NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1059271419|pdb|5I5F|A]
View 

Chain A, Inner membrane protein YejM

Protein Classification

DUF3413 domain-containing protein( domain architecture ID 17609232)

DUF3413 domain-containing protein with an alkaline phosphatase/sulfatase domain, similar to Salmonella enterica membrane-anchored periplasmic protein YejM

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
LapC_YejM_PbgA NF038282
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ...
1-586 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: 1189.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A         1 MVTHRQRYREKVSQMVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIV 80
Cdd:NF038282   1 MVTNRQRYREKVSQMISWGHWFALFNILLSLGLGSRYLFVSDWPSSLAGRIYALVSWLGHFSFIVFAAYLLILFPLTFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        81 MSQRLMRFLSAILATAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKL 160
Cdd:NF038282  81 MSQRLLRFLSAILATAGLTLLLVDSEVFTRFHLHLNPVVWELVINPDQGEMARDWQLMFISVPVIFLVEMLFATWSWQKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       161 RSLTRRRhFARPLAAFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPE 240
Cdd:NF038282 161 RSLNRRR-FGKPLAALFISAFFASHLMYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVQQGNPE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       241 AVSVQYPLSNLHYRDMGTGQNVLLITVDGLNYSRFEKQMPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDG 320
Cdd:NF038282 240 ALSVEYPLSDLSFRDKGSGYNLLLIVVDGLNNSDIAKAMPALARFAEQNVQFTQHYSSGNQNDTGLFGLFYGISPSYLDG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       321 VLSTRTPAALITALNQQGYQLGLFSSDGFASPLYRQALLSDFSMPAAQTQSDAQTASQWIDWLGRYAQEdNRWFSWISFN 400
Cdd:NF038282 320 ILSSRKPSALITALNQQGYQFGLFSSDGFKSPLYRQALLSDFSLPPPQSQSDAQTTSQWQQWLNGQKNT-NPWFSYLNLN 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       401 GTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLTPEENRFDWSQGHLQVPLVIHWPGT 480
Cdd:NF038282 399 GTSTASDDGKQKQRRYQRGAADVDQQINTVLDTLKERGLLDNTVVVITASHGVALDDNDDNFKFNRAQLQVPLVIHWPGT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       481 PAQRINVLTDHTDVMTTLMQRLLHVSTPANEYSQGQDIFTVPRRHNWVTAADGSTLAITTPQMTLVLNNNGHYQTYDLHG 560
Cdd:NF038282 479 PAQTINKLTDHQDVMTTLMQRLLHVSTAAADYSQGEDLFAAQRRHNWVATGDDGTLVITTPTQTLVLDNNGSYRAYDLNG 558
                        570       580
                 ....*....|....*....|....*.
5I5F_A       561 EKIKDQKPQLSLLLQVLTEEKRFIAN 586
Cdd:NF038282 559 REIKDQKPQLALLLQVLTEEKRFIAN 584
 
Name Accession Description Interval E-value
LapC_YejM_PbgA NF038282
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ...
1-586 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: 1189.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A         1 MVTHRQRYREKVSQMVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIV 80
Cdd:NF038282   1 MVTNRQRYREKVSQMISWGHWFALFNILLSLGLGSRYLFVSDWPSSLAGRIYALVSWLGHFSFIVFAAYLLILFPLTFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        81 MSQRLMRFLSAILATAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKL 160
Cdd:NF038282  81 MSQRLLRFLSAILATAGLTLLLVDSEVFTRFHLHLNPVVWELVINPDQGEMARDWQLMFISVPVIFLVEMLFATWSWQKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       161 RSLTRRRhFARPLAAFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPE 240
Cdd:NF038282 161 RSLNRRR-FGKPLAALFISAFFASHLMYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVQQGNPE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       241 AVSVQYPLSNLHYRDMGTGQNVLLITVDGLNYSRFEKQMPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDG 320
Cdd:NF038282 240 ALSVEYPLSDLSFRDKGSGYNLLLIVVDGLNNSDIAKAMPALARFAEQNVQFTQHYSSGNQNDTGLFGLFYGISPSYLDG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       321 VLSTRTPAALITALNQQGYQLGLFSSDGFASPLYRQALLSDFSMPAAQTQSDAQTASQWIDWLGRYAQEdNRWFSWISFN 400
Cdd:NF038282 320 ILSSRKPSALITALNQQGYQFGLFSSDGFKSPLYRQALLSDFSLPPPQSQSDAQTTSQWQQWLNGQKNT-NPWFSYLNLN 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       401 GTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLTPEENRFDWSQGHLQVPLVIHWPGT 480
Cdd:NF038282 399 GTSTASDDGKQKQRRYQRGAADVDQQINTVLDTLKERGLLDNTVVVITASHGVALDDNDDNFKFNRAQLQVPLVIHWPGT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       481 PAQRINVLTDHTDVMTTLMQRLLHVSTPANEYSQGQDIFTVPRRHNWVTAADGSTLAITTPQMTLVLNNNGHYQTYDLHG 560
Cdd:NF038282 479 PAQTINKLTDHQDVMTTLMQRLLHVSTAAADYSQGEDLFAAQRRHNWVATGDDGTLVITTPTQTLVLDNNGSYRAYDLNG 558
                        570       580
                 ....*....|....*....|....*.
5I5F_A       561 EKIKDQKPQLSLLLQVLTEEKRFIAN 586
Cdd:NF038282 559 REIKDQKPQLALLLQVLTEEKRFIAN 584
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
15-585 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: 883.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       15 MVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIVMSQRLMRFLSAILA 94
Cdd:COG3083   1 LISWGHWFALFNILLALLIGSRYLFIADWPGTLLGRLYLLVSWLGHFSFLVFALYLLLLFPLSFLVPSQRLFRGLSVILA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       95 TAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKLRSLtRRRHFARPLA 174
Cdd:COG3083  81 TAGLTLLLVDTEVFQRFHLHLNPLVWDLLFNPDQGELARDWQLLFIPVPLIFLLEMLLATWSWRKLRSL-ERRRFGKPVA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      175 AFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPEAVSVQYPLSNLHYR 254
Cdd:COG3083 160 ALFLVSFLASHLIYIWADANFYRPITMQRANLPLSYPMTARSFLEKHGLLDAQEYQQRLEEQGNPEASSLNYPLHPLQFS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      255 DMGTGQNVLLITVDGLNYSRFEKQ-MPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDGVLSTRTPAALITA 333
Cdd:COG3083 240 DPAKPPNILLIVVDSLRADMLDPEvMPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLFYGLPGNYWDSILAERTPPVLIDA 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      334 LNQQGYQLGLFSSDGFASPLYRQALLSDFSMPAAQT-----QSDAQTASQWIDWLGRYaQEDNRWFSWISFNGTN----- 403
Cdd:COG3083 320 LQQQGYQFGLFSSAGFNSPLFRQTIFSDVSLPRLHTpggpaQRDRQITAQWLQWLDQR-DSDRPWFSYLFLDAPHaysfp 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      404 ------------------IDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLTPEENRF--- 462
Cdd:COG3083 399 adypkpfqpsedcnylalDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYwgh 478
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      463 --DWSQGHLQVPLVIHWPGTPAQRINVLTDHTDVMTTLMQRLLHVSTPANEYSQGQDIFTVPRRHNWVTAADGSTLAITT 540
Cdd:COG3083 479 nsNFSRYQLQVPLVIHWPGTPPQVISKLTSHLDIVPTLMQRLLGVQNPASDYSQGEDLFDPQRRRDWVLAGDYRNLAIIT 558
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*
5I5F_A      541 PQMTLVLNNNGHYQTYDLHGEKIKDQKPQLSLLLQVLTEEKRFIA 585
Cdd:COG3083 559 PDRITVLDPSGNYQVYDRDYRPLKDAKPPLGLLLQVLTELKRFYA 603
DUF3413 pfam11893
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. ...
7-253 9.09e-133

