|
Name |
Accession |
Description |
Interval |
E-value |
| LapC_YejM_PbgA |
NF038282 |
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ... |
1-571 |
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: 1037.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 1 MLMKRQHYREKLSQMISWGHWFVLFNIFLTLILGSRYLFVSDWPTSLLGRVYALVSWLGHFSFIVFVVYLLTLFPLTFII 80
Cdd:NF038282 1 MVTNRQRYREKVSQMISWGHWFALFNILLSLGLGSRYLFVSDWPSSLAGRIYALVSWLGHFSFIVFAAYLLILFPLTFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 81 FSQRLLRFFSVILATSGLALLIIDGETFTRFHLHITPMIWAFLINPEQTQLSRDWQYLFIVIPIIFSIEMLFSIFCWQKL 160
Cdd:NF038282 81 MSQRLLRFLSAILATAGLTLLLVDSEVFTRFHLHLNPVVWELVINPDQGEMARDWQLMFISVPVIFLVEMLFATWSWQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 161 RKFTKKIFVNLLIGLFITAFCTSHILYSWADANFYRPITMQRSNLPLSYPMTARKFLQKHGLLNQQKYEKQLIENDKLNA 240
Cdd:NF038282 161 RSLNRRRFGKPLAALFISAFFASHLMYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVQQGNPEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 241 PSIEYPLSKVTFDDKGSGYNLLLIGINGINTPYFEKAMPKTAAFAEAHLQFKNHYSSGSKEETGLLGLFYGISSTYLDSI 320
Cdd:NF038282 241 LSVEYPLSDLSFRDKGSGYNLLLIVVDGLNNSDIAKAMPALARFAEQNVQFTQHYSSGNQNDTGLFGLFYGISPSYLDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 321 FFTRKPSVLIRSLEAQGYQFGLFSSDGFKNPLYRQALFTDFSLPSPMLQSNRKTTEEWYEWFSKKLNTRPWFSYIHFNTA 400
Cdd:NF038282 321 LSSRKPSALITALNQQGYQFGLFSSDGFKSPLYRQALLSDFSLPPPQSQSDAQTTSQWQQWLNGQKNTNPWFSYLNLNGT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 401 STALEPDETRIK-------NIDQQISEMIDVLKKDPQFTKTVIIITGAYAAAENQNK------RIPSKVPLIVYWPKIST 467
Cdd:NF038282 401 STASDDGKQKQRryqrgaaDVDQQINTVLDTLKERGLLDNTVVVITASHGVALDDNDdnfkfnRAQLQVPLVIHWPGTPA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 468 QIIHKLTSHQDIMATIMQKLLHTKTAVKEYSQGENLFTPERLYPWILTKKNKELLVVTPRKTIALDDNGSYHTYDQNGIL 547
Cdd:NF038282 481 QTINKLTDHQDVMTTLMQRLLHVSTAAADYSQGEDLFAAQRRHNWVATGDDGTLVITTPTQTLVLDNNGSYRAYDLNGRE 560
|
570 580
....*....|....*....|....
gi 506354691 548 IQNDTSELSLLLQVLTETKRFIAD 571
Cdd:NF038282 561 IKDQKPQLALLLQVLTEEKRFIAN 584
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
15-570 |
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: 712.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 15 MISWGHWFVLFNIFLTLILGSRYLFVSDWPTSLLGRVYALVSWLGHFSFIVFVVYLLTLFPLTFIIFSQRLLRFFSVILA 94
Cdd:COG3083 1 LISWGHWFALFNILLALLIGSRYLFIADWPGTLLGRLYLLVSWLGHFSFLVFALYLLLLFPLSFLVPSQRLFRGLSVILA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 95 TSGLALLIIDGETFTRFHLHITPMIWAFLINPEQTQLSRDWQYLFIVIPIIFSIEMLFSIFCWQKLRKFTKKIFVNLLIG 174
Cdd:COG3083 81 TAGLTLLLVDTEVFQRFHLHLNPLVWDLLFNPDQGELARDWQLLFIPVPLIFLLEMLLATWSWRKLRSLERRRFGKPVAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 175 LFITAFCTSHILYSWADANFYRPITMQRSNLPLSYPMTARKFLQKHGLLNQQKYEKQLIENDKLNAPSIEYPLSKVTFDD 254
Cdd:COG3083 161 LFLVSFLASHLIYIWADANFYRPITMQRANLPLSYPMTARSFLEKHGLLDAQEYQQRLEEQGNPEASSLNYPLHPLQFSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 255 KGSGYNLLLIGINGINTPYF-EKAMPKTAAFAEAHLQFKNHYSSGSKEETGLLGLFYGISSTYLDSIFFTRKPSVLIRSL 333
