158 VsdGLVLVH----TSNGMLQALNESDGAVKWTVN 187
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 72-123 1.45e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 40.24  E-value: 1.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557786117   72 EKLQYLWKSTLNLPEDLLrVPDESLFlNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:pfam00550   1 ERLRELLAEVLGVPAEEI-DPDTDLF-DLGLDSLLAVELIARLEEEFGVEIP 50
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 8-123 6.63e-04

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 43.13  E-value: 6.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117     8 VKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKID--------VSELNKIYLNYINLKSENKLSGKE----DLWEKLq 75
Cdd:TIGR03443  786 IREY----LKKKLPSYAIPTVIVPLKKLPLNPNGKVDkpalpfpdTAQLAAVAKNRSASAADEEFTETEreirDLWLEL- 860

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 557786117    76 ylwkstlnLPEDLLRV-PDESlFLNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:TIGR03443  861 --------LPNRPATIsPDDS-FFDLGGHSILATRMIFELRKKLNVELP 900
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2-50 2.73e-03

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 40.65  E-value: 2.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557786117   2 VSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDV----SELNK 50
Cdd:PRK04813 451 FEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRkaliEEVNK 503
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 12-53 7.99e-03

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 39.02  E-value: 7.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 557786117  12 IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYL 53
Cdd:COG0318  405 LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
 
Name Accession Description Interval E-value
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 265-606 7.61e-13

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 70.35  E-value: 7.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  265 TQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILGDRIesSACVSKCGNFIVV 344
Cdd:TIGR03300  35 QPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGK--VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  345 GCYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTT--GLIYIGSHDQHAYALDIYRKKCVWkskcggtVFSS--PCLN 420
Cdd:TIGR03300 111 GTEKGEVIALDAEDGKELW----RAKLSSEVLSPPLVanGLVVVRTNDGRLTALDAATGERLW-------TYSRvtPPLT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  421 L--------IPHHLYFATLGGLLLAVNPATGNVIWKHSCGKP-----------LFSSPqccsqyicigCVDGNLLCFTHF 481
Cdd:TIGR03300 180 LrgsaspviADGGVLVGFAGGKLVALDLQTGQPLWEQRVALPkgrtelerlvdVDGDP----------VVDGGQVYAVSY 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  482 GEQVWQFSTSGpifsspctspseqkiffgshdcfiyccnmkGHLQWKFETTSrvYATPFAFHNYngsnemlLAAASTDGK 561
Cdd:TIGR03300 250 QGRVAALDLRS------------------------------GRVLWKRDASS--YQGPAVDDNR-------LYVTDADGV 290

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 557786117  562 VWILESQSGQ-LQSVYELPGEVFSSPVVLESMLIIGCRDNYVYCLD 606
Cdd:TIGR03300 291 VVALDRRSGSeLWKNDELKYRQLTAPAVLGGYLVVGDFEGYLHWLD 336
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
 382-606 1.77e-12

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 68.90  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 382 GLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQC 461
Cdd:cd10276   39 DMVYAADANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSPPT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 462 CSQ-YICIGCVDGNLLCF-THFGEQVWQFSTSGPIFSSPCTSP---SEQKIFFGSHDCFIYCCNMK-GHLQWKFETTSRV 535
Cdd:cd10276  119 YADgKIYVGTGDGRLYYCnAETGKVVWNRTSTAPELSLRGGAApvgAYDVVFVGDGNGTVVALNTGtGVDIWEFSVSEPR 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557786117 536 YATPFA--------FHNYNGSnemlLAAASTDGKVWILESQSGQLQSVYELpGEVFSSPVVLESMLIIGCRDNYVYCLD 606
Cdd:cd10276  199 GRTELPrmidssvtYVVVGGY----LYSTSYQGYLVALDFESGQFLWSRKA-SGGTSTSTDANGRVYVGDGEGSLYCLD 272
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 250-447 2.52e-11

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 65.61  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 250 SCVAKVSEEGKPA---IGTQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILG 326
Cdd:COG1520    9 SGFSSEDDEPPPAplpEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDR--VYAADADGRVAALDAATGKELWRVDLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 327 DRIesSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTT--GLIYIGSHDQHAYALDIYRKKCV 404
Cdd:COG1520   87 EPL--SGGVGADGGLVVVGTEDGEVIALDADDGEELW----RARLSSEVLAAPAVagGRVVVRTGDGRVYALDAATGERL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557786117 405 WkskcggtVFSS--PCLNL--------IPHHLYFATLGGLLLAVNPATGNVIW 447
Cdd:COG1520  161 W-------SYQRpvPALTLrgtsspviVGGAVLVGFANGKLVALDLANGQPLW 206
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 308-528 9.05e-11