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: 387.37  E-value: 9.09e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A          7 RYREKVSQMVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIVMSQRLM 86
Cdd:pfam11893   1 QYRDKVSQLISWGHWFALFNIILALLIGLRYLFSADWPSTLLGWLYLLVSWLGHFSFLAFALYLLVLFPLTFLIPYSRLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A         87 RFLSAILATAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKLRSLtRR 166
Cdd:pfam11893  81 RGLAAIIATAGLTLLLVDTEVFDQYGFHLNPVVWDLLLNGDQSELSRSWQLLFIVIPVILLLELLLANWVWKKLRKL-QR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        167 RHFARPLAAFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPEAVSVQY 246
Cdd:pfam11893 160 KKIGKPVAAFLLLCFLASHLIHIWADANLYRPITMQRANFPLSYPMTAKSFLEKHGLLDLESYQQRLAEQGNPPAQPLNY 239

                  ....*..
5I5F_A        247 PLSNLHY 253
Cdd:pfam11893 240 PLHPLQC 246
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
261-519 7.71e-44

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: 157.32  E-value: 7.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      261 NVLLITVDGLNYSRF------EKQMPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGY--MDGVLSTRTPAALIT 332
Cdd:cd16148   2 NVILIVIDSLRADHLgcygydRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYhgVWGGPLEPDDPTLAE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      333 ALNQQGYQLGLFSSDGFASPL---------YRQALLSDFSMPAAQTQSDAQTASQWIDWLGRYAQEDNrWFSWISFngtn 403
Cdd:cd16148  82 ILRKAGYYTAAVSSNPHLFGGpgfdrgfdtFEDFRGQEGDPGEEGDERAERVTDRALEWLDRNADDDP-FFLFLHY---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      404 idDSNQKNFvkRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGipltpEE---------NRFDWSQGHLQVPLV 474
Cdd:cd16148 157 --FDPHEPY--LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG-----EEfgehglywgHGSNLYDEQLHVPLI 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
5I5F_A      475 IHWPG-TPAQRINVLTDHTDVMTTLMQRLLhvsTPANEYSQGQDIF 519
Cdd:cd16148 228 IRWPGkEPGKRVDALVSHIDIAPTLLDLLG---VEPPDYSDGRSLL 270
PRK13759 PRK13759
arylsulfatase; Provisional
381-558 9.19e-06

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 48.51  E-value: 9.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       381 DWlgRYAQE-DNRWFSWISFNGtNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGiPLTPEE 459
Cdd:PRK13759 237 DW--EYAEDqDPEGGSIDALRG-NLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG-DMLGDH 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       460 NRFDWS---QGHLQVPLVIHWPG--TPAQRINVLtDHT----DVMTTLMQrLLHVSTPanEYSQGQDI--FTVPRRHNWV 528
Cdd:PRK13759 313 YLFRKGypyEGSAHIPFIIYDPGglLAGNRGTVI-DQVvelrDIMPTLLD-LAGGTIP--DDVDGRSLknLIFGQYEGWR 388
                        170       180       190
                 ....*....|....*....|....*....|....*...
5I5F_A       529 TAADG-------STLAITTPQMTLVLN-NNGHYQTYDL 558
Cdd:PRK13759 389 PYLHGehalgysSDNYLTDGKWKYIWFsQTGEEQLFDL 426
 
