|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14061 |
PRK14061 |
unknown domain/lipoate-protein ligase A fusion protein; Provisional |
1-562 |
0e+00 |
|
unknown domain/lipoate-protein ligase A fusion protein; Provisional
Pssm-ID: 172552 [Multi-domain] Cd Length: 562 Bit Score: 1188.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPDEKRIQAILDQ 80
Cdd:PRK14061 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPDEKRIQAILDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
Cdd:PRK14061 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 161 TTNILRLMLLLSLAIGVVLTRTLLQGKRTRWQQSPFLLTASKPVPEEEESEKKECPITTRKEIVMSTLRLLISDSYDPWF 240
Cdd:PRK14061 161 TTNILRLMLLLSLAIGVVLTRTLLQGKRTRWQQSPFLLTASKPVPEEEESEKKECPITTRKEIVMSTLRLLISDSYDPWF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 241 NLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEY 320
Cdd:PRK14061 241 NLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 321 DKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAK 400
Cdd:PRK14061 321 DKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 401 GITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAHYGERVEAEIISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLL 480
Cdd:PRK14061 401 GITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAHYGERVEAEIISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 481 DERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPDQEKELRELSTWIAGA 560
Cdd:PRK14061 481 DERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPDQEKELRELSTWIAGA 560
|
..
gi 15834599 561 VR 562
Cdd:PRK14061 561 VR 562
|
|
| lipoyltrans |
TIGR00545 |
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ... |
228-554 |
1.50e-177 |
|
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine lipoyltransferase, which transfers the lipoyl group from lipoyl-AMP to the specific Lys of lipoate-dependent enzymes. However, it does not first activate lipoic acid with ATP to create lipoyl-AMP and pyrophosphate. Another member of this group, lipoate-protein ligase A from E. coli, catalyzes both the activation and the transfer of lipoate. Homology between the two is full-length, except for the bovine mitochondrial targeting signal, but is strongest toward the N-terminus. [Protein fate, Protein modification and repair]
Pssm-ID: 161920 [Multi-domain] Cd Length: 324 Bit Score: 503.58 E-value: 1.50e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 228 LRLLISDSYDPWFNLAVEECIFRQMPATQR--VLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHD 305
Cdd:TIGR00545 1 TRILTSPSNDPYFNLALEEYLFKEFPKTQRgkVLLFWQNANTIVIGRNQNTWAEVNLKELEEDNVNLFRRFSGGGAVFHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 306 LGNTCFTFMAGK--PEYDK-TISTSIVLNALNALGVSAEASGRNDLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNAD 382
Cdd:TIGR00545 81 LGNICFSFITPKdgKEFENaKIFTRNVIKALNSLGVEAELSGRNDLVVD----GRKISGSAYYITKDRGFHHGTLLFDAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 383 LSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAhYGERVEAEIISPDKTPDLPNFAEtfAR 462
Cdd:TIGR00545 157 LSKLAKYLNVDKTKIESKGITSVRSRVVNVKEYLPNITTEQFLEEMTQAFFT-YTERVETYILDENKTPDVEKRAK--ER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 463 QSSWEWNFGQAPAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVd 542
Cdd:TIGR00545 234 FQSWEWNFGKTPKFNFKNKKRFTAGGFELHVQVEKGKIVDCKFFGDFLSVADITPVTNRLIGQKYDYDTFAKELENLDV- 312
|
330
....*....|..
