|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-337 |
2.42e-89 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 280.97 E-value: 2.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIedNGQQLKPGAIT 128
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV--WGGPLEPDDPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAGFAGGFVLDRRFGLDQGFDVYsSPFDLHKGVSTDPGDVKrlGEEVAQDAQAWLDQNAAH-PFFLFLH 207
Cdd:cd16148 79 LAEILRKAGYYTAAVSSNPHLFGGPGFDRGFDTF-EDFRGQEGDPGEEGDER--AERVTDRALEWLDRNADDdPFFLFLH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 208 LYDLHTPYslperlqarygrpGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERT-HGYFIYQSTL 286
Cdd:cd16148 156 YFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWgHGSNLYDEQL 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 287 RVPLIFHWPATARAAvsRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLS 337
Cdd:cd16148 223 HVPLIIRWPGKEPGK--RVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
33-419 |
1.15e-79 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 259.81 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 33 AIAGPVPFAATEAKPAPSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFS 112
Cdd:COG3119 8 LLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 113 NGIEDNGQQ----LKPGAITLARVLKSRGYRTAGFaggfvldrrfgldqG-FDVYSSpfdlhkgvstdpgdvkrlgEEVA 187
Cdd:COG3119 88 TGVTDNGEGynggLPPDEPTLAELLKEAGYRTALF--------------GkWHLYLT-------------------DLLT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 188 QDAQAWLDQNAAH--PFFLFLHLYDLHTPYSLPERLQARY-----------------------GRPGYDSELRYVEGVLG 242
Cdd:COG3119 135 DKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKYdgkdiplppnlaprdlteeelrrARAAYAAMIEEVDDQVG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 243 EFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHGYFIYQSTLRVPLIFHWPATARAAvSRVLEPVSLLDVAPTILQAL 322
Cdd:COG3119 215 RLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGKIKAG-SVSDALVSLIDLLPTLLDLA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 323 GLPSPPEFQGRALLSLAgnTSPAGSPRavpsrrdEEIYSEslyahnHFGTSALRSLRRGSFKYIE----APRAELYDLVH 398
Cdd:COG3119 294 GVPIPEDLDGRSLLPLL--TGEKAEWR-------DYLYWE------YPRGGGNRAIRTGRWKLIRyyddDGPWELYDLKN 358
|
410 420
....*....|....*....|.
gi 1401176184 399 DPGESHNLFQEKKSVASSFHE 419
Cdd:COG3119 359 DPGETNNLAADYPEVVAELRA 379
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-410 |
3.70e-64 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 219.01 E-value: 3.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNG-------QQ 121
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenagaysRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 122 LKPGAITLARVLKSRGYRTaGFAGGF-VLDRRFGLDQGFDVYSSPfdlhkgVSTDPGDVkrlgeevAQDAQAWLDQNAAH 200
Cdd:cd16033 81 LPPGVETFSEDLREAGYRN-GYVGKWhVGPEETPLDYGFDEYLPV------ETTIEYFL-------ADRAIEMLEELAAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 201 --PFFLFLHLYDLHTPYSLPERLQARY----------------GRPG-YDSELRYVEGV--------------------- 240
Cdd:cd16033 147 dkPFFLRVNFWGPHDPYIPPEPYLDMYdpediplpesfaddfeDKPYiYRRERKRWGVDtedeedwkeiiahywgyitli 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 241 ---LGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHGYFIYQSTLRVPLIFHWPATARAAvSRVLEPVSLLDVAPT 317
Cdd:cd16033 227 ddaIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFMYEETYRIPLIIKWPGVIAAG-QVVDEFVSLLDLAPT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 318 ILQALGLPSPPEFQGRALLSL-AGNTSPAGspravpsrrDEEIYSESlyaHNHFGTSALRSLRRGSFKYIEAP--RAELY 394
Cdd:cd16033 306 ILDLAGVDVPPKVDGRSLLPLlRGEQPEDW---------RDEVVTEY---NGHEFYLPQRMVRTDRYKYVFNGfdIDELY 373
|
410
....*....|....*.
gi 1401176184 395 DLVHDPGESHNLFQEK 410
Cdd:cd16033 374 DLESDPYELNNLIDDP 389
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
49-333 |
6.24e-60 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 201.90 E-value: 6.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDN---GQQLKPG 125
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNvgnGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 126 AITLARVLKSRGYRTAGFaGGfvldrrfgldqgfdvysspfdLHkgvstdpgdvkrlgeevaQDAQAWLDQNAA-HPFFL 204
Cdd:cd16022 81 EPTLAELLKEAGYRTALI-GK---------------------WH------------------DEAIDFIERRDKdKPFFL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 205 FLHLYDLHTPYslperlqarygrpGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHGYFIYQS 284
Cdd:cd16022 121 YVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEG 187
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1401176184 285 TLRVPLIFHWPATARAAvSRVLEPVSLLDVAPTILQALGLPSPPEFQGR 333
Cdd:cd16022 188 GIRVPFIVRWPGKIPAG-QVSDALVSLLDLLPTLLDLAGIEPPEGLDGR 235
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
49-406 |
1.31e-59 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 207.38 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDN-GQQLKPGAI 127
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNnGPLFDASQP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 128 TLARVLKSRGYRTaGFAGGFVL-DRRFGLDQGFDVYSS----PFDLHKGVSTDPGDVKRLG---EEVAQDAQAWLDQN-A 198
Cdd:cd16031 83 TYPKLLRKAGYQT-AFIGKWHLgSGGDLPPPGFDYWVSfpgqGSYYDPEFIENGKRVGQKGyvtDIITDKALDFLKERdK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 199 AHPFFLFLHLYDLHTPYSLPERLQARY-----------------GRP----------------GYDSELRY--------- 236
Cdd:cd16031 162 DKPFCLSLSFKAPHRPFTPAPRHRGLYedvtipepetfddddyaGRPewareqrnrirgvldgRFDTPEKYqrymkdylr 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 237 -VEGV---LGEFIGFLQRRGLLETSLLVFTSDHGESLGEHG---ERTHgyfiYQSTLRVPLIFHWPATARAAvSRVLEPV 309
Cdd:cd16031 242 tVTGVddnVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGlfdKRLM----YEESIRVPLIIRDPRLIKAG-TVVDALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 310 SLLDVAPTILQALGLPSPPEFQGRALLSLAGNTSPAGspravpsrRDEEIYSESLYAHNHFGTSALRSLRRGSFKYI--- 386
Cdd:cd16031 317 LNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPVD--------WRKEFYYEYYEEPNFHNVPTHEGVRTERYKYIyyy 388
|
410 420
....*....|....*....|.
gi 1401176184 387 -EAPRAELYDLVHDPGESHNL 406
Cdd:cd16031 389 gVWDEEELYDLKKDPLELNNL 409
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-401 |
5.52e-54 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 188.52 E-value: 5.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAIT 128
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAGFAGgfvLDRRfGLDQ--GFDvysspFDlhkgvstdpgdvkrlgEEVAQDAQAWLDQNAAH--PFFL 204
Cdd:cd16037 81 WGHALRAAGYETVLIGK---LHFR-GEDQrhGFR-----YD----------------RDVTEAAVDWLREEAADdkPWFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 205 FLHLYDLHTPYSLPERLQARY---GRPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHGYFi 281
Cdd:cd16037 136 FVGFVAPHFPLIAPQEFYDLYvrrARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTM- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 282 YQSTLRVPLIFHWPAtaRAAVSRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGNtspagspravPSRRDEEIYS 361
Cdd:cd16037 215 YEESVRVPMIISGPG--IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEG----------PDDPDRVVFS 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1401176184 362 ESlyaHNHFGTSALRSLRRGSFKYI--EAPRAELYDLVHDPG 401
Cdd:cd16037 283 EY---HAHGSPSGAFMLRKGRWKYIyyVGYPPQLFDLENDPE 321
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-406 |
2.34e-53 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 189.32 E-value: 2.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAIT 128
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPDAPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTA--------GFAGGFVL--------DRRFGLD--QGFDVYSSPFDLHKGVSTDPGDVKRLGEEVAQ-- 188
Cdd:cd16034 82 IADVLKDAGYRTGyigkwhldGPERNDGRaddytpppERRHGFDywKGYECNHDHNNPHYYDDDGKRIYIKGYSPDAEtd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 189 DAQAWLDQNAA--HPFFLFLHLYDLHTPY-SLPERLQARYgrPGYDSELR-------------------Y---VEGV--- 240
Cdd:cd16034 162 LAIEYLENQADkdKPFALVLSWNPPHDPYtTAPEEYLDMY--DPKKLLLRpnvpedkkeeaglredlrgYyamITALddn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 241 LGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHGYFiYQSTLRVPLIFHWPATARAAVsRVLEPVSLLDVAPTILQ 320
Cdd:cd16034 240 IGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVP-YEESIRVPFIIRYPGKIKAGR-VVDLLINTVDIMPTLLG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 321 ALGLPSPPEFQGRALLS-LAGNTspagspravPSRRDEEIYSESLYAHNHFG--TSALRSLRRGSFKYIEAPRAE--LYD 395
Cdd:cd16034 318 LCGLPIPDTVEGRDLSPlLLGGK---------DDEPDSVLLQCFVPFGGGSArdGGEWRGVRTDRYTYVRDKNGPwlLFD 388
|
410
....*....|.
gi 1401176184 396 LVHDPGESHNL 406
Cdd:cd16034 389 NEKDPYQLNNL 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
49-406 |
6.94e-53 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 187.33 E-value: 6.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSqGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDN---GQQLKPG 125
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGN-VVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrsrGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 126 AITLARVLKSRGYRTAgfaggfvldrRFGLDQGFDVYSSPFDLHKGvstDPGDVKRLGEEVAQDAQAWLDQNAAH-PFFL 204
Cdd:cd16027 80 VKTLPELLREAGYYTG----------LIGKTHYNPDAVFPFDDEMR---GPDDGGRNAWDYASNAADFLNRAKKGqPFFL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 205 FLHLYDLHTPYSLPERLQARYGR-----PGY--D------------SELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDH 265
Cdd:cd16027 147 WFGFHDPHRPYPPGDGEEPGYDPekvkvPPYlpDtpevredladyyDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 266 GESLgeHGERThgyFIYQSTLRVPLIFHWPATARAAvSRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLSLagNTSPA 345
Cdd:cd16027 227 GMPF--PRAKG---TLYDSGLRVPLIVRWPGKIKPG-SVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPL--LKGEK 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401176184 346 GSPRavpsrrdEEIYSEslyAHNHFGTSAL-RSLRRGSFKYIEAPRA-ELYDLVHDPGESHNL 406
Cdd:cd16027 299 DPGR-------DYVFAE---RDRHDETYDPiRSVRTGRYKYIRNYMPeELYDLKNDPDELNNL 351
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
49-414 |
1.46e-50 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 182.36 E-value: 1.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIED----------- 117
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 118 -------NGQQLKPGAITLARVLKSRGYRTAGF----AGGfvLDRRFGLDQGFDV------------YSSPFDLHKGVST 174
Cdd:cd16144 81 tklipppSTTRLPLEEVTIAEALKDAGYATAHFgkwhLGG--EGGYGPEDQGFDVniggtgnggppsYYFPPGKPNPDLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 175 DPGDVKRLGEEVAQDAQAWLDQNAAHPFFLFLHLYDLHTPYSLPERLQARY-----GRPGYDSELRY---VEGV---LGE 243
Cdd:cd16144 159 DGPEGEYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIEKYekkkkGLRKGQKNPVYaamIESLdesVGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 244 FIGFLQRRGLLETSLLVFTSDHGeSLGEHGERT------HGY--FIYQSTLRVPLIFHWPATArAAVSRVLEPVSLLDVA 315
Cdd:cd16144 239 ILDALEELGLADNTLVIFTSDNG-GLSTRGGPPtsnaplRGGkgSLYEGGIRVPLIVRWPGVI-KPGSVSDVPVIGTDLY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 316 PTILQALGLPSPPEFQ--GRALLS-LAGNTSPagspravpsRRDEEIYSESLYAHNHFGTSAlRSLRRGSFKYI---EAP 389
Cdd:cd16144 317 PTFLELAGGPLPPPQHldGVSLVPlLKGGEAD---------LPRRALFWHFPHYHGQGGRPA-SAIRKGDWKLIefyEDG 386
|
410 420
....*....|....*....|....*
gi 1401176184 390 RAELYDLVHDPGESHNLFQEKKSVA 414
Cdd:cd16144 387 RVELYNLKNDIGETNNLAAEMPEKA 411
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
49-400 |
2.86e-50 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 178.54 E-value: 2.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAIT 128
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAgFAGG--FVldrrfGLDQ--GFDvysspFDlhkgvstdpgdvkrlgEEVAQDAQAWLDQNAAH---- 200
Cdd:cd16032 81 FAHYLRAAGYRTA-LSGKmhFV-----GPDQlhGFD-----YD----------------EEVAFKAVQKLYDLARGedgr 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 201 PFFLFLHLYDLHTPYSLPERLQARY---GRPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHG---E 274
Cdd:cd16032 134 PFFLTVSFTHPHDPYVIPQEYWDLYvrrARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGlwyK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 275 RTHgyfiYQSTLRVPLIFHWPatARAAVSRVLEPVSLLDVAPTILQALG---LPSPPEFQGRALLSLAGNTSPAGsprav 351
Cdd:cd16032 214 MSF----FEGSARVPLIISAP--GRFAPRRVAEPVSLVDLLPTLVDLAGggtAPHVPPLDGRSLLPLLEGGDSGG----- 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 352 psrrDEEIYSEslyaHNHFGTSA-LRSLRRGSFKYI--EAPRAELYDLVHDP 400
Cdd:cd16032 283 ----EDEVISE----YLAEGAVApCVMIRRGRWKFIycPGDPDQLFDLEADP 326
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
49-406 |
8.63e-48 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 175.14 E-value: 8.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAIT 128
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAGF---------AGGFVLDRRF----GLDQGFDvyssPFDLHKGVSTDPGDVKRLgeevAQDAQAWLD 195
Cdd:cd16028 81 LALELRKAGYDPALFgytdtspdpRGLAPLDPRLlsyeLAMPGFD----PVDRLDEYPAEDSDTAFL----TDRAIEYLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 196 QNAAHPFFLFLHLYDLHTPYSLPERLQARYG------------------------------------------------- 226
Cdd:cd16028 153 ERQDEPWFLHLSYIRPHPPFVAPAPYHALYDpadvpppiraeslaaeaaqhpllaaflerieslsfspgaanaadlddee 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 227 ----RPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHGYFiYQSTLRVPLIFHWPATARAAV 302
Cdd:cd16028 233 vaqmRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKDGF-FDQAYRVPLIVRDPRREADAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 303 --SRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGNTSPAGSPRAVPSrrdEEIYSESLYAH--NHFGTSA---- 374
Cdd:cd16028 312 rgQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSDWRDAVHY---EYDFRDVSTRRpqEALGLSPdecs 388
|
410 420 430
....*....|....*....|....*....|....
