|
Name |
Accession |
Description |
Interval |
E-value |
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
15-613 |
0e+00 |
|
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: 807.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 15 LITWGHWFSFFNIILAMLIATRYLGSISWPSTTLGVTYLIISWIGHFSFLSFVTYLLTIFPLSFILPREKPLRFISAIIA 94
Cdd:COG3083 1 LISWGHWFALFNILLALLIGSRYLFIADWPGTLLGRLYLLVSWLGHFSFLVFALYLLLLFPLSFLVPSQRLFRGLSVILA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 95 TLALVLLLIDTQVFQLFKFHLNGQVWQLLLDQAQTEEGSIWSIIFVAVPAIFLLQLLLSAYVWRKINKRKRRQYGNQVGL 174
Cdd:COG3083 81 TAGLTLLLVDTEVFQRFHLHLNPLVWDLLFNPDQGELARDWQLLFIPVPLIFLLEMLLATWSWRKLRSLERRRFGKPVAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 175 ALLVCFILTHLVNSWADATLYQPITMQRANFPLSYPMTARSFLAKHGWLDLEQYEKKAEDQGSAE-HRLLYPLRPLSVSA 253
Cdd:COG3083 161 LFLVSFLASHLIYIWADANFYRPITMQRANLPLSYPMTARSFLEKHGLLDAQEYQQRLEEQGNPEaSSLNYPLHPLQFSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 254 PSDHKNLLVVVVDSLRADMLNNINMPNLQRYADNHFNFRQHMSGGNDEAMGMFSLFYGLPGHYYGDIRADKRPPVLFDEM 333
Cdd:COG3083 241 PAKPPNILLIVVDSLRADMLDPEVMPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLFYGLPGNYWDSILAERTPPVLIDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 334 LRQDYQFGLFGALE-DAKQYRQSLLAGLRKQVFVSRQ---TDDRRLIDDWQQWLGTRTADRPWFSLVYLSSPGDYQVPAS 409
Cdd:COG3083 321 QQQGYQFGLFSSAGfNSPLFRQTIFSDVSLPRLHTPGgpaQRDRQITAQWLQWLDQRDSDRPWFSYLFLDAPHAYSFPAD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 410 IKGPFQPeLTRFNPATAYRPENLQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNETQSNSWGYD 489
Cdd:COG3083 401 YPKPFQP-SEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYWGHN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 490 SNYSTYQVQVPLVLAWPGAEPAPQAQASSHLDLVPTLMKNMLGVRNPYRDYSTGRNLFEAS-TRTWLLAGDQNDFAIYQG 568
Cdd:COG3083 480 SNFSRYQLQVPLVIHWPGTPPQVISKLTSHLDIVPTLMQRLLGVQNPASDYSQGEDLFDPQrRRDWVLAGDYRNLAIITP 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1430952382 569 NTITQFNKQGDFELLDRDtYRPIKHGTPDMGTLIQVMNELNRFYR 613
Cdd:COG3083 560 DRITVLDPSGNYQVYDRD-YRPLKDAKPPLGLLLQVLTELKRFYA 603
|
|
| LapC_YejM_PbgA |
NF038282 |
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ... |
1-611 |
0e+00 |
|
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory system that controls the activity of LpxC, the enzyme that catalyzes the first committed step in the LPS synthesis. The earlier report (2015) by Dalebroux, et al (PMID: 25856753), which assigned a role in cardiolipin transport and introduced the name PbgA (phoPQ-barrier gene A), is no longer considered accurate.
Pssm-ID: 468449 [Multi-domain] Cd Length: 584 Bit Score: 528.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 1 MVETGNPYRDNVSRLITWGHWFSFFNIILAMLIATRYLGSISWPSTTLGVTYLIISWIGHFSFLSFVTYLLTIFPLSFIL 80
Cdd:NF038282 1 MVTNRQRYREKVSQMISWGHWFALFNILLSLGLGSRYLFVSDWPSSLAGRIYALVSWLGHFSFIVFAAYLLILFPLTFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 81 PREKPLRFISAIIATLALVLLLIDTQVFQLFKFHLNGQVWQLLLDQAQTEEGSIWSIIFVAVPAIFLLQLLLSAYVWRKI 160
Cdd:NF038282 81 MSQRLLRFLSAILATAGLTLLLVDSEVFTRFHLHLNPVVWELVINPDQGEMARDWQLMFISVPVIFLVEMLFATWSWQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 161 NKRKRRQYGNQVGLALLVCFILTHLVNSWADATLYQPITMQRANFPLSYPMTARSFLAKHGWLDLEQYEKKAEDQGSAEH 240
Cdd:NF038282 161 RSLNRRRFGKPLAALFISAFFASHLMYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVQQGNPEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 241 -RLLYPLRPLSVSAPSDHKNLLVVVVDSLRADMLNNiNMPNLQRYADNHFNFRQHMSGGNDEAMGMFSLFYGLPGHYYGD 319
Cdd:NF038282 241 lSVEYPLSDLSFRDKGSGYNLLLIVVDGLNNSDIAK-AMPALARFAEQNVQFTQHYSSGNQNDTGLFGLFYGISPSYLDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 320 IRADKRPPVLFDEMLRQDYQFGLFGALE-DAKQYRQSLLA-----GLRKQvfvsrqtDDRRLIDDWQQWLGTRTADRPWF 393
Cdd:NF038282 320 ILSSRKPSALITALNQQGYQFGLFSSDGfKSPLYRQALLSdfslpPPQSQ-------SDAQTTSQWQQWLNGQKNTNPWF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 394 SLVylsspgdyqvpasikgpfqpeltRFNPATAYRPENLQKlENRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSN 473
Cdd:NF038282 393 SYL-----------------------NLNGTSTASDDGKQK-QRRYQRGAADVDQQINTVLDTLKERGLLDNTVVVITAS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 474 HGQEFNETQSNswgydSNYSTYQVQVPLVLAWPGAEPAPQAQASSHLDLVPTLMKNMLGVRNPYRDYSTGRNLFEASTR- 552
Cdd:NF038282 449 HGVALDDNDDN-----FKFNRAQLQVPLVIHWPGTPAQTINKLTDHQDVMTTLMQRLLHVSTAAADYSQGEDLFAAQRRh 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430952382 553 TWLLAGDQNDFAIYQGNTITQFNKQGDFELLDRDTyRPIKHGTPDMGTLIQVMNELNRF 611
Cdd:NF038282 524 NWVATGDDGTLVITTPTQTLVLDNNGSYRAYDLNG-REIKDQKPQLALLLQVLTEEKRF 581
|
|
| DUF3413 |
pfam11893 |
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. ... |
7-251 |
2.18e-124 |
|
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 250 amino acids in length. This domain is found associated with pfam00884.
