|
Name |
Accession |
Description |
Interval |
E-value |
| HSL_N |
pfam06350 |
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ... |
307-615 |
2.89e-161 |
|
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.
:
Pssm-ID: 461882 Cd Length: 306 Bit Score: 478.29 E-value: 2.89e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 307 MTQSLVTLAEDNIAFFSSqGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAH 386
Cdd:pfam06350 1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 387 LLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDeGLTADFLREYVTLHKGCFY 466
Cdd:pfam06350 80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 467 GRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNIT 546
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21328446 547 EMEVLSSLANMASATVRVSRLLSLPPEAFEMPlTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQD 615
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
|
|
| Abhydrolase super family |
cl21494 |
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ... |
647-795 |
5.25e-39 |
|
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.
The actual alignment was detected with superfamily member pfam07859:
Pssm-ID: 473884 [Multi-domain] Cd Length: 208 Bit Score: 144.28 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 647 IVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERICLAGDSA 726
Cdd:pfam07859 1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21328446 727 GGNLCFTVALRAAAYGVRVPDGIMAAYPATMLqPAASPSRLLSLM--DPLLPLSVLSKCVSAYAGAKTEDH 795
Cdd:pfam07859 81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
|
|
| PRK10263 super family |
cl35903 |
DNA translocase FtsK; Provisional |
4-115 |
6.82e-06 |
|
DNA translocase FtsK; Provisional
The actual alignment was detected with superfamily member PRK10263:
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.47 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 4 GSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPL---TQQETPAQHDAESQKEPRAQQK 80
Cdd:PRK10263 718 GANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVapqPQYQQPQQPVAPQPQYQQPQQP 797
|
90 100 110
....*....|....*....|....*....|....*
gi 21328446 81 SASQEEFLAPQKPAPQQSPYIQrvllTQQEAASQQ 115
Cdd:PRK10263 798 VAPQPQYQQPQQPVAPQPQYQQ----PQQPVAPQP 828
|
|
| tolA super family |
cl35847 |
cell envelope integrity inner membrane protein TolA; Provisional |
48-276 |
1.63e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
The actual alignment was detected with superfamily member PRK09510:
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 48 QQKPASNQRPLTQQETPAQHDAES--QKEPRAQQKSASQE-EFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLGK--- 121
Cdd:PRK09510 68 QQQQKSAKRAEEQRKKKEQQQAEElqQKQAAEQERLKQLEkERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaka 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 122 ----ESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQETPEQSDKQTTPVQGAKSK 197
Cdd:PRK09510 148 kaeaEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 198 QGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVG-SSSDTDSPATMGGMVAQGVKLGFK-GKSGYKVmSGYS 275
Cdd:PRK09510 228 AKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGkNAPKTGGGAKGNGAQGAGAGNGKKgGASGADI-DQYA 306
|
.
gi 21328446 276 G 276
Cdd:PRK09510 307 G 307
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HSL_N |
pfam06350 |
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ... |
307-615 |
2.89e-161 |
|
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.
Pssm-ID: 461882 Cd Length: 306 Bit Score: 478.29 E-value: 2.89e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 307 MTQSLVTLAEDNIAFFSSqGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAH 386
Cdd:pfam06350 1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 387 LLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDeGLTADFLREYVTLHKGCFY 466
Cdd:pfam06350 80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 467 GRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNIT 546
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21328446 547 EMEVLSSLANMASATVRVSRLLSLPPEAFEMPlTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQD 615
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
|
|
| Abhydrolase_3 |
pfam07859 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
647-795 |
5.25e-39 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 400284 [Multi-domain] Cd Length: 208 Bit Score: 144.28 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 647 IVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERICLAGDSA 726
Cdd:pfam07859 1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21328446 727 GGNLCFTVALRAAAYGVRVPDGIMAAYPATMLqPAASPSRLLSLM--DPLLPLSVLSKCVSAYAGAKTEDH 795
Cdd:pfam07859 81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
636-766 |
9.63e-37 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 137.70 E-value: 9.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 636 RPQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGST 715
Cdd:COG0657 5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 21328446 716 GERICLAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLqpAASPSR 766
Cdd:COG0657 85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
636-736 |
5.79e-19 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 89.01 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 636 RPQqaPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGST 715
Cdd:PRK10162 75 YPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGIN 152
|
90 100
....*....|....*....|.