gi 1401176184 375 LRSLRRGSFKYI--EAPRAELYDLVHDPGESHNL 406
Cdd:cd16028 389 LAVIRDERWKYVhfAALPPLLFDLKNDPGELRDL 422
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
49-406 |
4.16e-45 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 166.58 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGI------EDNGQQL 122
Cdd:cd16026 2 PNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLpgvvgpPGSKGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 123 KPGAITLARVLKSRGYRTA-------GFAGGFvldrrFGLDQGFDVY--------SSPFDLHKGVSTDPGDVKRLGEEV- 186
Cdd:cd16026 82 PPDEITIAEVLKKAGYRTAlvgkwhlGHQPEF-----LPTRHGFDEYfgipysndMWPFPLYRNDPPGPLPPLMENEEVi 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 187 -------------AQDAQAWLDQNAAHPFFLFLHLYDLHTPYSLPERLQARYGRPGY-DSelryVEGV---LGEFIGFLQ 249
Cdd:cd16026 157 eqpadqssltqryTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYgDV----VEELdwsVGRILDALK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 250 RRGLLETSLLVFTSDHGESLGEHGE-------RTHGYFIYQSTLRVPLIFHWPATARA-AVSRvlEPVSLLDVAPTILQA 321
Cdd:cd16026 233 ELGLEENTLVIFTSDNGPWLEYGGHggsagplRGGKGTTWEGGVRVPFIAWWPGVIPAgTVSD--ELASTMDLLPTLAAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 322 LG--LPSPPEFQGRALLSLAgnTSPAGSPravpsrRDEEIYseslyahnHFGTSALRSLRRGSFKYI------------- 386
Cdd:cd16026 311 AGapLPEDRVIDGKDISPLL--LGGSKSP------PHPFFY--------YYDGGDLQAVRSGRWKLHlpttyrtgtdpgg 374
|
410 420
....*....|....*....|....
gi 1401176184 387 ----EAPRAELYDLVHDPGESHNL 406
Cdd:cd16026 375 ldptKLEPPLLYDLEEDPGETYNV 398
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
49-324 |
1.11e-44 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 162.21 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAI- 127
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRTEp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 128 TLARVLKSRGYRTAGFAGGFV--LDRRFGLDQGFDvysSPFDLHKGVSTDPGDVKRLG---------EEVAQDAQAWLDQ 196
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLgwYNNQSPCNLGFD---KFFGRNTGSDLYADPPDVPYncsgggvsdEALLDEALEFLDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 197 NaAHPFFLFLHLYDLHTPYSLPERLQARYG------------RPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSD 264
Cdd:pfam00884 158 N-DKPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSD 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401176184 265 HGESLGEHGERTHG--YFI-YQSTLRVPLIFHWPATARAAvSRVLEPVSLLDVAPTILQALGL 324
Cdd:pfam00884 237 HGESLGEGGGYLHGgkYDNaPEGGYRVPLLIWSPGGKAKG-QKSEALVSHVDLFPTILDLAGI 298
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
49-411 |
1.09e-42 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 160.43 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRaDHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQ---QLKPG 125
Cdd:cd16030 3 PNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSyfrKVAPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 126 AITLARVLKSRGYRTAGF------AGGFVLDR--------------RFGLDQGFDVYSSPFDLHKGVSTDPGDVK--RLG 183
Cdd:cd16030 82 AVTLPQYFKENGYTTAGVgkifhpGIPDGDDDpaswdeppnppgpeKYPPGKLCPGKKGGKGGGGGPAWEAADVPdeAYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 184 -EEVAQDAQAWLDQ--NAAHPFFL----------------FLHLYDLHT--------PYSLPERLQARYG-RPGYDS--- 232
Cdd:cd16030 162 dGKVADEAIEQLRKlkDSDKPFFLavgfykphlpfvapkkYFDLYPLESiplpnpfdPIDLPEVAWNDLDdLPKYGDipa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 233 ----------------ELR--------YVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGE---RThgyfIYQST 285
Cdd:cd16030 242 lnpgdpkgplpdeqarELRqayyasvsYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHwgkHT----LFEEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 286 LRVPLIFHWP-ATARAAVSRvlEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGNTSPAGSPRAVPSrrdeeiysesl 364
Cdd:cd16030 318 TRVPLIIRAPgVTKPGKVTD--ALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAKWKDAAFSQ----------- 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1401176184 365 YAHNHFGTSALRSLRrgsFKYIEAPRA------ELYDLVHDPGESHNLFQEKK 411
Cdd:cd16030 385 YPRPSIMGYSIRTER---YRYTEWVDFdkvgaeELYDHKNDPNEWKNLANDPE 434
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
49-406 |
2.46e-41 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 156.22 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLT-----STYPFSNGIEDNGQQLK 123
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTglhtgHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 124 PGAITLARVLKSRGYRTA-------GFAG--------GFvlDRRFG-LDQGF--DVYSS---------PFDLHKGVSTDP 176
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAafgkwglGGPGtpghptkqGF--DYFYGyLDQVHahNYYPEylwrngekvPLPNNVIPPLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 177 GDVKRLGEEV------AQDAQAWLDQNAAHPFFLFLHlYDL-HTPYSLPERLQARYGRP---------------GYDSEL 234
Cdd:cd16145 159 GNNAGGGGGTyshdlfTDEALDFIRENKDKPFFLYLA-YTLpHAPLQVPDDGPYKYKPKdpgiyaylpwpqpekAYAAMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 235 RYVEGVLGEFIGFLQRRGLLETSLLVFTSDHG---ESLGEH-------GERTHGYF--IYQSTLRVPLIFHWPATaRAAV 302
Cdd:cd16145 238 TRLDRDVGRILALLKELGIDENTLVVFTSDNGphsEGGSEHdpdffdsNGPLRGYKrsLYEGGIRVPFIARWPGK-IPAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 303 SRVLEPVSLLDVAPTILQALGLPSPPEFQGRALL-SLAGNtspagspravpsrrDEEIYSESLYAHNHFGTSAlRSLRRG 381
Cdd:cd16145 317 SVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLpTLLGK--------------PQQQQHDYLYWEFYEGGGA-QAVRMG 381
|
410 420
....*....|....*....|....*....
gi 1401176184 382 SFKYIEAPRA----ELYDLVHDPGESHNL 406
Cdd:cd16145 382 GWKAVRHGKKdgpfELYDLSTDPGETNNL 410
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
49-420 |
7.35e-41 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 154.63 E-value: 7.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQ--VSaqvPLTLPSHVSLLTSTYPFSNGIED---NGQQLK 123
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfhVS---PVCAPTRAALLTGRYPFRTGVWHtilGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 124 PGAITLARVLKSRGYRTAGFaGGFVLDRRFGL---DQGFDVY--------SSPFDLHKGVSTDPgDVKRLGEEVAQD--- 189
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIF-GKWHLGDNYPYrpqDRGFDEVlghggggiGQYPDYWGNDYFDD-TYYHNGKFVKTEgyc 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 190 -------AQAWLDQNAAHPFFLFLHLYDLHTPYSLPERLQARYGRPGYDSELRYVEGV-------LGEFIGFLQRRGLLE 255
Cdd:cd16146 156 tdvffdeAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYGMieniddnVGRLLAKLKELGLEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 256 TSLLVFTSDHGESLGEH-----GERTHGYFIYQSTLRVPLIFHWPATARAAvSRVLEPVSLLDVAPTILQALGL--PSPP 328
Cdd:cd16146 236 NTIVIFMSDNGPAGGVPkrfnaGMRGKKGSVYEGGHRVPFFIRWPGKILAG-KDVDTLTAHIDLLPTLLDLCGVklPEGI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 329 EFQGRALLS-LAGNTSPAgspravpsrRDEEIYSES---LYAHNHFGTSALRSlrrGSFKYI--EAPRAELYDLVHDPGE 402
Cdd:cd16146 315 KLDGRSLLPlLKGESDPW---------PERTLFTHSgrwPPPPKKKRNAAVRT---GRWRLVspKGFQPELYDIENDPGE 382
|
410
....*....|....*...
gi 1401176184 403 SHNLFQEKKSVASSFHEH 420
Cdd:cd16146 383 ENDVADEHPEVVKRLKAA 400
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
49-411 |
1.22e-40 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 155.60 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGI---EDNGQQLKPg 125
Cdd:PRK13759 7 PNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRvgyGDVVPWNYK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 126 aITLARVLKSRGYRTAGFAG----------GF---VLD----------RRFGLDQgFDVYSSPFDLhKGVSTDPgDVKRL 182
Cdd:PRK13759 86 -NTLPQEFRDAGYYTQCIGKmhvfpqrnllGFhnvLLHdgylhsgrneDKSQFDF-VSDYLAWLRE-KAPGKDP-DLTDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 183 G-------------EE-------VAQDAQAWL-DQNAAHPFFLFLHLYDLHTPYSLPERL-------------------- 221
Cdd:PRK13759 162 GwdcnswvarpwdlEErlhptnwVGSESIEFLrRRDPTKPFFLKMSFARPHSPYDPPKRYfdmykdadipdphigdweya 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 222 --------------------QARYGRPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHGYfI 281
Cdd:PRK13759 242 edqdpeggsidalrgnlgeeYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGY-P 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 282 YQSTLRVPLIFHWPATARAA--VSRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGNTSPAgsPRAVpsrrdeei 359
Cdd:PRK13759 321 YEGSAHIPFIIYDPGGLLAGnrGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEG--WRPY-------- 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 360 ysesLYAHNHFGTSALRSLRRGSFKYIEAP---RAELYDLVHDPGESHNLFQEKK 411
Cdd:PRK13759 391 ----LHGEHALGYSSDNYLTDGKWKYIWFSqtgEEQLFDLKKDPHELHNLSPSEK 441
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
483-728 |
2.73e-38 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 143.72 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 483 ALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDD 562
Cdd:COG2956 15 GLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 563 AARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTD 642
Cdd:COG2956 95 AEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 643 PSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQfTPAREALDR 722
Cdd:COG2956 175 PDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS-DDLLLALAD 253
|
....*.
gi 1401176184 723 LELDRK 728
Cdd:COG2956 254 LLERKE 259
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-406 |
1.50e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 144.29 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQ-VSAQvPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAI 127
Cdd:cd16152 2 PNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENaFTPQ-PVCGPARACLQTGLYPTETGCFRNGIPLPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 128 TLARVLKSRGYRT--------AGFAGGFVLDRrfgldqgfdvysspfdlhkgvstdpgdvkrlgeevaqdAQAWLDQ-NA 198
Cdd:cd16152 81 TLAHYFRDAGYETgyvgkwhlAGYRVDALTDF--------------------------------------AIDYLDNrQK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 199 AHPFFLFL------HLYDLHTP------------YSLPERLQARYGR-----PGYDSELRYVEGVLGEFIGFLQRRGLLE 255
Cdd:cd16152 123 DKPFFLFLsylephHQNDRDRYvapegsaerfanFWVPPDLAALPGDwaeelPDYLGCCERLDENVGRIRDALKELGLYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 256 TSLLVFTSDHGESL----GEHGERTHgyfiyQSTLRVPLIFHWPATARAAvsRVLEPVSLLDVAPTILQALGLPSPPEFQ 331
Cdd:cd16152 203 NTIIVFTSDHGCHFrtrnAEYKRSCH-----ESSIRVPLVIYGPGFNGGG--RVEELVSLIDLPPTLLDAAGIDVPEEMQ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 332 GRALLSLAGNTSPAgspravpsrRDEEIY---SESlyahnHFGtsalRSLRRGSFKY-IEAPRAE--------------L 393
Cdd:cd16152 276 GRSLLPLVDGKVED---------WRNEVFiqiSES-----QVG----RAIRTDRWKYsVAAPDKDgwkdsgsdvyvedyL 337
|
410
....*....|...
gi 1401176184 394 YDLVHDPGESHNL 406
Cdd:cd16152 338 YDLEADPYELVNL 350
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-407 |
1.78e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 145.07 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAIT 128
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAgFAGgfvldRRfgldqgfDVYSSPFDlhKGVSTDPgDvkrlgEEVAQDAQAWLDQ-NAAHPFFLFLH 207
Cdd:cd16150 81 LLKTLKDAGYHVA-WAG-----KN-------DDLPGEFA--AEAYCDS-D-----EACVRTAIDWLRNrRPDKPFCLYLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 208 LYDLHTPYSLPE------------RLQARYGRPGYDS--------------------ELR--------YVEGVLGEFIGF 247
Cdd:cd16150 140 LIFPHPPYGVEEpwfsmidreklpPRRPPGLRAKGKPsmlegiekqgldrwseerwrELRatylgmvsRLDHQFGRLLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 248 LQRRGLLETSLLVFTSDHGESLGEHG--ERThgyfiyQSTL-----RVPLIFHWPATarAAVSRVLEPVSLLDVAPTILQ 320
Cdd:cd16150 220 LKETGLYDDTAVFFFSDHGDYTGDYGlvEKW------PNTFedcltRVPLIIKPPGG--PAGGVSDALVELVDIPPTLLD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 321 ALGLPSPPEFQGRALLS-LAGNTSPAGspRAVPS----RRDEE-----------IYSESLYAHNHfGTSALR--SLRRGS 382
Cdd:cd16150 292 LAGIPLSHTHFGRSLLPvLAGETEEHR--DAVFSeggrLHGEEqamegghgpydLKWPRLLQQEE-PPEHTKavMIRTRR 368
|
410 420
....*....|....*....|....*..