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 62.42  E-value: 9.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  308 RMKAVDFYSGKVKWEQILGDRIESSACVSkcGNFIVVGCYNGLVYVLKSNSGEKYWMFTTEDAVKSSATMDptTGLIYIG 387
Cdd:pfam13360   4 VVTALDAATGAELWRVDLETGLGGGVAVD--GGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVA--GGRVFVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  388 SHDQHAYALDIYRKKCVW---KSKCGGTVFSSPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKP---------- 454
Cdd:pfam13360  80 AGDGSLIALDAADGRRLWsyqRSGEPLALRSSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAPrgtnelerlv 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557786117  455 -LFSSPQCCSQYICIGCVDGNLLCF-THFGEQVWQfstsgPIFSSPCT-SPSEQKIFFGSHDCFIYCCNMK-GHLQWK 528
Cdd:pfam13360 160 dITGTPVVAGGRVFASAYQGRLVAFdAATGRRLWT-----REISGPNGpILDGDLLYVVSDDGELYALDRAtGAVVWK 232
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 5-48 5.22e-10

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 62.10  E-value: 5.22e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 557786117   5 DASVKEYIFKELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd17654  405 GESSSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
 265-607 3.35e-09

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 58.88  E-value: 3.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 265 TQKMELHVRWRSDTGKC----VDASPLVViptfdksSTTVYIGSHSHRMKAVDFYSGKVKWEQILGDRIESSACVSKCGN 340
Cdd:cd10276    9 TPEFDPEVLWSKSVGNGgmagIDLTPVVA-------GDMVYAADANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGNG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 341 FIVVGCYNGLVYVLKSNSGEKYWMFTTEDAVKSSAtmdPTT--GLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPC 418
Cdd:cd10276   82 KIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSP---PTYadGKIYVGTGDGRLYYCNAETGKVVWNRTSTAPELSLRG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 419 ------LNLIphhlYFATLG-GLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQYICIGCVDGNL-LCFTHFGEQVW---- 486
Cdd:cd10276  159 gaapvgAYDV----VFVGDGnGTVVALNTGTGVDIWEFSVSEPRGRTELPRMIDSSVTYVVVGGyLYSTSYQGYLValdf 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 487 ---QFSTSGPIFSSPCTS-PSEQKIFFGSHDCFIYCCNMK-GHLQWKFE-TTSRVYATP-FAFHNYngsnemLLAAASTD 559
Cdd:cd10276  235 esgQFLWSRKASGGTSTStDANGRVYVGDGEGSLYCLDAStGDELWSQTvLLGRVLSSPaIYVGVY------IYVTDNAE 308

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 557786117 560 GKVWILESQSGQL-------QSVYELPGevfssPVVLESMLIIGCRDNYVYCLDL 607
Cdd:cd10276  309 GYLYCLKDNDGLTvarvevdYSQYILQG-----PAVSDGWLYYGTDDGYLYALTR 358
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 272-448 2.69e-08

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 54.72  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  272 VRWRSDTGKCVDASPLVviptfdkSSTTVYIGSHSHRMKAVDFYSGKVKWEQilgDRIESSACVS------KCGNFIVVG 345
Cdd:pfam13360  55 LLWRQTLSGEVLGAPLV-------AGGRVFVVAGDGSLIALDAADGRRLWSY---QRSGEPLALRssgspaVVGDTVVAG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  346 CYNGLVYVLKSNSGEKYWMF-------TTEDAVKSSATMDPT--TGLIYIGSHDQHAYALDIYRKKCVWKskcggTVFSS 416
Cdd:pfam13360 125 FSSGKLVALDPATGKVRWEAplaaprgTNELERLVDITGTPVvaGGRVFASAYQGRLVAFDAATGRRLWT-----REISG 199

                         170       180       190
                  ....*....|....*....|....*....|...
gi 557786117  417 PCLNLIPH-HLYFATLGGLLLAVNPATGNVIWK 448
Cdd:pfam13360 200 PNGPILDGdLLYVVSDDGELYALDRATGAVVWK 232
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 348-571 5.81e-08