Name Accession Description Interval E-value
LapC_YejM_PbgA NF038282
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ...
1-586 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: 1189.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A         1 MVTHRQRYREKVSQMVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIV 80
Cdd:NF038282   1 MVTNRQRYREKVSQMISWGHWFALFNILLSLGLGSRYLFVSDWPSSLAGRIYALVSWLGHFSFIVFAAYLLILFPLTFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        81 MSQRLMRFLSAILATAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKL 160
Cdd:NF038282  81 MSQRLLRFLSAILATAGLTLLLVDSEVFTRFHLHLNPVVWELVINPDQGEMARDWQLMFISVPVIFLVEMLFATWSWQKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       161 RSLTRRRhFARPLAAFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPE 240
Cdd:NF038282 161 RSLNRRR-FGKPLAALFISAFFASHLMYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVQQGNPE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       241 AVSVQYPLSNLHYRDMGTGQNVLLITVDGLNYSRFEKQMPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDG 320
Cdd:NF038282 240 ALSVEYPLSDLSFRDKGSGYNLLLIVVDGLNNSDIAKAMPALARFAEQNVQFTQHYSSGNQNDTGLFGLFYGISPSYLDG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       321 VLSTRTPAALITALNQQGYQLGLFSSDGFASPLYRQALLSDFSMPAAQTQSDAQTASQWIDWLGRYAQEdNRWFSWISFN 400
Cdd:NF038282 320 ILSSRKPSALITALNQQGYQFGLFSSDGFKSPLYRQALLSDFSLPPPQSQSDAQTTSQWQQWLNGQKNT-NPWFSYLNLN 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       401 GTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLTPEENRFDWSQGHLQVPLVIHWPGT 480
Cdd:NF038282 399 GTSTASDDGKQKQRRYQRGAADVDQQINTVLDTLKERGLLDNTVVVITASHGVALDDNDDNFKFNRAQLQVPLVIHWPGT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       481 PAQRINVLTDHTDVMTTLMQRLLHVSTPANEYSQGQDIFTVPRRHNWVTAADGSTLAITTPQMTLVLNNNGHYQTYDLHG 560
Cdd:NF038282 479 PAQTINKLTDHQDVMTTLMQRLLHVSTAAADYSQGEDLFAAQRRHNWVATGDDGTLVITTPTQTLVLDNNGSYRAYDLNG 558
                        570       580
                 ....*....|....*....|....*.
5I5F_A       561 EKIKDQKPQLSLLLQVLTEEKRFIAN 586
Cdd:NF038282 559 REIKDQKPQLALLLQVLTEEKRFIAN 584
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
15-585 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: 883.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       15 MVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIVMSQRLMRFLSAILA 94
Cdd:COG3083   1 LISWGHWFALFNILLALLIGSRYLFIADWPGTLLGRLYLLVSWLGHFSFLVFALYLLLLFPLSFLVPSQRLFRGLSVILA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       95 TAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKLRSLtRRRHFARPLA 174
Cdd:COG3083  81 TAGLTLLLVDTEVFQRFHLHLNPLVWDLLFNPDQGELARDWQLLFIPVPLIFLLEMLLATWSWRKLRSL-ERRRFGKPVA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      175 AFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPEAVSVQYPLSNLHYR 254
Cdd:COG3083 160 ALFLVSFLASHLIYIWADANFYRPITMQRANLPLSYPMTARSFLEKHGLLDAQEYQQRLEEQGNPEASSLNYPLHPLQFS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      255 DMGTGQNVLLITVDGLNYSRFEKQ-MPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDGVLSTRTPAALITA 333
Cdd:COG3083 240 DPAKPPNILLIVVDSLRADMLDPEvMPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLFYGLPGNYWDSILAERTPPVLIDA 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      334 LNQQGYQLGLFSSDGFASPLYRQALLSDFSMPAAQT-----QSDAQTASQWIDWLGRYaQEDNRWFSWISFNGTN----- 403
Cdd:COG3083 320 LQQQGYQFGLFSSAGFNSPLFRQTIFSDVSLPRLHTpggpaQRDRQITAQWLQWLDQR-DSDRPWFSYLFLDAPHaysfp 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      404 ------------------IDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLTPEENRF--- 462
Cdd:COG3083 399 adypkpfqpsedcnylalDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYwgh 478
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      463 --DWSQGHLQVPLVIHWPGTPAQRINVLTDHTDVMTTLMQRLLHVSTPANEYSQGQDIFTVPRRHNWVTAADGSTLAITT 540
Cdd:COG3083 479 nsNFSRYQLQVPLVIHWPGTPPQVISKLTSHLDIVPTLMQRLLGVQNPASDYSQGEDLFDPQRRRDWVLAGDYRNLAIIT 558
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*
5I5F_A      541 PQMTLVLNNNGHYQTYDLHGEKIKDQKPQLSLLLQVLTEEKRFIA 585
Cdd:COG3083 559 PDRITVLDPSGNYQVYDRDYRPLKDAKPPLGLLLQVLTELKRFYA 603
DUF3413 pfam11893
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. ...
7-253 9.09e-133

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: 387.37  E-value: 9.09e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A          7 RYREKVSQMVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIVMSQRLM 86
Cdd:pfam11893   1 QYRDKVSQLISWGHWFALFNIILALLIGLRYLFSADWPSTLLGWLYLLVSWLGHFSFLAFALYLLVLFPLTFLIPYSRLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A         87 RFLSAILATAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKLRSLtRR 166
Cdd:pfam11893  81 RGLAAIIATAGLTLLLVDTEVFDQYGFHLNPVVWDLLLNGDQSELSRSWQLLFIVIPVILLLELLLANWVWKKLRKL-QR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        167 RHFARPLAAFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPEAVSVQY 246
Cdd:pfam11893 160 KKIGKPVAAFLLLCFLASHLIHIWADANLYRPITMQRANFPLSYPMTAKSFLEKHGLLDLESYQQRLAEQGNPPAQPLNY 239

                  ....*..
5I5F_A        247 PLSNLHY 253
Cdd:pfam11893 240 PLHPLQC 246
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
261-519 7.71e-44