gi 1401176184 383 FKYI--EAPRAELYDLVHDPGESHNLF 407
Cdd:cd16150 369 YKYVyrLYEPDELYDLEADPLELHNLI 395
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
49-418 |
2.94e-37 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 145.60 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAIT 128
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAgFAGGFVLD--RRFGLD---QGFDvyssP---FDLHKGVS--TDPGDVKR-----------LGEE-- 185
Cdd:cd16156 81 IGQRLSDNGIHTA-YIGKWHLDggDYFGNGicpQGWD----PdywYDMRNYLDelTEEERRKSrrgltsleaegIKEEft 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 186 ----VAQDAQAWLDQNAAHPFFLFLHLYDLHTPYSLPERLQARY----------------GRPGY-------------DS 232
Cdd:cd16156 156 yghrCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYASMYkdfefpkgenayddleNKPLHqrlwagakphedgDK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 233 ELRYVEGVLG--EFIGFLQRRGL------LETSLLVFTSDHGESLGEHGERTHGYFIYQSTLRVPLIFHWPATARAAVSr 304
Cdd:cd16156 236 GTIKHPLYFGcnSFVDYEIGRVLdaadeiAEDAWVIYTSDHGDMLGAHKLWAKGPAVYDEITNIPLIIRGKGGEKAGTV- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 305 VLEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGNtspagsPRAVPSRrdeEIYSE-SLYAHNHFGTSALRSLR---R 380
Cdd:cd16156 315 TDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIED------PEIPENR---GVFVEfGRYEVDHDGFGGFQPVRcvvD 385
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1401176184 381 GSFKYI--EAPRAELYDLVHDPGESHNLFQEK--KSVASSFH 418
Cdd:cd16156 386 GRYKLVinLLSTDELYDLEKDPYEMHNLIDDPdyADVRDQLH 427
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
49-406 |
1.09e-36 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 142.34 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQ-GVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPF--------SNGIEDNg 119
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWrsrlkggvLGGFSPP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 120 qQLKPGAITLARVLKSRGYRTAGFA-----------GGFVLDRRFGLDqgFDvYSSP---------FDLHKGVSTdpGDV 179
Cdd:cd16143 80 -LIEPDRVTLAKMLKQAGYRTAMVGkwhlgldwkkkDGKKAATGTGKD--VD-YSKPikggpldhgFDYYFGIPA--SEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 180 krlGEEVAQDAQAWLDQNAAH--PFFLFLHLYDLHTPYSLPERLQaryGRPGYDSELRYV---EGVLGEFIGFLQRRGLL 254
Cdd:cd16143 154 ---LPTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQ---GKSGAGPYGDFVyelDWVVGRILDALKELGLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 255 ETSLLVFTSDHG-------ESLGEHGERTHGYF------IYQSTLRVPLIFHWPATARAA-VSRvlEPVSLLDVAPTILQ 320
Cdd:cd16143 228 ENTLVIFTSDNGpspyadyKELEKFGHDPSGPLrgmkadIYEGGHRVPFIVRWPGKIPAGsVSD--QLVSLTDLFATLAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 321 ALGLPSPpefQGRALLSLagNTSPAGSPRAVPSRRdeeiysESLYAHNHFGTsalRSLRRGSFKYIE------------- 387
Cdd:cd16143 306 IVGQKLP---DNAAEDSF--SFLPALLGPKKQEVR------ESLVHHSGNGS---FAIRKGDWKLIDgtgsggfsyprgk 371
|
410 420
....*....|....*....|...
gi 1401176184 388 ----APRAELYDLVHDPGESHNL 406
Cdd:cd16143 372 eklgLPPGQLYNLSTDPGESNNL 394
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-335 |
4.00e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 134.81 E-value: 4.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQG----------VSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDN 118
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 119 G---QQLKPGAITLARVLKSRGYRTAGF----AGGFVldrRFgLDQGFDVYSSPF-DLHKGVSTDpgdvkrlgeevaqda 190
Cdd:cd16153 82 EaahPALDHGLPTFPEVLKKAGYQTASFgkshLEAFQ---RY-LKNANQSYKSFWgKIAKGADSD--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 191 qawldqnaaHPFFLFLHLYDLHTPYSLPERLQARYgrpGYDSELRYVEGVLGEFIGFLQRRGLL---ETSLLVFTSDHGE 267
Cdd:cd16153 143 ---------KPFFVRLSFLQPHTPVLPPKEFRDRF---DYYAFCAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGW 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 268 SLGEHG-ERTHGyFIYQSTlRVPLIFHWPATARA-AVSRVLEPVSLLDVAPTILQALGLP--SPPEFQGRAL 335
Cdd:cd16153 211 HLGEQGiLAKFT-FWPQSH-RVPLIVVSSDKLKApAGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDL 280
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
513-723 |
3.43e-34 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 131.78 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 513 RLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQH 592
Cdd:COG2956 11 WYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 593 KYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKA 672
Cdd:COG2956 91 LLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 673 IDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRL 723
Cdd:COG2956 171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAEL 221
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-406 |
4.28e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 131.57 E-value: 4.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQvPLTLPSHVSLLTSTYPFSNGIedNGQQLKPGAIT 128
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYV--VFGYLDPKQKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAGF----AGGFVLD----RRFGLDQ--------GFDVYSSPFDLH------KGVSTDPGDvkrLGEEV 186
Cdd:cd16151 78 FGHLLKDAGYATAIAgkwqLGGGRGDgdypHEFGFDEyclwqlteTGEKYSRPATPTfnirngKLLETTEGD---YGPDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 187 AQD-AQAWLDQNAAHPFFLFLHLYDLHTPY-SLPE------RLQARYGRPGYDSEL-RYVEGVLGEFIGFLQRRGLLETS 257
Cdd:cd16151 155 FADfLIDFIERNKDQPFFAYYPMVLVHDPFvPTPDspdwdpDDKRKKDDPEYFPDMvAYMDKLVGKLVDKLEELGLRENT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 258 LLVFTSDHGeslgehgerTHGYFIYQST---------------LRVPLIFHWPATARAA-VSRVLepVSLLDVAPTILQA 321
Cdd:cd16151 235 IIIFTGDNG---------THRPITSRTNgrevrggkgkttdagTHVPLIVNWPGLIPAGgVSDDL--VDFSDFLPTLAEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 322 LGLPSPPEFQ--GRALLS-LAGNTSpagspravpSRRDEEIYsesLYAHNHFGTSALRSLRRGSFKYIEAPRaeLYDLVH 398
Cdd:cd16151 304 AGAPLPEDYPldGRSFAPqLLGKTG---------SPRREWIY---WYYRNPHKKFGSRFVRTKRYKLYADGR--FFDLRE 369
|
....*...
gi 1401176184 399 DPGESHNL 406
Cdd:cd16151 370 DPLEKNPL 377
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-327 |
1.03e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 126.97 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIED----------- 117
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDwivegshgktk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 118 NGQQLKPGAITLARVLKSRGYRTaGFAGGFvldrrfgldqgfdvysspfdlHkgvstdpgdvkrLGEevaqDAQAWLDQN 197
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRC-GLSGKW---------------------H------------LGD----DAADFLRRR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 198 AAH--PFFLFLHLYDLHTPYslperlqarygrpGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHG-- 273
Cdd:cd16149 123 AEAekPFFLSVNYTAPHSPW-------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGiw 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1401176184 274 ERTHGYF---IYQSTLRVPLIFHWPATARAAvSRVLEPVSLLDVAPTILQALGLPSP 327
Cdd:cd16149 190 GKGNGTFplnMYDNSVKVPFIIRWPGVVPAG-RVVDSLVSAYDFFPTLLELAGVDPP 245
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
537-727 |
5.02e-32 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 124.73 E-value: 5.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 537 LKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHY 616
Cdd:COG0457 1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 617 NLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRER 696
Cdd:COG0457 81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRY 160
|
170 180 190
....*....|....*....|....*....|.
gi 1401176184 697 SEAVREFRQALALDPQFTPAREALDRLELDR 727
Cdd:COG0457 161 EEALELLEKLEAAALAALLAAALGEAALALA 191
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-411 |
1.62e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 126.91 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLT----LPSHVSLLTSTYPFSngIEDNGQ-QLK 123
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWSgavcVPSRAMLMTGRTLFH--APEGGKaAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 124 PGAITLARVLKSRGYRT-------AGFAGGFV--LDRRFGLDQGFDVY---SSPfdlHKGVSTDPGDVKRLGEEVAQDAQ 191
Cdd:cd16155 81 SDDKTWPETFKKAGYRTfatgkwhNGFADAAIefLEEYKDGDKPFFMYvafTAP---HDPRQAPPEYLDMYPPETIPLPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 192 AWLDQnaaHPFF---LFLHLYDLH----TPYSLPERLQARYGrpgydselrYVEGV---LGEFIGFLQRRGLLETSLLVF 261
Cdd:cd16155 158 NFLPQ---HPFDngeGTVRDEQLApfprTPEAVRQHLAEYYA---------MITHLdaqIGRILDALEASGELDNTIIVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 262 TSDHGESLGEHGerTHG-YFIYQSTLRVPLIFHWPATARAAVSRvlEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAG 340
Cdd:cd16155 226 TSDHGLAVGSHG--LMGkQNLYEHSMRVPLIISGPGIPKGKRRD--ALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIR 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 341 NTSPAgsPRavpsrrdEEIYseSLYAHNHfgtsalRSLRRGSFKYI----EAPRAELYDLVHDPGESHNLFQEKK 411
Cdd:cd16155 302 GEKKA--VR-------DTLY--GAYRDGQ------RAIRDDRWKLIiyvpGVKRTQLFDLKKDPDELNNLADEPE 359
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
48-406 |
4.35e-31 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 126.02 E-value: 4.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 48 APSVILISVDTLRADHLSCYSSQgVSTPHIDALAKGGTLFVQ--VSaqvPLTLPSHVSLLTSTYPFSNGI--EDNGQQLK 123
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfhTT---ALCSPTRAALLTGRNHHQVGMgtMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 124 PG--------AITLARVLKSRGYRTAGF------AGGFvldrrfgldqgfdvYSSpfdlhkgvstdpgdvkrlgEEVAQD 189
Cdd:cd16025 78 PGyegylpdsAATIAEVLKDAGYHTYMSgkwhlgPDDY--------------YST-------------------DDLTDK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 190 AQAWLDQNAAH--PFFLFLHLYDLHTPYSLPERLQARY-GR--PGYDsELR----------------------------- 235
Cdd:cd16025 125 AIEYIDEQKAPdkPFFLYLAFGAPHAPLQAPKEWIDKYkGKydAGWD-ALReerlerqkelglipadtkltprppgvpaw 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 236 --------------------YVEGV---LGEFIGFLQRRGLLETSLLVFTSDHGESlGEHG---------ERTHGyFIYQ 283
Cdd:cd16025 204 dslspeekklearrmevyaaMVEHMdqqIGRLIDYLKELGELDNTLIIFLSDNGAS-AEPGwanasntpfRLYKQ-ASHE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 284 STLRVPLIFHWPATARAAVSRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGnTS--PAGSPRAVPSRRDeEIYS 361
Cdd:cd16025 282 GGIRTPLIVSWPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPQLPLDG-VSllPTLDGAAAPSRRR-TQYF 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 362 EslyahnHFGTsalRSLRRGSFK-------YIEAPRAELYDLVHDPGESHNL 406
Cdd:cd16025 360 E------LFGN---RAIRKGGWKavalhppPGWGDQWELYDLAKDPSETHDL 402
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
37-337 |
6.48e-31 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 128.23 E-value: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 37 PVPFAATEAKPaPSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNG-- 114
Cdd:COG1368 224 PTPNPFGPAKK-PNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGsp 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 115 IEDNGQQLKPgaiTLARVLKSRGYRTA---GFAGGFvlDRR--FGLDQGFDV------YSSPFDLHKGVStDpgdvkrlg 183
Cdd:COG1368 303 YKRPGQNNFP---SLPSILKKQGYETSffhGGDGSF--WNRdsFYKNLGFDEfydredFDDPFDGGWGVS-D-------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 184 EEVAQDAQAWLDQnAAHPFFLFLHLYDLHTPYSLPERLQARYGRPGYDSElRYVEGV------LGEFIGFLQRRGLLETS 257
Cdd:COG1368 369 EDLFDKALEELEK-LKKPFFAFLITLSNHGPYTLPEEDKKIPDYGKTTLN-NYLNAVryadqaLGEFIEKLKKSGWYDNT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 258 LLVFTSDHGESLGEHGERTHGYFIYqstlRVPLIFHWPATARAAVSRVLepVSLLDVAPTILQALGLPSPPEFQ-GRALL 336
Cdd:COG1368 447 IFVIYGDHGPRSPGKTDYENPLERY----RVPLLIYSPGLKKPKVIDTV--GSQIDIAPTLLDLLGIDYPSYYAfGRDLL 520
|
.
gi 1401176184 337 S 337
Cdd:COG1368 521 S 521
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
49-323 |
3.27e-30 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 120.48 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPL--TLPSHVSLLTSTYPFSNGIEDNGQQLKPGA 126
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGggTANGEFEVLTGLPPLPLGSGSYTLYKLNPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 127 ITLARVLKSRGYRTA---GFAGGFVLDRRFGLDQGFD-VYS-------SPFDLHKGVStdpgDvkrlgEEVAQDAQAWLD 195
Cdd:cd16015 81 PSLPSILKEQGYETIfihGGDASFYNRDSVYPNLGFDeFYDledfpddEKETNGWGVS----D-----ESLFDQALEELE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 196 QNAAHPFFLFLHLYDLHTPYSLPERLQARYGRPGYDSEL--RYVEGV------LGEFIGFLQRRGLLETSLLVFTSDHGE 267
Cdd:cd16015 152 ELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTEleNYLNAIhytdkaLGEFIEKLKKSGLYENTIIVIYGDHLP 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1401176184 268 SLGEHGERThgYFIYQSTLRVPLIFHWPATARAAvsRVLEPVSLLDVAPTILQALG 323
Cdd:cd16015 232 SLGSDYDET--DEDPLDLYRTPLLIYSPGLKKPK--KIDRVGSQIDIAPTLLDLLG 283
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
507-727 |
8.63e-29 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 115.49 E-value: 8.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 507 PDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGS 586
Cdd:COG0457 5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 587 VLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAR 666
Cdd:COG0457 85 ALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 667 EALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRLELDR 727
Cdd:COG0457 165 ELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLL 225
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
525-717 |
1.68e-28 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 121.64 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 525 RHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHV 604
Cdd:COG3914 25 ELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 605 LTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHY 684
Cdd:COG3914 105 LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALN 184
|
170 180 190
....*....|....*....|....*....|...