Cdd:COG3083 241 PAKPPNILLIVVDSLRADMLdPEVMPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLFYGLPGNYWDSILAERTPPVLIDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 334 EAQGYQFGLFSSDGFKNPLYRQALFTDFSLPSP-----MLQSNRKTTEEWYEWFSKKLNTRPWFSYIHFNTASTALEPDE 408
Cdd:COG3083 321 QQQGYQFGLFSSAGFNSPLFRQTIFSDVSLPRLhtpggPAQRDRQITAQWLQWLDQRDSDRPWFSYLFLDAPHAYSFPAD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 409 TRIK------------------------------NIDQQISEMIDVLKKDPQFTKTVIIITGAYAAAENQNK-------- 450
Cdd:COG3083 401 YPKPfqpsedcnylaldnesdptpfknryrnavhYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGqnywghns 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 451 ---RIPSKVPLIVYWPKISTQIIHKLTSHQDIMATIMQKLLHTKTAVKEYSQGENLFTPERLYPWILTKKNKELLVVTPR 527
Cdd:COG3083 481 nfsRYQLQVPLVIHWPGTPPQVISKLTSHLDIVPTLMQRLLGVQNPASDYSQGEDLFDPQRRRDWVLAGDYRNLAIITPD 560
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 506354691 528 KTIALDDNGSYHTYDQNGILIQNDTSELSLLLQVLTETKRFIA 570
Cdd:COG3083 561 RITVLDPSGNYQVYDRDYRPLKDAKPPLGLLLQVLTELKRFYA 603
|
|
| DUF3413 |
pfam11893 |
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. ... |
7-252 |
2.60e-119 |
|
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: 352.71 E-value: 2.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 7 HYREKLSQMISWGHWFVLFNIFLTLILGSRYLFVSDWPTSLLGRVYALVSWLGHFSFIVFVVYLLTLFPLTFIIFSQRLL 86
Cdd:pfam11893 1 QYRDKVSQLISWGHWFALFNIILALLIGLRYLFSADWPSTLLGWLYLLVSWLGHFSFLAFALYLLVLFPLTFLIPYSRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 87 RFFSVILATSGLALLIIDGETFTRFHLHITPMIWAFLINPEQTQLSRDWQYLFIVIPIIFSIEMLFSIFCWQKLRKFTKK 166
Cdd:pfam11893 81 RGLAAIIATAGLTLLLVDTEVFDQYGFHLNPVVWDLLLNGDQSELSRSWQLLFIVIPVILLLELLLANWVWKKLRKLQRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 167 IFVNLLIGLFITAFCTSHILYSWADANFYRPITMQRSNLPLSYPMTARKFLQKHGLLNQQKYEKQLIENDKLNAPSIEYP 246
Cdd:pfam11893 161 KIGKPVAAFLLLCFLASHLIHIWADANLYRPITMQRANFPLSYPMTAKSFLEKHGLLDLESYQQRLAEQGNPPAQPLNYP 240
|
....*.
gi 506354691 247 LSKVTF 252
Cdd:pfam11893 241 LHPLQC 246
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
278-504 |
1.04e-27 |
|
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: 112.26 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 278 MPKTAAFAEAHLQFKNHYSSGSKEETGLLGLFYGISSTYLDSIFF--TRKPSVLIRSLEAQGYQFGLFSSDG--FKNPLY 353
Cdd:cd16148 26 TPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGplEPDDPTLAEILRKAGYYTAAVSSNPhlFGGPGF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 354 RQALFTDF-------SLPSPMLQSNRKTTEEWYEWFSKKLNTRPWFSYIHFNTAStalEPDETR--IKNIDQQISEMIDV 424
Cdd:cd16148 106 DRGFDTFEdfrgqegDPGEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPH---EPYLYDaeVRYVDEQIGRLLDK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 425 LKKDPQFTKTVIIITG---------------AYAAAENQnkripSKVPLIVYWPKISTQI-IHKLTSHQDIMATIMQKLL 488
Cdd:cd16148 183 LKELGLLEDTLVIVTSdhgeefgehglywghGSNLYDEQ-----LHVPLIIRWPGKEPGKrVDALVSHIDIAPTLLDLLG 257
|
250
....*....|....*.