gi 15834599 543 FPDQEKELRELS 554
Cdd:TIGR00545 313 FKEYFGELTPEQ 324
|
|
| AhpA |
COG3726 |
Uncharacterized membrane protein Smp affecting hemolysin expression [Function unknown]; |
1-205 |
1.60e-97 |
|
Uncharacterized membrane protein Smp affecting hemolysin expression [Function unknown];
Pssm-ID: 442940 Cd Length: 208 Bit Score: 294.90 E-value: 1.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPDEkRIQAILDQ 80
Cdd:COG3726 2 MIKAKLKKRLHRTLIVLICLALLVILLQGASYFSLGSQLALSNQVENLARLLVRQAAFSASPLLVNNDKNE-RLTALLNQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
Cdd:COG3726 81 LTKESRILDASVYDADGELLAQSGEALSVRDRLGLDGPLAGSYFRQQIVEPIFGKDGPLGFLRVTLDTHVLATEQHQVDN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15834599 161 TTNILRLMLLLSLAIGVVLTRTLLQGKRTRwqQSPFLLTASKPVP 205
Cdd:COG3726 161 TTNLLRLMLLLALLIGILLARTLLRFRRTR--QSPFLLTASKPVK 203
|
|
| SMP_2 |
pfam10144 |
Bacterial virulence factor haemolysin; Members of this family of bacterial proteins are ... |
1-160 |
5.65e-85 |
|
Bacterial virulence factor haemolysin; Members of this family of bacterial proteins are membrane proteins that effect the expression of haemolysin under anaerobic conditions.
Pssm-ID: 431085 Cd Length: 159 Bit Score: 260.71 E-value: 5.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSpDEKRIQAILDQ 80
Cdd:pfam10144 1 MARAKLKFRLHRTVIILICLALLVVLLQGASYFSLGHQLARSNQVEELAHLLVRQVAFSLSPLLVDNA-DNERITAILDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
Cdd:pfam10144 80 LTKESRILDASVYDNDGTLVAHSGEALSVRDRLGLDGPRAGSYFNQQIVEPIFGKDGPIGFLRVTLDTHYLATEAKQVDN 159
|
|
| BPL_LplA_LipB |
cd16435 |
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ... |
229-432 |
1.11e-72 |
|
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes.
Pssm-ID: 319740 Cd Length: 198 Bit Score: 230.50 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 229 RLLISDSYDPWFNLAVEECIFRQMPA-TQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLG 307
Cdd:cd16435 1 FVEVLDSVDYESAWAAQEKSLRENVSnQSSTLLLWEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHDPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 308 NTCFTFMAGKP-----EYDKTISTSIVLNALNALGVSAEAS-GRNDLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNA 381
Cdd:cd16435 81 QLVFSPVIGPNvefmiSKFNLIIEEGIRDAIADFGQSAEVKwGRNDLWID----NRKVCGIAVRVVKEAIFHGIALNLNQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15834599 382 DLSRLANYLNPDKKklaakgitsVRSRVTNLTELLPGIPHEQVCEAITEAF 432
Cdd:cd16435 157 DLENFTEIIPCGYK---------PERVTSLSLELGRKVTVEQVLERVLAAF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14061 |
PRK14061 |
unknown domain/lipoate-protein ligase A fusion protein; Provisional |
1-562 |
0e+00 |
|
unknown domain/lipoate-protein ligase A fusion protein; Provisional
Pssm-ID: 172552 [Multi-domain] Cd Length: 562 Bit Score: 1188.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPDEKRIQAILDQ 80
Cdd:PRK14061 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPDEKRIQAILDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
Cdd:PRK14061 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 161 TTNILRLMLLLSLAIGVVLTRTLLQGKRTRWQQSPFLLTASKPVPEEEESEKKECPITTRKEIVMSTLRLLISDSYDPWF 240
Cdd:PRK14061 161 TTNILRLMLLLSLAIGVVLTRTLLQGKRTRWQQSPFLLTASKPVPEEEESEKKECPITTRKEIVMSTLRLLISDSYDPWF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 241 NLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEY 320
Cdd:PRK14061 241 NLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 321 DKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAK 400
Cdd:PRK14061 321 DKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 401 GITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAHYGERVEAEIISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLL 480
Cdd:PRK14061 401 GITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAHYGERVEAEIISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 481 DERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPDQEKELRELSTWIAGA 560
Cdd:PRK14061 481 DERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPDQEKELRELSTWIAGA 560
|
..