Pssm-ID: 432169 Cd Length: 246 Bit Score: 366.96 E-value: 2.18e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 7 PYRDNVSRLITWGHWFSFFNIILAMLIATRYLGSISWPSTTLGVTYLIISWIGHFSFLSFVTYLLTIFPLSFILPREKPL 86
Cdd:pfam11893 1 QYRDKVSQLISWGHWFALFNIILALLIGLRYLFSADWPSTLLGWLYLLVSWLGHFSFLAFALYLLVLFPLTFLIPYSRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 87 RFISAIIATLALVLLLIDTQVFQLFKFHLNGQVWQLLLDQAQTEEGSIWSIIFVAVPAIFLLQLLLSAYVWRKINKRKRR 166
Cdd:pfam11893 81 RGLAAIIATAGLTLLLVDTEVFDQYGFHLNPVVWDLLLNGDQSELSRSWQLLFIVIPVILLLELLLANWVWKKLRKLQRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 167 QYGNQVGLALLVCFILTHLVNSWADATLYQPITMQRANFPLSYPMTARSFLAKHGWLDLEQYEKKAEDQGSAE-HRLLYP 245
Cdd:pfam11893 161 KIGKPVAAFLLLCFLASHLIHIWADANLYRPITMQRANFPLSYPMTAKSFLEKHGLLDLESYQQRLAEQGNPPaQPLNYP 240
|
....*.
gi 1430952382 246 LRPLSV 251
Cdd:pfam11893 241 LHPLQC 246
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
258-548 |
8.82e-58 |
|
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: 195.07 E-value: 8.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 258 KNLLVVVVDSLRADMLN-----NINMPNLQRYADNHFNFRQHMSGGNDEAMGMFSLFYGLPGHYYGDIRA--DKRPPVLF 330
Cdd:cd16148 1 MNVILIVIDSLRADHLGcygydRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGplEPDDPTLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 331 DEMLRQDYQFGLFGAledakQYRQSLLAGLRKQVFV-------------SRQTDDRRLIDDWQQWLGTRTADRPWFSLVY 397
Cdd:cd16148 81 EILRKAGYYTAAVSS-----NPHLFGGPGFDRGFDTfedfrgqegdpgeEGDERAERVTDRALEWLDRNADDDPFFLFLH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 398 LSSPgdyqvpasiKGPFqpeltrfnpatayrpenlqklenRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQE 477
Cdd:cd16148 156 YFDP---------HEPY-----------------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430952382 478 FNETQSNsWGYDSNYSTYQVQVPLVLAWPGAEPAPQ-AQASSHLDLVPTLMkNMLGVRNPyrDYSTGRNLFE 548
Cdd:cd16148 204 FGEHGLY-WGHGSNLYDEQLHVPLIIRWPGKEPGKRvDALVSHIDIAPTLL-DLLGVEPP--DYSDGRSLLP 271
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
258-528 |
4.15e-28 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 114.44 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 258 KNLLVVVVDSLRADMLNNI-----NMPNLQRYADNHFNFRQHMSGGNDEAMGMFSLFYGLPGHYYG-----DIRADKRPP 327
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYgyprpTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGsyvstPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 328 VLFDEMLRQDYQFGLFGALEDAKQYRQSLLAGLRKQVF-------------------VSRQTDDRRLIDDWQQWLgtRTA 388
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFgrntgsdlyadppdvpyncSGGGVSDEALLDEALEFL--DNN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 389 DRPWFS-LVYLSSPGDYQVPAsikgPFQPELTRFNPATAYRPENLqkleNRYKNAVFYTDQLLEQMLTQLQLQGLDDQTI 467
Cdd:pfam00884 159 DKPFFLvLHTLGSHGPPYYPD----RYPEKYATFKPSSCSEEQLL----NSYDNTLLYTDDAIGRVLDKLEENGLLDNTL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430952382 468 VVVTSNHGQEFNETQSNS-WGYDSNYSTYQVQVPLVLAWPGAEPAPQ--AQASSHLDLVPTLMK 528
Cdd:pfam00884 231 VVYTSDHGESLGEGGGYLhGGKYDNAPEGGYRVPLLIWSPGGKAKGQksEALVSHVDLFPTILD 294
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
25-572 |
6.22e-26 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 112.44 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 25 FNIILAMLIATR-YLGSISWPSTTLGVTYLIISWIGHFSFLSFVTYLLTIFPLSFILPREKPLRFISAIIATLALVLLLI 103
Cdd:COG1368 1 FFLLFLLLLSLRlVFLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 104 DTQVFQLFKFHLNGQVWQLLlDQAQTEEGSIWS--IIFVAVPAIFLLQLLLSAYVWRKINKRKRRQYGNQVGLALLVCFI 181
Cdd:COG1368 81 DILYYRFFGDRLNFSDLDYL-GDTGEVLGSLLSsyDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 182 L----------THLVNSWADATLYQPITmqrANFPLSYPMTARSFLAKHgwlDLEQYEKKAEDQGSAEHRllyplRPLSV 251
Cdd:COG1368 160 LlgirlgedrpLNLSDAFSRNNFVNELG---LNGPYSFYDALRNNKAPA---TYSEEEALEIKKYLKSNR-----PTPNP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 252 SAPSDHKNLLVVVVDSLRADMLNNIN-----MPNLQRYADNHFNFRQHMSGGNDEAMGMFSLFYGLPGhyygdirADKRP 326
Cdd:COG1368 229 FGPAKKPNVVVILLESFSDFFIGALGngkdvTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPP-------LPGGS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 327 PVlfdEMLRQDYQFGLFGALEDaKQY--------------RQSLLAGLRKQVFVSRQT-----------DDRRLIDDWQQ 381
Cdd:COG1368 302 PY---KRPGQNNFPSLPSILKK-QGYetsffhggdgsfwnRDSFYKNLGFDEFYDREDfddpfdggwgvSDEDLFDKALE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 382 WLgtRTADRPWFSLVY-LSSPGDYQVPasikgpfqpeltrfnPATAYRPENLQKLENRYKNAVFYTDQLLEQMLTQLQLQ 460
Cdd:COG1368 378 EL--EKLKKPFFAFLItLSNHGPYTLP---------------EEDKKIPDYGKTTLNNYLNAVRYADQALGEFIEKLKKS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 461 GLDDQTIVVVTSNHGQEFNETQSNSWGYDSNystyqvQVPLVLAWPG-AEPAPQAQASSHLDLVPTLMkNMLGVRNPYrD 539
Cdd:COG1368 441 GWYDNTIFVIYGDHGPRSPGKTDYENPLERY------RVPLLIYSPGlKKPKVIDTVGSQIDIAPTLL-DLLGIDYPS-Y 512
|
570 580 590
....*....|....*....|....*....|...