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: 157.32  E-value: 7.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      261 NVLLITVDGLNYSRF------EKQMPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGY--MDGVLSTRTPAALIT 332
Cdd:cd16148   2 NVILIVIDSLRADHLgcygydRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYhgVWGGPLEPDDPTLAE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      333 ALNQQGYQLGLFSSDGFASPL---------YRQALLSDFSMPAAQTQSDAQTASQWIDWLGRYAQEDNrWFSWISFngtn 403
Cdd:cd16148  82 ILRKAGYYTAAVSSNPHLFGGpgfdrgfdtFEDFRGQEGDPGEEGDERAERVTDRALEWLDRNADDDP-FFLFLHY---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      404 idDSNQKNFvkRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGipltpEE---------NRFDWSQGHLQVPLV 474
Cdd:cd16148 157 --FDPHEPY--LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG-----EEfgehglywgHGSNLYDEQLHVPLI 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
5I5F_A      475 IHWPG-TPAQRINVLTDHTDVMTTLMQRLLhvsTPANEYSQGQDIF 519
Cdd:cd16148 228 IRWPGkEPGKRVDALVSHIDIAPTLLDLLG---VEPPDYSDGRSLL 270
Sulfatase pfam00884
Sulfatase;
260-502 2.16e-32

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 126.38  E-value: 2.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        260 QNVLLITVDGL--------NYSRFEkqMPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDGVLST-----RT 326
Cdd:pfam00884   1 PNVVLVLGESLrapdlglyGYPRPT--TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTpvglpRT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        327 PAALITALNQQGYQLGL-------------FSSDGFASPLYRQALLSDFSMPAAQT-------QSDAQTASQWIDWLgry 386
Cdd:pfam00884  79 EPSLPDLLKRAGYNTGAigkwhlgwynnqsPCNLGFDKFFGRNTGSDLYADPPDVPyncsgggVSDEALLDEALEFL--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A        387 AQEDNRWFSWISFNGTNI-----------------DDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITA 449
Cdd:pfam00884 156 DNNDKPFFLVLHTLGSHGppyypdrypekyatfkpSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTS 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
5I5F_A        450 GRGIPLTP------EENRFDWSQGHLQVPLVIHWPGT--PAQRINVLTDHTDVMTTLMQRL 502
Cdd:pfam00884 236 DHGESLGEgggylhGGKYDNAPEGGYRVPLLIWSPGGkaKGQKSEALVSHVDLFPTILDLA 296
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
21-519 7.89e-28

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 117.83  E-value: 7.89e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       21 WFALFNILLATLLgsrYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIVMSQRLMRFLSAILATAGMTL 100
Cdd:COG1368   1 FFLLFLLLLSLRL---VFLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      101 LLIDSEVFTRFHLHLNPIVWELVINPDQ-NEMARDWQLMFISVPVILLIEMLFATWSWQKlRSLTRRRHFARPLAAFFFV 179
Cdd:COG1368  78 LVADILYYRFFGDRLNFSDLDYLGDTGEvLGSLLSSYDLLLLLDLLLLLLLLLLLYRLLK-KLRKSLPWRKRLALLLLLL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      180 SFIASHLIYIWAdanfyRPITMQRA--------NLPLSYPMTarrflekhgLLDAQEYQRRLVEQGNPEAVSVQYPLSNL 251
Cdd:COG1368 157 ALLLLGIRLGED-----RPLNLSDAfsrnnfvnELGLNGPYS---------FYDALRNNKAPATYSEEEALEIKKYLKSN 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      252 HYRDMGTGQ----NVLLITVDGLNYSRFEKQ------MPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDGV 321
Cdd:COG1368 223 RPTPNPFGPakkpNVVVILLESFSDFFIGALgngkdvTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSP 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      322 LST---RTPAALITALNQQGYQ--------------LGLFSSDGFASPLYRqallSDFSMPAAQT--QSDAQTASQWIDW 382
Cdd:COG1368 303 YKRpgqNNFPSLPSILKKQGYEtsffhggdgsfwnrDSFYKNLGFDEFYDR----EDFDDPFDGGwgVSDEDLFDKALEE 378
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      383 LgryAQEDNRWFSwISFNGTN-----IDDSNQK------NFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGR 451
Cdd:COG1368 379 L---EKLKKPFFA-FLITLSNhgpytLPEEDKKipdygkTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDH 454
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
5I5F_A      452 GIPLtPEENRFDWSQGHLQVPLVIHWPG-TPAQRINVLTDHTDVMTTLMQrLLHVSTPaNEYSQGQDIF 519
Cdd:COG1368 455 GPRS-PGKTDYENPLERYRVPLLIYSPGlKKPKVIDTVGSQIDIAPTLLD-LLGIDYP-SYYAFGRDLL 520
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
261-559 2.11e-19

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 90.32  E-value: 2.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      261 NVLLITVDGLNYSRF------EKQMPELATFAEQNIDFTRHMSSG--------------NTTDNGIFGLFYGISPGYMDG 320
Cdd:COG3119  25 NILFILADDLGYGDLgcygnpLIKTPNIDRLAAEGVRFTNAYVTSpvcspsraslltgrYPHRTGVTDNGEGYNGGLPPD 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      321 VLStrtpaaLITALNQQGYQLGLFSSDGfaspLYRQALLSDFSmpaaqtqsdaqtasqwIDWLGRYAQEDNRWFSWISFN 400
Cdd:COG3119 105 EPT------LAELLKEAGYRTALFGKWH----LYLTDLLTDKA----------------IDFLERQADKDKPFFLYLAFN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      401 GT----------------------------NIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRG 452
Cdd:COG3119 159 APhapyqapeeyldkydgkdiplppnlaprDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      453 IPLtpEENRFDWSQGHL-----QVPLVIHWPG--TPAQRINVLTDHTDVMTTLMQrLLHVSTPANeySQGQDIFTV---- 521
Cdd:COG3119 239 PSL--GEHGLRGGKGTLyeggiRVPLIVRWPGkiKAGSVSDALVSLIDLLPTLLD-LAGVPIPED--LDGRSLLPLltge 313
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
5I5F_A      522 ---PRRHN-WVTAADGSTLAITTPQMTLVLN--NNGHYQTYDLH 559
Cdd:COG3119 314 kaeWRDYLyWEYPRGGGNRAIRTGRWKLIRYydDDGPWELYDLK 357
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
261-498 4.80e-15