gi 1401176184 685 NLGLVFRAKRERSEAVREFRQALALDPQFTPAR 717
Cdd:COG3914 185 NLGNALQDLGRLEEAIAAYRRALELDPDNADAH 217
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
49-322 |
1.72e-28 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 114.44 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLF-VQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQ------ 121
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSAdpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 122 ----LKPGAITLARVLKSRGYRTAgfaggfvldrRFGLDQGFDvysspfdlhkgvstdpgdvkrlgeevaqdaqawlDQN 197
Cdd:cd00016 81 raagKDEDGPTIPELLKQAGYRTG----------VIGLLKAID----------------------------------ETS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 198 AAHPFFLFLHLYDLHTPYSLPERLqarygRPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTH 277
Cdd:cd00016 117 KEKPFVLFLHFDGPDGPGHAYGPN-----TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPK 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1401176184 278 GYFIYQSTL---RVPLIFHWPATARAAVSRvlEPVSLLDVAPTILQAL 322
Cdd:cd00016 192 ADGKADKSHtgmRVPFIAYGPGVKKGGVKH--ELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-338 |
1.91e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 116.15 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQvsAQVPLTL--PSHVSLLTSTYPFSNGIEDNGQ-----Q 121
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFEN--HYTAACMcsPSRSTLYTGLHPQQTGVTDTLGspmqpL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 122 LKPGAITLARVLKSRGYRTA--------GFAGGfvldrrfGLDQgfdvysspfdlhkgvstDPGdvkrlgeeVAQDAQAW 193
Cdd:cd16035 79 LSPDVPTLGHMLRAAGYYTAykgkwhlsGAAGG-------GYKR-----------------DPG--------IAAQAVEW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 194 LDQNAAH-----PFFLFLHL---YDLHtpYSLPERLQARYGRPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDH 265
Cdd:cd16035 127 LRERGAKnadgkPWFLVVSLvnpHDIM--FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDH 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1401176184 266 GESLGEHGERTHGYFIYQSTLRVPLIFHWPAtARAAVSRVLEPVSLLDVAPTILQALGLPSP------PEFQGRALLSL 338
Cdd:cd16035 205 GEMGGAHGLRGKGFNAYEEALHVPLIISHPD-LFGTGQTTDALTSHIDLLPTLLGLAGVDAEarateaPPLPGRDLSPL 282
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
542-728 |
3.22e-27 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 111.74 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 542 ANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGAL 621
Cdd:COG2956 6 AAALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 622 ATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVR 701
Cdd:COG2956 86 YLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIE 165
|
170 180
....*....|....*....|....*..
gi 1401176184 702 EFRQALALDPQFTPAREALDRLELDRK 728
Cdd:COG2956 166 ALEKALKLDPDCARALLLLAELYLEQG 192
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
49-408 |
1.07e-26 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 114.46 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNgqQLKPGA-- 126
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPG--VFYPGSrg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 127 ------ITLARVLKSRGYRTA---------GFAGGFV-----LDRRFGL----DQG-----------------FDVYSSP 165
Cdd:cd16158 80 glplneTTIAEVLKTVGYQTAmvgkwhlgvGLNGTYLpthqgFDHYLGIpyshDQGpcqnltcfppnipcfggCDQGEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 166 FDLHKG--VSTDPGDVKRLGEEVAQDAQAWLDQNAAH--PFFLFLHLYDLHTPYSLPERLQARYGRPGYDSELRYVEGVL 241
Cdd:cd16158 160 CPLFYNesIVQQPVDLLTLEERYAKFAKDFIADNAKEgkPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 242 GEFIGFLQRRGLLETSLLVFTSDHGESL------GEHGERTHGY-FIYQSTLRVPLIFHWPATARAAVSRVLepVSLLDV 314
Cdd:cd16158 240 GELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKCGKgTTYEGGVREPAIAYWPGRIKPGVTHEL--ASTLDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 315 APTILQALGLPSPP-EFQGRALLSLAGNTSPagSPRAV----PSRRDEE--IYS---ESLYAH------NHFGTSALRSL 378
Cdd:cd16158 318 LPTIAKLAGAPLPNvTLDGVDMSPILFEQGK--SPRQTffyyPTSPDPDkgVFAvrwGKYKAHfytqgaAHSGTTPDKDC 395
|
410 420 430
....*....|....*....|....*....|.
gi 1401176184 379 RRGSF-KYIEAPRaeLYDLVHDPGESHNLFQ 408
Cdd:cd16158 396 HPSAElTSHDPPL--LFDLSQDPSENYNLLG 424
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
475-709 |
2.12e-26 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 115.09 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 475 EEYEDYGHALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSE 554
Cdd:COG3914 9 LAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 555 FALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENH 634
Cdd:COG3914 89 QALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 635 LKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLgLVFRAKRERSEAVREFRQALAL 709
Cdd:COG3914 169 LRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL-LFALRQACDWEVYDRFEELLAA 242
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
49-407 |
1.52e-25 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 109.56 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLScyssQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYP-----FSNGIEDNG---- 119
Cdd:cd16147 2 PNIVLILTDDQDVELGS----MDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgvTNNSPPGGGypkf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 120 QQLKPGAITLARVLKSRGYRTAgFAGGF--VLDRRFGLDQ---GFDVYSSPFDLHKG---VSTDPGDVKRLGEE------ 185
Cdd:cd16147 78 WQNGLERSTLPVWLQEAGYRTA-YAGKYlnGYGVPGGVSYvppGWDEWDGLVGNSTYynyTLSNGGNGKHGVSYpgdylt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 186 --VAQDAQAWLDQNAAH--PFFLFLHLYDLHTPY-------SLPERLQARYGRPGYD------------------SELRY 236
Cdd:cd16147 157 dvIANKALDFLRRAAADdkPFFLVVAPPAPHGPFtpapryaNLFPNVTAPPRPPPNNpdvsdkphwlrrlpplnpTQIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 237 ------------------VEGVLGEfigfLQRRGLLETSLLVFTSDHGESLGEHGERTHGYFIYQSTLRVPLIFHWPATA 298
Cdd:cd16147 237 idelyrkrlrtlqsvddlVERLVNT----LEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 299 RAAVSRvlEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGNTSpagspRAVPSRRDEEIYSESLYAHNhfgtsalrsl 378
Cdd:cd16147 313 AGVTVD--QLVSNIDLAPTILDLAGAPPPSDMDGRSCGDSNNNTY-----KCVRTVDDTYNLLYFEWCTG---------- 375
|
410 420
....*....|....*....|....*....
gi 1401176184 379 rrgsFKyieapraELYDLVHDPGESHNLF 407
Cdd:cd16147 376 ----FR-------ELYDLTTDPYQLTNLA 393
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
49-407 |
4.38e-25 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 107.62 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQ---GVSTPHIDALAKGGTLFVQVSAQVPLTlPSHVSLLTSTYPFSNG-----IEDNGQ 120
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGigrGAPTPNIDRLAKEGLRFTSFYVEPSCT-PGRAAFITGRHPIRTGlttvgLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 121 QLKPGAITLARVLKSRGYRTAGFA----GGfvLDRRFGLDQGFDVYSSPFdLHkgvstdpgdvkRLGEEVAQDAQAWLDQ 196
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGkwhlGD--EDGRLPTDHGFDEFYGNL-YH-----------TIDEEIVDKAIDFIKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 197 NAA--HPFFLFLHLYDLHTPYSLPERLQARYGRPG-YDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESL---- 269
Cdd:cd16142 146 NAKadKPFFLYVNFTKMHFPTLPSPEFEGKSSGKGkYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQdvwp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 270 --------GEHGERTHGyfiyqsTLRVPLIFHWPATARAAvsRVL-EPVSLLDVAPTILQALGLPSPPEFQGRALLSLAG 340
Cdd:cd16142 226 dggytpfrGEKGTTWEG------GVRVPAIVRWPGKIKPG--RVSnEIVSHLDWFPTLAALAGAPDPKDKLLGKDRHIDG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 341 -NTSPAGSPRAVPSRRDEEIYseslyahnhFGTSALRSLRRGSFKY----------------IEAPRAELYDLVHDPGES 403
Cdd:cd16142 298 vDQSPFLLGKSEKSRRSEFFY---------FGEGELGAVRWKNWKVhfkaqedtggptgepfYVLTFPLIFNLRRDPKER 368
|
....
gi 1401176184 404 HNLF 407
Cdd:cd16142 369 YDVT 372
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
49-406 |
1.79e-24 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 106.10 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQvPLTLPSHVSLLTSTYPF----SNGIEDNGQQ--L 122
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIhtgmQHGVILAGEPygL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 123 KPGAITLARVLKSRGYRT-------AGFAG--------GFvlDRRFGL----------DQGFDVYSSPFDLHKGVSTDPG 177
Cdd:cd16029 80 PLNETLLPQYLKELGYAThlvgkwhLGFYTweytptnrGF--DSFYGYyggaedyythTSGGANDYGNDDLRDNEEPAWD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 178 DVKRLGEEV-AQDAQAWLDQ-NAAHPFFLFLHLYDLHTPYSLPERLQARYGRPGYDSE----------LRYVEGVLGEFI 245
Cdd:cd16029 158 YNGTYSTDLfTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKdedrrtyaamVSALDESVGNVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 246 GFLQRRGLLETSLLVFTSDHG------------------ESLGEHGERTHGyFIYqSTLRVPLifhwpataRAAVSRvlE 307
Cdd:cd16029 238 DALKAKGMLDNTLIVFTSDNGgptgggdggsnyplrggkNTLWEGGVRVPA-FVW-SPLLPPK--------RGTVSD--G 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 308 PVSLLDVAPTILQALG--LPSPPEFQGRAL-LSLAGNTspagspravPSRRDEEIYSeslyAHNHFGTSALRSLRRGSFK 384
Cdd:cd16029 306 LMHVTDWLPTLLSLAGgdPDDLPPLDGVDQwDALSGGA---------PSPRTEILLN----IDDITRTTGGAAIRVGDWK 372
|
410 420
....*....|....*....|..
gi 1401176184 385 YIEAprAELYDLVHDPGESHNL 406
Cdd:cd16029 373 LIVG--KPLFNIENDPCERNDL 392
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
483-728 |
1.36e-23 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 106.71 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 483 ALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDD 562
Cdd:TIGR02917 438 ILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQEGNPDD 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 563 AARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTD 642
Cdd:TIGR02917 518 AIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAILNEAADAA 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 643 PSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDR 722
Cdd:TIGR02917 598 PDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQ 677
|
....*.
gi 1401176184 723 LELDRK 728
Cdd:TIGR02917 678 LLLAAK 683
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
579-713 |
1.82e-23 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 96.80 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 579 RAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVR 658
Cdd:COG4783 5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 659 RGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQF 713
Cdd:COG4783 85 AGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
48-328 |
1.93e-23 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 102.93 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 48 APSVILISVDTLRADHLSC-YSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDN-------G 119
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGAnWAPNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNflptsvgG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 120 QQLKpgAITLARVLKSRGYRTAGFaGGFVLDRR---FGLDQGFDVYSS-PFdlhkgvSTDpgdvKRLGEEVAQDAQAWLD 195
Cdd:cd16161 81 LPLN--ETTLAEVLRQAGYATGMI-GKWHLGQReayLPNSRGFDYYFGiPF------SHD----SSLADRYAQFATDFIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 196 QNAA--HPFFLFLHLYDLHTPYSLPERLQ-ARYGRPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHG------ 266
Cdd:cd16161 148 RASAkdRPFFLYAALAHVHVPLANLPRFQsPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkc 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 267 ---ESLGEHGERTHGYF--IYQST----LRVPLIFHWPATARAAV-SRVLepVSLLDVAPTILQALGLPSPP 328
Cdd:cd16161 228 elaVGPGTGDWQGNLGGsvAKASTweggHREPAIVYWPGRIPANStSAAL--VSTLDIFPTVVALAGASLPP 297
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
481-720 |
5.86e-23 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 104.78 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 481 GHALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRL 560
Cdd:TIGR02917 164 GLAQLALAENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 561 DDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALK 640
Cdd:TIGR02917 244 EEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 641 ----------------------------------TDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNL 686
Cdd:TIGR02917 324 yapnshqarrllasiqlrlgrvdeaiatlspalgLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQL 403
|
250 260 270
....*....|....*....|....*....|....