gi 1430952382 540 YSTGRNLFEAstrtwllagDQNDFAIYQGNTIT 572
Cdd:COG1368 513 YAFGRDLLSP---------DTDPFAFRNGGFIT 536
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
241-586 |
1.50e-18 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 88.01 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 241 RLLYPLRPLSVSAPSDHKNLLVVVVDSLRADML-----NNINMPNLQRYADNHFNFRQH--------------MSGGNDE 301
Cdd:COG3119 7 LLLALLAAAAAAAAAKRPNILFILADDLGYGDLgcygnPLIKTPNIDRLAAEGVRFTNAyvtspvcspsraslLTGRYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 302 AMGMFSLFYGLPGHYYGDIradkrppVLFDEMLRQ-DYQFGLFGaledaKQYrqsllaglrkqvfvsrQTDDRRLIDDWQ 380
Cdd:COG3119 87 RTGVTDNGEGYNGGLPPDE-------PTLAELLKEaGYRTALFG-----KWH----------------LYLTDLLTDKAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 381 QWLGTRTA-DRPWFslVYLSSP---GDYQVPASIKGPFQPE---LTRFNPATAYRPENLQKLENRYKNAVFYTDQLLEQM 453
Cdd:COG3119 139 DFLERQADkDKPFF--LYLAFNaphAPYQAPEEYLDKYDGKdipLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 454 LTQLQLQGLDDQTIVVVTSNHGQEFNEtqsnsWGYDSN-YSTYQ--VQVPLVLAWPGAEPAPQ--AQASSHLDLVPTLMK 528
Cdd:COG3119 217 LDALEELGLADNTIVVFTSDNGPSLGE-----HGLRGGkGTLYEggIRVPLIVRWPGKIKAGSvsDALVSLIDLLPTLLD 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430952382 529 nMLGVRNPyrDYSTGRNLF------EASTRTWLLA---GDQNDFAIYQGN--TITQFNKQGDFEL--LDRD 586
Cdd:COG3119 292 -LAGVPIP--EDLDGRSLLplltgeKAEWRDYLYWeypRGGGNRAIRTGRwkLIRYYDDDGPWELydLKND 359
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
258-530 |
4.42e-17 |
|
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: 80.93 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 258 KNLLVVVVDSLRADMLNNINM-----PNLQRYADN--HFNFRQ----------HMS---GGNDEAMGMFSLFYGLPGHYY 317
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNpapttPNLKRLASEgaTFNFRSvspptssapnHAAlltGAYPTLHGYTGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 318 GDIRADKRPPVLFDEMLRQDYQFGLFGALEDAKQyrqsllaglrkqvfvsrqtddrrliddwqqwlgtRTADRPWFSLVY 397
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLLKAIDE----------------------------------TSKEKPFVLFLH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 398 LSSPgDYQVPASikGPFQPEltrfnpatayrpenlqklenrYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQE 477
Cdd:cd00016 127 FDGP-DGPGHAY--GPNTPE---------------------YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430952382 478 FNE--TQSNSWGYDSNYSTyQVQVPLVLAWPGAEPAPQAQAS-SHLDLVPTLMKNM 530
Cdd:cd00016 183 DKGhgGDPKADGKADKSHT-GMRVPFIAYGPGVKKGGVKHELiSQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
372-539 |
2.23e-12 |
|
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: 68.39 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 372 DRRLIDDWQQWLGTRTA----DRPWFSLVYLSSPGDYQvpasikgpfqpeltrFNPATAyrpENLQKLENRYKNAVFYTD 447
Cdd:cd16035 116 DPGIAAQAVEWLRERGAknadGKPWFLVVSLVNPHDIM---------------FPPDDE---ERWRRFRNFYYNLIRDVD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 448 QLLEQMLTQLQLQGLDDQTIVVVTSNHGqefnETQSNSWGYDSNYSTY--QVQVPLVLAWPGAEPAPQ-AQA-SSHLDLV 523
Cdd:cd16035 178 RQIGRVLDALDASGLADNTIVVFTSDHG----EMGGAHGLRGKGFNAYeeALHVPLIISHPDLFGTGQtTDAlTSHIDLL 253
|
170
....*....|....*.
gi 1430952382 524 PTLMkNMLGVRNPYRD 539
Cdd:cd16035 254 PTLL-GLAGVDAEARA 268
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
389-562 |
3.43e-12 |
|
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: 67.99 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 389 DRPWFSLVYLSSPGDyqvpasikgPFQPeltrfnpatayRPE--NLQKLENR--YKNAVFYTDQLLEQMLTQLQLQGLDD 464
Cdd:cd16032 132 GRPFFLTVSFTHPHD---------PYVI-----------PQEywDLYVRRARraYYGMVSYVDDKVGQLLDTLERTGLAD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 465 QTIVVVTSNHGQEFNEtqSNSWgYDSNYSTYQVQVPLVLAWPG-AEPAPQAQASSHLDLVPTLMKNMLGVRNPYRDYSTG 543
Cdd:cd16032 192 DTIVIFTSDHGDMLGE--RGLW-YKMSFFEGSARVPLIISAPGrFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPPLDG 268
|
170
....*....|....*....
gi 1430952382 544 RNLFEastrtwLLAGDQND 562
Cdd:cd16032 269 RSLLP------LLEGGDSG 281
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
372-547 |
6.79e-12 |
|
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: 67.53 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 372 DRRLIDDWQQWLGTRTADRPWFSLVYLSSPgdyqvpasiKGPFQP---ELTRFNPATAYRPENLQKLEN------RYKNA 442
Cdd:cd16027 124 AWDYASNAADFLNRAKKGQPFFLWFGFHDP---------HRPYPPgdgEEPGYDPEKVKVPPYLPDTPEvredlaDYYDE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 443 VFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNetQSNSWGYDSNystyqVQVPLVLAWPGAEPAPQAQAS--SHL 520
Cdd:cd16027 195 IERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP--RAKGTLYDSG-----LRVPLIVRWPGKIKPGSVSDAlvSFI 267
|
170 180
....*....|....*....|....*..
gi 1430952382 521 DLVPTLMkNMLGVRNPyrDYSTGRNLF 547
Cdd:cd16027 268 DLAPTLL-DLAGIEPP--EYLQGRSFL 291
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
259-537 |
5.05e-10 |
|
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: 60.14 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 259 NLLVVVVDSLRADML-----NNINMPNLQRYADNHFNFRQH--------------MSGgndeamgMFSLFYGLPGHYYGD 319
Cdd:cd16022 2 NILLIMTDDLGYDDLgcygnPDIKTPNLDRLAAEGVRFTNAyvaspvcspsraslLTG-------RYPHRHGVRGNVGNG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 320 IRADKRPPVLFDEMLRQDYQFGLFGaledaKQYRQSLlaglrkqvfvsrqtddrrliddwqQWLGTRTADRPWFslVYLS 399
Cdd:cd16022 75 GGLPPDEPTLAELLKEAGYRTALIG-----KWHDEAI------------------------DFIERRDKDKPFF--LYVS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 400 spgdYQVPASikgPFqpeltrfnpatayrpenlqklenRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFN 479
Cdd:cd16022 124 ----FNAPHP---PF-----------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLG 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430952382 480 ETQSNSWGydsnYSTYQ--VQVPLVLAWPGAEPAPQA--QASSHLDLVPTLMKnMLGVRNPY 537
Cdd:cd16022 174 DHGLRGKK----GSLYEggIRVPFIVRWPGKIPAGQVsdALVSLLDLLPTLLD-LAGIEPPE 230
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
388-526 |
1.06e-09 |
|
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: 60.69 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 388 ADRPWFslVYLSspgdYQVP-ASIKGP-FQPELTRFNPATAYRPENLQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDDQ 465
Cdd:cd16145 186 KDKPFF--LYLA----YTLPhAPLQVPdDGPYKYKPKDPGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLKELGIDEN 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430952382 466 TIVVVTSNHG--QEFNETQSNSWgYDSN-------YSTYQ--VQVPLVLAWPGAEPApqAQASSHL----DLVPTL 526
Cdd:cd16145 260 TLVVFTSDNGphSEGGSEHDPDF-FDSNgplrgykRSLYEggIRVPFIARWPGKIPA--GSVSDHPsafwDFMPTL 332
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
258-546 |
2.07e-09 |
|
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: 59.94 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 258 KNLLVVVVDSLRADML---NN--INMPNLQRYADNHFNFRQhmsggndeAMGMF--------SLFYGLPGHYYGD----- 319
Cdd:cd16150 1 PNIVIFVADQLRADSLghlGNpaAVTPNLDALAAEGVRFSN--------AYCQNpvcspsrcSFLTGWYPHVNGHrtlhh 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 320 -IRADKrpPVLFDEMLRQDYQFGLFGALEDAKQYRQsllaglrkqvFVSRQTDDRRLIDDWQQWLGTRTADRPWFSLVYL 398
Cdd:cd16150 73 lLRPDE--PNLLKTLKDAGYHVAWAGKNDDLPGEFA----------AEAYCDSDEACVRTAIDWLRNRRPDKPFCLYLPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 399 SSP-GDYQVPA----SIKGPFQPELTRFNPATAYRPENLQKLENR----------------YKNAVFYTDQLLEQMLTQL 457
Cdd:cd16150 141 IFPhPPYGVEEpwfsMIDREKLPPRRPPGLRAKGKPSMLEGIEKQgldrwseerwrelratYLGMVSRLDHQFGRLLEAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 458 QLQGLDDQTIVVVTSNHGQ---EFNETQSNswgyDSNYSTYQVQVPLVLAWPGaepAPQAQASSHL----DLVPTLMkNM 530
Cdd:cd16150 221 KETGLYDDTAVFFFSDHGDytgDYGLVEKW----PNTFEDCLTRVPLIIKPPG---GPAGGVSDALvelvDIPPTLL-DL 292
|
330
....*....|....*.