gi 15834599 561 VR 562
Cdd:PRK14061 561 VR 562
|
|
| lplA |
PRK03822 |
lipoate-protein ligase A; Provisional |
225-562 |
0e+00 |
|
lipoate-protein ligase A; Provisional
Pssm-ID: 179655 Cd Length: 338 Bit Score: 800.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 225 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 304
Cdd:PRK03822 1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 305 DLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 384
Cdd:PRK03822 81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNSLGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 385 RLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAHYGERVEAEIISPDKTPDLPNFAETFARQS 464
Cdd:PRK03822 161 RLANYLNPDKKKLQAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEVISPDKTPDLPGFAETFARQS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 465 SWEWNFGQAPAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFP 544
Cdd:PRK03822 241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQIFTDSLNPAPLEALAGRLQGCLYRADALQQECEALIVDFP 320
|
330
....*....|....*...
gi 15834599 545 DQEKELRELSTWIAGAVR 562
Cdd:PRK03822 321 EQEKELRELSAWLAGAVR 338
|
|
| lipoyltrans |
TIGR00545 |
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ... |
228-554 |
1.50e-177 |
|
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine lipoyltransferase, which transfers the lipoyl group from lipoyl-AMP to the specific Lys of lipoate-dependent enzymes. However, it does not first activate lipoic acid with ATP to create lipoyl-AMP and pyrophosphate. Another member of this group, lipoate-protein ligase A from E. coli, catalyzes both the activation and the transfer of lipoate. Homology between the two is full-length, except for the bovine mitochondrial targeting signal, but is strongest toward the N-terminus. [Protein fate, Protein modification and repair]
Pssm-ID: 161920 [Multi-domain] Cd Length: 324 Bit Score: 503.58 E-value: 1.50e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 228 LRLLISDSYDPWFNLAVEECIFRQMPATQR--VLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHD 305
Cdd:TIGR00545 1 TRILTSPSNDPYFNLALEEYLFKEFPKTQRgkVLLFWQNANTIVIGRNQNTWAEVNLKELEEDNVNLFRRFSGGGAVFHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 306 LGNTCFTFMAGK--PEYDK-TISTSIVLNALNALGVSAEASGRNDLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNAD 382
Cdd:TIGR00545 81 LGNICFSFITPKdgKEFENaKIFTRNVIKALNSLGVEAELSGRNDLVVD----GRKISGSAYYITKDRGFHHGTLLFDAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 383 LSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAhYGERVEAEIISPDKTPDLPNFAEtfAR 462
Cdd:TIGR00545 157 LSKLAKYLNVDKTKIESKGITSVRSRVVNVKEYLPNITTEQFLEEMTQAFFT-YTERVETYILDENKTPDVEKRAK--ER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 463 QSSWEWNFGQAPAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVd 542
Cdd:TIGR00545 234 FQSWEWNFGKTPKFNFKNKKRFTAGGFELHVQVEKGKIVDCKFFGDFLSVADITPVTNRLIGQKYDYDTFAKELENLDV- 312
|
330
....*....|..