gi 506354691 489 htkTAVKEYSQGENLF 504
Cdd:cd16148 258 ---VEPPDYSDGRSLL 270
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LapC_YejM_PbgA |
NF038282 |
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ... |
1-571 |
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: 1037.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 1 MLMKRQHYREKLSQMISWGHWFVLFNIFLTLILGSRYLFVSDWPTSLLGRVYALVSWLGHFSFIVFVVYLLTLFPLTFII 80
Cdd:NF038282 1 MVTNRQRYREKVSQMISWGHWFALFNILLSLGLGSRYLFVSDWPSSLAGRIYALVSWLGHFSFIVFAAYLLILFPLTFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 81 FSQRLLRFFSVILATSGLALLIIDGETFTRFHLHITPMIWAFLINPEQTQLSRDWQYLFIVIPIIFSIEMLFSIFCWQKL 160
Cdd:NF038282 81 MSQRLLRFLSAILATAGLTLLLVDSEVFTRFHLHLNPVVWELVINPDQGEMARDWQLMFISVPVIFLVEMLFATWSWQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 161 RKFTKKIFVNLLIGLFITAFCTSHILYSWADANFYRPITMQRSNLPLSYPMTARKFLQKHGLLNQQKYEKQLIENDKLNA 240
Cdd:NF038282 161 RSLNRRRFGKPLAALFISAFFASHLMYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVQQGNPEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 241 PSIEYPLSKVTFDDKGSGYNLLLIGINGINTPYFEKAMPKTAAFAEAHLQFKNHYSSGSKEETGLLGLFYGISSTYLDSI 320
Cdd:NF038282 241 LSVEYPLSDLSFRDKGSGYNLLLIVVDGLNNSDIAKAMPALARFAEQNVQFTQHYSSGNQNDTGLFGLFYGISPSYLDGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 321 FFTRKPSVLIRSLEAQGYQFGLFSSDGFKNPLYRQALFTDFSLPSPMLQSNRKTTEEWYEWFSKKLNTRPWFSYIHFNTA 400
Cdd:NF038282 321 LSSRKPSALITALNQQGYQFGLFSSDGFKSPLYRQALLSDFSLPPPQSQSDAQTTSQWQQWLNGQKNTNPWFSYLNLNGT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 401 STALEPDETRIK-------NIDQQISEMIDVLKKDPQFTKTVIIITGAYAAAENQNK------RIPSKVPLIVYWPKIST 467
Cdd:NF038282 401 STASDDGKQKQRryqrgaaDVDQQINTVLDTLKERGLLDNTVVVITASHGVALDDNDdnfkfnRAQLQVPLVIHWPGTPA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 468 QIIHKLTSHQDIMATIMQKLLHTKTAVKEYSQGENLFTPERLYPWILTKKNKELLVVTPRKTIALDDNGSYHTYDQNGIL 547
Cdd:NF038282 481 QTINKLTDHQDVMTTLMQRLLHVSTAAADYSQGEDLFAAQRRHNWVATGDDGTLVITTPTQTLVLDNNGSYRAYDLNGRE 560
|
570 580
....*....|....*....|....