gi 1430952382 531 LGVRNPYRDYstGRNL 546
Cdd:cd16150 293 AGIPLSHTHF--GRSL 306
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
252-476 |
2.25e-09 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 59.76 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 252 SAPSDHKNLLVVVVDSLRADMLNNINMPNLQRYADNHFNFRQHMSG------------------------GN---DEAMG 304
Cdd:COG1524 18 AAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVfpsttapahttlltglypgehgivGNgwyDPELG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 305 MFSLFYGLPGHYYGDIRADKRPPvLFDEMLRQDYQFGLFG--ALEDAKQYRQSLLAGLR-KQVFVSRQTDDRRLIDDWQQ 381
Cdd:COG1524 98 RVVNSLSWVEDGFGSNSLLPVPT-IFERARAAGLTTAAVFwpSFEGSGLIDAARPYPYDgRKPLLGNPAADRWIAAAALE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 382 wlgTRTADRPWFSLVYLSSPgDYQvpASIKGPFQPEltrfnpatayrpenlqklenrYKNAVFYTDQLLEQMLTQLQLQG 461
Cdd:COG1524 177 ---LLREGRPDLLLVYLPDL-DYA--GHRYGPDSPE---------------------YRAALREVDAALGRLLDALKARG 229
|
250
....*....|....*
gi 1430952382 462 LDDQTIVVVTSNHGQ 476
Cdd:COG1524 230 LYEGTLVIVTADHGM 244
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
258-532 |
4.22e-09 |
|
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: 58.08 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 258 KNLLVVVVDSLRADMLNNIN-----MPNLQRYADNHFNFRQHMSGGNDE--AMGMFSLFYGLP----GHYYGDIRADKRP 326
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVggedlTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPplplGSGSYTLYKLNPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 327 PVLFDEMLRQDYQ-FGLFGAleDAKQY-RQSLLAGLRKQVFVSRQ--TDDRRLIDDW-----------QQWLgTRTADRP 391
Cdd:cd16015 81 PSLPSILKEQGYEtIFIHGG--DASFYnRDSVYPNLGFDEFYDLEdfPDDEKETNGWgvsdeslfdqaLEEL-EELKKKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 392 WFSLVY-LSSPGDYQVPASIKGPFQPEltrfnpatayrpENLQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVV 470
Cdd:cd16015 158 FFIFLVtMSNHGPYDLPEEKKDEPLKV------------EEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430952382 471 TSNHGQEFNETQSNSWGYDSNYStyqvQVPLVLAWPG-AEPAPQAQASSHLDLVPTLMkNMLG 532
Cdd:cd16015 226 YGDHLPSLGSDYDETDEDPLDLY----RTPLLIYSPGlKKPKKIDRVGSQIDIAPTLL-DLLG 283
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
454-546 |
8.75e-09 |
|
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: 56.86 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 454 LTQLQLQGLDDQTIVVVTSNHGqeFNETQSNSWG----------YDSNystyqVQVPLVLAWPGAEPAPQAQAS--SHLD 521
Cdd:cd16149 159 LDELEELGLTENTLVIFTSDNG--FNMGHHGIWGkgngtfplnmYDNS-----VKVPFIIRWPGVVPAGRVVDSlvSAYD 231
|
90 100
....*....|....*....|....*
gi 1430952382 522 LVPTLMKnMLGVRNPYRDYSTGRNL 546
Cdd:cd16149 232 FFPTLLE-LAGVDPPADPRLPGRSF 255
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
257-592 |
1.31e-08 |
|
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: 57.19 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 257 HKNLLVVVVDSLRADML-----NNINMPNLQRYADNHFNFRQHMSG--------GndeamgmfSLFYGL-P---GHYYGD 319
Cdd:cd16034 1 KPNILFIFADQHRAQALgcagdDPVKTPNLDRLAKEGVVFTNAVSNypvcspyrA--------SLLTGQyPltnGVFGND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 320 IRADKRPPVLFDEMLRQDYQFGLFGAL------EDAKQYRQSLLAGLRKQVF---VSRQTDDRRL----------IDDWQ 380
Cdd:cd16034 73 VPLPPDAPTIADVLKDAGYRTGYIGKWhldgpeRNDGRADDYTPPPERRHGFdywKGYECNHDHNnphyydddgkRIYIK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 381 QWL-------------GTRTADRPWFslVYLS----SPGDYQVPasikgpfQPELTRFNPATAYRPENL---QKLENRYK 440
Cdd:cd16034 153 GYSpdaetdlaieyleNQADKDKPFA--LVLSwnppHDPYTTAP-------EEYLDMYDPKKLLLRPNVpedKKEEAGLR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 441 NAV--FYT-----DQLLEQMLTQLQLQGLDDQTIVVVTSNHGQ---EFNETQSNSWgYDSNystyqVQVPLVLAWPGAEP 510
Cdd:cd16034 224 EDLrgYYAmitalDDNIGRLLDALKELGLLENTIVVFTSDHGDmlgSHGLMNKQVP-YEES-----IRVPFIIRYPGKIK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 511 APQ--AQASSHLDLVPTLMkNMLGVRNPY----RDYSTgrnlfeastrtwLLAGDQNDFAIYQgnTITQFNKQGDFELLD 584
Cdd:cd16034 298 AGRvvDLLINTVDIMPTLL-GLCGLPIPDtvegRDLSP------------LLLGGKDDEPDSV--LLQCFVPFGGGSARD 362
|
....*...
gi 1430952382 585 RDTYRPIK 592
Cdd:cd16034 363 GGEWRGVR 370
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
416-534 |
2.85e-08 |
|
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: 55.32 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 416 PELTRFNPATAYRPEN--LQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDdqTIVVVTSNHGQEFNEtqSNSWGYDSNYS 493
Cdd:cd16017 163 EEFAKFTPDCDNELQScsKEELINAYDNSILYTDYVLSQIIERLKKKDKD--AALIYFSDHGESLGE--NGLYLHGAPYA 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1430952382 494 T-YQVQVPLVL----AWPGAEPAPQAQAS-----SHLDLVPTLMkNMLGVR 534
Cdd:cd16017 239 PkEQYHVPFIIwssdSYKQRYPVERLRANkdrpfSHDNLFHTLL-GLLGIK 288
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
387-540 |
5.76e-07 |
|
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: 52.09 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 387 TADRPWFSLVYLSSpgdYQVPasikgpfQPELTRFNPATAYRpenlqkleNRYKNAVFYTDQLLEQMLTQLQLQGLDDQT 466
Cdd:cd16161 151 AKDRPFFLYAALAH---VHVP-------LANLPRFQSPTSGR--------GPYGDALQEMDDLVGQIMDAVKHAGLKDNT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 467 IVVVTSNHG-----------QEFNETQSNSWGYDSNYSTYQ--VQVPLVLAWPGAEPA--PQAQASSHLDLVPTLMKNML 531
Cdd:cd16161 213 LTWFTSDNGpwevkcelavgPGTGDWQGNLGGSVAKASTWEggHREPAIVYWPGRIPAnsTSAALVSTLDIFPTVVALAG 292
|
....*....
gi 1430952382 532 GVRNPYRDY 540
Cdd:cd16161 293 ASLPPGRIY 301
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
258-546 |
1.02e-06 |
|
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: 51.45 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 258 KNLLVVVVDSLRADMLNN-----INMPNLQRYADNHFNF-------------RQhmsggndeamgmfSLFYGL------- 312
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCygnpiVKTPNIDRLAAEGVRFtnaytpspvccpaRA-------------SLLTGLyphehgv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 313 ------PGHYYGDIRADKRppvLFDEMLRQ-DYQFGLFG-----ALEDAKQYrqsllaGLRKQVFVSrQTDDRRLIDDWQ 380
Cdd:cd16033 68 lnnvenAGAYSRGLPPGVE---TFSEDLREaGYRNGYVGkwhvgPEETPLDY------GFDEYLPVE-TTIEYFLADRAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 381 QWLGTRTA-DRPWFSLV--------------YLS--SPGDYQVPASIKGPF-------QPELTRFNPATAYRpENLQKLE 436
Cdd:cd16033 138 EMLEELAAdDKPFFLRVnfwgphdpyippepYLDmyDPEDIPLPESFADDFedkpyiyRRERKRWGVDTEDE-EDWKEII 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 437 NRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGqefnETQSNSWGYDSNYSTYQ--VQVPLVLAWPGAEPAPQA 514
Cdd:cd16033 217 AHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHG----DALGAHRLWDKGPFMYEetYRIPLIIKWPGVIAAGQV 292
|
330 340 350
....*....|....*....|....*....|....
gi 1430952382 515 QAS--SHLDLVPTLMkNMLGVRNPYRdySTGRNL 546
Cdd:cd16033 293 VDEfvSLLDLAPTIL-DLAGVDVPPK--VDGRSL 323
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
374-525 |
1.67e-06 |
|
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: 50.89 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 374 RLIDDWQQWLGTRtADRPWFslVYLSSPgdyqvpasikgpfQPELTRFNPAtayRPENLQKlENRYKNAVFYTDQLLEQM 453
Cdd:cd16160 179 TLVGDAKSFIEDN-QENPFF--LYFSFP-------------QTHTPLFASK---RFKGKSK-RGRYGDNINEMSWAVGEV 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430952382 454 LTQLQLQGLDDQTIVVVTSNHG--QEFNETQSNSW---GYDSNYSTYQVQVPLVLAWPGA-EPAPQAQASSHLDLVPT 525
Cdd:cd16160 239 LDTLVDTGLDQNTLVFFLSDHGphVEYCLEGGSTGglkGGKGNSWEGGIRVPFIAYWPGTiKPRVSHEVVSTMDIFPT 316
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
257-554 |
1.86e-06 |
|
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: 50.30 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 257 HKNLLVVVVDSLRADML----NNINM-PNLQRYADNHFNFRQhmsggndeamgMFS-----------LFYGL----PGHY 316
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLgcygQPLDLtPNLDALAEEGVLFEN-----------AFTpqpvcgparacLQTGLypteTGCF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 317 YGDIRADKRPPVLFDEMLRQDYQFGLFGaledaKQYrqslLAGLRkqvfVSRQTDdrRLIDdwqqWLGTRTADRPWFSLV 396
Cdd:cd16152 70 RNGIPLPADEKTLAHYFRDAGYETGYVG-----KWH----LAGYR----VDALTD--FAID----YLDNRQKDKPFFLFL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 397 YLSSP------GDYQVPASIKGPFqpeltrfnpATAYRPENLQKLENR-------YKNAVFYTDQLLEQMLTQLQLQGLD 463
Cdd:cd16152 131 SYLEPhhqndrDRYVAPEGSAERF---------ANFWVPPDLAALPGDwaeelpdYLGCCERLDENVGRIRDALKELGLY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 464 DQTIVVVTSNHGQEFnETQSNSW---GYDSNystyqVQVPLVLAWPGAEP-APQAQASSHLDLVPTLMKnMLGVRNPyrD 539
Cdd:cd16152 202 DNTIIVFTSDHGCHF-RTRNAEYkrsCHESS-----IRVPLVIYGPGFNGgGRVEELVSLIDLPPTLLD-AAGIDVP--E 272
|
330
....*....|....*...
gi 1430952382 540 YSTGRNL---FEASTRTW 554
Cdd:cd16152 273 EMQGRSLlplVDGKVEDW 290
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
314-548 |
1.87e-06 |
|
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: 50.07 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 314 GHY---YGDIRADKRPPVLFDEMLRQDYQFGLFGAlEDAKQYRQSLLAglRKQVFVSRQTDDRRLIDdwqqwlgtrtADR 390
Cdd:cd16153 77 GVYgfeAAHPALDHGLPTFPEVLKKAGYQTASFGK-SHLEAFQRYLKN--ANQSYKSFWGKIAKGAD----------SDK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 391 PWFslVYLSspgdYQVPASIKGPFQPELTRFnpatayrpenlqklenRYKNAVFYTDQLLEQMLTQLQLQGLD---DQTI 467
Cdd:cd16153 144 PFF--VRLS----FLQPHTPVLPPKEFRDRF----------------DYYAFCAYGDAQVGRAVEAFKAYSLKqdrDYTI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 468 VVVTSNHGQEFNETqsnswGYDSNYSTYQ--VQVPLVLAWPGAEPAPQAQA----SSHLDLVPTLMKnMLGVRNPYRDYS 541
Cdd:cd16153 202 VYVTGDHGWHLGEQ-----GILAKFTFWPqsHRVPLIVVSSDKLKAPAGKVrhdfVEFVDLAPTLLA-AAGVDVDAPDYL 275
|
....*..
gi 1430952382 542 TGRNLFE 548
Cdd:cd16153 276 DGRDLFE 282
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
372-547 |
1.94e-06 |
|
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: 50.23 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 372 DRRLIDDWQQWLGTR-TADRPWFSLVYLSSPgdyqvpasikgpfqpeltRFnPATAyrPENLQKLENR-----YKNAVFY 445
Cdd:cd16037 112 DRDVTEAAVDWLREEaADDKPWFLFVGFVAP------------------HF-PLIA--PQEFYDLYVRraraaYYGLVEF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 446 TDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNEtqSNSWGyDSNYstYQ--VQVPLVLAWPG-AEPAPQAQASSHLDL 522
Cdd:cd16037 171 LDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGE--RGLWG-KSTM--YEesVRVPMIISGPGiPAGKRVKTPVSLVDL 245
|
170 180
....*....|....*....|....*
gi 1430952382 523 VPTLMKnMLGVRNPyrDYSTGRNLF 547
Cdd:cd16037 246 APTILE-AAGAPPP--PDLDGRSLL 267
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
386-527 |
2.61e-06 |
|
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: 50.24 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 386 RTADRPWFslVYLS-----SPgdYQVPASIKGPFQpeltrfnpatayrpenlqKLENRYKNAVFY-----TDQLLEQMLT 455
Cdd:cd16146 169 ENKDKPFF--AYLAtnaphGP--LQVPDKYLDPYK------------------DMGLDDKLAAFYgmienIDDNVGRLLA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 456 QLQLQGLDDQTIVVVTSNHGQefneTQSNSWGYDSN-----YSTYQ--VQVPLVLAWPGAEPAPQ--AQASSHLDLVPTL 526
Cdd:cd16146 227 KLKELGLEENTIVIFMSDNGP----AGGVPKRFNAGmrgkkGSVYEggHRVPFFIRWPGKILAGKdvDTLTAHIDLLPTL 302
|
.
gi 1430952382 527 M 527
Cdd:cd16146 303 L 303
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
386-536 |
2.83e-06 |
|
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: 49.85 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 386 RTADRPWFslVYLSspgDYQVPASIKGPfqPELTRfnpatAYRpENLQKLENRYKNAVF-----YTDQLLEQMLTQLQLQ 460
Cdd:cd16144 180 QNKDKPFF--LYLS---HYAVHTPIQAR--PELIE-----KYE-KKKKGLRKGQKNPVYaamieSLDESVGRILDALEEL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 461 GLDDQTIVVVTSNHGQEFNETQSNSwgydSNY-------STYQ--VQVPLVLAWPGAEPAPQA--QASSHLDLVPTLMkN 529
Cdd:cd16144 247 GLADNTLVIFTSDNGGLSTRGGPPT----SNAplrggkgSLYEggIRVPLIVRWPGVIKPGSVsdVPVIGTDLYPTFL-E 321
|
....*..
gi 1430952382 530 MLGVRNP 536
Cdd:cd16144 322 LAGGPLP 328
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
452-526 |
1.54e-05 |
|
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: 47.56 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 452 QMLTQLQLQGLDDQTIVVVTSNHGQEFNETqsNSWGY-----DSNYSTYQ--VQVPLVLAWPGAEPAPQA--QASSHLDL 522
Cdd:cd16026 226 RILDALKELGLEENTLVIFTSDNGPWLEYG--GHGGSagplrGGKGTTWEggVRVPFIAWWPGVIPAGTVsdELASTMDL 303
|
....
gi 1430952382 523 VPTL 526
Cdd:cd16026 304 LPTL 307
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
442-526 |
2.47e-05 |
|
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: 47.18 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 442 AVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNETqsNSWGYDSNY--STyqvQVPLVLAWPGAEPAPQA--QAS 517
Cdd:cd16030 266 SVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEH--GHWGKHTLFeeAT---RVPLIIRAPGVTKPGKVtdALV 340
|
....*....
gi 1430952382 518 SHLDLVPTL 526
Cdd:cd16030 341 ELVDIYPTL 349
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
412-527 |
3.44e-05 |
|
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: 46.44 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 412 GPFQPelTRFNPATAYRPENLQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGqefNETQSNSWGYDSN 491
Cdd:cd16151 182 DPFVP--TPDSPDWDPDDKRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNG---THRPITSRTNGRE 256
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1430952382 492 YSTYQ-------VQVPLVLAWPGAepAPQAQASSHL----DLVPTLM 527
Cdd:cd16151 257 VRGGKgkttdagTHVPLIVNWPGL--IPAGGVSDDLvdfsDFLPTLA 301
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
447-527 |
5.89e-05 |
|
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: 45.62 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 447 DQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNEtqsNSWGYDSN--YSTyQVQVPLVLAWPGAePAPQA--QASSHLDL 522
Cdd:cd16147 252 DDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQ---HRLPPGKRtpYEE-DIRVPLLVRGPGI-PAGVTvdQLVSNIDL 326
|
....*
gi 1430952382 523 VPTLM 527
Cdd:cd16147 327 APTIL 331
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
429-527 |
2.87e-04 |
|
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: 43.67 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 429 PENLQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNEtqsnsWGYDSNYSTYQ--VQVPLVLAWP 506
Cdd:cd16031 229 PEKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGE-----HGLFDKRLMYEesIRVPLIIRDP 303
|
90 100
....*....|....*....|....*
gi 1430952382 507 GAEPApqAQASSHL----DLVPTLM 527
Cdd:cd16031 304 RLIKA--GTVVDALvlniDFAPTIL 326
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
359-527 |
2.94e-04 |
|
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: 43.30 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 359 GLRKQVFVSRQTDDRRLIDDWQ------QWLGTRTAD--RPWFSLVYLSSPGDYQVPASikGPfqpeltRFNpatayrpe 430
Cdd:cd16171 126 GRPTVNLVGDRSTVRVMLKDWQntdkavHWIRKEAPNltQPFALYLGLNLPHPYPSPSM--GE------NFG-------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 431 NLQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNETQSNswgYDSNYSTYQVQVPLVLAWPGAEP 510
Cdd:cd16171 190 SIRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQF---YKMSMYEGSSHVPLLIMGPGIKA 266
|
170
....*....|....*...