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: 74.78  E-value: 4.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      261 NVLLITVDGLNYSRF------EKQMPELATFAEQNIDFTRhmssgnttdngifglFYGISPgymdgvLSTRTPAALITAL 334
Cdd:cd16022   2 NILLIMTDDLGYDDLgcygnpDIKTPNLDRLAAEGVRFTN---------------AYVASP------VCSPSRASLLTGR 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      335 NQQGYQLGLFSSDGFASPLYRQALlsdfsmpaAQTQSDA--QTAS--QW----IDWLGRYAQeDNRWFSWISFNGT-NId 405
Cdd:cd16022  61 YPHRHGVRGNVGNGGGLPPDEPTL--------AELLKEAgyRTALigKWhdeaIDFIERRDK-DKPFFLYVSFNAPhPP- 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      406 dsnqknFVkrYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLtpEENRFDWSQGHL-----QVPLVIHWPGT 480
Cdd:cd16022 131 ------FA--YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDML--GDHGLRGKKGSLyeggiRVPFIVRWPGK 200
                       250       260
                ....*....|....*....|
5I5F_A      481 PA--QRINVLTDHTDVMTTL 498
Cdd:cd16022 201 IPagQVSDALVSLLDLLPTL 220
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
260-502 1.61e-14

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: 74.26  E-value: 1.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      260 QNVLLITVDGLNYSRFEKQ------MPELATFAEQNIDFTRHMSS--GNTTDNGIFGLFYGISPGYMDGVLST----RTP 327
Cdd:cd16015   1 PNVIVILLESFSDPYIDKDvggedlTPNLNKLAKEGLYFGNFYSPgfGGGTANGEFEVLTGLPPLPLGSGSYTlyklNPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      328 AALITALNQQGYQL--------------GLFSSDGFasplYRQALLSDFSMPAAQT----QSDAQTASQWIDWLGryAQE 389
Cdd:cd16015  81 PSLPSILKEQGYETifihggdasfynrdSVYPNLGF----DEFYDLEDFPDDEKETngwgVSDESLFDQALEELE--ELK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      390 DNRWFSWI-------------SFNGTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLT 456
Cdd:cd16015 155 KKPFFIFLvtmsnhgpydlpeEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLG 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
5I5F_A      457 PEENRFD-WSQGHLQVPLVIHWPG-TPAQRINVLTDHTDVMTTLMQRL 502
Cdd:cd16015 235 SDYDETDeDPLDLYRTPLLIYSPGlKKPKKIDRVGSQIDIAPTLLDLL 282
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
410-558 1.88e-14

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: 75.30  E-value: 1.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      410 KNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLtpeenrfdWSQGHLQ----------VPLVIHWPG 479
Cdd:cd16034 223 REDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDML--------GSHGLMNkqvpyeesirVPFIIRYPG 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      480 --TPAQRINVLTDHTDVMTTLMqRLLHVSTPANEysQGQD-----------------IFTVPRRHNWVTAADGSTLAITT 540
Cdd:cd16034 295 kiKAGRVVDLLINTVDIMPTLL-GLCGLPIPDTV--EGRDlsplllggkddepdsvlLQCFVPFGGGSARDGGEWRGVRT 371
                       170
                ....*....|....*...
5I5F_A      541 PQMTLVLNNNGHYQTYDL 558
Cdd:cd16034 372 DRYTYVRDKNGPWLLFDN 389
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
261-519 8.68e-14

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: 73.31  E-value: 8.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      261 NVLLITVD--GLNYSRF---EKQMPELATFAEQNIDFTRHMSSG--------------NTTDNGIFGLFYGISPgYMDGV 321
Cdd:cd16027   2 NILWIIADdlSPDLGGYggnVVKTPNLDRLAAEGVRFTNAFTTApvcspsrsalltglYPHQNGAHGLRSRGFP-LPDGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      322 LStrtpaaLITALNQQGYQLGLFSSDGFAsPLYRQALLSDFSMPAAQTQSDAQTASQWIDWLGRyAQEDNRWFSWISFNG 401
Cdd:cd16027  81 KT------LPELLREAGYYTGLIGKTHYN-PDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNR-AKKGQPFFLWFGFHD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      402 T---NIDDSNQKNFVK---------------------RYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLtP 457
Cdd:cd16027 153 PhrpYPPGDGEEPGYDpekvkvppylpdtpevredlaDYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPF-P 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
5I5F_A      458 EENRFDWSQGhLQVPLVIHWPG--TPAQRINVLTDHTDVMTTLMQrLLHVSTPanEYSQGQDIF 519
Cdd:cd16027 232 RAKGTLYDSG-LRVPLIVRWPGkiKPGSVSDALVSFIDLAPTLLD-LAGIEPP--EYLQGRSFL 291
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
261-502 3.87e-13

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: 69.37  E-value: 3.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      261 NVLLITVDGLNYSRFEKQM------PELATFAEQNIDFTRHMSSGNTT--------DNGIFGLFYGISPGYMDGVLSTRT 326
Cdd:cd00016   2 HVVLIVLDGLGADDLGKAGnpapttPNLKRLASEGATFNFRSVSPPTSsapnhaalLTGAYPTLHGYTGNGSADPELPSR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      327 PAALITA-------LNQQGYQLGLFssdGFASPLYRQALLSDFsmpaaqtqsdaqtasqwidwlgryaqednrwFSWISF 399
Cdd:cd00016  82 AAGKDEDgptipelLKQAGYRTGVI---GLLKAIDETSKEKPF-------------------------------VLFLHF 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      400 NGTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITA---GRGIPLTPEENRFDWSQGHL---QVPL 473
Cdd:cd00016 128 DGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTAdhgGIDKGHGGDPKADGKADKSHtgmRVPF 207
                       250       260       270
                ....*....|....*....|....*....|
5I5F_A      474 VIHWPGTPAQRINV-LTDHTDVMTTLMQRL 502
Cdd:cd00016 208 IAYGPGVKKGGVKHeLISQYDIAPTLADLL 237
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
369-499 1.36e-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: 68.77  E-value: 1.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      369 TQSDAQTASQWIDWL---GRYAQEDNRWFSWISF-NGTNI-----DDSNQKNFVKRYASAASDVDAQINRVLNALREAGK 439
Cdd:cd16035 113 YKRDPGIAAQAVEWLrerGAKNADGKPWFLVVSLvNPHDImfppdDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGL 192
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5I5F_A      440 FDNTVVIITA----------GRGIPLTP-EENrfdwsqghLQVPLVIHWPGTP--AQRINVLTDHTDVMTTLM 499
Cdd:cd16035 193 ADNTIVVFTSdhgemggahgLRGKGFNAyEEA--------LHVPLIISHPDLFgtGQTTDALTSHIDLLPTLL 257
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
416-518 2.44e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 67.26  E-value: 2.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      416 YASAASDVDAQINRVLNALREAGKFDNTVVIITA------------GRG---IPLtpeeNRFDWSqghLQVPLVIHWPGT 480
Cdd:cd16149 144 YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSdngfnmghhgiwGKGngtFPL----NMYDNS---VKVPFIIRWPGV 216
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
5I5F_A      481 --PAQRINVLTDHTDVMTTLMQrLLHVSTPANEYSQGQDI 518
Cdd:cd16149 217 vpAGRVVDSLVSAYDFFPTLLE-LAGVDPPADPRLPGRSF 255
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
423-568 7.85e-12