gi 506354691 548 IQNDTSELSLLLQVLTETKRFIAD 571
Cdd:NF038282 561 IKDQKPQLALLLQVLTEEKRFIAN 584
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
15-570 |
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: 712.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 15 MISWGHWFVLFNIFLTLILGSRYLFVSDWPTSLLGRVYALVSWLGHFSFIVFVVYLLTLFPLTFIIFSQRLLRFFSVILA 94
Cdd:COG3083 1 LISWGHWFALFNILLALLIGSRYLFIADWPGTLLGRLYLLVSWLGHFSFLVFALYLLLLFPLSFLVPSQRLFRGLSVILA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 95 TSGLALLIIDGETFTRFHLHITPMIWAFLINPEQTQLSRDWQYLFIVIPIIFSIEMLFSIFCWQKLRKFTKKIFVNLLIG 174
Cdd:COG3083 81 TAGLTLLLVDTEVFQRFHLHLNPLVWDLLFNPDQGELARDWQLLFIPVPLIFLLEMLLATWSWRKLRSLERRRFGKPVAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 175 LFITAFCTSHILYSWADANFYRPITMQRSNLPLSYPMTARKFLQKHGLLNQQKYEKQLIENDKLNAPSIEYPLSKVTFDD 254
Cdd:COG3083 161 LFLVSFLASHLIYIWADANFYRPITMQRANLPLSYPMTARSFLEKHGLLDAQEYQQRLEEQGNPEASSLNYPLHPLQFSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 255 KGSGYNLLLIGINGINTPYF-EKAMPKTAAFAEAHLQFKNHYSSGSKEETGLLGLFYGISSTYLDSIFFTRKPSVLIRSL 333
Cdd:COG3083 241 PAKPPNILLIVVDSLRADMLdPEVMPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLFYGLPGNYWDSILAERTPPVLIDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 334 EAQGYQFGLFSSDGFKNPLYRQALFTDFSLPSP-----MLQSNRKTTEEWYEWFSKKLNTRPWFSYIHFNTASTALEPDE 408
Cdd:COG3083 321 QQQGYQFGLFSSAGFNSPLFRQTIFSDVSLPRLhtpggPAQRDRQITAQWLQWLDQRDSDRPWFSYLFLDAPHAYSFPAD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 409 TRIK------------------------------NIDQQISEMIDVLKKDPQFTKTVIIITGAYAAAENQNK-------- 450
Cdd:COG3083 401 YPKPfqpsedcnylaldnesdptpfknryrnavhYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGqnywghns 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 451 ---RIPSKVPLIVYWPKISTQIIHKLTSHQDIMATIMQKLLHTKTAVKEYSQGENLFTPERLYPWILTKKNKELLVVTPR 527
Cdd:COG3083 481 nfsRYQLQVPLVIHWPGTPPQVISKLTSHLDIVPTLMQRLLGVQNPASDYSQGEDLFDPQRRRDWVLAGDYRNLAIITPD 560
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 506354691 528 KTIALDDNGSYHTYDQNGILIQNDTSELSLLLQVLTETKRFIA 570
Cdd:COG3083 561 RITVLDPSGNYQVYDRDYRPLKDAKPPLGLLLQVLTELKRFYA 603
|
|
| DUF3413 |
pfam11893 |
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. ... |
7-252 |
2.60e-119 |
|
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: 352.71 E-value: 2.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 7 HYREKLSQMISWGHWFVLFNIFLTLILGSRYLFVSDWPTSLLGRVYALVSWLGHFSFIVFVVYLLTLFPLTFIIFSQRLL 86
Cdd:pfam11893 1 QYRDKVSQLISWGHWFALFNIILALLIGLRYLFSADWPSTLLGWLYLLVSWLGHFSFLAFALYLLVLFPLTFLIPYSRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 87 RFFSVILATSGLALLIIDGETFTRFHLHITPMIWAFLINPEQTQLSRDWQYLFIVIPIIFSIEMLFSIFCWQKLRKFTKK 166
Cdd:pfam11893 81 RGLAAIIATAGLTLLLVDTEVFDQYGFHLNPVVWDLLLNGDQSELSRSWQLLFIVIPVILLLELLLANWVWKKLRKLQRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 167 IFVNLLIGLFITAFCTSHILYSWADANFYRPITMQRSNLPLSYPMTARKFLQKHGLLNQQKYEKQLIENDKLNAPSIEYP 246
Cdd:pfam11893 161 KIGKPVAAFLLLCFLASHLIHIWADANLYRPITMQRANFPLSYPMTAKSFLEKHGLLDLESYQQRLAEQGNPPAQPLNYP 240
|
....*.
gi 506354691 247 LSKVTF 252
Cdd:pfam11893 241 LHPLQC 246
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
278-504 |
1.04e-27 |
|
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: 112.26 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 278 MPKTAAFAEAHLQFKNHYSSGSKEETGLLGLFYGISSTYLDSIFF--TRKPSVLIRSLEAQGYQFGLFSSDG--FKNPLY 353
Cdd:cd16148 26 TPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGplEPDDPTLAEILRKAGYYTAAVSSNPhlFGGPGF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 354 RQALFTDF-------SLPSPMLQSNRKTTEEWYEWFSKKLNTRPWFSYIHFNTAStalEPDETR--IKNIDQQISEMIDV 424
Cdd:cd16148 106 DRGFDTFEdfrgqegDPGEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPH---EPYLYDaeVRYVDEQIGRLLDK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 425 LKKDPQFTKTVIIITG---------------AYAAAENQnkripSKVPLIVYWPKISTQI-IHKLTSHQDIMATIMQKLL 488
Cdd:cd16148 183 LKELGLLEDTLVIVTSdhgeefgehglywghGSNLYDEQ-----LHVPLIIRWPGKEPGKrVDALVSHIDIAPTLLDLLG 257
|
250
....*....|....*.