gi 1430952382 511 APQAQA-SSHLDLVPTLM 527
Cdd:cd16171 267 GQQVSDvVSLVDIYPTML 284
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
445-564 |
6.61e-04 |
|
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: 42.52 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 445 YTDQLLE------QMLTQLQLQGLDDQTIVVVTSNHGQEFNetqsnSWgYDSNYSTYQ----------VQVPLVLAWPGA 508
Cdd:cd16142 182 YADSMVElddhvgQILDALDELGIADNTIVIFTTDNGPEQD-----VW-PDGGYTPFRgekgttweggVRVPAIVRWPGK 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430952382 509 EPApqAQAS----SHLDLVPTLM---------KNMLGVRNPY-----RDYSTGRNlfEASTRTWLLAGDQNDFA 564
Cdd:cd16142 256 IKP--GRVSneivSHLDWFPTLAalagapdpkDKLLGKDRHIdgvdqSPFLLGKS--EKSRRSEFFYFGEGELG 325
|
|
| SLC-NCS1sbd_NRT1-like |
cd11482 |
nucleobase-cation-symport-1 (NCS1) transporter NRT1-like; solute-binding domain; This fungal ... |
16-103 |
9.66e-04 |
|
nucleobase-cation-symport-1 (NCS1) transporter NRT1-like; solute-binding domain; This fungal NCS1 subfamily includes various Saccharomyces cerevisiae transporters: nicotinamide riboside transporter 1 (Nrt1p, also called Thi71p), Dal4p (allantoin permease), Fui1p (uridine permease), Fur4p (uracil permease), and Thi7p (thiamine transporter). NCS1s are essential components of salvage pathways for nucleobases and related metabolites. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters, and solute carrier 6 family neurotransmitter transporters.
Pssm-ID: 271375 Cd Length: 480 Bit Score: 42.12 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 16 ITWGHWFSFFNIILAMLIATRYLGSISWpSTTLGVTYLIISWIGHFS----------------FLSFVTYLLTIFPLSFI 79
Cdd:cd11482 86 ASFGIYGSYFPVIIRVVLAIVWFGVQAW-TGGQCVTVMLRAIFPSFLnipntlpasagittaqLIGFFLFWLIQLPFLFI 164
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90 100
....*....|....*....|....*
gi 1430952382 80 LPRE-KPLRFISAIIATLALVLLLI 103
Cdd:cd11482 165 PPEKlRHLFTVKAVIVPIAALGLLI 189
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| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
438-528 |
1.55e-03 |
|
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: 41.50 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 438 RYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNETQSNS-----WG--YDSNYSTYQ---VQVPLVLAWPG 507
Cdd:cd16159 280 RYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGeygggNGgiYGGKKMGGWeggIRVPTIVRWPG 359
|
90 100
....*....|....*....|...
gi 1430952382 508 AEPAPQ--AQASSHLDLVPTLMK 528
Cdd:cd16159 360 VIPPGSviDEPTSLMDIFPTVAA 382
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|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
427-480 |
2.23e-03 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 40.79 E-value: 2.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430952382 427 YRPE--------NLQKLENRYKNAVFYTDQLLEQMLTQLQlqglDDQTIVVVTSNHGQEFNE 480
Cdd:PRK11560 414 YQPEcigvdsgcSKAQLINSYDNSVLYVDHFISSVIDQLR----DKKAIVFYAADHGESINE 471
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| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
413-547 |
4.01e-03 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 40.22 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 413 PFQPELTRfnpaTAYRPENLQKLENRYKNAVFYTDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNEtqSNSWGYDSNY 492
Cdd:COG2194 392 KFTPTCDT----NDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGE--NGLYLHGTPY 465
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 493 ST---YQVQVPLVLaW--PGAEPAP-------QAQAS---SHLDLVPTLMkNMLGVRNPYrdYSTGRNLF 547
Cdd:COG2194 466 AIapdEQTHVPMIM-WlsDGYAQRYgidfaclKARADkpySHDNLFHTLL-GLLDVRTSV--YDPELDIL 531
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| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
446-526 |
5.04e-03 |
|
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: 39.49 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 446 TDQLLEQMLTQLQLQGLDDQTIVVVTSNHG--QEFNETQSNSWGYDSNY-------STYQ--VQVPLVLAWPGAEPAPQ- 513
Cdd:cd16143 210 LDWVVGRILDALKELGLAENTLVIFTSDNGpsPYADYKELEKFGHDPSGplrgmkaDIYEggHRVPFIVRWPGKIPAGSv 289
|
90
....*....|....
gi 1430952382 514 -AQASSHLDLVPTL 526
Cdd:cd16143 290 sDQLVSLTDLFATL 303
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
446-558 |
9.08e-03 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 38.86 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 446 TDQLLEQMLTQLQLQGLDDQTIVVVTSNHGQEFNETqsnswgydsnYSTYQVQV----PLVLAW---------PGAEPAP 512
Cdd:pfam02995 313 LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKL----------RRTSQGMLeerlPLMSIRyppwfretyPQAVENL 382
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430952382 513 QAQA---SSHLDLVPTLM---------KNMLGVRNPYRDYSTGRNLFEA--STRTWLLAG 558
Cdd:pfam02995 383 ELNAnrlTTPFDLHATLKdilhlgelsDKELQDRMKALDCPRGISLFLPipDNRTCSDAG 442
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