gi 21328446 716 GERICLAGDSAGGNLCFTVAL 736
Cdd:PRK10162 153 MSRIGFAGDSAGAMLALASAL 173
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
4-115 |
6.82e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.47 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 4 GSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPL---TQQETPAQHDAESQKEPRAQQK 80
Cdd:PRK10263 718 GANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVapqPQYQQPQQPVAPQPQYQQPQQP 797
|
90 100 110
....*....|....*....|....*....|....*
gi 21328446 81 SASQEEFLAPQKPAPQQSPYIQrvllTQQEAASQQ 115
Cdd:PRK10263 798 VAPQPQYQQPQQPVAPQPQYQQ----PQQPVAPQP 828
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
48-276 |
1.63e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 48 QQKPASNQRPLTQQETPAQHDAES--QKEPRAQQKSASQE-EFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLGK--- 121
Cdd:PRK09510 68 QQQQKSAKRAEEQRKKKEQQQAEElqQKQAAEQERLKQLEkERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaka 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 122 ----ESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQETPEQSDKQTTPVQGAKSK 197
Cdd:PRK09510 148 kaeaEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 198 QGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVG-SSSDTDSPATMGGMVAQGVKLGFK-GKSGYKVmSGYS 275
Cdd:PRK09510 228 AKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGkNAPKTGGGAKGNGAQGAGAGNGKKgGASGADI-DQYA 306
|
.
gi 21328446 276 G 276
Cdd:PRK09510 307 G 307
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
25-235 |
5.58e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 44.32 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 25 LEPGPEKTPIaQPESKTLQGSNTQQKPASNQRPLTQQETPAQhdaesqkepraqqksASQEEFLAPQKPAPQQSPyiqrv 104
Cdd:NF033875 46 LDTQPGTTTV-QPDNPDPQSGSETPKTAVSEEATVQKDTTSQ---------------PTKVEEVASEKNGAEQSS----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 105 lLTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEA----------ESTPAAQAKPGAKREPS-APT 173
Cdd:NF033875 105 -ATPNDTTNAQQPTVGAEKSAQEQPVVSPETTNEPLGQPTEVAPAENEAnkstsipkefETPDVDKAVDEAKKDPNiTVV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21328446 174 ESTSQETPEQSDKQTtpvqGAKSKqgsltELGFLTKLQELSIQRSALEWKALSEWVTDSESE 235
Cdd:NF033875 184 EKPAEDLGNVSSKDL----AAKEK-----EVDQLQKEQAKKIAQQAAELKAKNEKIAKENAE 236
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
23-199 |
2.04e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.21 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 23 TPLEPGP---EKTPIAQPESKTLQGSNTQQKPASNQRPLTQQETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSp 99
Cdd:pfam05109 587 TPNATSPtvgETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTS- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 100 yiQRVLLTQQEAAsqqgpglGKESITQQEPALRQRHvaqpgpgpgepppaqQEAESTPAaqAKPGAKREPSAPTESTSQE 179
Cdd:pfam05109 666 --HMPLLTSAHPT-------GGENITQVTPASTSTH---------------HVSTSSPA--PRPGTTSQASGPGNSSTST 719
|
170 180
....*....|....*....|.
gi 21328446 180 TP-EQSDKQTTPVQGAKSKQG 199
Cdd:pfam05109 720 KPgEVNVTKGTPPKNATSPQA 740
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HSL_N |
pfam06350 |
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ... |
307-615 |
2.89e-161 |
|
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.
Pssm-ID: 461882 Cd Length: 306 Bit Score: 478.29 E-value: 2.89e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 307 MTQSLVTLAEDNIAFFSSqGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAH 386
Cdd:pfam06350 1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 387 LLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDeGLTADFLREYVTLHKGCFY 466
Cdd:pfam06350 80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 467 GRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNIT 546
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21328446 547 EMEVLSSLANMASATVRVSRLLSLPPEAFEMPlTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQD 615
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
|
|
| Abhydrolase_3 |
pfam07859 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
647-795 |
5.25e-39 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 400284 [Multi-domain] Cd Length: 208 Bit Score: 144.28 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 647 IVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERICLAGDSA 726
Cdd:pfam07859 1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21328446 727 GGNLCFTVALRAAAYGVRVPDGIMAAYPATMLqPAASPSRLLSLM--DPLLPLSVLSKCVSAYAGAKTEDH 795
Cdd:pfam07859 81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
636-766 |
9.63e-37 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 137.70 E-value: 9.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 636 RPQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGST 715
Cdd:COG0657 5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 21328446 716 GERICLAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLqpAASPSR 766
Cdd:COG0657 85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
636-736 |
5.79e-19 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 89.01 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 636 RPQqaPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGST 715
Cdd:PRK10162 75 YPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGIN 152
|
90 100
....*....|....*....|.
gi 21328446 716 GERICLAGDSAGGNLCFTVAL 736
Cdd:PRK10162 153 MSRIGFAGDSAGAMLALASAL 173
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
637-730 |
1.92e-10 |
|
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.