gi 506354691 489 htkTAVKEYSQGENLF 504
Cdd:cd16148 258 ---VEPPDYSDGRSLL 270
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
21-508 |
9.63e-21 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 95.88 E-value: 9.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 21 WFVLFNIFLTLILgsrYLFVSDWPTSLLGRVYALVSWLGHFSFIVFVVYLLTLFPLTFIIFSQRLLRFFSVILATSGLAL 100
Cdd:COG1368 1 FFLLFLLLLSLRL---VFLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 101 LIIDGETFTRFHLHITPMIWAFLINP-EQTQLSRDWQYLFIVIPIIFSIEMLFSIFCWQKLRKFTKKIFVNLLIGLFITA 179
Cdd:COG1368 78 LVADILYYRFFGDRLNFSDLDYLGDTgEVLGSLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 180 FCTSHILYSWAdanfyRPITMQRS------------NLPLSYPMTARKFLQKHGLLNQQKYEKQLIENDKLNAPSIeypl 247
Cdd:COG1368 158 LLLLGIRLGED-----RPLNLSDAfsrnnfvnelglNGPYSFYDALRNNKAPATYSEEEALEIKKYLKSNRPTPNP---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 248 skvtfDDKGSGYNLLLI------------GINGIN-TPYFEKAMPKTaafaeahLQFKNHYSSGSKEETGLLGLFYGISS 314
Cdd:COG1368 229 -----FGPAKKPNVVVIllesfsdffigaLGNGKDvTPFLDSLAKES-------LYFGNFYSQGGRTSRGEFAVLTGLPP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 315 TYLDSIFFT---RKPSVLIRSLEAQGYQ--F---GLFSSDGFKNpLYRQALFTDF----SLPSPMlqsnrktTEEW---- 378
Cdd:COG1368 297 LPGGSPYKRpgqNNFPSLPSILKKQGYEtsFfhgGDGSFWNRDS-FYKNLGFDEFydreDFDDPF-------DGGWgvsd 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 379 ---YEWFSKKLNT--RPWFSYI-----HF------------NTASTALEPDETRIKNIDQQISEMIDVLKKDPQFTKTVI 436
Cdd:COG1368 369 edlFDKALEELEKlkKPFFAFLitlsnHGpytlpeedkkipDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIF 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506354691 437 IITG-----AYAAAENQNKRIPSKVPLIVYWPKIST-QIIHKLTSHQDIMATIMqKLLHTKTAvKEYSQGENLFTPER 508
Cdd:COG1368 449 VIYGdhgprSPGKTDYENPLERYRVPLLIYSPGLKKpKVIDTVGSQIDIAPTLL-DLLGIDYP-SYYAFGRDLLSPDT 524
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
278-485 |
5.85e-13 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 69.76 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 278 MPKTAAFAEAHLQFKNHYSSGSKEETGLLGLFYGISSTYLDSIFFT-----RKPSVLIRSLEAQGYQFGL---------- 342
Cdd:pfam00884 26 TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTpvglpRTEPSLPDLLKRAGYNTGAigkwhlgwyn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 343 ---FSSDGFKNPLYRQALFTDFSLP-------SPMLQSNRKTTEEWYEWfsKKLNTRPWFSYIHFN------------TA 400
Cdd:pfam00884 106 nqsPCNLGFDKFFGRNTGSDLYADPpdvpyncSGGGVSDEALLDEALEF--LDNNDKPFFLVLHTLgshgppyypdryPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 401 STALEPDETR------------IKNIDQQISEMIDVLKKDPQFTKTVIIITG--AYAAAENQNKRIPSK----------V 456
Cdd:pfam00884 184 KYATFKPSSCseeqllnsydntLLYTDDAIGRVLDKLEENGLLDNTLVVYTSdhGESLGEGGGYLHGGKydnapeggyrV 263
|
250 260 270
....*....|....*....|....*....|.