gi 1401176184 687 GLVFRAKRERSEAVREFRQALALDPQFTPAREAL 720
Cdd:TIGR02917 404 GISKLSQGDPSEAIADLETAAQLDPELGRADLLL 437
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
49-323 |
6.04e-23 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 99.20 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLScyssQGVSTPHIDALAKGGTLFVQVSAQVP-LTLPSHVSLLTSTYPFSNGIEDN-------GQ 120
Cdd:cd16018 1 PPLIVISIDGFRWDYLD----RAGLTPNLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYPESHGIVGNyfydpktNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 121 QLKP----------GAITLARVLKSRGYRTAGFaggF--VLDRRFgldQGFDVYSSPFDLHKGVSTDPgdvkRLGEEVAQ 188
Cdd:cd16018 77 EFSDsdwvwdpwwiGGEPIWVTAEKAGLKTASY---FwpGSEVAI---IGYNPTPIPLGGYWQPYNDS----FPFEERVD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 189 DAQAWLDQNAahPFFLFLHLYDL------HTPYSlPERLQArygrpgydseLRYVEGVLGEFIGFLQRRGLLETSLLVFT 262
Cdd:cd16018 147 TILEWLDLER--PDLILLYFEEPdsaghkYGPDS-PEVNEA----------LKRVDRRLGYLIEALKERGLLDDTNIIVV 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 263 SDHG-ESLGehgerTHGYFIYQSTLRVPLIFHWPAtarAAVSRVLEPVSLLDVAPTILQALG 323
Cdd:cd16018 214 SDHGmTDVG-----THGYDNELPDMRAIFIARGPA---FKKGKKLGPFRNVDIYPLMCNLLG 267
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
480-713 |
1.06e-22 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 97.77 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 480 YGHALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHR 559
Cdd:COG0457 12 NNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 560 LDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEAL 639
Cdd:COG0457 92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1401176184 640 KTDPsSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQF 713
Cdd:COG0457 172 AAAL-AALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYR 244
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
39-337 |
1.97e-22 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 102.29 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 39 PFAATEAKPAPSVILISVDTLRADHLscyssQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSL---LTSTYpfSNGI 115
Cdd:COG3083 235 PLQFSDPAKPPNILLIVVDSLRADML-----DPEVMPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLfygLPGNY--WDSI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 116 EDNGQQlkPGAITlarVLKSRGYRTAGFAGgfvldrrfgldQGFdvYSSPFD-------LHKGVSTDPGDVKRlGEEVAQ 188
Cdd:COG3083 308 LAERTP--PVLID---ALQQQGYQFGLFSS-----------AGF--NSPLFRqtifsdvSLPRLHTPGGPAQR-DRQITA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 189 DAQAWLD-QNAAHPFFLFL-----HLYDLHTPY------------------SLPERLQARYgrpgyDSELRYVEGVLGEF 244
Cdd:COG3083 369 QWLQWLDqRDSDRPWFSYLfldapHAYSFPADYpkpfqpsedcnylaldneSDPTPFKNRY-----RNAVHYVDSQIGRV 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 245 IGFLQRRGLLETSLLVFTSDHGESLGEHGERTHG----YFIYQstLRVPLIFHWPATARAAVSRvlePVSLLDVAPTILQ 320
Cdd:COG3083 444 LDTLEQRGLLENTIVIITADHGEEFNENGQNYWGhnsnFSRYQ--LQVPLVIHWPGTPPQVISK---LTSHLDIVPTLMQ 518
|
330 340
....*....|....*....|
gi 1401176184 321 -ALGLPSPPE--FQGRALLS 337
Cdd:COG3083 519 rLLGVQNPASdySQGEDLFD 538
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
49-400 |
2.90e-22 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 99.15 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQLKPGAIT 128
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 129 LARVLKSRGYRTAGF------AGGFVLDRR---------FGLDQgfdvYSSPF-DLHKGVSTDpgDVKRLGEEVAQDAQA 192
Cdd:cd16171 81 WMDRLEKHGYHTQKYgkldytSGHHSVSNRveawtrdvpFLLRQ----EGRPTvNLVGDRSTV--RVMLKDWQNTDKAVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 193 WLDQNAA---HPFFLFLHLYDLH---TPYSLPERLQARYGRPGYDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHG 266
Cdd:cd16171 155 WIRKEAPnltQPFALYLGLNLPHpypSPSMGENFGSIRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 267 ESLGEHgERTHGYFIYQSTLRVPLIFHWPATAraAVSRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLSLAGNTSPAG 346
Cdd:cd16171 235 ELAMEH-RQFYKMSMYEGSSHVPLLIMGPGIK--AGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSESSIKE 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 347 SPRAVPsrRDEEIYSEslyAHNHFGTSALRSLRRGSFKYIE-------APraELYDLVHDP 400
Cdd:cd16171 312 SPSRVP--HPDWVLSE---FHGCNVNASTYMLRTNSWKYIAyadgnsvPP--QLFDLSKDP 365
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
51-324 |
9.22e-22 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 96.15 E-value: 9.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 51 VILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPShVSLLTSTYPFSNGIEDNGQQlkpgaiTLA 130
Cdd:cd16017 5 VVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVS-LPCMLSFANRENYDRAYYQE------NLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 131 RVLKSRGYRTA-----GFAGGFVlDRRFGLDQGFDVYSSPFDLHKGVSTDpgdvkrlgEEVAQDAQAWLDQNAaHPFFLF 205
Cdd:cd16017 78 DLAKKAGYKTYwisnqGGCGGYD-TRISAIAKIETVFTNKGSCNSSNCYD--------EALLPLLDEALADSS-KKKLIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 206 LHLYDLHTPYS--LPE-----------RLQARYGRP---GYDSELRYVEGVLGEFIGFLQRRGllETSLLVFTSDHGESL 269
Cdd:cd16017 148 LHLMGSHGPYYdrYPEefakftpdcdnELQSCSKEElinAYDNSILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401176184 270 GEHGERTHG--YFIYQSTlRVPLIF---------HWPATARAAVSRvlePVSLLDVAPTILQALGL 324
Cdd:cd16017 226 GENGLYLHGapYAPKEQY-HVPFIIwssdsykqrYPVERLRANKDR---PFSHDNLFHTLLGLLGI 287
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
49-406 |
3.39e-21 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 97.12 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGI--------EDNGQ 120
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggtrvflPWDIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 121 QLKPGAITLARVLKSRGYRTaGFAGGFVLD---------RRFGLDQGFDVYSS--PFDLH-------------------- 169
Cdd:cd16160 82 GLPKTEVTMAEALKEAGYTT-GMVGKWHLGinennhsdgAHLPSHHGFDFVGTnlPFTNSwacddtgrhvdfpdrsacfl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 170 ---KGVSTDPGDVKRLGEEVAQDAQAWLDQNAAHPFFLFLHLYDLHTPYSLPERLQARYGRPGYDSELRYVEGVLGEFIG 246
Cdd:cd16160 161 yynDTIVEQPIQHEHLTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 247 FLQRRGLLETSLLVFTSDHGESLG--EHGERTHGY-----FIYQSTLRVPLIFHWPATARAAVSRvlEPVSLLDVAPTIL 319
Cdd:cd16160 241 TLVDTGLDQNTLVFFLSDHGPHVEycLEGGSTGGLkggkgNSWEGGIRVPFIAYWPGTIKPRVSH--EVVSTMDIFPTFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 320 QALG--LPSPPEFQGRALLS-LAGNTspagspravPSRRDEEIY--SESLYA------HNHFGTSALRS-------LRRG 381
Cdd:cd16160 319 DLAGgtLPTDRIYDGLSITDlLLGEA---------DSPHDDILYycCSRLMAvrygsyKIHFKTQPLPSqesldpnCDGG 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 1401176184 382 SFKY-------------IEAPRAELYDLVHDPGESHNL 406
Cdd:cd16160 390 GPLSdyivcydcedecvTKHNPPLIFDVEKDPGEQYPL 427
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
49-338 |
9.09e-21 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 96.59 E-value: 9.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGIEDNGQQ------- 121
Cdd:cd16159 2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMrvilfta 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 122 ----LKPGAITLARVLKSRGYRTA-------GFAGGFVLDRRFG-LDQGFD-VYSSPFDLHKGVSTDPG----------- 177
Cdd:cd16159 82 ssggLPPNETTFAEVLKQQGYSTAligkwhlGLHCESRNDFCHHpLNHGFDyFYGLPLTNLKDCGDGSNgeydlsfdplf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 178 -------------------------------------------------------------------DVKRLGEEVAQDA 190
Cdd:cd16159 162 plltafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfncilmrnhevveqpmSLENLTQRLTKEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 191 QAWLDQNAAHPFFLFLHLYDLHTP-YSLPERL-QARYGRPGyDS--ELRYVegvLGEFIGFLQRRGLLETSLLVFTSDHG 266
Cdd:cd16159 242 ISFLERNKERPFLLVMSFLHVHTAlFTSKKFKgRSKHGRYG-DNveEMDWS---VGQILDALDELGLKDNTFVYFTSDNG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 267 ---ESLGEHGERTHGYFIY---------QSTLRVPLIFHWPATARAAvSRVLEPVSLLDVAPTILQALGLPSPPEFQ--G 332
Cdd:cd16159 318 ghlEEISVGGEYGGGNGGIyggkkmggwEGGIRVPTIVRWPGVIPPG-SVIDEPTSLMDIFPTVAALAGAPLPSDRIidG 396
|
....*.
gi 1401176184 333 RALLSL 338
Cdd:cd16159 397 RDLMPL 402
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
489-728 |
1.53e-20 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 97.08 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 489 AGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQ 568
Cdd:TIGR02917 274 KKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 569 VTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEA 648
Cdd:TIGR02917 354 PALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 649 YNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRLELDRK 728
Cdd:TIGR02917 434 DLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQEG 513
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
542-679 |
1.55e-20 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 88.33 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 542 ANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGAL 621
Cdd:COG4783 2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1401176184 622 ATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKF 679
Cdd:COG4783 82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
542-720 |
1.59e-20 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 96.22 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 542 ANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHK-----YHEARGHFEHVLTVDPRDYVAHY 616
Cdd:COG3914 3 AAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAaaaalLALAAGEAAAAAAALLLLAALLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 617 NLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRER 696
Cdd:COG3914 83 LAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRL 162
|
170 180
....*....|....*....|....
gi 1401176184 697 SEAVREFRQALALDPQFTPAREAL 720
Cdd:COG3914 163 EEAIAALRRALELDPDNAEALNNL 186
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
596-724 |
3.41e-20 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 86.98 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 596 EARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDL 675
Cdd:COG4235 1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1401176184 676 EPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRLE 724
Cdd:COG4235 81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLEASIA 129
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
528-649 |
6.56e-19 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 83.52 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 528 AAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTV 607
Cdd:COG4235 1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1401176184 608 DPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAY 649
Cdd:COG4235 81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPAR 122
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
432-728 |
9.08e-19 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 91.30 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 432 QEAEMAQALSPDVVERLnsLGYAGVSAQRRSPPDS--------GPDPKDrieeyedYGHALTLAAA----GRMDQANELL 499
Cdd:TIGR02917 520 QRFEKVLTIDPKNLRAI--LALAGLYLRTGNEEEAvawlekaaELNPQE-------IEPALALAQYylgkGQLKKALAIL 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 500 QQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTR 579
Cdd:TIGR02917 591 NEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 580 AEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNtLGSLYVRR 659
Cdd:TIGR02917 671 AQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNAIK-LHRALLAS 749
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1401176184 660 GDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRLELDRK 728
Cdd:TIGR02917 750 GNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLNNLAWLYLELK 818
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
522-712 |
9.70e-19 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 85.74 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 522 KLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELlgsvlleqhkyhearghf 601
Cdd:COG4785 8 LLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALAL------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 602 ehvltvdPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFAS 681
Cdd:COG4785 70 -------PDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAY 142
|
170 180 190
....*....|....*....|....*....|.
gi 1401176184 682 AHYNLGLVFRAKRERSEAVREFRQALALDPQ 712
Cdd:COG4785 143 AYLNRGIALYYLGRYELAIADLEKALELDPN 173
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
510-643 |
6.76e-18 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 80.62 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 510 VSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLL 589
Cdd:COG4783 4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1401176184 590 EQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDP 643
Cdd:COG4783 84 KAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
610-723 |
8.62e-18 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 80.62 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 610 RDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLV 689
Cdd:COG4783 2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81
|
90 100 110
....*....|....*....|....*....|....
gi 1401176184 690 FRAKRERSEAVREFRQALALDPQFTPAREALDRL 723
Cdd:COG4783 82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARA 115
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
41-266 |
1.81e-17 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 84.80 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 41 AATEAKPAPSVILISVDTLRADHLscyssQGVSTPHIDALAKGGTLFVQVSAQVP-LTLPSHVSLLTSTYPFSNGIEDNG 119
Cdd:COG1524 16 AAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFPsTTAPAHTTLLTGLYPGEHGIVGNG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 120 QqlkpgaitLARVLKSRGYRTAGFAGGFVLDRRFGL--------DQGFDVYS-SPFDLHKGVSTDPGDVKRLGEEVAQDA 190
Cdd:COG1524 91 W--------YDPELGRVVNSLSWVEDGFGSNSLLPVptiferarAAGLTTAAvFWPSFEGSGLIDAARPYPYDGRKPLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 191 QAWLDQNAA----------HPFFLFLHL----YDLHtpyslperlqaRYGR--PGYDSELRYVEGVLGEFIGFLQRRGLL 254
Cdd:COG1524 163 NPAADRWIAaaalellregRPDLLLVYLpdldYAGH-----------RYGPdsPEYRAALREVDAALGRLLDALKARGLY 231
|
250
....*....|..
gi 1401176184 255 ETSLLVFTSDHG 266
Cdd:COG1524 232 EGTLVIVTADHG 243
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
481-708 |
2.80e-17 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 86.29 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 481 GHALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAhFDLGVSEFALHRL 560
Cdd:TIGR02917 674 GLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNA-IKLHRALLASGNT 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 561 DDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLgALATLEQQWADAENHLKEALK 640
Cdd:TIGR02917 753 AEAVKTLEAWLKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLNNL-AWLYLELKDPRALEYAERALK 831
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1401176184 641 TDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALA 708
Cdd:TIGR02917 832 LAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARKELDKLLN 899
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
562-682 |
1.17e-16 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 76.97 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 562 DAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKT 641
Cdd:COG4235 1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1401176184 642 DPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASA 682
Cdd:COG4235 81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPA 121
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
478-611 |
1.41e-16 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 76.77 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 478 EDYGHALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFAL 557
Cdd:COG4783 6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1401176184 558 HRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRD 611
Cdd:COG4783 86 GDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
492-720 |
1.45e-16 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 83.98 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 492 MDQANELLQQLLGKT----PDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAAREL 567
Cdd:TIGR02917 103 QGKFQQVLDELPGKTllddEGAAELLALRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALI 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 568 QVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAE 647
Cdd:TIGR02917 183 DEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPL 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401176184 648 AYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREAL 720
Cdd:TIGR02917 263 AHYLKALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQARRLL 335
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
521-708 |
1.46e-16 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 79.19 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 521 QKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELL---GSVLLEQHKYHEA 597
Cdd:COG4785 13 ALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLYyerGVAYDSLGDYDLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 598 RGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEP 677
Cdd:COG4785 93 IADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 678 KFASAHYNLGLVFRAKR--------------------ERSEAVREFRQALA 708
Cdd:COG4785 173 NDPERALWLYLAERKLDpekalallledwatayllqgDTEEARELFKLALA 223
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
559-711 |
4.03e-16 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 76.15 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 559 RLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEA 638
Cdd:COG5010 1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401176184 639 LKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDP 711
Cdd:COG5010 81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
525-677 |
4.11e-16 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 76.15 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 525 RHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHV 604
Cdd:COG5010 1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401176184 605 LTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEP 677
Cdd:COG5010 81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
494-611 |
7.75e-16 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 74.66 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 494 QANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAI 573
Cdd:COG4235 1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1401176184 574 EPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRD 611
Cdd:COG4235 81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
627-711 |
7.82e-16 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 73.28 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 627 QWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRArEALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQA 706
Cdd:COG3063 7 DLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERA 85
|
....*
gi 1401176184 707 LALDP 711
Cdd:COG3063 86 LELDP 90
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
49-327 |
8.07e-16 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 80.59 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 49 PSVILISVDTLRADHLSCYSSQGVSTPHIDALAKGGTLFVQVSAQVPLTLPSHVSLLTSTYPFSNGI-EDNG-------- 119
Cdd:cd16157 2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFyTTNAharnaytp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 120 QQLKPG----AITLARVLKSRGYRTaGFAGGFVLDRR---FGLDQGFDVYSSPFDLHKG-----------VSTDPGDVKR 181
Cdd:cd16157 82 QNIVGGipdsEILLPELLKKAGYRN-KIVGKWHLGHRpqyHPLKHGFDEWFGAPNCHFGpydnkaypnipVYRDWEMIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 182 LGEEVA---------------QDAQAWLD--QNAAHPFFLFLHLYDLHTPYSLPERLQARYGRPGYDSELRYVEGVLGEF 244
Cdd:cd16157 161 YYEEFKidkktgesnltqiylQEALEFIEkqHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 245 IGFLQRRGLLETSLLVFTSDHGESL---GEHGErTHGYFI------YQSTLRVPLIFHWPATARAA-VSRVLEpvSLLDV 314
Cdd:cd16157 241 LESLKSLGIENNTFVFFSSDNGAALisaPEQGG-SNGPFLcgkqttFEGGMREPAIAWWPGHIKPGqVSHQLG--SLMDL 317
|
330
....*....|...
gi 1401176184 315 APTILQALGLPSP 327
Cdd:cd16157 318 FTTSLALAGLPIP 330
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
51-266 |
1.67e-15 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 78.62 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 51 VILISVDTLRADhlscYSSQGVSTPHIDALAKGGTLFVQVSAQVP-LTLPSHVSLLTSTYPFSNGIEDN----------- 118
Cdd:pfam01663 1 LLVISLDGFRAD----YLDRFELTPNLAALAKEGVSAPNLTPVFPtLTFPNHYTLVTGLYPGSHGIVGNtfydpktgeyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 119 ----GQQLKP----GAITLARVLKsRGYRTA--GFAGGFVldrrfgldqgfdVYSSPFDLHKGVSTDPGDVKRLGEEVAQ 188
Cdd:pfam01663 77 vfviSDPEDPrwwqGEPIWDTAAK-AGVRAAalFWPGSEV------------DYSTYYGTPPRYLKDDYNNSVPFEDRVD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 189 DA--QAWLDQNAAH-----PFFLFLHLYDL------HTPYSlPERLQArygrpgydseLRYVEGVLGEFIGFLQRRGLLE 255
Cdd:pfam01663 144 TAvlQTWLDLPFADvaaerPDLLLVYLEEPdyaghrYGPDS-PEVEDA----------LRRVDRAIGDLLEALDERGLFE 212
|
250
....*....|.
gi 1401176184 256 TSLLVFTSDHG 266
Cdd:pfam01663 213 DTNVIVVSDHG 223
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
587-678 |
2.07e-15 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 72.13 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 587 VLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENhLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAR 666
Cdd:COG3063 1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEAL 79
|
90
....*....|..
gi 1401176184 667 EALSKAIDLEPK 678
Cdd:COG3063 80 AYLERALELDPS 91
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
483-673 |
1.49e-14 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 74.38 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 483 ALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFdlgvsefalhrldd 562
Cdd:COG2956 117 AEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL-------------- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 563 aarelqvtlaiepyytraeeLLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTD 642
Cdd:COG2956 183 --------------------LLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELD 242
|
170 180 190
....*....|....*....|....*....|.
gi 1401176184 643 PSSAeAYNTLGSLYVRRGDWGRAREALSKAI 673
Cdd:COG2956 243 PSDD-LLLALADLLERKEGLEAALALLERQL 272
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
486-711 |
2.95e-14 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 74.56 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 486 LAAAGRMDQANELLQQLLGKTPDLVSV-RLSLGINQQklSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAA 564
Cdd:COG3071 95 LLDQGQAEQALATLEALRAGAPRHPQVlRLLLQAYRQ--LGDWEELLELLPALRKHKALSAEEAQALERRAYLGLLRQAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 565 RELQVTLAIE---PYYTRAEELL----GSVLLEQHKYHEARGHFEHVLTVDPRD-YVAHYNLGALATLEQQWADAENhlk 636
Cdd:COG3071 173 RDAEALKALWkalPRAERRDPELaaayARALIALGDHDEAERLLREALKRQWDPrLVRLYGRLQGGDPAKQLKRAEK--- 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 637 eALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKfASAHYNLGLVFRAKRERSEAVREFRQALALDP 711
Cdd:COG3071 250 -WLKKHPNDPDLLLALGRLCLRNQLWGKAREYLEAALALRPS-AEAYAELARLLEQLGDPEEAAEHYRKALALAL 322
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
483-712 |
1.54e-13 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 74.35 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 483 ALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDD 562
Cdd:TIGR02917 336 ASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 563 AARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTD 642
Cdd:TIGR02917 416 AIADLETAAQLDPELGRADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIE 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 643 PSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQ 712
Cdd:TIGR02917 496 PDFFPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQ 565
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
614-717 |
3.41e-13 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 69.56 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 614 AHYNLGALATLEQQWADAENHLKEALKtDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAK 693
Cdd:COG4785 42 ADLALALAAAALAAAALAAERIDRALA-LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLL 120
|
90 100
....*....|....*....|....
gi 1401176184 694 RERSEAVREFRQALALDPQFTPAR 717
Cdd:COG4785 121 GDYDAALEDFDRALELDPDYAYAY 144
|
|
| type_IV_pilW |
TIGR02521 |
type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF ... |
584-727 |
1.72e-12 |
|
type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF and PilW. This outer membrane protein is required both for pilus stability and for pilus function such as adherence to human cells. Members of this family contain copies of the TPR (tetratricopeptide repeat) domain.
Pssm-ID: 131573 [Multi-domain] Cd Length: 234 Bit Score: 67.75 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 584 LGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWG 663
Cdd:TIGR02521 37 LALGYLEQGDLEVAKENLDKALEHDPDDYLAYLALALYYQQLGELEKAEDSFRRALTLNPNNGDVLNNYGTFLCQQGKYE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401176184 664 RAREALSKAID--LEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRLELDR 727
Cdd:TIGR02521 117 QAMQQFEQAIEdpLYPQPARSLENAGLCALKAGDFDKAEKYLTRALQIDPQRPESLLELAELYYLR 182
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
437-640 |
4.00e-12 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 66.48 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 437 AQALSPDVVERLNSLGYAGVSAQRRSPPDSGPDPKDRIEEYEDYGHALTLAAAGRmDQANELLQQLLgkTPDLVSVRLSL 516
Cdd:COG4785 3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAA-LAAERIDRALA--LPDLAQLYYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 517 GINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHE 596
Cdd:COG4785 80 GVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1401176184 597 ARGHFEHVLTVDPRD-------YVAHYNLG---ALATLEQQWA----------DAENHLKEALK 640
Cdd:COG4785 160 AIADLEKALELDPNDperalwlYLAERKLDpekALALLLEDWAtayllqgdteEARELFKLALA 223
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
655-728 |
1.39e-11 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 61.34 E-value: 1.39e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1401176184 655 LYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAvREFRQALALDPQFTPAREALDRLELDRK 728
Cdd:COG3063 1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEALLNLAELLLELG 73
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
625-724 |
4.30e-11 |
|
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 60.39 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 625 EQQWADAENHLKEALKTDPSS---AEAYNTLGSLYVRRGDWGRAREALSKAIDLEP---KFASAHYNLGLVFRAKRERSE 698
Cdd:COG1729 6 AGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPdspKAPDALLKLGLSYLELGDYDK 85
|
90 100
....*....|....*....|....*.
gi 1401176184 699 AVREFRQALALDPQFTPAREALDRLE 724
Cdd:COG1729 86 ARATLEELIKKYPDSEAAKEARARLA 111
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
607-723 |
5.38e-11 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 61.51 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 607 VDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNL 686
Cdd:COG5010 15 LLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNL 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 1401176184 687 GLVFRAKRERSEAVREFRQALALDPQFTPAREALDRL 723
Cdd:COG5010 95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAAL 131
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
520-612 |
7.67e-11 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 59.03 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 520 QQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAaRELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARG 599
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEALLNLAELLLELGDYDEALA 80
|
90
....*....|...
gi 1401176184 600 HFEHVLTVDPRDY 612
Cdd:COG3063 81 YLERALELDPSAL 93
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
520-720 |
9.44e-11 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 65.49 E-value: 9.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 520 QQKLSRHAAAAEsFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARG 599
Cdd:TIGR02917 33 LQKNKYKAAIIQ-LKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYPKNQVLPLLARAYLLQGKFQQVLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 600 HFEHVLTVDPRDYVAHYNLGALATLEQ-QWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPK 678
Cdd:TIGR02917 112 ELPGKTLLDDEGAAELLALRGLAYLGLgQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADPG 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1401176184 679 FASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREAL 720
Cdd:TIGR02917 192 NVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLAL 233
|
|
| 3a0801s09 |
TIGR00990 |
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
517-725 |
1.43e-10 |
|
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 64.62 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 517 GINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEP-----YYTRAEelLGSVLLEq 591
Cdd:TIGR00990 338 GTFKCLKGKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSedpdiYYHRAQ--LHFIKGE- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 592 hkYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSK 671
Cdd:TIGR00990 415 --FAQAGKDYQKSIDLDPDFIFSHIQLGVTQYKEGSIASSMATFRRCKKNFPEAPDVYNYYGELLLDQNKFDEAIEKFDT 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 672 AIDLEPKFASAHYNLG-------LVFRAKRERSEAVREFRQALALDPQFTPAREALDRLEL 725
Cdd:TIGR00990 493 AIELEKETKPMYMNVLplinkalALFQWKQDFIEAENLCEKALIIDPECDIAVATMAQLLL 553
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
472-609 |
2.17e-10 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 59.59 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 472 DRIEEYEDYGHALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLG 551
Cdd:COG5010 16 LLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLA 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1401176184 552 VSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDP 609
Cdd:COG5010 96 LLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
466-712 |
2.95e-10 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 63.95 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 466 SGPDPKDRIEEYEDYghaltlAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANAL 545
Cdd:TIGR02917 18 GDQSPEELIEAAKSY------LQKNKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYPKNQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 546 AHFDLGVSEFALHRLDDAARELQ-VTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATL 624
Cdd:TIGR02917 92 VLPLLARAYLLQGKFQQVLDELPgKTLLDDEGAAELLALRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 625 EQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFR 704
Cdd:TIGR02917 172 ENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHAD 251
|
....*...
gi 1401176184 705 QALALDPQ 712
Cdd:TIGR02917 252 ALLKKAPN 259
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
482-678 |
3.25e-10 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 62.24 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 482 HALTLAA-----AGRMDQANELLQQLL--GKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLgVSE 554
Cdd:COG3071 120 QVLRLLLqayrqLGDWEELLELLPALRkhKALSAEEAQALERRAYLGLLRQAARDAEALKALWKALPRAERRDPEL-AAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 555 FA-----LHRLDDAARELQVTLAIEPyytrAEELLGS-VLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQW 628
Cdd:COG3071 199 YAraliaLGDHDEAERLLREALKRQW----DPRLVRLyGRLQGGDPAKQLKRAEKWLKKHPNDPDLLLALGRLCLRNQLW 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1401176184 629 ADAENHLKEALKTDPSsAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPK 678
Cdd:COG3071 275 GKAREYLEAALALRPS-AEAYAELARLLEQLGDPEEAAEHYRKALALALG 323
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
521-643 |
2.71e-09 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 56.51 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 521 QKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGH 600
Cdd:COG5010 31 LAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEY 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1401176184 601 FEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDP 643
Cdd:COG5010 111 YEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| 3a0801s09 |
TIGR00990 |
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
483-675 |
3.60e-09 |
|
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 60.00 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 483 ALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDD 562
Cdd:TIGR00990 372 ASMNLELGDPDKAEEDFDKALKLNSEDPDIYYHRAQLHFIKGEFAQAGKDYQKSIDLDPDFIFSHIQLGVTQYKEGSIAS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 563 AARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGAL---ATLEQQW----ADAENHL 635
Cdd:TIGR00990 452 SMATFRRCKKNFPEAPDVYNYYGELLLDQNKFDEAIEKFDTAIELEKETKPMYMNVLPLinkALALFQWkqdfIEAENLC 531
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1401176184 636 KEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDL 675
Cdd:TIGR00990 532 EKALIIDPECDIAVATMAQLLLQQGDVDEALKLFERAAEL 571
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
483-575 |
4.34e-09 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 55.40 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 483 ALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDD 562
Cdd:COG4235 24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAE 103
|
90
....*....|...
gi 1401176184 563 AARELQVTLAIEP 575
Cdd:COG4235 104 AIAAWQKLLALLP 116
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
588-678 |
6.59e-09 |
|
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 54.23 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 588 LLEQHKYHEARGHFEHVLTVDPRDYV---AHYNLGALATLEQQWADAENHLKEALKTDPSS---AEAYNTLGSLYVRRGD 661
Cdd:COG1729 3 LLKAGDYDEAIAAFKAFLKRYPNSPLapdALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGD 82
|
90
....*....|....*..
gi 1401176184 662 WGRAREALSKAIDLEPK 678
Cdd:COG1729 83 YDKARATLEELIKKYPD 99
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
433-575 |
9.24e-09 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 54.97 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 433 EAEMAQALSPDVVERLNSLGYAGVSAQRRSPPDSGPDPKDRIEEYEDYGHALTLAAAGRMDQANELLQQLLGKTPDLVSV 512
Cdd:COG5010 11 PLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPEL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401176184 513 RLSLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEP 575
Cdd:COG5010 91 YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
486-575 |
1.12e-08 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 52.87 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 486 LAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAEsFQEALKSDPANALAHFDLGVSEFALHRLDDAAR 565
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALA 80
|
90
....*....|
gi 1401176184 566 ELQVTLAIEP 575
Cdd:COG3063 81 YLERALELDP 90
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
230-294 |
1.96e-08 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 57.56 E-value: 1.96e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1401176184 230 YDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHG--YFIY-QSTLRVPLIFhW 294
Cdd:COG2194 414 YDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGtpYAIApDEQTHVPMIM-W 480
|
|
| gliding_GltE |
NF033758 |
adventurous gliding motility TPR repeat lipoprotein GltE; GltE (also called AglT) is a ... |
601-728 |
4.13e-08 |
|
adventurous gliding motility TPR repeat lipoprotein GltE; GltE (also called AglT) is a tetratricopeptide repeat protein with a lipoprotein signal peptide and a role in A-motility (adventurous gliding motility) in Myxococcus xanthus and other delta-proteobacteria.
Pssm-ID: 468174 [Multi-domain] Cd Length: 411 Bit Score: 55.98 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 601 FEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFA 680
Cdd:NF033758 75 FKAALEADPNLAEAEYNLGVLAERQGKTDEAVARYKAALKKKPTLRQASENLAVMAQNAGDVAGAVALYQDVLKRYPDDA 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1401176184 681 SAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRLELDRK 728
Cdd:NF033758 155 SSRARLAEIYRQTGDHDKAMELSRAALMRDPQSTTALKVMMRSYLDRK 202
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
435-639 |
4.24e-08 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 54.63 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 435 EMAQALSPDVVERLNSLGYAgvsaqrrsppdsgpdpkdrieeyedyghaltLAAAGRMDQANELLQQLLGKTPDLVSVRL 514
Cdd:COG0457 66 EQALELDPDDAEALNNLGLA-------------------------------LQALGRYEEALEDYDKALELDPDDAEALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 515 SLGINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKY 594
Cdd:COG0457 115 NLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1401176184 595 HEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEAL 639
Cdd:COG0457 195 VLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALA 239
|
|
| ACL4-like |
cd24142 |
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
559-675 |
8.95e-08 |
|
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.
Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 54.56 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 559 RLDDAARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDP----------------RDYVAHYN----- 617
Cdd:cd24142 15 NFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPdggyekylylgqlsggEEALQYYEkgiei 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 618 ----LGALATLEQQWADAENHLK---------------------------------EALKTDPSSAEAYNTLGSLYVRRG 660
Cdd:cd24142 95 leeeLQALQAASAEAEEEAEELKrklssalcalaeiymtdlcdepdaeqrceelitKALELDPTNPEALQTLASLRISQQ 174
|
170
....*....|....*
gi 1401176184 661 DWGRAREALSKAIDL 675
Cdd:cd24142 175 RPDEAKEALRRSLEL 189
|
|
| TPR_11 |
pfam13414 |
TPR repeat; |
653-690 |
3.73e-07 |
|
TPR repeat;
Pssm-ID: 315977 [Multi-domain] Cd Length: 42 Bit Score: 47.08 E-value: 3.73e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1401176184 653 GSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVF 690
Cdd:pfam13414 1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAY 38
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
614-675 |
1.80e-06 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 46.23 E-value: 1.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 614 AHYNLGALATLEQQWADAENHLKEAL--------KTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDL 675
Cdd:pfam13424 5 ALNNLAAVLRRLGRYDEALELLEKALeiarrllgPDHPLTATTLLNLGRLYLELGRYEEALELLERALAL 74
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
203-278 |
2.19e-06 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 50.93 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 203 FLFLHLYDLHTP-YSLPERLQARYGRP-----------------GYDSELRYVEGVLGEFIGFLQrrGLLETSLLVFTSD 264
Cdd:PRK09598 361 LLILHLAGSHGPnYDNKYPLNFRVFKPvcssvelsscskeslinAYDNTIFYNDYLLDKIISMLK--NLKQPALMIYLSD 438
|
90
....*....|....
gi 1401176184 265 HGESLGEHGERTHG 278
Cdd:PRK09598 439 HGESLGEGAFYLHG 452
|
|
| PRK11788 |
PRK11788 |
tetratricopeptide repeat protein; Provisional |
488-646 |
3.63e-06 |
|
tetratricopeptide repeat protein; Provisional
Pssm-ID: 236983 [Multi-domain] Cd Length: 389 Bit Score: 49.81 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 488 AAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPAN---ALAHF--DLGVSEFALHRLDD 562
Cdd:PRK11788 119 KAGLLDRAEELFLQLVDEGDFAEGALQQLLEIYQQEKDWQKAIDVAERLEKLGGDSlrvEIAHFycELAQQALARGDLDA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 563 AARELQVTLAIEPYYTRAEELLGSVLLEQHKYHEARGHFEHVLTVDPrDYVAHYnLGALATLEQ---QWADAENHLKEAL 639
Cdd:PRK11788 199 ARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEEQDP-EYLSEV-LPKLMECYQalgDEAEGLEFLRRAL 276
|
....*..
gi 1401176184 640 KTDPSSA 646
Cdd:PRK11788 277 EEYPGAD 283
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
230-294 |
4.90e-06 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 49.67 E-value: 4.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1401176184 230 YDSELRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGESLGEHGERTHG--YFIYQST-LRVPLIFhW 294
Cdd:PRK11598 420 YDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGlpYAIAPDQqTHVPMLL-W 486
|
|
| PRK11447 |
PRK11447 |
cellulose synthase subunit BcsC; Provisional |
483-712 |
6.31e-06 |
|
cellulose synthase subunit BcsC; Provisional
Pssm-ID: 183140 [Multi-domain] Cd Length: 1157 Bit Score: 49.70 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 483 ALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGinqQKLSR---HAAAAESFQEALKSDPanalahfdlgvsefalHR 559
Cdd:PRK11447 276 GLAAVDSGQGGKAIPELQQAVRANPKDSEALGALG---QAYSQqgdRARAVAQFEKALALDP----------------HS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 560 LDDAARE--LQVT---LAIEPyytraeellGSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENH 634
Cdd:PRK11447 337 SNRDKWEslLKVNrywLLIQQ---------GDAALKANNLAQAERLYQQARQVDNTDSYAVLGLGDVAMARKDYAAAERY 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 635 LKEALKTDPSSAEAYNTLGSLYVR------------------------------------------RGDWGRAREALSKA 672
Cdd:PRK11447 408 YQQALRMDPGNTNAVRGLANLYRQqspekalafiaslsasqrrsiddierslqndrlaqqaealenQGKWAQAAELQRQR 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1401176184 673 IDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQ 712
Cdd:PRK11447 488 LALDPGSVWLTYRLAQDLRQAGQRSQADALMRRLAQQKPN 527
|
|
| COG4700 |
COG4700 |
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown]; |
565-718 |
8.19e-06 |
|
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
Pssm-ID: 443735 [Multi-domain] Cd Length: 249 Bit Score: 47.95 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 565 RELQVTLAIEP-YYTRAEelLGSVLLEQHKYHEARGHFEHVLT-VDPRDYVAHYNLGALATLEQQWADAENHLKEALKTD 642
Cdd:COG4700 77 RELEKALEFADtVQNRVR--LADALLELGRYDEAIELYEEALTgIFADDPHILLGLAQALFELGRYAEALETLEKLIAKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1401176184 643 PS--SAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFAsAHYNLGLvFRAKRERSEAVREFRQALALDPQFTPARE 718
Cdd:COG4700 155 PDfkSSDAHLLYARALEALGDLEAAEAELEALARRYSGPE-ARYRYAK-FLARQGRTAEAKELLEEILDEAKHMPKHY 230
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
260-338 |
1.32e-05 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 48.36 E-value: 1.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1401176184 260 VFTSDHGESLGEHgeRTHGYFIYQStlrvplifhwpatARAAVSRVLEPVSLLDVAPTILQALGLPSPPEFQGRALLSL 338
Cdd:COG3379 404 VFDPPTGPRTGTH--RPDGIFLAAG-------------PGIAPGARLEDADLYDVAPTILALLGLPVPRDMDGRVLVEA 467
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
522-614 |
2.29e-05 |
|
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 44.21 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 522 KLSRHAAAAESFQEALKSDPANAL---AHFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAEE---LLGSVLLEQHKYH 595
Cdd:COG1729 5 KAGDYDEAIAAFKAFLKRYPNSPLapdALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDallKLGLSYLELGDYD 84
|
90
....*....|....*....
gi 1401176184 596 EARGHFEHVLTVDPRDYVA 614
Cdd:COG1729 85 KARATLEELIKKYPDSEAA 103
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
580-728 |
2.43e-05 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 47.77 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 580 AEELL--GSVLLEQHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYV 657
Cdd:TIGR02917 22 PEELIeaAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYPKNQVLPLLARAYL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 658 RRGDWGRAREALSKAIDL-EPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRLELDRK 728
Cdd:TIGR02917 102 LQGKFQQVLDELPGKTLLdDEGAAELLALRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALAEN 173
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
644-712 |
2.96e-05 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 42.76 E-value: 2.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1401176184 644 SSAEAYNTLGSLYVRRGDWGRAREALSKAIDL-----EPKF---ASAHYNLGLVFRAKRERSEAVREFRQALALDPQ 712
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIarrllGPDHpltATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
480-544 |
4.40e-05 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 43.84 E-value: 4.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 480 YGHALTLAAAGRMDQANELLQQLLGKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANA 544
Cdd:COG4235 55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADA 119
|
|
| PRK11788 |
PRK11788 |
tetratricopeptide repeat protein; Provisional |
613-681 |
4.73e-05 |
|
tetratricopeptide repeat protein; Provisional
Pssm-ID: 236983 [Multi-domain] Cd Length: 389 Bit Score: 46.34 E-value: 4.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 613 VAHY--NLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFAS 681
Cdd:PRK11788 179 IAHFycELAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEEQDPEYLS 249
|
|
| ACL4-like |
cd24142 |
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
635-709 |
5.28e-05 |
|
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.
Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 45.70 E-value: 5.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1401176184 635 LKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEP-KFASAHYNLG-LVfrakrERSEAVREFRQALAL 709
Cdd:cd24142 23 LQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPdGGYEKYLYLGqLS-----GGEEALQYYEKGIEI 94
|
|
| TPR_19 |
pfam14559 |
Tetratricopeptide repeat; |
625-683 |
7.76e-05 |
|
Tetratricopeptide repeat;
Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 41.03 E-value: 7.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1401176184 625 EQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAH 683
Cdd:pfam14559 1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYA 59
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
259-336 |
9.19e-05 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 45.48 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 259 LVFTSDHG-------ESLGE-HgeRTHgyfiyqSTLRVPLIFhwpaTARAAVSRVLEPVSLLDVAPTILQALGLPSPPEF 330
Cdd:cd16010 430 LLITADHGnaeemidPETGGpH--TAH------TTNPVPFII----VDPGLKRKLLKDGGLADVAPTILDLLGIEKPKEM 497
|
....*.
gi 1401176184 331 QGRALL 336
Cdd:cd16010 498 TGKSLI 503
|
|
| HemYx |
COG3898 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to HemY-type ... |
579-727 |
1.14e-04 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to HemY-type protoporphyrinogen oxidase) [Function unknown];
Pssm-ID: 443105 [Multi-domain] Cd Length: 468 Bit Score: 45.27 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 579 RAEELLGSV----LLE------QHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEA 648
Cdd:COG3898 109 KAERLLDRPpltlLLEaqaaqlAGDREAARRAFEAMLEDPETRFLGLRGLMVEALRRGDTEAALALAEEALALAPKLPWA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 649 YNTLGSLYVRRGDWGRAREALSKAID---LEPKFASAHYNLGLVFRAKR----ERSEAVREFRQALALDPQFTPAREALD 721
Cdd:COG3898 189 QDALLELQAAAGDWDGALATLDAALKaglLDKDVARRRRAVLLTARAREleegDPDEARELAIEALKLAPDLVPAAVLAA 268
|
....*.
gi 1401176184 722 RLELDR 727
Cdd:COG3898 269 RLLIAQ 274
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
486-568 |
1.14e-04 |
|
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 41.90 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 486 LAAAGRMDQANELLQQLLGKTPD---LVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANAL---AHFDLGVSEFALHR 559
Cdd:COG1729 3 LLKAGDYDEAIAAFKAFLKRYPNsplAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELGD 82
|
....*....
gi 1401176184 560 LDDAARELQ 568
Cdd:COG1729 83 YDKARATLE 91
|
|
| PRK02603 |
PRK02603 |
photosystem I assembly protein Ycf3; Provisional |
614-698 |
1.31e-04 |
|
photosystem I assembly protein Ycf3; Provisional
Pssm-ID: 179448 [Multi-domain] Cd Length: 172 Bit Score: 43.12 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 614 AHYNLGALATLEQQWADAENHLKEALK--TDPS--SAEAYNtLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLV 689
Cdd:PRK02603 37 VYYRDGMSAQADGEYAEALENYEEALKleEDPNdrSYILYN-MGIIYASNGEHDKALEYYHQALELNPKQPSALNNIAVI 115
|
....*....
gi 1401176184 690 FRAKRERSE 698
Cdd:PRK02603 116 YHKRGEKAE 124
|
|
| TPR_hemY_coli |
TIGR00540 |
heme biosynthesis-associated TPR protein; Members of this protein family are uncharacterized ... |
635-706 |
1.59e-04 |
|
heme biosynthesis-associated TPR protein; Members of this protein family are uncharacterized tetratricopeptide repeat (TPR) proteins invariably found in heme biosynthesis gene clusters. The absence of any invariant residues other than Ala argues against this protein serving as an enzyme per se. The gene symbol hemY assigned in E. coli is unfortunate in that an unrelated protein, protoporphyrinogen oxidase (HemG in E. coli) is designated HemY in Bacillus subtilis. [Unknown function, General]
Pssm-ID: 273126 [Multi-domain] Cd Length: 367 Bit Score: 44.59 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 635 LKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKfASAHYNLGLVFRAKRERSEAVREFRQA 706
Cdd:TIGR00540 297 AEKWLKKHPDDALLLLALGRLCLRQQLWGKAQSYLEASLSLAPT-EEAHLELAQLFEQLGDTEAAAQHYRKS 367
|
|
| TPR |
smart00028 |
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
680-713 |
1.80e-04 |
|
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.
Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 39.35 E-value: 1.80e-04
10 20 30
....*....|....*....|....*....|....
gi 1401176184 680 ASAHYNLGLVFRAKRERSEAVREFRQALALDPQF 713
Cdd:smart00028 1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
|
|
| Mgr3-like |
cd24145 |
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; ... |
467-722 |
2.82e-04 |
|
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; Mgr3 (also called mitochondrial genome-required protein 3) is a component of the mitochondrial inner membrane i-AAA protease supercomplex, which degrades misfolded mitochondrial proteins. The supercomplex is composed of Mgr1, Mgr3, and Yme1. Mgr3, together with Mgr1, functions in an adapter complex that targets substrates to the i-AAA protease for degradation.
Pssm-ID: 467945 [Multi-domain] Cd Length: 307 Bit Score: 43.49 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 467 GPDPKDRIEEYEDyghALTLAAAGRMDQanellqqllgKTPDLVSVRLSLGINQQKLSRHAAAAES----FQEALKSDPA 542
Cdd:cd24145 21 KPDPQKALKYYKE---ALEQADELGMDP----------FSDEVTGIRIKIAEMLEKLGMYKAAYEVlerlYLDCLRWTLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 543 NALAHF------DLGVS--------------EFALHRLDDAARELQVTLAiEPYYTRAE-----ELLGSVLLEQHKYHEA 597
Cdd:cd24145 88 DDESERghlikrDLRISiklgelnkdselgkWELRERLLKKAVEILLKLG-ELWMSPSEvgaflEELATAYDLYGRFCLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 598 RGHFEHVLTVDPRDYVAHYNLGAL---------ATLEQQWADAENHLKEALKTDPSSAEAYNTLGSlyvrrgDWgrAREA 668
Cdd:cd24145 167 LPLYMQALSLKGQILLSQANCHSLvlmnneaaeLALHALRKPLSSTLIEASRLPQKSRDQLLEAAL------KW--AQKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1401176184 669 LSKAIDLEPK---------FASAHYNLGLVFRAKRERSEAVREFRQALAL--DPQFT----PAREALDR 722
Cdd:cd24145 239 LDVAKSIKPKdrdpecdqaCALALYNLGVIAEMLGNLDEARKLYKEAISLakELGFEegvkEAEDELKR 307
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
579-640 |
2.82e-04 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 40.06 E-value: 2.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 579 RAEELLGSVLLEQHKYHEARGHFEHVLTV--------DPRDYVAHYNLGALATLEQQWADAENHLKEALK 640
Cdd:pfam13424 4 TALNNLAAVLRRLGRYDEALELLEKALEIarrllgpdHPLTATTLLNLGRLYLELGRYEEALELLERALA 73
|
|
| TPR-S |
pfam20308 |
Tetratricopeptide Repeats-Sensor; This entry represents a sensor domain consisting of 7 TPR ... |
594-675 |
2.85e-04 |
|
Tetratricopeptide Repeats-Sensor; This entry represents a sensor domain consisting of 7 TPR repeats forming a tightly-wound solenoid structure harbouring a deep central pocket. The TPR-S binding pocket is lined with several conserved aromatic and polar residues predicted to bind a NAD+-derived nucleotide in prokaryotic NAD+-derived nucleotide-activated effector conflict systems. It has been acquired at the base of the choanoflagellate-animal lineage as a core component of the ASK signalosome.
Pssm-ID: 466458 [Multi-domain] Cd Length: 105 Bit Score: 40.72 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 594 YHEARGHFEHVLTVdPRDYVAHYNLG-ALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSLYVRR-GDWGRAREALSK 671
Cdd:pfam20308 2 YDAAVELLEALLAL-PEDARAQEQLAlALARLPGDRDEALDVLEDLIERLGEDPETLGLLGRIYKRLwLESAEDREALDQ 80
|
....
gi 1401176184 672 AIDL 675
Cdd:pfam20308 81 AIEA 84
|
|
| TPR_16 |
pfam13432 |
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ... |
651-712 |
3.36e-04 |
|
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.
Pssm-ID: 433202 [Multi-domain] Cd Length: 68 Bit Score: 39.63 E-value: 3.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 651 TLGSLYVRRGDWGRAREALSKAIDLE---PKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQ 712
Cdd:pfam13432 2 ALARAALRAGDYDDAAAALEAALARFpesPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPG 66
|
|
| TPR_2 |
pfam07719 |
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ... |
646-678 |
4.35e-04 |
|
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.
Pssm-ID: 429619 [Multi-domain] Cd Length: 33 Bit Score: 38.27 E-value: 4.35e-04
10 20 30
....*....|....*....|....*....|...
gi 1401176184 646 AEAYNTLGSLYVRRGDWGRAREALSKAIDLEPK 678
Cdd:pfam07719 1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
|
|
| TPR |
smart00028 |
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
646-679 |
4.77e-04 |
|
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.
Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 37.81 E-value: 4.77e-04
10 20 30
....*....|....*....|....*....|....
gi 1401176184 646 AEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKF 679
Cdd:smart00028 1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
|
|
| TPR_1 |
pfam00515 |
Tetratricopeptide repeat; |
680-713 |
4.90e-04 |
|
Tetratricopeptide repeat;
Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 37.79 E-value: 4.90e-04
10 20 30
....*....|....*....|....*....|....
gi 1401176184 680 ASAHYNLGLVFRAKRERSEAVREFRQALALDPQF 713
Cdd:pfam00515 1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
234-327 |
6.36e-04 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 42.17 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 234 LRYVEGVLGEFIGFLQRRGLLETSLLVFTSDHGES-LGEHGerthgyfiyQST---LRVPLIFHWPATARAAVSRVLEP- 308
Cdd:cd16024 173 LKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMTdAGNHG---------GSSpgeTSVPLLFISPKFSSKPSNADGELs 243
|
90 100
....*....|....*....|...
gi 1401176184 309 ----VSLLDVAPTILQALGLPSP 327
Cdd:cd16024 244 yyetVQQVDLAPTLALLLGLPIP 266
|
|
| TPR_2 |
pfam07719 |
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ... |
680-712 |
6.51e-04 |
|
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.
Pssm-ID: 429619 [Multi-domain] Cd Length: 33 Bit Score: 37.50 E-value: 6.51e-04
10 20 30
....*....|....*....|....*....|...
gi 1401176184 680 ASAHYNLGLVFRAKRERSEAVREFRQALALDPQ 712
Cdd:pfam07719 1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
|
|
| tol_pal_ybgF |
TIGR02795 |
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ... |
647-723 |
6.78e-04 |
|
tol-pal system protein YbgF; Members of this protein family are the product of one of seven genes regularly clustered in operons to encode the proteins of the tol-pal system, which is critical for maintaining the integrity of the bacterial outer membrane. The gene for this periplasmic protein has been designated orf2 and ybgF. All members of the seed alignment were from unique tol-pal gene regions from completed bacterial genomes. The architecture of this protein is a signal sequence, a low-complexity region usually rich in Asn and Gln, a well-conserved region with tandem repeats that resemble the tetratricopeptide (TPR) repeat, involved in protein-protein interaction.
Pssm-ID: 188247 [Multi-domain] Cd Length: 117 Bit Score: 39.96 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 647 EAYNTLGSLYVRRGDWGRAREALSKAIDLEPKF---ASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTPAREALDRL 723
Cdd:TIGR02795 1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKStyaPNAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKSPKAPDALLKL 80
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
259-336 |
7.35e-04 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 42.73 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 259 LVFTSDHG-------ESLGE----HgerthgyfiyqSTLRVPLIFhwpaTARAAVSRVLEPVSLLDVAPTILQALGLPSP 327
Cdd:COG0696 436 LLITADHGnaeqmidPDTGGphtaH-----------TTNPVPFIL----VGGDKGVKLREDGRLADIAPTILELMGLPQP 500
|
....*....
gi 1401176184 328 PEFQGRALL 336
Cdd:COG0696 501 AEMTGKSLI 509
|
|
| TPR_1 |
pfam00515 |
Tetratricopeptide repeat; |
646-679 |
8.76e-04 |
|
Tetratricopeptide repeat;
Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 37.40 E-value: 8.76e-04
10 20 30
....*....|....*....|....*....|....
gi 1401176184 646 AEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKF 679
Cdd:pfam00515 1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
259-337 |
9.49e-04 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 42.40 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 259 LVFTSDHG--ESLG--EHGE--RTHgyfiyqSTLRVPLIFHWPATARaavsrvLEPVSLLDVAPTILQALGLPSPPEFQG 332
Cdd:PRK05434 435 LLITADHGnaEQMIdpETGQphTAH------TTNPVPFILVGGKALR------LEGGKLADIAPTILDLLGLEQPAEMTG 502
|
....*
gi 1401176184 333 RALLS 337
Cdd:PRK05434 503 KSLIE 507
|
|
| TPR_16 |
pfam13432 |
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ... |
480-544 |
1.16e-03 |
|
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.
Pssm-ID: 433202 [Multi-domain] Cd Length: 68 Bit Score: 38.09 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1401176184 480 YGHALTLAAAGRMDQANELLQQLL---GKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPANA 544
Cdd:pfam13432 1 LALARAALRAGDYDDAAAALEAALarfPESPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPGDP 68
|
|
| COG4700 |
COG4700 |
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown]; |
523-698 |
1.29e-03 |
|
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
Pssm-ID: 443735 [Multi-domain] Cd Length: 249 Bit Score: 41.02 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 523 LSRHAAAAESFQEALKSDPANALA-HFDLGVSEFALHRLDDAARELQVTLAIEPYYTRAE--ELLGSVLLEQHKYHEARG 599
Cdd:COG4700 102 LGRYDEAIELYEEALTGIFADDPHiLLGLAQALFELGRYAEALETLEKLIAKNPDFKSSDahLLYARALEALGDLEAAEA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 600 HFEHVltvdprdyVAHYnlgalatleqqwadaenhlkealktdpSSAEAYNTLGSLYVRRGDWGRAREALsKAIDLEPKF 679
Cdd:COG4700 182 ELEAL--------ARRY---------------------------SGPEARYRYAKFLARQGRTAEAKELL-EEILDEAKH 225
|
170 180
....*....|....*....|..
gi 1401176184 680 ASAHY---NLGLVFRAKRERSE 698
Cdd:COG4700 226 MPKHYrrlNREWIREAKKLLKS 247
|
|
| COG4700 |
COG4700 |
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown]; |
486-606 |
1.47e-03 |
|
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
Pssm-ID: 443735 [Multi-domain] Cd Length: 249 Bit Score: 41.02 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 486 LAAAGRMDQANELLQQLL-GKTPDLVSVRLSLGINQQKLSRHAAAAESFQEALKSDPA--NALAHFDLGVSEFALHRLDD 562
Cdd:COG4700 99 LLELGRYDEAIELYEEALtGIFADDPHILLGLAQALFELGRYAEALETLEKLIAKNPDfkSSDAHLLYARALEALGDLEA 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1401176184 563 AARELQVTLAiepYYTRAEEL--LGSVLLEQHKYHEARGHFEHVLT 606
Cdd:COG4700 179 AEAELEALAR---RYSGPEARyrYAKFLARQGRTAEAKELLEEILD 221
|
|
| TPR_17 |
pfam13431 |
Tetratricopeptide repeat; |
634-667 |
1.48e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 433201 [Multi-domain] Cd Length: 34 Bit Score: 36.75 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|....
gi 1401176184 634 HLKEALKTDPSSAEAYNTLGSLYVRRGDWGRARE 667
Cdd:pfam13431 1 LYLKALELDPNNADAYYNLAVLLLELGQSETALQ 34
|
|
| PRK11189 |
PRK11189 |
lipoprotein NlpI; Provisional |
566-712 |
1.69e-03 |
|
lipoprotein NlpI; Provisional
Pssm-ID: 236875 [Multi-domain] Cd Length: 296 Bit Score: 41.03 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 566 ELQVTLAiepyytRAEELLGSVLLEQHKYheARGHFEHVLTVDprdyvahyNLGaLATLeqqwadAENHLKEALKTDPSS 645
Cdd:PRK11189 41 QQEVILA------RLNQILASRDLTDEER--AQLHYERGVLYD--------SLG-LRAL------ARNDFSQALALRPDM 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 646 AEAYNTLGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVF----RAKrersEAVREFRQALALDPQ 712
Cdd:PRK11189 98 ADAYNYLGIYLTQAGNFDAAYEAFDSVLELDPTYNYAYLNRGIALyyggRYE----LAQDDLLAFYQDDPN 164
|
|
| TPR_19 |
pfam14559 |
Tetratricopeptide repeat; |
591-655 |
3.89e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 36.41 E-value: 3.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401176184 591 QHKYHEARGHFEHVLTVDPRDYVAHYNLGALATLEQQWADAENHLKEALKTDPSSAEAYNTLGSL 655
Cdd:pfam14559 1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAKL 65
|
|
| PRK11788 |
PRK11788 |
tetratricopeptide repeat protein; Provisional |
631-728 |
4.03e-03 |
|
tetratricopeptide repeat protein; Provisional
Pssm-ID: 236983 [Multi-domain] Cd Length: 389 Bit Score: 40.18 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 631 AENHLKEALKTDPSSAEAYNTLGSLYVRRGDWGRAREA---LSKAIDLEPKFASAHY--NLGLVFRAKRERSEAVREFRQ 705
Cdd:PRK11788 126 AEELFLQLVDEGDFAEGALQQLLEIYQQEKDWQKAIDVaerLEKLGGDSLRVEIAHFycELAQQALARGDLDAARALLKK 205
|
90 100
....*....|....*....|...
gi 1401176184 706 ALALDPQFTPAREALDRLELDRK 728
Cdd:PRK11788 206 ALAADPQCVRASILLGDLALAQG 228
|
|
| TPR_19 |
pfam14559 |
Tetratricopeptide repeat; |
525-575 |
4.64e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 36.02 E-value: 4.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 525 RHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAIEP 575
Cdd:pfam14559 3 DYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADP 53
|
|
| YfgM |
COG2976 |
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ... |
494-678 |
5.44e-03 |
|
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];
Pssm-ID: 442215 [Multi-domain] Cd Length: 207 Bit Score: 38.68 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 494 QANELLQQLLGKtpdlvsvrlslgINQQKLSRHAAAAESFQEALKSDPANALAHFDLGVSEFALHRLDDAARELQVTLAI 573
Cdd:COG2976 52 EASALYEQLLEA------------LAAGDAAAAAAAAEKLIDDYGGTAYAALAALLLAKAAVDAGDLDKAAAQLQWVLDN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401176184 574 ---EPYYTRAEELLGSVLLEQHKYHEArghfehvltvdprdyvahynlgaLATLEQqwadaenhlkeaLKTDPSSAEAYN 650
Cdd:COG2976 120 akdPALKALARLRLARVLLAQKKYDEA-----------------------LATLDA------------VKPEAFAALYAE 164
|
170 180
....*....|....*....|....*...
gi 1401176184 651 TLGSLYVRRGDWGRAREALSKAIDLEPK 678
Cdd:COG2976 165 LRGDILLAQGDKAEARAAYQKALAALPE 192
|
|
| PRK11788 |
PRK11788 |
tetratricopeptide repeat protein; Provisional |
652-723 |
6.72e-03 |
|
tetratricopeptide repeat protein; Provisional
Pssm-ID: 236983 [Multi-domain] Cd Length: 389 Bit Score: 39.41 E-value: 6.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401176184 652 LGSLYVRRGDWGRAREALSKAIDLEPKFASAHYNLGLVFRAKRERSEAVREFRQALALDPQFTParEALDRL 723
Cdd:PRK11788 186 LAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEEQDPEYLS--EVLPKL 255
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
276-336 |
6.92e-03 |
|
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 39.44 E-value: 6.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401176184 276 THGYfIYQSTLRVPLIFHWPATARAAVSRvlePVSLLDVAPTILQALGLPSPPEFQGRALL 336
Cdd:cd16016 400 THGS-PYDYDTHVPLLFYGWGIKPGEIPR---PVEITDIAPTLAALLGIQPPNGCIGKPLL 456
|
|
| TPR_11 |
pfam13414 |
TPR repeat; |
626-660 |
7.50e-03 |
|
TPR repeat;
Pssm-ID: 315977 [Multi-domain] Cd Length: 42 Bit Score: 34.75 E-value: 7.50e-03
10 20 30
....*....|....*....|....*....|....*
gi 1401176184 626 QQWADAENHLKEALKTDPSSAEAYNTLGSLYVRRG 660
Cdd:pfam13414 8 GKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYKLG 42
|
|
| |