Pssm-ID: 466583 [Multi-domain] Cd Length: 215 Bit Score: 61.81 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 637 PQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQEL---GAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLG 713
Cdd:pfam20434 6 PKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALlkaGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYG 85
|
90
....*....|....*..
gi 21328446 714 STGERICLAGDSAGGNL 730
Cdd:pfam20434 86 IDTNKIALMGFSAGGHL 102
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
4-115 |
6.82e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.47 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 4 GSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPL---TQQETPAQHDAESQKEPRAQQK 80
Cdd:PRK10263 718 GANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVapqPQYQQPQQPVAPQPQYQQPQQP 797
|
90 100 110
....*....|....*....|....*....|....*
gi 21328446 81 SASQEEFLAPQKPAPQQSPYIQrvllTQQEAASQQ 115
Cdd:PRK10263 798 VAPQPQYQQPQQPVAPQPQYQQ----PQQPVAPQP 828
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
48-276 |
1.63e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 48 QQKPASNQRPLTQQETPAQHDAES--QKEPRAQQKSASQE-EFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLGK--- 121
Cdd:PRK09510 68 QQQQKSAKRAEEQRKKKEQQQAEElqQKQAAEQERLKQLEkERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaka 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 122 ----ESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQETPEQSDKQTTPVQGAKSK 197
Cdd:PRK09510 148 kaeaEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 198 QGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVG-SSSDTDSPATMGGMVAQGVKLGFK-GKSGYKVmSGYS 275
Cdd:PRK09510 228 AKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGkNAPKTGGGAKGNGAQGAGAGNGKKgGASGADI-DQYA 306
|
.
gi 21328446 276 G 276
Cdd:PRK09510 307 G 307
|
|
| PRK10927 |
PRK10927 |
cell division protein FtsN; |
23-206 |
4.07e-04 |
|
cell division protein FtsN;
Pssm-ID: 236797 [Multi-domain] Cd Length: 319 Bit Score: 43.90 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 23 TPLEP---GPEKTPIA-QPESKTL----QGSNTQQKPASNQRPLTQQeTPAQHDAESQKEPRAQQKSASQEEflapqkpa 94
Cdd:PRK10927 98 APTEPsagGEVKTPEQlTPEQRQLleqmQADMRQQPTQLVEVPWNEQ-TPEQRQQTLQRQRQAQQLAEQQRL-------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 95 pQQSPYIQRVLLTQQEAASQQGPglgkesITQQEPALRQRHVAQPGPGPGepppaQQEAEST--PAAQAKPGAKREPSAP 172
Cdd:PRK10927 169 -AQQSRTTEQSWQQQTRTSQAAP------VQAQPRQSKPASTQQPYQDLL-----QTPAHTTaqSKPQQAAPVTRAADAP 236
|
170 180 190
....*....|....*....|....*....|....
gi 21328446 173 TESTSQETPEQSDKQTTPVQGAKSKQGSLTELGF 206
Cdd:PRK10927 237 KPTAEKKDERRWMVQCGSFRGAEQAETVRAQLAF 270
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
25-235 |
5.58e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 44.32 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 25 LEPGPEKTPIaQPESKTLQGSNTQQKPASNQRPLTQQETPAQhdaesqkepraqqksASQEEFLAPQKPAPQQSPyiqrv 104
Cdd:NF033875 46 LDTQPGTTTV-QPDNPDPQSGSETPKTAVSEEATVQKDTTSQ---------------PTKVEEVASEKNGAEQSS----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 105 lLTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEA----------ESTPAAQAKPGAKREPS-APT 173
Cdd:NF033875 105 -ATPNDTTNAQQPTVGAEKSAQEQPVVSPETTNEPLGQPTEVAPAENEAnkstsipkefETPDVDKAVDEAKKDPNiTVV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21328446 174 ESTSQETPEQSDKQTtpvqGAKSKqgsltELGFLTKLQELSIQRSALEWKALSEWVTDSESE 235
Cdd:NF033875 184 EKPAEDLGNVSSKDL----AAKEK-----EVDQLQKEQAKKIAQQAAELKAKNEKIAKENAE 236
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
12-201 |
7.28e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.92 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 12 DWQPEPH-QRPITPLEPGPEK-TPIAQPESKTLQGSNTQQKPASNQRPLTQQ------------ETPAQHDAESQKEPRA 77
Cdd:PRK10263 359 AWQPVPGpQTGEPVIAPAPEGyPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPaaeqpaqqpyyaPAPEQPAQQPYYAPAP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 78 QQKSASQEEFLAPQ----KPAPQQSPYIQRVLLTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEA 153
Cdd:PRK10263 439 EQPVAGNAWQAEEQqstfAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAR 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21328446 154 ESTPAA---QAKPGAKREP-----SAPTESTSQETPEQSDKQTTPVqGAKSKQGSL 201
Cdd:PRK10263 519 EREQLAawyQPIPEPVKEPepiksSLKAPSVAAVPPVEAAAAVSPL-ASGVKKATL 573
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
17-246 |
1.14e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 17 PHQRPITPLEPGPEKTPIAQP-------ESKTLQGSNTQQKP----ASNQRPLTQQETPAQHDAESQKEPRAQQKSASQE 85
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPpppgpppPSLPLGGSVAPGGDvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 86 efLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGA 165
Cdd:PHA03247 2900 --LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 166 KREPSAPtestSQETPEQSDKQTT--PVQGAKSKQGSLTelgfltkLQELSIQRSALEWKALseWVTDSESESDVGSSSD 243
Cdd:PHA03247 2978 RVPQPAP----SREAPASSTPPLTghSLSRVSSWASSLA-------LHEETDPPPVSLKQTL--WPPDDTEDSDADSLFD 3044
|
...