gi 506354691 457 PLIVYWPKI--STQIIHKLTSHQDIMATIMQ 485
Cdd:pfam00884 264 PLLIWSPGGkaKGQKSEALVSHVDLFPTILD 294
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
262-487 |
1.13e-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: 59.62 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 262 LLIGINGIN-TPYFEKAMPKTaafaeahLQFKNHYSSGSKEET--GLLGLFYGISSTYLDSIFFTRKPSVLIRS----LE 334
Cdd:cd16015 16 IDKDVGGEDlTPNLNKLAKEG-------LYFGNFYSPGFGGGTanGEFEVLTGLPPLPLGSGSYTLYKLNPLPSlpsiLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 335 AQGYQ----------F----GLFSSDGFKNPLYRQALFTDFSLPSPMLQSNRKTTEEWYEWFsKKLNTRPWFSYI----- 395
Cdd:cd16015 89 EQGYEtifihggdasFynrdSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEEL-EELKKKPFFIFLvtmsn 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 396 HF---------------NTASTALEPDETRIKNIDQQISEMIDVLKKDPQFTKTVIIITG----------AYAAAENQNK 450
Cdd:cd16015 168 HGpydlpeekkdeplkvEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGdhlpslgsdyDETDEDPLDL 247
|
250 260 270
....*....|....*....|....*....|....*...
gi 506354691 451 RipsKVPLIVYWPKIST-QIIHKLTSHQDIMATIMQKL 487
Cdd:cd16015 248 Y---RTPLLIYSPGLKKpKKIDRVGSQIDIAPTLLDLL 282
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
380-483 |
3.48e-09 |
|
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: 57.45 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 380 EWFSKKLNTRPWFSYIHFNT--------AStalepdetrIKNIDQQISEMIDVLKKDPQFTKTVIIIT---GAY--AAAE 446
Cdd:cd16022 107 DFIERRDKDKPFFLYVSFNAphppfayyAM---------VSAIDDQIGRILDALEELGLLDNTLIVFTsdhGDMlgDHGL 177
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 506354691 447 NQNKRIP----SKVPLIVYWPKI--STQIIHKLTSHQDIMATI 483
Cdd:cd16022 178 RGKKGSLyeggIRVPFIVRWPGKipAGQVSDALVSLLDLLPTL 220
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
333-484 |
1.29e-07 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 54.11 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 333 LEAQGYQFGLFssdGfKNPLYRQALFTDFSLpspmlqsnrktteewyEWFSKKLNT-RPWFSYIHF-------------- 397
Cdd:COG3119 112 LKEAGYRTALF---G-KWHLYLTDLLTDKAI----------------DFLERQADKdKPFFLYLAFnaphapyqapeeyl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 398 ------------NTASTALEPDETR---------IKNIDQQISEMIDVLKKDPQFTKTVIIIT---GAYAAAENQN--KR 451
Cdd:COG3119 172 dkydgkdiplppNLAPRDLTEEELRraraayaamIEEVDDQVGRLLDALEELGLADNTIVVFTsdnGPSLGEHGLRggKG 251
|
170 180 190
....*....|....*....|....*....|....*....
gi 506354691 452 IP----SKVPLIVYWPKIST--QIIHKLTSHQDIMATIM 484
Cdd:COG3119 252 TLyeggIRVPLIVRWPGKIKagSVSDALVSLIDLLPTLL 290
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
364-487 |
7.75e-07 |
|
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: 51.88 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 364 PSPMLQSNRKTTEE-------WYEWFSKKLNTRPWFSYIHFNTASTALEPDETR------IKNIDQQISEMIDVLKKDPQ 430
Cdd:cd16028 184 PADVPPPIRAESLAaeaaqhpLLAAFLERIESLSFSPGAANAADLDDEEVAQMRatylglIAEVDDHLGRLFDYLKETGQ 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506354691 431 FTKTVIIIT----------------GAYAAAenqnkripSKVPLIVYWPK-----ISTQIIHKLTSHQDIMATIMQKL 487
Cdd:cd16028 264 WDDTLIVFTsdhgeqlgdhwlwgkdGFFDQA--------YRVPLIVRDPRreadaTRGQVVDAFTESVDVMPTILDWL 333
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
411-542 |
9.17e-07 |
|
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: 51.42 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 411 IKNIDQQISEMIDVLKKDPQFTKTVIIIT-------GAYaaaENQNKRIP----SKVPLIVYWP-KIST-QIIHKLTSHQ 477
Cdd:cd16034 233 ITALDDNIGRLLDALKELGLLENTIVVFTsdhgdmlGSH---GLMNKQVPyeesIRVPFIIRYPgKIKAgRVVDLLINTV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 478 DIMATIM-----------------QKLLHTKTAVKEYSQgenLFTPERLYPWILTKKNKELLVVTPRKTIALDDNGSYHT 540
Cdd:cd16034 310 DIMPTLLglcglpipdtvegrdlsPLLLGGKDDEPDSVL---LQCFVPFGGGSARDGGEWRGVRTDRYTYVRDKNGPWLL 386
|
..