gi 15834599 543 FPDQEKELRELS 554
Cdd:TIGR00545 313 FKEYFGELTPEQ 324
|
|
| PRK11246 |
PRK11246 |
YtjB family periplasmic protein; |
1-205 |
5.91e-149 |
|
YtjB family periplasmic protein;
Pssm-ID: 236885 Cd Length: 218 Bit Score: 426.80 E-value: 5.91e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPDEKRIQAILDQ 80
Cdd:PRK11246 1 MARAKLKFRLHRTAIVLICLALLVALMQGASWFSQSHQRARNPQLEELARTLARQVALSLAPLMRSDSPDEKRIQAILDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
Cdd:PRK11246 81 LTDESRILDASVYDEQGDLIARSGESVNVRDRLALDGKKAGSYFNQQIVEPIAGKNGPLGFLRLTLDTHTLATEAKQVDN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15834599 161 TTNILRLMLLLSLAIGVVLTRTLLQGKRTRWQQSPFLLTASKPVP 205
Cdd:PRK11246 161 TTNILRLMLLLALAIGIVLTRTLLQGKRTRWQQSPFLLTASKPVP 205
|
|
| AhpA |
COG3726 |
Uncharacterized membrane protein Smp affecting hemolysin expression [Function unknown]; |
1-205 |
1.60e-97 |
|
Uncharacterized membrane protein Smp affecting hemolysin expression [Function unknown];
Pssm-ID: 442940 Cd Length: 208 Bit Score: 294.90 E-value: 1.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSPDEkRIQAILDQ 80
Cdd:COG3726 2 MIKAKLKKRLHRTLIVLICLALLVILLQGASYFSLGSQLALSNQVENLARLLVRQAAFSASPLLVNNDKNE-RLTALLNQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
Cdd:COG3726 81 LTKESRILDASVYDADGELLAQSGEALSVRDRLGLDGPLAGSYFRQQIVEPIFGKDGPLGFLRVTLDTHVLATEQHQVDN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15834599 161 TTNILRLMLLLSLAIGVVLTRTLLQGKRTRwqQSPFLLTASKPVP 205
Cdd:COG3726 161 TTNLLRLMLLLALLIGILLARTLLRFRRTR--QSPFLLTASKPVK 203
|
|
| LplA |
COG0095 |
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ... |
229-472 |
4.81e-94 |
|
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis
Pssm-ID: 439865 Cd Length: 246 Bit Score: 287.52 E-value: 4.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 229 RLLISDSYDPWFNLAVEECIFRQM--PATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDL 306
Cdd:COG0095 1 RLIDSGSTDPAFNLALDEALLEEVaeGEDPPTLRLWRNPPTVVIGRFQNVLPEVNLEYVEEHGIPVVRRISGGGAVYHDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 307 GNTCFTFMAGKPEYDKTIS------TSIVLNALNALGVSAEASGRNDLVVktaeGDRKVSGSAYRETKDRGFHHGTLLLN 380
Cdd:COG0095 81 GNLNYSLILPEDDVPLSIEesyrklLEPILEALRKLGVDAEFSGRNDIVV----DGRKISGNAQRRRKGAVLHHGTLLVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 381 ADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLP-GIPHEQVCEAITEAFFAHYGERVEAEiISPDKTPDLPNFAET 459
Cdd:COG0095 157 GDLEKLAKVLRVPYEKLRDKGIKSVRSRVTNLSELLGtDITREEVKEALLEAFAEVLGVLEPGE-LTDEELEAAEELAEE 235
|
250
....*....|...
gi 15834599 460 faRQSSWEWNFGQ 472
Cdd:COG0095 236 --KYSSWEWNYGR 246
|
|
| SMP_2 |
pfam10144 |
Bacterial virulence factor haemolysin; Members of this family of bacterial proteins are ... |
1-160 |
5.65e-85 |
|
Bacterial virulence factor haemolysin; Members of this family of bacterial proteins are membrane proteins that effect the expression of haemolysin under anaerobic conditions.
Pssm-ID: 431085 Cd Length: 159 Bit Score: 260.71 E-value: 5.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 1 MARTKLKFRLHRAVIVLFCLALLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNVAPLMRTDSpDEKRIQAILDQ 80
Cdd:pfam10144 1 MARAKLKFRLHRTVIILICLALLVVLLQGASYFSLGHQLARSNQVEELAHLLVRQVAFSLSPLLVDNA-DNERITAILDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 81 LTDESRILDAGVYDEQGDLIARSGESVEVRDRLALDGKKAGGYFNQQIVEPIAGKNGPLGYLRLTLDTHTLATEAQQVDN 160
Cdd:pfam10144 80 LTKESRILDASVYDNDGTLVAHSGEALSVRDRLGLDGPRAGSYFNQQIVEPIFGKDGPIGFLRVTLDTHYLATEAKQVDN 159
|
|
| BPL_LplA_LipB |
cd16435 |
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ... |
229-432 |
1.11e-72 |
|
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes.