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: 67.19  E-value: 7.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      423 VDAQINRVLNALREAGKFDNTVVIITAGRGiPLTPEENRFD----------WSQGHlQVPLVIHWPGT--PAQRINVLTD 490
Cdd:cd16146 217 IDDNVGRLLAKLKELGLEENTIVIFMSDNG-PAGGVPKRFNagmrgkkgsvYEGGH-RVPFFIRWPGKilAGKDVDTLTA 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      491 HTDVMTTLMQrLLHVSTPA--------------NEYSQGQDIFTVPRRHNWVTAADG-STLAITTPQMTLVLNNNGHYQT 555
Cdd:cd16146 295 HIDLLPTLLD-LCGVKLPEgikldgrsllpllkGESDPWPERTLFTHSGRWPPPPKKkRNAAVRTGRWRLVSPKGFQPEL 373
                       170
                ....*....|....*...
5I5F_A      556 YDLH---GEK--IKDQKP 568
Cdd:cd16146 374 YDIEndpGEEndVADEHP 391
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
261-521 1.97e-10

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: 62.87  E-value: 1.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      261 NVLLITVD-------GLNYSRFEKQMPELATFAEQNIDFTRHMSSGNTTDNGIFGLF---YGISPGYMDGVLSTRT---- 326
Cdd:cd16161   3 NFLLLFADdlgwgdlGANWAPNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMtgrLGLRNGVGHNFLPTSVgglp 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      327 --PAALITALNQQGYQLGLF-------------SSDGFAS----PlyrqallsdFSMPAAQTQSDAQTASQWIdwlGRYA 387
Cdd:cd16161  83 lnETTLAEVLRQAGYATGMIgkwhlgqreaylpNSRGFDYyfgiP---------FSHDSSLADRYAQFATDFI---QRAS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      388 QEDNRWFSWISFNGTNIDDSNQKNFVK------RYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPL------ 455
Cdd:cd16161 151 AKDRPFFLYAALAHVHVPLANLPRFQSptsgrgPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGPWEvkcela 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      456 ----TPEENRF---------DWSQGHlQVPLVIHWPG-TPAQRI-NVLTDHTDVMTTLMqRLLHVSTPANEYSQGQDIFT 520
Cdd:cd16161 231 vgpgTGDWQGNlggsvakasTWEGGH-REPAIVYWPGrIPANSTsAALVSTLDIFPTVV-ALAGASLPPGRIYDGKDLSP 308

                .
5I5F_A      521 V 521
Cdd:cd16161 309 V 309
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
422-498 6.90e-10

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: 61.06  E-value: 6.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      422 DVDAQINRVLNALREAGKFDNTVVIITAGRGiPLTPEENRFDWSQGHL-----------------QVPLVIHWPGT--PA 482
Cdd:cd16143 209 ELDWVVGRILDALKELGLAENTLVIFTSDNG-PSPYADYKELEKFGHDpsgplrgmkadiyegghRVPFIVRWPGKipAG 287
                        90
                ....*....|....*.
5I5F_A      483 QRINVLTDHTDVMTTL 498
Cdd:cd16143 288 SVSDQLVSLTDLFATL 303
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
410-517 7.88e-10

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 61.04  E-value: 7.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      410 KNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIP-----LTPEENRFDWSqghLQVPLVIHWPGTPA-Q 483
Cdd:cd16155 188 RQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAvgshgLMGKQNLYEHS---MRVPLIISGPGIPKgK 264
                        90       100       110
                ....*....|....*....|....*....|....
5I5F_A      484 RINVLTDHTDVMTTLMQrLLHVSTPanEYSQGQD 517
Cdd:cd16155 265 RRDALVYLQDVFPTLCE-LAGIEIP--ESVEGKS 295
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
388-500 9.95e-10

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: 61.12  E-value: 9.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      388 QEDNRWFSWISFNGTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGipltpeENRFD-WSQ 466
Cdd:cd16028 212 RIESLSFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG------EQLGDhWLW 285
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
5I5F_A      467 GHL-------QVPLVIHWPGTPA-----QRINVLTDHTDVMTTLMQ 500
Cdd:cd16028 286 GKDgffdqayRVPLIVRDPRREAdatrgQVVDAFTESVDVMPTILD 331
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
372-498 1.58e-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: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 59.85  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      372 DAQTASQWIDWLGRYAQEDNRWFSWISFNGTNIDDSNQKNFVKR------YASAASDVDAQINRVLNALREAGKFDNTVV 445
Cdd:cd16142 132 DEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKssgkgkYADSMVELDDHVGQILDALDELGIADNTIV 211
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5I5F_A      446 IIT------------AG----RGIPLTPEEnrfdwsqGHLQVPLVIHWPGT--PAQRINVLTDHTDVMTTL 498
Cdd:cd16142 212 IFTtdngpeqdvwpdGGytpfRGEKGTTWE-------GGVRVPAIVRWPGKikPGRVSNEIVSHLDWFPTL 275
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
379-518 1.74e-09