gi 506354691 541 YD 542
Cdd:cd16034 387 FD 388
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
414-485 |
1.23e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 47.99 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 414 IDQQISEMIDVLKKDPQFTKTVIIIT---GAYAAAENQ-NKRIP-----SKVPLIVYWPKIS--TQIIHKLTSHQDIMAT 482
Cdd:cd16033 226 IDDAIGRILDALEELGLADDTLVIFTsdhGDALGAHRLwDKGPFmyeetYRIPLIIKWPGVIaaGQVVDEFVSLLDLAPT 305
|
...
gi 506354691 483 IMQ 485
Cdd:cd16033 306 ILD 308
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
411-484 |
1.67e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 46.82 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 411 IKNIDQQISEMIDVLKKDPQFTKTVIIIT-------GA-------YAAAENQNkripsKVPLIVYWPKIST--QIIHKLT 474
Cdd:cd16035 173 IRDVDRQIGRVLDALDASGLADNTIVVFTsdhgemgGAhglrgkgFNAYEEAL-----HVPLIISHPDLFGtgQTTDALT 247
|
90
....*....|
gi 506354691 475 SHQDIMATIM 484
Cdd:cd16035 248 SHIDLLPTLL 257
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
380-483 |
2.70e-05 |
|
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: 45.87 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 380 EWFSKKlntRPWFSYIHFNTASTAL-----EPDETR--IKNIDQQISEMIDVLKKDPQFTKTVIIITGAYAAAENQNKRI 452
Cdd:cd00016 113 DETSKE---KPFVLFLHFDGPDGPGhaygpNTPEYYdaVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGD 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 506354691 453 PSK------------VPLIVYWPKISTQ-IIHKLTSHQDIMATI 483
Cdd:cd00016 190 PKAdgkadkshtgmrVPFIAYGPGVKKGgVKHELISQYDIAPTL 233
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
387-485 |
3.40e-04 |
|
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: 43.20 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 387 NTRPWFSyihfntastaLEPDETR------------IKNIDQQISEMIDVLKKDPQFTKTVIIIT---GA-----YAAAE 446
Cdd:cd16025 199 GVPAWDS----------LSPEEKKlearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLsdnGAsaepgWANAS 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 506354691 447 N----QNKRIPS----KVPLIVYWPK-------ISTQIIHkLTshqDIMATIMQ 485
Cdd:cd16025 269 NtpfrLYKQASHeggiRTPLIVSWPKgikakggIRHQFAH-VI---DIAPTILE 318
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
411-483 |
2.34e-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: 40.65 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 411 IKNIDQQISEMIDVLKKDPQFTKTVIIIT----GAYAAAENQNKRI---PS---------------KVPLIVYWPK--IS 466
Cdd:cd16143 207 VYELDWVVGRILDALKELGLAENTLVIFTsdngPSPYADYKELEKFghdPSgplrgmkadiyegghRVPFIVRWPGkiPA 286
|
90
....*....|....*..
gi 506354691 467 TQIIHKLTSHQDIMATI 483
Cdd:cd16143 287 GSVSDQLVSLTDLFATL 303
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
414-504 |
7.71e-03 |
|
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: 38.68 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506354691 414 IDQQISEMIDVLKKDPQFTKTVIIIT-------GAYAAAENQNKRIPS-KVPLIVYWPKIST-QIIHKLTSHQDIMATIM 484
Cdd:cd16037 171 LDENIGRVLDALEELGLLDNTLIIYTsdhgdmlGERGLWGKSTMYEESvRVPMIISGPGIPAgKRVKTPVSLVDLAPTIL 250
|
90 100
....*....|....*....|
gi 506354691 485 QkllHTKTAVKEYSQGENLF 504
Cdd:cd16037 251 E---AAGAPPPPDLDGRSLL 267
|
|
| |