gi 21328446 244 TDS 246
Cdd:PHA03247 3045 SDS 3047
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
23-199 |
2.04e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.21 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 23 TPLEPGP---EKTPIAQPESKTLQGSNTQQKPASNQRPLTQQETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSp 99
Cdd:pfam05109 587 TPNATSPtvgETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTS- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 100 yiQRVLLTQQEAAsqqgpglGKESITQQEPALRQRHvaqpgpgpgepppaqQEAESTPAaqAKPGAKREPSAPTESTSQE 179
Cdd:pfam05109 666 --HMPLLTSAHPT-------GGENITQVTPASTSTH---------------HVSTSSPA--PRPGTTSQASGPGNSSTST 719
|
170 180
....*....|....*....|.
gi 21328446 180 TP-EQSDKQTTPVQGAKSKQG 199
Cdd:pfam05109 720 KPgEVNVTKGTPPKNATSPQA 740
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
5-192 |
2.20e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 5 SKSVSRSDwQPEPHQRPITPLEPGPEKTPiAQPESKTLQGSNTQ-QKPASNQRPLTQQETPAQHDAESQKEPRAQQksas 83
Cdd:PTZ00449 585 PKHPKDPE-EPKKPKRPRSAQRPTRPKSP-KLPELLDIPKSPKRpESPKSPKRPPPPQRPSSPERPEGPKIIKSPK---- 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 84 qeeflAPQKPAPQQSP-YIQRVLLTQQEAASQQgpglgKESITQqepalrqrhVAQPGPGPGEPPPAQQEAESTPAAQAK 162
Cdd:PTZ00449 659 -----PPKSPKPPFDPkFKEKFYDDYLDAAAKS-----KETKTT---------VVLDESFESILKETLPETPGTPFTTPR 719
|
170 180 190
....*....|....*....|....*....|
gi 21328446 163 PGAKREPSAPtESTSQETPEQSDKQTTPVQ 192
Cdd:PTZ00449 720 PLPPKLPRDE-EFPFEPIGDPDAEQPDDIE 748
|
|
| Say1_Mug180 |
pfam10340 |
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ... |
596-730 |
3.27e-03 |
|
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.
Pssm-ID: 313549 Cd Length: 374 Bit Score: 40.97 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 596 TGPGPVLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPR--PQQ-APRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQ 672
Cdd:pfam10340 71 TGSSPTRYNLPSEDLLPNYGEIFTHKYLNQDMIDSTKFWLRkvPETfDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGK 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21328446 673 ELG-APIISIDYSLAPEAP----FPRALEECFFAYCWAIKhcaLLGSTgeRICLAGDSAGGNL 730
Cdd:pfam10340 151 YFPdMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYLTL---TKGCK--NVTLMGDSAGGNL 208
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
24-259 |
9.85e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.07 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 24 PLEPGPEKTPIAQPESKTlqgsntqQKPASNQRPLTQQETPAQHDA-ESQKEPRAQQKSASQEEFLAP-QKPAPQQSPYI 101
Cdd:PRK10263 336 PVEPVTQTPPVASVDVPP-------AQPTVAWQPVPGPQTGEPVIApAPEGYPQQSQYAQPAVQYNEPlQQPVQPQQPYY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 102 QRVllTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAkpgAKREPSAPTESTSQETP 181
Cdd:PRK10263 409 APA--AEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQ---TYQQPAAQEPLYQQPQP 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21328446 182 EQSDKQTTPVQGAKSKQGSLTELGFLTKLQElsiqRSALEWKALSEW---VTDSESESD-VGSSSDTDSPATMGGM---- 253
Cdd:PRK10263 484 VEQQPVVEPEPVVEETKPARPPLYYFEEVEE----KRAREREQLAAWyqpIPEPVKEPEpIKSSLKAPSVAAVPPVeaaa 559
|
250
....*....|
gi 21328446 254 ----VAQGVK 259
Cdd:PRK10263 560 avspLASGVK 569
|
|
| |