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 53.95  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  348 NGLVYVLKSNSGEKYWMFTTEDAVKSSATMDptTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPCLNLIphHLY 427
Cdd:pfam13360   2 DGVVTALDAATGAELWRVDLETGLGGGVAVD--GGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVAGG--RVF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  428 FATLGGLLLAVNPATGNVIWKHSCGKPLF-----SSPQCCSQYICIGCVDGNLLCF---ThfGEQVWQFSTSGP------ 493
Cdd:pfam13360  78 VVAGDGSLIALDAADGRRLWSYQRSGEPLalrssGSPAVVGDTVVAGFSSGKLVALdpaT--GKVRWEAPLAAPrgtnel 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  494 -----IFSSPctSPSEQKIFFGSHDCFIYCCNMkghlqwkfETTSRVYATPFAfhnynGSNEMLLAA-----ASTDGKVW 563
Cdd:pfam13360 156 erlvdITGTP--VVAGGRVFASAYQGRLVAFDA--------ATGRRLWTREIS-----GPNGPILDGdllyvVSDDGELY 220


                  ....*...
gi 557786117  564 ILESQSGQ 571
Cdd:pfam13360 221 ALDRATGA 228
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 2-48 2.16e-07

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 53.69  E-value: 2.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 557786117   2 VSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd05930  396 VPDEGGEldEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
PRK05691 PRK05691
peptide synthase; Validated
 6-112 1.34e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 51.71  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117    6 ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNkiyLNYINLKSENKLSGKEDLWEKLQYLWKSTLNLP 85
Cdd:PRK05691 2649 AALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APDPELNRQAYQAPRSELEQQLAQIWREVLNVE 2725

                          90       100
                  ....*....|....*....|....*..
gi 557786117   86 edllRVPDESLFLNSGGDSLKSIRLLS 112
Cdd:PRK05691 2726 ----RVGLGDNFFELGGDSILSIQVVS 2748
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 404-612 1.43e-06

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 50.70  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  404 VWKSKCGGTVFSSPcLNLIPHH----LYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQYICIGCVDGNLLCFT 479
Cdd:TIGR03300  43 VWSASVGDGVGHYY-LRLQPAVaggkVYAADADGTVAALDAETGKRLWRVDLDERLSGGVGADGGLVFVGTEKGEVIALD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  480 HF-GEQVWQFSTSGPIFSSPCTspSEQKIFFGSHDCFIYCCNMK-GHLQWKFET-----TSRVYATPFAFHNyngsnemL 552
Cdd:TIGR03300 122 AEdGKELWRAKLSSEVLSPPLV--ANGLVVVRTNDGRLTALDAAtGERLWTYSRvtpplTLRGSASPVIADG-------G 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557786117  553 LAAASTDGKVWILESQSGQL---QSVYELPG--------EVFSSPVVLESMLIIGCRDNYVYCLDLLGGNQ 612
Cdd:TIGR03300 193 VLVGFAGGKLVALDLQTGQPlweQRVALPKGrtelerlvDVDGDPVVDGGQVYAVSYQGRVAALDLRSGRV 263
PQQ_DH_like cd00216
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
 310-500 4.40e-06

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


Pssm-ID: 199833 [Multi-domain]  Cd Length: 434  Bit Score: 49.53  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 310 KAVDFYSGKVKWEQILGDRIESSACVSKCGNFIVVG------------------CYNGLVYVLKSNSGEKYWMF--TTED 369
Cdd:cd00216  176 TDRNTPTGDEHTWTSGGGTGWSSAAYDAELNLIYVGggnptpwnwggnrtpgdnLYTSSIVAVNADTGEMKWQYqtTPHD 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 370 AVKSSATMDPT----------TGLIYIGSHDQHAYALDIYRKKCVWKSKCGGtVFSSPclnliPHHLYFATLGGLLLAVN 439
Cdd:cd00216  256 AWDYDGDNTPVladikvkgkkVKVLFAPAKNGNFYVLDRRNGELVSARPLVP-DSYDP-----DRELFYVPANGRIMALD 329

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786117 440 PATGNVIWKHSCGKPLFSSP-QCCSQYICIGCVDGNLLCF-THFGEQVWQFSTSGPIFSSPCT 500
Cdd:cd00216  330 PVTGVVVWEKSELHPLLGGPlSTAGNLVFVGTSDGYLKAYnADTGEKLWQQKVPSGFQAEPVT 392
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 272-407 6.89e-06

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 47.78  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  272 VRWRSDTGkcvdASPLVVIPTFDKS--STTVYIGSHSHRMKAVDFYSGKVKWEQIL-----GDRIE-----SSACVSKCG 339
Cdd:pfam13360  95 RLWSYQRS----GEPLALRSSGSPAvvGDTVVAGFSSGKLVALDPATGKVRWEAPLaaprgTNELErlvdiTGTPVVAGG 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557786117  340 NFIVVGcYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKS 407
Cdd:pfam13360 171 RVFASA-YQGRLVAFDAATGRRLW----TREISGPNGPILDGDLLYVVSDDGELYALDRATGAVVWKT 233
PRK12467 PRK12467
peptide synthase; Provisional
 16-152 7.32e-06

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 49.39  E-value: 7.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117   16 LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiylNYINLKSENKLSGKEDLWEKLQYLWKSTLnlpeDLLRVPDES 95
Cdd:PRK12467  980 LRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK---PDASAVQATFVAPQTELEKRLAAIWADVL----KVERVGLTD 1052

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786117   96 LFLNSGGDSLKSIRLLSEIEKLVGTSVPglLEIILSSSILEIYnhiLQTVVPDEDVT 152
Cdd:PRK12467 1053 NFFELGGHSLLATQVISRVRQRLGIQVP--LRTLFEHQTLAGF---AQAVAAQQQGA 1104
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 67-123 2.97e-05

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 42.53  E-value: 2.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786117  67 KEDLWEKLQYLWKSTLNLPEDLLRvPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:COG0236    3 REELEERLAEIIAEVLGVDPEEIT-PDDSFFEDLGLDSLDAVELIAALEEEFGIELP 58
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
 348-450 3.04e-05

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 46.46  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 348 NGLVYVLKSNSGEKYW---------MFTTEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPC 418
Cdd:PRK11138  78 AGLVKALDADTGKEIWsvdlsekdgWFSKNKSALLSGGVTVAGGKVYIGSEKGQVYALNAEDGEVAWQTKVAGEALSRPV 157

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557786117 419 L--NLIPHHlyfaTLGGLLLAVNPATGNVIWKHS 450
Cdd:PRK11138 158 VsdGLVLVH----TSNGMLQALNESDGAVKWTVN 187
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 433-611 3.68e-05

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 45.47  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  433 GLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQYICIGCVDGNLLCFTHF-GEQVWQFSTSGPIFSSPctSPSEQKIFFGS 511
Cdd:pfam13360   3 GVVTALDAATGAELWRVDLETGLGGGVAVDGGRLFVATGGGQLVALDAAtGKLLWRQTLSGEVLGAP--LVAGGRVFVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  512 HDCFIYCCNMK-GHLQWKFETTSRVYAtpfafHNYNGSNEM---LLAAASTDGKVWILESQSGQLQ-----------SVY 576
Cdd:pfam13360  81 GDGSLIALDAAdGRRLWSYQRSGEPLA-----LRSSGSPAVvgdTVVAGFSSGKLVALDPATGKVRweaplaaprgtNEL 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 557786117  577 ELPGEVFSSPVVLESMLIIGCRDNYVYCLDLLGGN 611
Cdd:pfam13360 156 ERLVDITGTPVVAGGRVFASAYQGRLVAFDAATGR 190
PRK05691 PRK05691
peptide synthase; Validated
 1-123 6.83e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 46.31  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117    1 MVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNyiNLKSENKLSGKEDLWEKLQYLWKS 80
Cdd:PRK05691 4175 TVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIG--QLQSQAYLAPRNELEQTLATIWAD 4252

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 557786117   81 TLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:PRK05691 4253 VLKVE----RVGVHDNFFELGGHSLLATQIASRVQKALQRNVP 4291
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 426-596 8.18e-05

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 45.19  E-value: 8.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 426 LYFATLGGLLLAVNPATGNVIWKHSCGKPLfsspqccsqyicigcvdgnllcfthfgeqvwqfstSGPIFSspctspSEQ 505
Cdd:COG1520   60 VYAADADGRVAALDAATGKELWRVDLGEPL-----------------------------------SGGVGA------DGG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 506 KIFFGSHDCFIYCCNMK-GHLQWKFETTSRVYATPFAfhnyngSNEMLLaAASTDGKVWILESQSGQLQSVYELPGEVF- 583
Cdd:COG1520   99 LVVVGTEDGEVIALDADdGEELWRARLSSEVLAAPAV------AGGRVV-VRTGDGRVYALDAATGERLWSYQRPVPALt 171

                        170
                 ....*....|....*..
gi 557786117 584 ----SSPVVLESMLIIG 596
Cdd:COG1520  172 lrgtSSPVIVGGAVLVG 188
PQQ_DH_like cd00216
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
 278-415 1.21e-04

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


Pssm-ID: 199833 [Multi-domain]  Cd Length: 434  Bit Score: 44.91  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 278 TGKCVDASPLVVIpTFDKSSTTVYIGSHShRMKAVDFYSGKVKWEQILGDRIESSAcVSKCGNFIVVGCYNGLVYVLKSN 357
Cdd:cd00216  296 NGELVSARPLVPD-SYDPDRELFYVPANG-RIMALDPVTGVVVWEKSELHPLLGGP-LSTAGNLVFVGTSDGYLKAYNAD 372

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557786117 358 SGEKYWMFTTEDAVKS---SATMDPTTGL-IYIGSHDqhAYALDIYRKKCVWKSKCGGTVFS 415
Cdd:cd00216  373 TGEKLWQQKVPSGFQAepvTYEVDGEQYVlIQAGGGG--AFPLWGGMADLTRGTQMGGTVVV 432
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 72-123 1.45e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 40.24  E-value: 1.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557786117   72 EKLQYLWKSTLNLPEDLLrVPDESLFlNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:pfam00550   1 ERLRELLAEVLGVPAEEI-DPDTDLF-DLGLDSLLAVELIARLEEEFGVEIP 50
PRK12316 PRK12316
peptide synthase; Provisional
 16-123 1.47e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 45.33  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117   16 LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLnyiNLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDES 95
Cdd:PRK12316 2466 LAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDV---SQLRQAYVAPQEGLEQRLAAIWQAVLKVE----QVGLDD 2538

                          90       100
                  ....*....|....*....|....*...
gi 557786117   96 LFLNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:PRK12316 2539 HFFELGGHSLLATQVVSRVRQDLGLEVP 2566
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 5-48 1.76e-04

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 44.50  E-value: 1.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 557786117   5 DASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd12117  444 AAELRAF----LRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 16-48 2.05e-04

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 44.23  E-value: 2.05e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 557786117  16 LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd12115  415 LGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
PRK12316 PRK12316
peptide synthase; Provisional
 16-123 2.88e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 44.18  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117   16 LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDES 95
Cdd:PRK12316 5022 LRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP---DASLLQQAYVAPRSELEQQVAAIWAEVLQLE----RVGLDD 5094

                          90       100
                  ....*....|....*....|....*...
gi 557786117   96 LFLNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:PRK12316 5095 NFFELGGHSLLAIQVTSRIQLELGLELP 5122
PRK12316 PRK12316
peptide synthase; Provisional
 3-112 3.01e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 44.18  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117    3 SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTL 82
Cdd:PRK12316 3493 DEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP---DAALLQQDYVAPVNELERRLAAIWADVL 3569

                          90       100       110
                  ....*....|....*....|....*....|
gi 557786117   83 NLPedllRVPDESLFLNSGGDSLKSIRLLS 112
Cdd:PRK12316 3570 KLE----QVGLTDNFFELGGDSIISLQVVS 3595
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 14-48 5.74e-04

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 42.68  E-value: 5.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 557786117  14 KELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd17653  397 SELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 523-613 5.86e-04

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 42.49  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 523 GHLQWKFETTSRVYATPfafhnynGSNEMLLAAASTDGKVWILESQSGQLQSVYELPGEVFSSPVVLESMLIIGCRDNYV 602
Cdd:COG1520   77 GKELWRVDLGEPLSGGV-------GADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAVAGGRVVVRTGDGRV 149

                         90
                 ....*....|.
gi 557786117 603 YCLDLLGGNQK 613
Cdd:COG1520  150 YALDAATGERL 160
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 8-123 6.63e-04

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 43.13  E-value: 6.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117     8 VKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKID--------VSELNKIYLNYINLKSENKLSGKE----DLWEKLq 75
Cdd:TIGR03443  786 IREY----LKKKLPSYAIPTVIVPLKKLPLNPNGKVDkpalpfpdTAQLAAVAKNRSASAADEEFTETEreirDLWLEL- 860

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 557786117    76 ylwkstlnLPEDLLRV-PDESlFLNSGGDSLKSIRLLSEIEKLVGTSVP 123
Cdd:TIGR03443  861 --------LPNRPATIsPDDS-FFDLGGHSILATRMIFELRKKLNVELP 900
PQQ_3 pfam13570
PQQ-like domain;
482-518 9.20e-04

PQQ-like domain;


Pssm-ID: 463925 [Multi-domain]  Cd Length: 36  Bit Score: 37.18  E-value: 9.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 557786117  482 GEQVWQFSTSGPIFSSPCTspSEQKIFFGSHDCFIYC 518
Cdd:pfam13570   1 GEVLWRFETGGPIVSSPAV--AGGLVYVGTGDGTLYA 35
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 390-612 1.01e-03

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 41.23  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  390 DQHAYALDIYRKKCVWKSKC-----GGTVFSSPclnliphHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQ 464
Cdd:pfam13360   2 DGVVTALDAATGAELWRVDLetglgGGVAVDGG-------RLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVAGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  465 YICIGCVDGNLLCF-THFGEQVWQFSTSGP---IFSSPCTSPSEQKIFFGSHDCFIYCCNMK-GHLQWKFETTS------ 533
Cdd:pfam13360  75 RVFVVAGDGSLIALdAADGRRLWSYQRSGEplaLRSSGSPAVVGDTVVAGFSSGKLVALDPAtGKVRWEAPLAAprgtne 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117  534 -----RVYATPFAFHNY----NGSNEMLLAAASTDGKVWILESQSgqlqsvyelpgevFSSPVVLESMLIIGCRDNYVYC 604
Cdd:pfam13360 155 lerlvDITGTPVVAGGRvfasAYQGRLVAFDAATGRRLWTREISG-------------PNGPILDGDLLYVVSDDGELYA 221


                  ....*...
gi 557786117  605 LDLLGGNQ 612
Cdd:pfam13360 222 LDRATGAV 229
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 12-48 1.36e-03

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 41.46  E-value: 1.36e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 557786117  12 IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd05945  413 IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 382-496 1.61e-03

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 40.95  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117 382 GLIYIGSHDQHAYALDIYRKKCVWKSKCGgTVFSSPcLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQC 461
Cdd:COG1520   58 DRVYAADADGRVAALDAATGKELWRVDLG-EPLSGG-VGADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAV 135

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 557786117 462 CSQYICIGCVDGNLLCF---ThfGEQVWQFSTSGPIFS 496
Cdd:COG1520  136 AGGRVVVRTGDGRVYALdaaT--GERLWSYQRPVPALT 171
PRK12316 PRK12316
peptide synthase; Provisional
 16-112 2.10e-03

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 41.48  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786117   16 LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDES 95
Cdd:PRK12316  968 LAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAP---EASVAQQGYVAPRNALERTLAAIWQDVLGVE----RVGLDD 1040

                          90
                  ....*....|....*..
gi 557786117   96 LFLNSGGDSLKSIRLLS 112
Cdd:PRK12316 1041 NFFELGGDSIVSIQVVS 1057
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2-50 2.73e-03

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 40.65  E-value: 2.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557786117   2 VSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDV----SELNK 50
Cdd:PRK04813 451 FEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRkaliEEVNK 503
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 15-44 2.74e-03

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 40.40  E-value: 2.74e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 557786117  15 ELQKYLPSHAVPDELVLIDSLPFTSHGKID 44
Cdd:cd17651  457 ALATHLPEYMVPSAFVLLDALPLTPNGKLD 486
PQQ_3 pfam13570
PQQ-like domain;
359-396 3.51e-03

PQQ-like domain;


Pssm-ID: 463925 [Multi-domain]  Cd Length: 36  Bit Score: 35.26  E-value: 3.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 557786117  359 GEKYWMFTTEDAVKSSATMDptTGLIYIGSHDQHAYAL 396
Cdd:pfam13570   1 GEVLWRFETGGPIVSSPAVA--GGLVYVGTGDGTLYAL 36
PQQ_3 pfam13570
PQQ-like domain;
317-354 4.07e-03

PQQ-like domain;


Pssm-ID: 463925 [Multi-domain]  Cd Length: 36  Bit Score: 35.26  E-value: 4.07e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 557786117  317 GKVKWEQILGDRIESSACVSkcGNFIVVGCYNGLVYVL 354
Cdd:pfam13570   1 GEVLWRFETGGPIVSSPAVA--GGLVYVGTGDGTLYAL 36
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 20-48 4.68e-03

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 39.95  E-value: 4.68e-03
                         10        20
                 ....*....|....*....|....*....
gi 557786117  20 LPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd17646  460 LPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 16-48 5.86e-03

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 39.54  E-value: 5.86e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 557786117  16 LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 48
Cdd:cd17652  403 LAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 12-53 7.99e-03

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 39.02  E-value: 7.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 557786117  12 IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYL 53
Cdd:COG0318  405 LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
 
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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