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: 60.28  E-value: 1.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      379 WIDWLGRYAQEDNRWFSWISFNGTnIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGipltpe 458
Cdd:cd16030 227 WNDLDDLPKYGDIPALNPGDPKGP-LPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG------ 299
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
5I5F_A      459 enrfdWS---QGH----------LQVPLVIHWPGTPA--QRINVLTDHTDVMTTLMQrLLHVstPANEYSQGQDI 518
Cdd:cd16030 300 -----WHlgeHGHwgkhtlfeeaTRVPLIIRAPGVTKpgKVTDALVELVDIYPTLAE-LAGL--PAPPCLEGKSL 366
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
386-500 1.87e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 59.93  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      386 YAQEDNRWfswisfNGTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITA------------GRGI 453
Cdd:cd16033 195 YRRERKRW------GVDTEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSdhgdalgahrlwDKGP 268
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
5I5F_A      454 PLTPEENRfdwsqghlqVPLVIHWPGT--PAQRINVLTDHTDVMTTLMQ 500
Cdd:cd16033 269 FMYEETYR---------IPLIIKWPGViaAGQVVDEFVSLLDLAPTILD 308
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
416-516 2.44e-09

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: 59.38  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      416 YASAASDVDAQINRVLNALREAGKFDNTVVIIT-------------AGRgiplTPeenrFDW-----SQGHLQVPLVIHW 477
Cdd:cd16025 221 YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLsdngasaepgwanASN----TP----FRLykqasHEGGIRTPLIVSW 292
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
5I5F_A      478 PGTPAQRiNVLTDH----TDVMTTLMQrLLHVSTPANEYSQGQ 516
Cdd:cd16025 293 PKGIKAK-GGIRHQfahvIDIAPTILE-LAGVEYPKTVNGVPQ 333
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
260-558 5.21e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 58.52  E-value: 5.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      260 QNVLLITVD--------GLNYSRFEKQMPELATFAEQNIDFTR--HMSSGNTTDNGIFGLFYGISPGYM--DGVLS---T 324
Cdd:cd16154   1 PNILLIIADdqgldssaQYSLSSDLPVTPTLDSLANSGIVFDNlwATPACSPTRATILTGKYGFRTGVLavPDELLlseE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      325 RTPAALITALNQQGYQLGLFS-----------SDGFASPLYRQAL---LSDFS-----MPAAQTQSDAQTASQW----ID 381
Cdd:cd16154  81 TLLQLLIKDATTAGYSSAVIGkwhlggndnspNNPGGIPYYAGILgggVQDYYnwnltNNGQTTNSTEYATTKLtnlaID 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      382 WLgryAQEDNRWFSWISFN-------------------GTNIDDSNQKNFVkrYASAASDVDAQINRVLNALREAGKfDN 442
Cdd:cd16154 161 WI---DQQTKPWFLWLAYNaphtpfhlppaelhsrsllGDSADIEANPRPY--YLAAIEAMDTEIGRLLASIDEEER-EN 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      443 TVVII-----TAGRGIPLTPEENRFDWS--QGHLQVPLVIHWPGTPAQ--RINVLTDHTDVMTTLMQrLLHVSTPANEYS 513
Cdd:cd16154 235 TIIIFigdngTPGQVVDLPYTRNHAKGSlyEGGINVPLIVSGAGVERAneRESALVNATDLYATIAE-LAGVDAAEIHDS 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
5I5F_A      514 QG-----QDIFTVPRRHNWVTAADGST--LAITTPQMTLVLNNNGHYQTYDL 558
Cdd:cd16154 314 VSfkpllSDVNASTRQYNYTEYESPTTtgWATRNQYYKLIESENGQEELYDL 365
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
380-524 5.60e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 57.94  E-value: 5.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      380 IDWLGRYAQEDNRWFSWISFNGTNIDDSNQKNFVKRY---ASAA-----SDVDAQINRVLNALREAGKFDNTVVIITAGR 451
Cdd:cd16037 120 VDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLYvrrARAAyyglvEFLDENIGRVLDALEELGLLDNTLIIYTSDH 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      452 GipltpeEN---RFDWSQGHL-----QVPLVIHWPGTPA-QRINVLTDHTDVMTTLMQrllHVSTPANEYSQGQDIFTVP 522
Cdd:cd16037 200 G------DMlgeRGLWGKSTMyeesvRVPMIISGPGIPAgKRVKTPVSLVDLAPTILE---AAGAPPPPDLDGRSLLPLA 270

                ..
5I5F_A      523 RR 524
Cdd:cd16037 271 EG 272
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
416-499 8.11e-09

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: 57.59  E-value: 8.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      416 YASAASDVDAQINRVLNALREAGKFDNTVVIITAG-------RGipLTPEENRFDWSqghLQVPLVIHWPGTPA-QRINV 487
Cdd:cd16032 166 YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDhgdmlgeRG--LWYKMSFFEGS---ARVPLIISAPGRFApRRVAE 240
                        90
                ....*....|..
5I5F_A      488 LTDHTDVMTTLM 499
Cdd:cd16032 241 PVSLVDLLPTLV 252
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
416-518 2.03e-08

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: 56.78  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      416 YASAASDVDAQINRVLNALREAGKFDNTVVIITA------GRGIPLTPeeNR-FDWSQGHL-----QVPLVIHWPG--TP 481
Cdd:cd16144 225 YAAMIESLDESVGRILDALEELGLADNTLVIFTSdngglsTRGGPPTS--NApLRGGKGSLyeggiRVPLIVRWPGviKP 302
                        90       100       110
                ....*....|....*....|....*....|....*..
5I5F_A      482 AQRINVLTDHTDVMTTLMQrLLHVSTPANEYSQGQDI 518
Cdd:cd16144 303 GSVSDVPVIGTDLYPTFLE-LAGGPLPPPQHLDGVSL 338
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
353-518 3.36e-07