Pssm-ID: 319740 Cd Length: 198 Bit Score: 230.50 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 229 RLLISDSYDPWFNLAVEECIFRQMPA-TQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLG 307
Cdd:cd16435 1 FVEVLDSVDYESAWAAQEKSLRENVSnQSSTLLLWEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHDPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 308 NTCFTFMAGKP-----EYDKTISTSIVLNALNALGVSAEAS-GRNDLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNA 381
Cdd:cd16435 81 QLVFSPVIGPNvefmiSKFNLIIEEGIRDAIADFGQSAEVKwGRNDLWID----NRKVCGIAVRVVKEAIFHGIALNLNQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15834599 382 DLSRLANYLNPDKKklaakgitsVRSRVTNLTELLPGIPHEQVCEAITEAF 432
Cdd:cd16435 157 DLENFTEIIPCGYK---------PERVTSLSLELGRKVTVEQVLERVLAAF 198
|
|
| LplA |
cd16443 |
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ... |
229-432 |
5.30e-71 |
|
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein.
Pssm-ID: 319742 Cd Length: 209 Bit Score: 226.37 E-value: 5.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 229 RLLISDSYDPWFNLAVEECIFRQMPA-TQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLG 307
Cdd:cd16443 2 RLIDSSGDPPAENLALDEALLRSVAApPTLRLYLWQNPPTVVIGRFQNPLEEVNLEYAEEDGIPVVRRPSGGGAVFHDLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 308 NTCFTFMAGKP----EYDKTISTSIVLNALNALGVSAEAS--GRNDLVVktaeGDRKVSGSAYRETKDRGFHHGTLLLNA 381
Cdd:cd16443 82 NLNYSLILPKEhpsiDESYRALSQPVIKALRKLGVEAEFGgvGRNDLVV----GGKKISGSAQRRTKGRILHHGTLLVDV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15834599 382 DLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPG-IPHEQVCEAITEAF 432
Cdd:cd16443 158 DLEKLARVLNVPYEKLKSKGPKSVRSRVTNLSELLGRdITVEEVKNALLEAF 209
|
|
| Lip_prot_lig_C |
pfam10437 |
Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial ... |
473-557 |
3.03e-22 |
|
Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB pfam03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.
Pssm-ID: 431286 [Multi-domain] Cd Length: 85 Bit Score: 90.99 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 473 APAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVD--FPDQEKEl 550
Cdd:pfam10437 1 SPEFNYKRSKRFDWGTIEVRLNVEKGIIKDIKIYGDFFGPGDIEELEEALIGVRYEKEAIEKALEDIDLEeyFGNITLE- 79
|
....*..
gi 15834599 551 rELSTWI 557
Cdd:pfam10437 80 -ELIELL 85
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
286-382 |
9.12e-07 |
|
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organizm probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.
Pssm-ID: 427135 Cd Length: 132 Bit Score: 48.21 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834599 286 EEDNVRLARRSSGG----GAVFHDLG---NTCFTFMAGKPEYD----KTISTSIVLNALNALGVSA--------EASGRN 346
Cdd:pfam03099 21 ESGGVVVVRRQTGGrgrgGNVWHSPKgclTYSLLLSKEHPNVDpsvlEFYVLELVLAVLEALGLYKpgisgipcFVKWPN 100
|
90 100 110
....*....|....*....|....*....|....*.
gi 15834599 347 DLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNAD 382
Cdd:pfam03099 101 DLYVN----GRKLAGILQRSTRGGTLHHGVIGLGVN 132
|
|
| |