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: 52.92  E-value: 3.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      353 LYRQAllsDFSMPAAQTQSDAQTASQWIdwlgryAQEDNRWFsWISFNGTNIDDSNQKnFVKRYASAASDVDAQINRVLN 432
Cdd:cd16031 187 LYEDV---TIPEPETFDDDDYAGRPEWA------REQRNRIR-GVLDGRFDTPEKYQR-YMKDYLRTVTGVDDNVGRILD 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      433 ALREAGKFDNTVVIITAGRGIPLTpEENRFD-WS--QGHLQVPLVIHWPGT--PAQRINVLTDHTDVMTTLMqRLLHVST 507
Cdd:cd16031 256 YLEEQGLADNTIIIYTSDNGFFLG-EHGLFDkRLmyEESIRVPLIIRDPRLikAGTVVDALVLNIDFAPTIL-DLAGVPI 333
                       170
                ....*....|.
5I5F_A      508 PanEYSQGQDI 518
Cdd:cd16031 334 P--EDMQGRSL 342
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
406-500 3.74e-07

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: 52.55  E-value: 3.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      406 DSNQKNFVKRYASAASdVDAQINRVLNALREAGKFDNTVVIITAgrgipltpeENRFDWSQGHLQ------------VPL 473
Cdd:cd16147 235 AYIDELYRKRLRTLQS-VDDLVERLVNTLEATGQLDNTYIIYTS---------DNGYHLGQHRLPpgkrtpyeedirVPL 304
                        90       100
                ....*....|....*....|....*...
5I5F_A      474 VIHWPGTPA-QRINVLTDHTDVMTTLMQ 500
Cdd:cd16147 305 LVRGPGIPAgVTVDQLVSNIDLAPTILD 332
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
260-449 5.32e-07

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 52.06  E-value: 5.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      260 QNVLLITVDGLNYSRFEK-QMPELATFAEQNIDFTRHMSSGNTT--------------------DNGIFGLFYGISPGYM 318
Cdd:COG1524  24 KKVVLILVDGLRADLLERaHAPNLAALAARGVYARPLTSVFPSTtapahttlltglypgehgivGNGWYDPELGRVVNSL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      319 DGVLSTRTPAALITA------LNQQGyqlglFSSDGFASPLYRQALLSDFSMP---------AAQTQSDAQTASQWIDWL 383
Cdd:COG1524 104 SWVEDGFGSNSLLPVptiferARAAG-----LTTAAVFWPSFEGSGLIDAARPypydgrkplLGNPAADRWIAAAALELL 178
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
5I5F_A      384 gryaQEDNRWFSWISFNgtNIDDSNQKNFV--KRYASAASDVDAQINRVLNALREAGKFDNTVVIITA 449
Cdd:COG1524 179 ----REGRPDLLLVYLP--DLDYAGHRYGPdsPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTA 240
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
415-570 1.03e-06

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: 51.41  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      415 RYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLTPEENRFD-----------WSQGHlQVPLVIHWPGT-PA 482
Cdd:cd16026 212 LYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSagplrggkgttWEGGV-RVPFIAWWPGViPA 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      483 -QRINVLTDHTDVMTTLMqRLLHVSTPANEYSQGQDIFTV------PRRHNWVTAADGSTL-AITTPQMTLVLNNNGHYQ 554
Cdd:cd16026 291 gTVSDELASTMDLLPTLA-ALAGAPLPEDRVIDGKDISPLllggskSPPHPFFYYYDGGDLqAVRSGRWKLHLPTTYRTG 369
                       170
                ....*....|....*.
5I5F_A      555 TYDLHGEKIKDQKPQL 570
Cdd:cd16026 370 TDPGGLDPTKLEPPLL 385
PRK13759 PRK13759
arylsulfatase; Provisional
381-558 9.19e-06

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 48.51  E-value: 9.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       381 DWlgRYAQE-DNRWFSWISFNGtNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGiPLTPEE 459
Cdd:PRK13759 237 DW--EYAEDqDPEGGSIDALRG-NLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG-DMLGDH 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A       460 NRFDWS---QGHLQVPLVIHWPG--TPAQRINVLtDHT----DVMTTLMQrLLHVSTPanEYSQGQDI--FTVPRRHNWV 528
Cdd:PRK13759 313 YLFRKGypyEGSAHIPFIIYDPGglLAGNRGTVI-DQVvelrDIMPTLLD-LAGGTIP--DDVDGRSLknLIFGQYEGWR 388
                        170       180       190
                 ....*....|....*....|....*....|....*...
5I5F_A       529 TAADG-------STLAITTPQMTLVLN-NNGHYQTYDL 558
Cdd:PRK13759 389 PYLHGehalgysSDNYLTDGKWKYIWFsQTGEEQLFDL 426
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
424-499 6.89e-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: 45.28  E-value: 6.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      424 DAQINRVLNALREAGKFDNTVVIITA--GRGIPLTPEEN-------RFDWSQGHLQVPLVIHWPGT--PAQRINVLTDHT 492
Cdd:cd16151 215 DKLVGKLVDKLEELGLRENTIIIFTGdnGTHRPITSRTNgrevrggKGKTTDAGTHVPLIVNWPGLipAGGVSDDLVDFS 294

                ....*..
5I5F_A      493 DVMTTLM 499
Cdd:cd16151 295 DFLPTLA 301
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
416-510 1.57e-03

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: 40.99  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I5F_A      416 YASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGiPLTPEENRF---DWSQGHLQVPLVIHWPGTPA-QRINVLTDH 491
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG-ELAMEHRQFykmSMYEGSSHVPLLIMGPGIKAgQQVSDVVSL 276
                        90
                ....*....|....*....
5I5F_A      492 TDVMTTLMQrLLHVSTPAN 510
Cdd:cd16171 277 VDIYPTMLD-IAGVPQPQN 294
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH