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Conserved domains on  [gi|555243212|ref|WP_023227659|]
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MULTISPECIES: sulfatase-like hydrolase/transferase [Salmonella]

Protein Classification

sulfatase_like and DUF4976 domain-containing protein( domain architecture ID 10888196)

sulfatase_like and DUF4976 domain-containing protein

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
66-480 1.69e-130

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: 385.79  E-value: 1.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  66 YNILLVVTDQERF-----FPTFPFPVPGRERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPyDL 140
Cdd:cd16035    1 PNILLILTDQERYpppwpAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQP-LL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 141 DPALGTTGHMMRELGYYTAYKGKWHLTeklekplpdekdedidvgdipepelhkimekygfadyhgigdiiGHSKGGYFY 220
Cdd:cd16035   80 SPDVPTLGHMLRAAGYYTAYKGKWHLS--------------------------------------------GAAGGGYKR 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 221 DSTTTAQTINWLRCKGQPlNDQHKPWFLAVNLVNPHDVMFIdtdkegekvqwrgeldqddntlaptqppenelyqaswpn 300
Cdd:cd16035  116 DPGIAAQAVEWLRERGAK-NADGKPWFLVVSLVNPHDIMFP--------------------------------------- 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 301 yplpanrhqsfneqgrppahleyqtaraalegqfPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFT 380
Cdd:cd16035  156 ----------------------------------PDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFT 201
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 381 ADHGELGGSHQMHGKGASVYKEQIHVPMIISHPAYPGN-RKCQALTCHLDIAPTLVGLTGLPEEKQHQALGNRKGVNFSG 459
Cdd:cd16035  202 SDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEAPPLPGRDLSP 281
                        410       420
                 ....*....|....*....|.
gi 555243212 460 LLKNPEGvavNAVRNASLYCY 480
Cdd:cd16035  282 LLTDADA---DAVRDGILFTY 299
DUF4976 super family cl20644
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ...
528-598 4.94e-08

Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.


The actual alignment was detected with superfamily member pfam16347:

Pssm-ID: 419068 [Multi-domain]  Cd Length: 103  Bit Score: 51.10  E-value: 4.94e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555243212  528 INDGRYKFARYFslrehNTPETWEdlikyndleLYDLKNDPDENHNLAADKQkYQDLILTMNEKLNKIIKD 598
Cdd:pfam16347  45 VRTERYKLIHFY-----NDIDEWE---------LYDLQKDPKEMNNVYGDPE-YAEVQAELKEELEELRKQ 100
 
Name Accession Description Interval E-value
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
66-480 1.69e-130

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: 385.79  E-value: 1.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  66 YNILLVVTDQERF-----FPTFPFPVPGRERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPyDL 140
Cdd:cd16035    1 PNILLILTDQERYpppwpAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQP-LL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 141 DPALGTTGHMMRELGYYTAYKGKWHLTeklekplpdekdedidvgdipepelhkimekygfadyhgigdiiGHSKGGYFY 220
Cdd:cd16035   80 SPDVPTLGHMLRAAGYYTAYKGKWHLS--------------------------------------------GAAGGGYKR 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 221 DSTTTAQTINWLRCKGQPlNDQHKPWFLAVNLVNPHDVMFIdtdkegekvqwrgeldqddntlaptqppenelyqaswpn 300
Cdd:cd16035  116 DPGIAAQAVEWLRERGAK-NADGKPWFLVVSLVNPHDIMFP--------------------------------------- 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 301 yplpanrhqsfneqgrppahleyqtaraalegqfPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFT 380
Cdd:cd16035  156 ----------------------------------PDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFT 201
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 381 ADHGELGGSHQMHGKGASVYKEQIHVPMIISHPAYPGN-RKCQALTCHLDIAPTLVGLTGLPEEKQHQALGNRKGVNFSG 459
Cdd:cd16035  202 SDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEAPPLPGRDLSP 281
                        410       420
                 ....*....|....*....|.
gi 555243212 460 LLKNPEGvavNAVRNASLYCY 480
Cdd:cd16035  282 LLTDADA---DAVRDGILFTY 299
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
67-598 7.33e-61

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 207.81  E-value: 7.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFPVPGRE-----RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPydLD 141
Cdd:COG3119   25 NILFILADDLGYGDLGCYGNPLIKtpnidRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG--LP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 142 PALGTTGHMMRELGYYTAYKGKWHLTeklekplpdekdedidvgdipepelhkimekygfadyhgigdiighskggyfYD 221
Cdd:COG3119  103 PDEPTLAELLKEAGYRTALFGKWHLY----------------------------------------------------LT 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 222 STTTAQTINWLRckgqPLNDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaPTQPPEN--ELYQASwp 299
Cdd:COG3119  131 DLLTDKAIDFLE----RQADKDKPFFLYLAFNAPHA---------------------------PYQAPEEylDKYDGK-- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 300 NYPLPANRHQSfneqgrppahleyqtaraalegqfPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVF 379
Cdd:COG3119  178 DIPLPPNLAPR------------------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVF 233
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 380 TADHGELGGSHQMHGKGASVYKEQIHVPMIISHPA-YPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrkGVNFS 458
Cdd:COG3119  234 TSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLD------GRSLL 307
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 459 GLLKNPEGvavnAVRnaslycygmilytDAHYLHrvialqrdkqktvaqikqeishlhpdFSHRSGTRMINDGRYKFARY 538
Cdd:COG3119  308 PLLTGEKA----EWR-------------DYLYWE--------------------------YPRGGGNRAIRTGRWKLIRY 344
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 539 fslreHNTPETWedlikyndlELYDLKNDPDENHNLAADkqkYQDLILTMNEKLNKIIKD 598
Cdd:COG3119  345 -----YDDDGPW---------ELYDLKNDPGETNNLAAD---YPEVVAELRALLEAWLKE 387
Sulfatase pfam00884
Sulfatase;
67-440 1.84e-24

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 104.04  E-value: 1.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212   67 NILLVVTDQERFFPTFPFPVPGR-----ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLglPWMPYDLD 141
Cdd:pfam00884   2 NVVLVLGESLRAPDLGLYGYPRPttpflDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVST--PVGLPRTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  142 PALGTtghMMRELGYYTAYKGKWHLTEKLEKPLPDEKDEDIdVGDIPEPELHKIMEKYGFadyhgigdiigHSKGGYFYD 221
Cdd:pfam00884  80 PSLPD---LLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKF-FGRNTGSDLYADPPDVPY-----------NCSGGGVSD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  222 STTTAQTINWLrckgqplNDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaptqppenelyqaswpny 301
Cdd:pfam00884 145 EALLDEALEFL-------DNNDKPFFLVLHTLGSHG-------------------------------------------- 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  302 PLPANRhqsfneqgrppahlEYQTARAALEGQFPDEDRrwrkLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTA 381
Cdd:pfam00884 174 PPYYPD--------------RYPEKYATFKPSSCSEEQ----LLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTS 235
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555243212  382 DHGEL---GGSHQMHGKGASVYKEQIHVPMII-SHPAYPGNRKCQALTCHLDIAPTLVGLTGL 440
Cdd:pfam00884 236 DHGESlgeGGGYLHGGKYDNAPEGGYRVPLLIwSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
67-609 4.63e-20

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 93.58  E-value: 4.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFPVPGRE-----RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFD-NLGLPWM-PYD 139
Cdd:PRK13759   8 NIILIMVDQMRGDCLGCNGNKAVEtpnldMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGyGDVVPWNyKNT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 140 LdpalgttGHMMRELGYYTAYKGKWH--------------LTEKLEKPLPDEKDEDIDVGDIPEPELhKIMEKYGFADYH 205
Cdd:PRK13759  88 L-------PQEFRDAGYYTQCIGKMHvfpqrnllgfhnvlLHDGYLHSGRNEDKSQFDFVSDYLAWL-REKAPGKDPDLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 206 GIGdIIGHSKGGYFYD-------STTTAQT-INWLRCKgqplnDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeld 277
Cdd:PRK13759 160 DIG-WDCNSWVARPWDleerlhpTNWVGSEsIEFLRRR-----DPTKPFFLKMSFARPH--------------------- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 278 qddntlAPTQPPEN--ELYQ-ASWPNyPLPANRHQSFNEQGRppahleyQTARAALEGQFPDED-RRWRKlldYYFNCIR 353
Cdd:PRK13759 213 ------SPYDPPKRyfDMYKdADIPD-PHIGDWEYAEDQDPE-------GGSIDALRGNLGEEYaRRARA---AYYGLIT 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 354 DCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHGKGASvYKEQIHVPMIISHPAYPGNRKCQALTCHL----D 429
Cdd:PRK13759 276 HIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYP-YEGSAHIPFIIYDPGGLLAGNRGTVIDQVvelrD 354
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 430 IAPTLVGLTGL--PEEKQHQALGNrkgvnfsgLLKNPEgvavNAVRNaslycygmilytdahYLHrvialqrdkqktvaq 507
Cdd:PRK13759 355 IMPTLLDLAGGtiPDDVDGRSLKN--------LIFGQY----EGWRP---------------YLH--------------- 392
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 508 ikqeISHlhpdFSHRSGTRMINDGRYKFARYFslreHNTPEtwedlikyndlELYDLKNDPDENHNLAADKqKYQDLILT 587
Cdd:PRK13759 393 ----GEH----ALGYSSDNYLTDGKWKYIWFS----QTGEE-----------QLFDLKKDPHELHNLSPSE-KYQPRLRE 448
                        570       580
                 ....*....|....*....|....
gi 555243212 588 MNEKLNKIIKD--EIGVDDGSFMP 609
Cdd:PRK13759 449 MRKKLVDHLRGreEGFVKDGKLVV 472
DUF4976 pfam16347
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ...
528-598 4.94e-08

Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.


Pssm-ID: 406689 [Multi-domain]  Cd Length: 103  Bit Score: 51.10  E-value: 4.94e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555243212  528 INDGRYKFARYFslrehNTPETWEdlikyndleLYDLKNDPDENHNLAADKQkYQDLILTMNEKLNKIIKD 598
Cdd:pfam16347  45 VRTERYKLIHFY-----NDIDEWE---------LYDLQKDPKEMNNVYGDPE-YAEVQAELKEELEELRKQ 100
 
Name Accession Description Interval E-value
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
66-480 1.69e-130

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: 385.79  E-value: 1.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  66 YNILLVVTDQERF-----FPTFPFPVPGRERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPyDL 140
Cdd:cd16035    1 PNILLILTDQERYpppwpAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQP-LL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 141 DPALGTTGHMMRELGYYTAYKGKWHLTeklekplpdekdedidvgdipepelhkimekygfadyhgigdiiGHSKGGYFY 220
Cdd:cd16035   80 SPDVPTLGHMLRAAGYYTAYKGKWHLS--------------------------------------------GAAGGGYKR 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 221 DSTTTAQTINWLRCKGQPlNDQHKPWFLAVNLVNPHDVMFIdtdkegekvqwrgeldqddntlaptqppenelyqaswpn 300
Cdd:cd16035  116 DPGIAAQAVEWLRERGAK-NADGKPWFLVVSLVNPHDIMFP--------------------------------------- 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 301 yplpanrhqsfneqgrppahleyqtaraalegqfPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFT 380
Cdd:cd16035  156 ----------------------------------PDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFT 201
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 381 ADHGELGGSHQMHGKGASVYKEQIHVPMIISHPAYPGN-RKCQALTCHLDIAPTLVGLTGLPEEKQHQALGNRKGVNFSG 459
Cdd:cd16035  202 SDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEAPPLPGRDLSP 281
                        410       420
                 ....*....|....*....|.
gi 555243212 460 LLKNPEGvavNAVRNASLYCY 480
Cdd:cd16035  282 LLTDADA---DAVRDGILFTY 299
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
67-598 7.33e-61

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 207.81  E-value: 7.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFPVPGRE-----RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPydLD 141
Cdd:COG3119   25 NILFILADDLGYGDLGCYGNPLIKtpnidRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGG--LP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 142 PALGTTGHMMRELGYYTAYKGKWHLTeklekplpdekdedidvgdipepelhkimekygfadyhgigdiighskggyfYD 221
Cdd:COG3119  103 PDEPTLAELLKEAGYRTALFGKWHLY----------------------------------------------------LT 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 222 STTTAQTINWLRckgqPLNDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaPTQPPEN--ELYQASwp 299
Cdd:COG3119  131 DLLTDKAIDFLE----RQADKDKPFFLYLAFNAPHA---------------------------PYQAPEEylDKYDGK-- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 300 NYPLPANRHQSfneqgrppahleyqtaraalegqfPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVF 379
Cdd:COG3119  178 DIPLPPNLAPR------------------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVF 233
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 380 TADHGELGGSHQMHGKGASVYKEQIHVPMIISHPA-YPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrkGVNFS 458
Cdd:COG3119  234 TSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLD------GRSLL 307
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 459 GLLKNPEGvavnAVRnaslycygmilytDAHYLHrvialqrdkqktvaqikqeishlhpdFSHRSGTRMINDGRYKFARY 538
Cdd:COG3119  308 PLLTGEKA----EWR-------------DYLYWE--------------------------YPRGGGNRAIRTGRWKLIRY 344
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 539 fslreHNTPETWedlikyndlELYDLKNDPDENHNLAADkqkYQDLILTMNEKLNKIIKD 598
Cdd:COG3119  345 -----YDDDGPW---------ELYDLKNDPGETNNLAAD---YPEVVAELRALLEAWLKE 387
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
91-593 5.65e-49

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: 176.57  E-value: 5.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGlPWMPYDLD--PALgttghmMRELGYYTAYKGKWHLTE 168
Cdd:cd16031   33 RLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG-PLFDASQPtyPKL------LRKAGYQTAFIGKWHLGS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 169 klekplpdekdedidVGDIPEPELHKIMEKYGFADYHGIGDIIG---HSKGGYFYDSTTtAQTINWLRckgqpLNDQHKP 245
Cdd:cd16031  106 ---------------GGDLPPPGFDYWVSFPGQGSYYDPEFIENgkrVGQKGYVTDIIT-DKALDFLK-----ERDKDKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 246 WFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlAPTQPPEN--ELYQASwpNYPLPANrhqsFNEQ---GRPPAh 320
Cdd:cd16031  165 FCLSLSFKAPH---------------------------RPFTPAPRhrGLYEDV--TIPEPET----FDDDdyaGRPEW- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 321 leyqtARAALEGQFPDEDRRWRKLLDY------YFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHG 394
Cdd:cd16031  211 -----AREQRNRIRGVLDGRFDTPEKYqrymkdYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLFD 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 395 KgASVYKEQIHVPMIISHP-AYPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrkGVNFSGLLKNPEGVavnAVR 473
Cdd:cd16031  286 K-RLMYEESIRVPLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQ------GRSLLPLLEGEKPV---DWR 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 474 NASLYcygmilytdaHYLHrvialqrdkqktvaqikqeishlHPDFSHRSGTRMINDGRYKFARYfslreHNTPETWedl 553
Cdd:cd16031  356 KEFYY----------EYYE-----------------------EPNFHNVPTHEGVRTERYKYIYY-----YGVWDEE--- 394
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 555243212 554 ikyndlELYDLKNDPDENHNLAADKQkYQDLILTMNEKLN 593
Cdd:cd16031  395 ------ELYDLKKDPLELNNLANDPE-YAEVLKELRKRLE 427
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
91-594 6.09e-49

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: 175.00  E-value: 6.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPYDLDPALGttgHMMRELGYYTAYKGKWHLTekl 170
Cdd:cd16027   30 RLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVKTLP---ELLREAGYYTGLIGKTHYN--- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 171 ekplPDEKDEDIDVGDIPEPELHKIMEKYGFADyhgigdiighskggyfydstttaqtiNWLRCKgqplnDQHKPWFLAV 250
Cdd:cd16027  104 ----PDAVFPFDDEMRGPDDGGRNAWDYASNAA--------------------------DFLNRA-----KKGQPFFLWF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 251 NLVNPHdVMFIDTDKEGEKVqwrgelDQDDNTLAPtqppenelyqaswpNYP-LPANRHQsfneqgrppahleyqtaraa 329
Cdd:cd16027  149 GFHDPH-RPYPPGDGEEPGY------DPEKVKVPP--------------YLPdTPEVRED-------------------- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 330 legqfpdedrrwrkLLDYYfNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGelggsHQMHGKGASVYKEQIHVPMI 409
Cdd:cd16027  188 --------------LADYY-DEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG-----MPFPRAKGTLYDSGLRVPLI 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 410 ISHPA-YPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrkGVNFSGLLKNPEGVAVNAVrnaslycYGMILYTDA 488
Cdd:cd16027  248 VRWPGkIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQ------GRSFLPLLKGEKDPGRDYV-------FAERDRHDE 314
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 489 HYLHRvialqrdkqktvaqikqeishlhpdfshrsgtRMINDGRYKFARYFslrehnTPEtwedlikyndlELYDLKNDP 568
Cdd:cd16027  315 TYDPI--------------------------------RSVRTGRYKYIRNY------MPE-----------ELYDLKNDP 345
                        490       500
                 ....*....|....*....|....*.
gi 555243212 569 DENHNLAADKqKYQDLILTMNEKLNK 594
Cdd:cd16027  346 DELNNLADDP-EYAEVLEELRAALDA 370
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
91-574 1.21e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 163.89  E-value: 1.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNlGLPwmpydLDPALGTTGHMMRELGYYTAYKGKWHLTEkl 170
Cdd:cd16034   32 RLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN-DVP-----LPPDAPTIADVLKDAGYRTGYIGKWHLDG-- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 171 ekplpDEKDEDIDVGDIPEPELhkimeKYGFADYHGIGDIIGHSKGGYFYDSTT------------TAQTINWLRCKGqp 238
Cdd:cd16034  104 -----PERNDGRADDYTPPPER-----RHGFDYWKGYECNHDHNNPHYYDDDGKriyikgyspdaeTDLAIEYLENQA-- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 239 lnDQHKPWFLAVNLVNPHDVMfiDTDKEGEKVQWrgelDQDDNTLAPTQPPEnelyqaswpnyplpanrhqsfneqgrpp 318
Cdd:cd16034  172 --DKDKPFALVLSWNPPHDPY--TTAPEEYLDMY----DPKKLLLRPNVPED---------------------------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 319 ahleyqtaraalegqfPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHGKGaS 398
Cdd:cd16034  216 ----------------KKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQ-V 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 399 VYKEQIHVPMIISHPA-YPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrkGVNFSGLLKNPEGvavNAVRNASL 477
Cdd:cd16034  279 PYEESIRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVE------GRDLSPLLLGGKD---DEPDSVLL 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 478 YCygmILYTDAHYlhrvialqrdkqktvaqikqeishlhpdFSHRSGTRMINDGRYKFARYFSlrehntPETWedlikyn 557
Cdd:cd16034  350 QC---FVPFGGGS----------------------------ARDGGEWRGVRTDRYTYVRDKN------GPWL------- 385
                        490
                 ....*....|....*..
gi 555243212 558 dleLYDLKNDPDENHNL 574
Cdd:cd16034  386 ---LFDNEKDPYQLNNL 399
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
67-592 4.01e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 162.78  E-value: 4.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFPVPGR-----ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPwMPYDLD 141
Cdd:cd16033    2 NILFIMTDQQRYDTLGCYGNPIVktpniDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENA-GAYSRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 142 PALG--TTGHMMRELGYYTAYKGKWHLteklekpLPDEKDEDidvgdipepelhkimekYGFADYHGIGDIIGHskggyf 219
Cdd:cd16033   81 LPPGveTFSEDLREAGYRNGYVGKWHV-------GPEETPLD-----------------YGFDEYLPVETTIEY------ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 220 ydsTTTAQTINWLRckgqPLNDQHKPWFLAVNLVNPHDVMFidtdkegekvqwrgeldqddntlaptqPPEN--ELYQAS 297
Cdd:cd16033  131 ---FLADRAIEMLE----ELAADDKPFFLRVNFWGPHDPYI---------------------------PPEPylDMYDPE 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 298 wpNYPLPANRHQSFNeqGRPPAHLEYqtarAALEGQFPDEDRRWRKLLDYYFNCIrdcdTHLD----RILNELDALKLTD 373
Cdd:cd16033  177 --DIPLPESFADDFE--DKPYIYRRE----RKRWGVDTEDEEDWKEIIAHYWGYI----TLIDdaigRILDALEELGLAD 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 374 KTIVVFTADHGELGGSHQMHGKGASVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTGLPEEKqhqalgnr 452
Cdd:cd16033  245 DTLVIFTSDHGDALGAHRLWDKGPFMYEETYRIPLIIKWPGViAAGQVVDEFVSLLDLAPTILDLAGVDVPP-------- 316
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 453 kgvNFSG--LLKNPEGVAVNAVRNAslycygmiLYTDAHYLHrvialqrdkqktvaqikqeishlhpdFSHRSgtRMIND 530
Cdd:cd16033  317 ---KVDGrsLLPLLRGEQPEDWRDE--------VVTEYNGHE--------------------------FYLPQ--RMVRT 357
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555243212 531 GRYKFAryfslreHNTPEtwedlikYNdlELYDLKNDPDENHNLAADKQkYQDLILTMNEKL 592
Cdd:cd16033  358 DRYKYV-------FNGFD-------ID--ELYDLESDPYELNNLIDDPE-YEEILREMRTRL 402
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
90-569 1.55e-39

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: 147.69  E-value: 1.55e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLglpwMPYDLDPAlgTTGHMMRELGYYTAYKGKWHltek 169
Cdd:cd16037   30 DRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNA----DPYDGDVP--SWGHALRAAGYETVLIGKLH---- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 170 lekplpdekdedidvgdipepelhkimekygfadYHGIGDiighsKGGYFYDSTTTAQTINWLRCKGQplndQHKPWFLA 249
Cdd:cd16037  100 ----------------------------------FRGEDQ-----RHGFRYDRDVTEAAVDWLREEAA----DDKPWFLF 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 250 VNLVNPHdvmfidtdkegekvqwrgeldqddntlaptqppenelyqaswpnYPLPAnrhqsfneqgrPPAHLEY--QTAR 327
Cdd:cd16037  137 VGFVAPH--------------------------------------------FPLIA-----------PQEFYDLyvRRAR 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 328 AAlegqfpdedrrwrklldyYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHGKGaSVYKEQIHVP 407
Cdd:cd16037  162 AA------------------YYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKS-TMYEESVRVP 222
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 408 MIISHPAYPGNRKCQALTCHLDIAPTLVGLTGLPEekqhqaLGNRKGVNFSGLLKNPEgvavnavrnaslycygmilytd 487
Cdd:cd16037  223 MIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPP------PPDLDGRSLLPLAEGPD---------------------- 274
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 488 ahylhrvialqrDKQKTVaqikqeISHLHPDFShRSGTRMINDGRYKFARYFSLREhntpetwedlikyndlELYDLKND 567
Cdd:cd16037  275 ------------DPDRVV------FSEYHAHGS-PSGAFMLRKGRWKYIYYVGYPP----------------QLFDLEND 319

                 ..
gi 555243212 568 PD 569
Cdd:cd16037  320 PE 321
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
91-579 1.86e-39

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: 150.42  E-value: 1.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNlglpwmPYDLDPALG--TT--GHMmRELGYYTAYKGK-WH 165
Cdd:cd16030   32 RLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDN------NSYFRKVAPdaVTlpQYF-KENGYTTAGVGKiFH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 166 lteklekplPDEKDEDIDVGDIPEPELHKIMEKYGFADYHGIGDIIGHSKGGYFYDST-----------TTAQTINWLRC 234
Cdd:cd16030  105 ---------PGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAAdvpdeaypdgkVADEAIEQLRK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 235 KGqplnDQHKPWFLAVNLVNPHdvmfidtdkegekVQWRgeldqddntlAPTQ-----PPENELYQASWPNYPLPANRHQ 309
Cdd:cd16030  176 LK----DSDKPFFLAVGFYKPH-------------LPFV----------APKKyfdlyPLESIPLPNPFDPIDLPEVAWN 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 310 SFNEqgRPPAHLEYQTARAALEGQFPDEdrRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGS 389
Cdd:cd16030  229 DLDD--LPKYGDIPALNPGDPKGPLPDE--QARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 390 HQMHGKgASVYKEQIHVPMIISHPAYPG-NRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrkGVNFSGLLKNPEgva 468
Cdd:cd16030  305 HGHWGK-HTLFEEATRVPLIIRAPGVTKpGKVTDALVELVDIYPTLAELAGLPAPPCLE------GKSLVPLLKNPS--- 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 469 vNAVRNASLycygmilytdahylhrvialqrdkqktvaqikqeISHLHPDFSHRSgtrmINDGRYKFARyfslrehntpe 548
Cdd:cd16030  375 -AKWKDAAF----------------------------------SQYPRPSIMGYS----IRTERYRYTE----------- 404
                        490       500       510
                 ....*....|....*....|....*....|.
gi 555243212 549 tWEDLIKYNDLELYDLKNDPDENHNLAADKQ 579
Cdd:cd16030  405 -WVDFDKVGAEELYDHKNDPNEWKNLANDPE 434
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
90-594 4.02e-39

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: 148.85  E-value: 4.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGL------------PWMPYDLDPALGTTGHMMRELGYY 157
Cdd:cd16144   30 DRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGrrgppdntklipPPSTTRLPLEEVTIAEALKDAGYA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 158 TAYKGKWHLTEKlEKPLPDEK--DEDIDVGDIPEPElhkimeKYGFADYHGIGDIIGHSKGGYFYDSTTTaQTINWLRck 235
Cdd:cd16144  110 TAHFGKWHLGGE-GGYGPEDQgfDVNIGGTGNGGPP------SYYFPPGKPNPDLEDGPEGEYLTDRLTD-EAIDFIE-- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 236 gqplNDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlAPTQPPENEL--YQAswpnYPLPANRHQSfne 313
Cdd:cd16144  180 ----QNKDKPFFLYLSHYAVH---------------------------TPIQARPELIekYEK----KKKGLRKGQK--- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 314 qgrppaHLEYqtarAALegqfpdedrrwrklldyyfncIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMH 393
Cdd:cd16144  222 ------NPVY----AAM---------------------IESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPP 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 394 --------GKGaSVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQAlgnrKGVNFSGLLKNP 464
Cdd:cd16144  271 tsnaplrgGKG-SLYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHL----DGVSLVPLLKGG 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 465 EGvavNAVRNAslycygmiLYTdaHYLHrvialqrdkqktvaqikqeishlhpdfSHRSGTRM---INDGRYKFARYFsl 541
Cdd:cd16144  346 EA---DLPRRA--------LFW--HFPH---------------------------YHGQGGRPasaIRKGDWKLIEFY-- 383
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 555243212 542 rehntpETWEdlikyndLELYDLKNDPDENHNLAAdkqKYQDLILTMNEKLNK 594
Cdd:cd16144  384 ------EDGR-------VELYNLKNDIGETNNLAA---EMPEKAAELKKKLDA 420
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
91-593 1.36e-38

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: 146.17  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCN--HQNTSN--VCTPSRSVLYTGLHM----PQTKMFDNLGLPWMPYdldpalgttghMMRELGYYTAYKG 162
Cdd:cd16155   33 RLARRGTSFTNayNMGGWSgaVCVPSRAMLMTGRTLfhapEGGKAAIPSDDKTWPE-----------TFKKAGYRTFATG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 163 KWHLteklekplpdekdedidvgdipepelhkimekyGFADyhgigdiighskggyfydstttaQTINWLrcKGQPLNDq 242
Cdd:cd16155  102 KWHN---------------------------------GFAD-----------------------AAIEFL--EEYKDGD- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 243 hKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaPTQPPEN--ELYQASwpNYPLPANrhqsFneqgrPPAH 320
Cdd:cd16155  123 -KPFFMYVAFTAPHD---------------------------PRQAPPEylDMYPPE--TIPLPEN----F-----LPQH 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 321 LEYQTARA----ALEGqFP-DEDRRWRKLLDYYfNCIrdcdTHLD----RILNELDALKLTDKTIVVFTADHGELGGSHQ 391
Cdd:cd16155  164 PFDNGEGTvrdeQLAP-FPrTPEAVRQHLAEYY-AMI----THLDaqigRILDALEASGELDNTIIVFTSDHGLAVGSHG 237
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 392 MHGKgASVYKEQIHVPMIISHPAYPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrkGVNFSGLLKNPEgvavNA 471
Cdd:cd16155  238 LMGK-QNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVE------GKSLLPVIRGEK----KA 306
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 472 VRNASLYCYgmilytdahylhrvialqrdkqktvaqikqeishlhpdfshRSGTRMINDGRYKFARYfslrehnTPETwe 551
Cdd:cd16155  307 VRDTLYGAY-----------------------------------------RDGQRAIRDDRWKLIIY-------VPGV-- 336
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 555243212 552 dlikyNDLELYDLKNDPDENHNLAADKqKYQDLILTMNEKLN 593
Cdd:cd16155  337 -----KRTQLFDLKKDPDELNNLADEP-EYQERLKKLLAELK 372
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
67-592 1.70e-35

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: 139.32  E-value: 1.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFpvpGR--------ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNlGLPwmpy 138
Cdd:cd16028    2 NVLFITADQWRADCLSCL---GHplvktpnlDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN-GTP---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 139 dLDPALGTTGHMMRELGYYTAYKGKWHLTeklekPLPD---EKDEDIDVGDIPEPelhkimekyGFADY---HGIGDiiG 212
Cdd:cd16028   74 -LDARHLTLALELRKAGYDPALFGYTDTS-----PDPRglaPLDPRLLSYELAMP---------GFDPVdrlDEYPA--E 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 213 HSKGGYFYDstttaQTINWLRCKGQplndqhKPWFLAVNLVNPHdvmfidtdkegekvqWrgeldqddNTLAPTqpPENE 292
Cdd:cd16028  137 DSDTAFLTD-----RAIEYLDERQD------EPWFLHLSYIRPH---------------P--------PFVAPA--PYHA 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 293 LYQASwpNYPLPaNRHQSFNEQGRP-P---AHLEYQTARAALEGQFPDED------RRWRKLldyYFNCIRDCDTHLDRI 362
Cdd:cd16028  181 LYDPA--DVPPP-IRAESLAAEAAQhPllaAFLERIESLSFSPGAANAADlddeevAQMRAT---YLGLIAEVDDHLGRL 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 363 LNELDALKLTDKTIVVFTADHGELGGSHQMHGKGAsVYKEQIHVPMIISHPAYPGN----RKCQALTCHLDIAPTLVGLT 438
Cdd:cd16028  255 FDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKDG-FFDQAYRVPLIVRDPRREADatrgQVVDAFTESVDVMPTILDWL 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 439 GLPEEKQHQalgnrkGVNFSGLLknpEGVAVNAVRNASLYCYgmiLYTDAHYLHRVIALQRDkqktvaqikqeishlhpd 518
Cdd:cd16028  334 GGEIPHQCD------GRSLLPLL---AGAQPSDWRDAVHYEY---DFRDVSTRRPQEALGLS------------------ 383
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555243212 519 fSHRSGTRMINDGRYKfaryfslrehntpetwedLIKYNDLE--LYDLKNDPDENHNLAADKqKYQDLILTMNEKL 592
Cdd:cd16028  384 -PDECSLAVIRDERWK------------------YVHFAALPplLFDLKNDPGELRDLAADP-AYAAVVLRYAQKL 439
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
67-441 8.19e-34

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: 129.09  E-value: 8.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFpvpGRE--------RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHmPQTkmFDNLGLPWMPY 138
Cdd:cd16022    2 NILLIMTDDLGYDDLGCY---GNPdiktpnldRLAAEGVRFTNAYVASPVCSPSRASLLTGRY-PHR--HGVRGNVGNGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 139 DLDPALGTTGHMMRELGYYTAYKGKWHlteklekplpdekdedidvgdipepelhkimekygfadyhgigdiighskggy 218
Cdd:cd16022   76 GLPPDEPTLAELLKEAGYRTALIGKWH----------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 219 fydstttAQTINWLRckgqpLNDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaptqppenelyqasw 298
Cdd:cd16022  103 -------DEAIDFIE-----RRDKDKPFFLYVSFNAPHP----------------------------------------- 129
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 299 pnyPLpanrhqsfneqgrppahleyqtaraalegqfpdedrrwrklldYYFNCIRDCDTHLDRILNELDALKLTDKTIVV 378
Cdd:cd16022  130 ---PF-------------------------------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIV 163
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555243212 379 FTADHGELGGSHQMHGKGASVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTGLP 441
Cdd:cd16022  164 FTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKiPAGQVSDALVSLLDLLPTLLDLAGIE 227
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
91-447 2.31e-32

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 126.12  E-value: 2.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHmpqtkmfdnlGLPWMPY--DLDPALGTTGHMMRELGYYTAYkgkwhlte 168
Cdd:cd16148   31 RLAAEGVVFDNHYSGSNPTLPSRFSLFTGLY----------PFYHGVWggPLEPDDPTLAEILRKAGYYTAA-------- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 169 klekplpdekdedidVGDIP----EPELHKimekyGFADYHGIGDIIG-HSKGGYFYDSTTTAQTINWLRckgqpLNDQH 243
Cdd:cd16148   93 ---------------VSSNPhlfgGPGFDR-----GFDTFEDFRGQEGdPGEEGDERAERVTDRALEWLD-----RNADD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 244 KPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlaptqppenELYQaswpnyplpanrhqsfneqgrppahley 323
Cdd:cd16148  148 DPFFLFLHYFDPH-----------------------------------EPYL---------------------------- 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 324 qtaraalegqfpdedrrwrklldyYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGE-LGGSHQMHGKGASVYKE 402
Cdd:cd16148  165 ------------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEeFGEHGLYWGHGSNLYDE 220
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 555243212 403 QIHVPMIISHPAYPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQ 447
Cdd:cd16148  221 QLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSD 265
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
67-598 2.79e-30

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 122.72  E-value: 2.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFpvpGRE--------RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNlGLPwmpy 138
Cdd:cd16152    3 NVIVFFTDQQRWDTLGCY---GQPldltpnldALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-GIP---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 139 dLDPALGTTGHMMRELGYYTAYKGKWHLteklekplpdekdedidvgdipepelhkimekygfadyhgigdiighskGGY 218
Cdd:cd16152   75 -LPADEKTLAHYFRDAGYETGYVGKWHL-------------------------------------------------AGY 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 219 FYDSTTTAqTINWLRCKgqplnDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqdDNTLAPTQPPENelYQASW 298
Cdd:cd16152  105 RVDALTDF-AIDYLDNR-----QKDKPFFLFLSYLEPHH----------------------QNDRDRYVAPEG--SAERF 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 299 PNYPLPANRhqsfneqgrppahleyqtarAALEGQfpdedrrWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVV 378
Cdd:cd16152  155 ANFWVPPDL--------------------AALPGD-------WAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIV 207
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 379 FTADHgelgGSHQMHGKGAsvYKEQ-----IHVPMIISHPAYPGNRKCQALTCHLDIAPTLVGLTGL--PEEKQhqalgn 451
Cdd:cd16152  208 FTSDH----GCHFRTRNAE--YKRSchessIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIdvPEEMQ------ 275
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 452 rkGVNFSGLLKNpegvAVNAVRNASLycygmilytdahylhrvialqrdkqktvAQIKQeishlhpdfsHRSGtRMINDG 531
Cdd:cd16152  276 --GRSLLPLVDG----KVEDWRNEVF----------------------------IQISE----------SQVG-RAIRTD 310
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555243212 532 RYKFARYFSlrehnTPETWEDL--IKYNDLELYDLKNDPDENHNLAADKQkYQDLILTMNEKLNKIIKD 598
Cdd:cd16152  311 RWKYSVAAP-----DKDGWKDSgsDVYVEDYLYDLEADPYELVNLIGRPE-YREVAAELRERLLARMAE 373
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
67-441 3.57e-29

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: 119.96  E-value: 3.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTD-QERFFPTFPFPVPGRERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNlGLPWMPYDLDPALG 145
Cdd:cd16147    3 NIVLILTDdQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNN-SPPGGGYPKFWQNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 146 ----TTGHMMRELGYYTAYKGKwhlteklekpLPDEKDEDIDVGDIPEpelhkimekyGFADYHGIGD----------II 211
Cdd:cd16147   82 lersTLPVWLQEAGYRTAYAGK----------YLNGYGVPGGVSYVPP----------GWDEWDGLVGnstyynytlsNG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 212 GHSKGGYFYD---STT--TAQTINWLRckgqPLNDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlAPT 286
Cdd:cd16147  142 GNGKHGVSYPgdyLTDviANKALDFLR----RAAADDKPFFLVVAPPAPH---------------------------GPF 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 287 QPPENelYQASWPNYPLPANRHQSFNEQGRPPAHLEYQTARAALEGQFPDED--RRWRKLLDyyfncirdCDTHLDRILN 364
Cdd:cd16147  191 TPAPR--YANLFPNVTAPPRPPPNNPDVSDKPHWLRRLPPLNPTQIAYIDELyrKRLRTLQS--------VDDLVERLVN 260
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555243212 365 ELDALKLTDKTIVVFTADHGELGGSHQMH-GKgASVYKEQIHVPMIISHPAYPGNRKCQALTCHLDIAPTLVGLTGLP 441
Cdd:cd16147  261 TLEATGQLDNTYIIYTSDNGYHLGQHRLPpGK-RTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAP 337
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
67-592 6.55e-29

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 119.65  E-value: 6.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFPVPGR-----ERLMKTGVTFCNH--QNTsnVCTPSRSVLYTGlhmpqtkmfdnlglpWMPYd 139
Cdd:cd16150    2 NIVIFVADQLRADSLGHLGNPAAvtpnlDALAAEGVRFSNAycQNP--VCSPSRCSFLTG---------------WYPH- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 140 ldpalgTTGH-------------MMREL---GYYTAYKGKWHLTeklekplPDEKDedidvgdipepelhkiMEKYGFAD 203
Cdd:cd16150   64 ------VNGHrtlhhllrpdepnLLKTLkdaGYHVAWAGKNDDL-------PGEFA----------------AEAYCDSD 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 204 YHGIgdiighskggyfydstttAQTINWLRCKGQPlndqhKPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntl 283
Cdd:cd16150  115 EACV------------------RTAIDWLRNRRPD-----KPFCLYLPLIFPH--------------------------- 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 284 aptqPPenelYQASWPNY------PLPANRHQSFNEQGRPPA--HLEYQtaraALEGqFPDEdrRWRKLLDYYFNCIRDC 355
Cdd:cd16150  145 ----PP----YGVEEPWFsmidreKLPPRRPPGLRAKGKPSMleGIEKQ----GLDR-WSEE--RWRELRATYLGMVSRL 209
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 356 DTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHGKGASVYKEQI-HVPMIISHPAYPGNRKCQALTCHLDIAPTL 434
Cdd:cd16150  210 DHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNTFEDCLtRVPLIIKPPGGPAGGVSDALVELVDIPPTL 289
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 435 VGLTGLPEEKQHQalgnrkGVNFSGLLKNPEGVAVNAVrnaslYCYGMILYTDAHYLhrvialqrDKQKTVAQIKQEISH 514
Cdd:cd16150  290 LDLAGIPLSHTHF------GRSLLPVLAGETEEHRDAV-----FSEGGRLHGEEQAM--------EGGHGPYDLKWPRLL 350
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555243212 515 LHPDFSHRSGTRMINDGRYKFARyfSLREHNtpetwedlikyndlELYDLKNDPDENHNLAADKQkYQDLILTMNEKL 592
Cdd:cd16150  351 QQEEPPEHTKAVMIRTRRYKYVY--RLYEPD--------------ELYDLEADPLELHNLIGDPA-YAEIIAEMKQRL 411
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
67-590 3.01e-28

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


Pssm-ID: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 118.25  E-value: 3.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFPVPGR-----ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNlglpwmpydlD 141
Cdd:cd16156    2 QFIFIMTDTQRWDMVGCYGNKAMktpnlDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN----------C 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 142 PALG----TTGHMMRELGYYTAYKGKWHL--TEKLEKPL-PDEKDED--ID----VGDIPEPELHKIMEKYGFADYHGIg 208
Cdd:cd16156   72 MALGdnvkTIGQRLSDNGIHTAYIGKWHLdgGDYFGNGIcPQGWDPDywYDmrnyLDELTEEERRKSRRGLTSLEAEGI- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 209 diighsKGGYFYDSTTTAQTINWLrckgqplnDQHK--PWFLAVNLVNPHDVMfidtdkegekvqwrgeldqddntLAPt 286
Cdd:cd16156  151 ------KEEFTYGHRCTNRALDFI--------EKHKdeDFFLVVSYDEPHHPF-----------------------LCP- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 287 qPPENELYQaswpNYPLPANRHQSFNEQGRPPAHLEYQTARaalegQFPDEDRRWRKLlDYYFNCIRDCDTHLDRILNEL 366
Cdd:cd16156  193 -KPYASMYK----DFEFPKGENAYDDLENKPLHQRLWAGAK-----PHEDGDKGTIKH-PLYFGCNSFVDYEIGRVLDAA 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 367 DalKLTDKTIVVFTADHGELGGSHQMHGKGASVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTGLPEEKQ 445
Cdd:cd16156  262 D--EIAEDAWVIYTSDHGDMLGAHKLWAKGPAVYDEITNIPLIIRGKGGeKAGTVTDTPVSHIDLAPTILDYAGIPQPKV 339
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 446 HQalgnrkGVNFSGLLKNPEGVAVNAVrnaslycygMILYTdahylhrvialqrdkqktvaqiKQEIShlHPDFSHRSGT 525
Cdd:cd16156  340 LE------GESILATIEDPEIPENRGV---------FVEFG----------------------RYEVD--HDGFGGFQPV 380
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555243212 526 RMINDGRYKFAryfslrehntpetwedLIKYNDLELYDLKNDPDENHNL------AADKQKYQDLILT-MNE 590
Cdd:cd16156  381 RCVVDGRYKLV----------------INLLSTDELYDLEKDPYEMHNLiddpdyADVRDQLHDELLDyMNE 436
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
90-575 3.11e-27

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: 114.22  E-value: 3.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPYDLDPALGTTGHMMRELGYYTAYKGKWHL--- 166
Cdd:cd16143   31 DRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLgld 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 167 -TEKLEKPLPDEKDEDIDV-GDIPEPELHkimekYGFaDYHgIGdiIGHSKggyfYDSTTTAQTINWLrcKGQPLNDqhK 244
Cdd:cd16143  111 wKKKDGKKAATGTGKDVDYsKPIKGGPLD-----HGF-DYY-FG--IPASE----VLPTLTDKAVEFI--DQHAKKD--K 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 245 PWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlAPTQPPEnelyqaswpnyplpanrhqSFNEQGRPPAHLEYq 324
Cdd:cd16143  174 PFFLYFALPAPH---------------------------TPIVPSP-------------------EFQGKSGAGPYGDF- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 325 taraalegqfpdedrrwrklldyyfncIRDCDTHLDRILNELDALKLTDKTIVVFTADHG----------ELGG---SHQ 391
Cdd:cd16143  207 ---------------------------VYELDWVVGRILDALKELGLAENTLVIFTSDNGpspyadykelEKFGhdpSGP 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 392 MHGKGASVYKEQIHVPMIISHPA-YPGNRKCQALTCHLDIAPTLVGLTGLPEEkQHQALgnrKGVNFSGLLKNPEGvavn 470
Cdd:cd16143  260 LRGMKADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLP-DNAAE---DSFSFLPALLGPKK---- 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 471 avrnaslycygmilytdahylhrvialqrdkqktvAQIKQEISHlhpdfSHRSGTRMINDGRYKFARYFSLREHNTPETW 550
Cdd:cd16143  332 -----------------------------------QEVRESLVH-----HSGNGSFAIRKGDWKLIDGTGSGGFSYPRGK 371
                        490       500
                 ....*....|....*....|....*
gi 555243212 551 EDLIKyNDLELYDLKNDPDENHNLA 575
Cdd:cd16143  372 EKLGL-PPGQLYNLSTDPGESNNLY 395
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
91-578 1.64e-24

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


Pssm-ID: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 106.52  E-value: 1.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPwMPYDLDPALGTTGHMMRELGYYTAYKGKWHL---- 166
Cdd:cd16145   31 RLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPG-GQDPLPPDDVTLAEVLKKAGYATAAFGKWGLggpg 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 167 TEKLEKPL------------------PDEKDEDIDVGDIPEPELHKIMEKYGFADYHGI--GDIIghskggyfydsttTA 226
Cdd:cd16145  110 TPGHPTKQgfdyfygyldqvhahnyyPEYLWRNGEKVPLPNNVIPPLDEGNNAGGGGGTysHDLF-------------TD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 227 QTINWLRckgqplNDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlAPTQPPENELYQASWPNYPLPAN 306
Cdd:cd16145  177 EALDFIR------ENKDKPFFLYLAYTLPH---------------------------APLQVPDDGPYKYKPKDPGIYAY 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 307 RHQSFNEQgrppahleyqtARAALegqfpdedrrwrklldyyfncIRDCDTHLDRILNELDALKLTDKTIVVFTADHG-- 384
Cdd:cd16145  224 LPWPQPEK-----------AYAAM---------------------VTRLDRDVGRILALLKELGIDENTLVVFTSDNGph 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 385 -ELGGSHQ---------MHGKGASVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnrk 453
Cdd:cd16145  272 sEGGSEHDpdffdsngpLRGYKRSLYEGGIRVPFIARWPGKiPAGSVSDHPSAFWDFMPTLADLAGAEPPEDID------ 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 454 GVNFSGLLKNpegvavnavrnaslycygmilytdahylhrvialQRDKQKTvaqikqeiSHLHPDFSHRSGTRMINDGRY 533
Cdd:cd16145  346 GISLLPTLLG----------------------------------KPQQQQH--------DYLYWEFYEGGGAQAVRMGGW 383
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 555243212 534 KfaryfsLREHNTPEtwedlikyNDLELYDLKNDPDENHNLAADK 578
Cdd:cd16145  384 K------AVRHGKKD--------GPFELYDLSTDPGETNNLAAQH 414
Sulfatase pfam00884
Sulfatase;
67-440 1.84e-24

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 104.04  E-value: 1.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212   67 NILLVVTDQERFFPTFPFPVPGR-----ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLglPWMPYDLD 141
Cdd:pfam00884   2 NVVLVLGESLRAPDLGLYGYPRPttpflDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVST--PVGLPRTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  142 PALGTtghMMRELGYYTAYKGKWHLTEKLEKPLPDEKDEDIdVGDIPEPELHKIMEKYGFadyhgigdiigHSKGGYFYD 221
Cdd:pfam00884  80 PSLPD---LLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKF-FGRNTGSDLYADPPDVPY-----------NCSGGGVSD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  222 STTTAQTINWLrckgqplNDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaptqppenelyqaswpny 301
Cdd:pfam00884 145 EALLDEALEFL-------DNNDKPFFLVLHTLGSHG-------------------------------------------- 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  302 PLPANRhqsfneqgrppahlEYQTARAALEGQFPDEDRrwrkLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTA 381
Cdd:pfam00884 174 PPYYPD--------------RYPEKYATFKPSSCSEEQ----LLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTS 235
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555243212  382 DHGEL---GGSHQMHGKGASVYKEQIHVPMII-SHPAYPGNRKCQALTCHLDIAPTLVGLTGL 440
Cdd:pfam00884 236 DHGESlgeGGGYLHGGKYDNAPEGGYRVPLLIwSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
90-439 2.26e-24

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: 104.20  E-value: 2.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTF----CNhqntSNVCTPSRSVLYTGLHMPQTKMFDNLGlpwmpyDLDPALGTTGHMMRELGYYTAYKGKWH 165
Cdd:cd16032   30 DRLAARGVVFdnayCN----SPLCAPSRASMMTGRLPSRIGAYDNAA------EFPADIPTFAHYLRAAGYRTALSGKMH 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 166 LteklekplpdekdedidVGdiPEpELHkimekygfadyhgigdiighskgGYFYDSTTTAQTINWLRCKGQPLNDQhkP 245
Cdd:cd16032  100 F-----------------VG--PD-QLH-----------------------GFDYDEEVAFKAVQKLYDLARGEDGR--P 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 246 WFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaPTQPPenelyQASWPNYplpanrhqsfneqgrppahleYQT 325
Cdd:cd16032  135 FFLTVSFTHPHD---------------------------PYVIP-----QEYWDLY---------------------VRR 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 326 ARAAlegqfpdedrrwrklldyYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHGKgASVYKEQIH 405
Cdd:cd16032  162 ARRA------------------YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYK-MSFFEGSAR 222
                        330       340       350
                 ....*....|....*....|....*....|....
gi 555243212 406 VPMIISHPAYPGNRKCQALTCHLDIAPTLVGLTG 439
Cdd:cd16032  223 VPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAG 256
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
91-575 6.02e-24

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: 104.57  E-value: 6.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPYDLDPALGTTGHMMRELGYYTAYKGKWHLtekl 170
Cdd:cd16026   32 RLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHL---- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 171 ekplpdekdedidvGDipEPELHKImeKYGFADYHGIgdiighskggyfydstttaqtinwlrckgqPLNDQHKPWflaV 250
Cdd:cd16026  108 --------------GH--QPEFLPT--RHGFDEYFGI------------------------------PYSNDMWPF---P 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 251 NLVNPHDVMFIDTDKEGEKVQWrgELDQDDNTLAPTQPP-----ENE-----LYQA-SWPNYPLpanrhqsfneqgrppa 319
Cdd:cd16026  137 LYRNDPPGPLPPLMENEEVIEQ--PADQSSLTQRYTDEAvdfieRNKdqpffLYLAhTMPHVPL---------------- 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 320 hleyqtaraalegqFPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHG------ELGGSHQM- 392
Cdd:cd16026  199 --------------FASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwleygGHGGSAGPl 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 393 HGKGASVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTG--LPEEkqhqalgnRK--GVNFSGLLKNPEgv 467
Cdd:cd16026  265 RGGKGTTWEGGVRVPFIAWWPGViPAGTVSDELASTMDLLPTLAALAGapLPED--------RVidGKDISPLLLGGS-- 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 468 avNAVRNASLYcygmilYTDAHYLHRVIalqrdkqktvaqikqeishlhpdfshrsgtrminDGRYKfARYFSLREHNTP 547
Cdd:cd16026  335 --KSPPHPFFY------YYDGGDLQAVR----------------------------------SGRWK-LHLPTTYRTGTD 371
                        490       500
                 ....*....|....*....|....*...
gi 555243212 548 ETWEDLIKYNDLELYDLKNDPDENHNLA 575
Cdd:cd16026  372 PGGLDPTKLEPPLLYDLEEDPGETYNVA 399
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
90-577 1.10e-21

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: 97.62  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTFcNHQNTSNVCTPSRSVLYTGLHMPQTKMFD-NLGLpwmpYDLDPALGTTGHMMRELGYYTAYKGKWHLte 168
Cdd:cd16146   30 DRLAAESVRF-TNFHVSPVCAPTRAALLTGRYPFRTGVWHtILGR----ERMRLDETTLAEVFKDAGYRTGIFGKWHL-- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 169 klekplpdekdedidvGDIP--EPELHKIMEKYGFADYHgIGDIIGHSKGGYFYDSTT----------------TAQTIN 230
Cdd:cd16146  103 ----------------GDNYpyRPQDRGFDEVLGHGGGG-IGQYPDYWGNDYFDDTYYhngkfvktegyctdvfFDEAID 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 231 WLRckgqplNDQHKPWF--LAVNLvnPHdvmfidtdkegekvqwrgeldqddntlAPTQPPENELYQaswpnyplpanrh 308
Cdd:cd16146  166 FIE------ENKDKPFFayLATNA--PH---------------------------GPLQVPDKYLDP------------- 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 309 qsFNEQGRPPAHleyqtarAAlegqfpdedrrwrklldyYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGG 388
Cdd:cd16146  198 --YKDMGLDDKL-------AA------------------FYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGG 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 389 SHQ-----MHGKGASVYKEQIHVPMIISHPA-YPGNRKCQALTCHLDIAPTLVGLTGLPEekqhQALGNRKGVNFSGLLK 462
Cdd:cd16146  251 VPKrfnagMRGKKGSVYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKL----PEGIKLDGRSLLPLLK 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 463 NPEgvavNAVRNASLYcygmilytdAHYlHRVIALQRDKQKTVaqikqeishlhpdfshrsgtrmINDGRYKFaryfsLR 542
Cdd:cd16146  327 GES----DPWPERTLF---------THS-GRWPPPPKKKRNAA----------------------VRTGRWRL-----VS 365
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 555243212 543 EHNTPetwedlikyndLELYDLKNDPDENHNLAAD 577
Cdd:cd16146  366 PKGFQ-----------PELYDIENDPGEENDVADE 389
PRK13759 PRK13759
arylsulfatase; Provisional
67-609 4.63e-20

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 93.58  E-value: 4.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQERFFPTFPFPVPGRE-----RLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFD-NLGLPWM-PYD 139
Cdd:PRK13759   8 NIILIMVDQMRGDCLGCNGNKAVEtpnldMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGyGDVVPWNyKNT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 140 LdpalgttGHMMRELGYYTAYKGKWH--------------LTEKLEKPLPDEKDEDIDVGDIPEPELhKIMEKYGFADYH 205
Cdd:PRK13759  88 L-------PQEFRDAGYYTQCIGKMHvfpqrnllgfhnvlLHDGYLHSGRNEDKSQFDFVSDYLAWL-REKAPGKDPDLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 206 GIGdIIGHSKGGYFYD-------STTTAQT-INWLRCKgqplnDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeld 277
Cdd:PRK13759 160 DIG-WDCNSWVARPWDleerlhpTNWVGSEsIEFLRRR-----DPTKPFFLKMSFARPH--------------------- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 278 qddntlAPTQPPEN--ELYQ-ASWPNyPLPANRHQSFNEQGRppahleyQTARAALEGQFPDED-RRWRKlldYYFNCIR 353
Cdd:PRK13759 213 ------SPYDPPKRyfDMYKdADIPD-PHIGDWEYAEDQDPE-------GGSIDALRGNLGEEYaRRARA---AYYGLIT 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 354 DCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHGKGASvYKEQIHVPMIISHPAYPGNRKCQALTCHL----D 429
Cdd:PRK13759 276 HIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYP-YEGSAHIPFIIYDPGGLLAGNRGTVIDQVvelrD 354
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 430 IAPTLVGLTGL--PEEKQHQALGNrkgvnfsgLLKNPEgvavNAVRNaslycygmilytdahYLHrvialqrdkqktvaq 507
Cdd:PRK13759 355 IMPTLLDLAGGtiPDDVDGRSLKN--------LIFGQY----EGWRP---------------YLH--------------- 392
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 508 ikqeISHlhpdFSHRSGTRMINDGRYKFARYFslreHNTPEtwedlikyndlELYDLKNDPDENHNLAADKqKYQDLILT 587
Cdd:PRK13759 393 ----GEH----ALGYSSDNYLTDGKWKYIWFS----QTGEE-----------QLFDLKKDPHELHNLSPSE-KYQPRLRE 448
                        570       580
                 ....*....|....*....|....
gi 555243212 588 MNEKLNKIIKD--EIGVDDGSFMP 609
Cdd:PRK13759 449 MRKKLVDHLRGreEGFVKDGKLVV 472
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
67-441 1.01e-19

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: 89.22  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTD-QERFFPTFPFPVPGR----ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLhMP-QTKMFD-----NLGLPW 135
Cdd:cd16149    2 NILFILTDdQGPWALGCYGNSEAVtpnlDRLAAEGVRFENFFCTSPVCSPARASLLTGR-MPsQHGIHDwivegSHGKTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 136 MPYDLDPALGTTGHMMRELGYYTAYKGKWHLTEKLEKPLPDEKDEDidvgdipepelhkimekygfadyhgigdiighsk 215
Cdd:cd16149   81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGDDAADFLRRRAEAE---------------------------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 216 ggyfydstttaqtinwlrckgqplndqhKPWFLAVNLVNPHDvmfidtdkegekvQWRgeldqddntlaptqppenelyq 295
Cdd:cd16149  127 ----------------------------KPFFLSVNYTAPHS-------------PWG---------------------- 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 296 aswpnyplpanrhqsfneqgrppahleyqtaraalegqfpdedrrwrklldyYFNCIRDCDTHLDRILNELDALKLTDKT 375
Cdd:cd16149  144 ----------------------------------------------------YFAAVTGVDRNVGRLLDELEELGLTENT 171
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555243212 376 IVVFTADHGELGGSHQMHGKG-----ASVYKEQIHVPMIISHP-AYPGNRKCQALTCHLDIAPTLVGLTGLP 441
Cdd:cd16149  172 LVIFTSDNGFNMGHHGIWGKGngtfpLNMYDNSVKVPFIIRWPgVVPAGRVVDSLVSAYDFFPTLLELAGVD 243
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
221-434 6.08e-18

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: 87.65  E-value: 6.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 221 DSTTTAQTINWLrcKGQplnDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeLDQDDNTLAPTQPPENelyqaswpn 300
Cdd:COG3083  363 DRQITAQWLQWL--DQR---DSDRPWFSYLFLDAPHA------------------YSFPADYPKPFQPSED--------- 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 301 yplpANRHQSFNEQGRPPahleyqtaraalegqfpdedrrwrkLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFT 380
Cdd:COG3083  411 ----CNYLALDNESDPTP-------------------------FKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIIT 461
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 555243212 381 ADHG-ELGGSHQMHGKGASVY-KEQIHVPMIIShpaYPGN--RKCQALTCHLDIAPTL 434
Cdd:COG3083  462 ADHGeEFNENGQNYWGHNSNFsRYQLQVPLVIH---WPGTppQVISKLTSHLDIVPTL 516
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
91-462 4.23e-16

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: 80.27  E-value: 4.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTF--CNHQNTsnvCTPSRSVLYTGLHMPQTKMFdNLGLPWMPYDLDPALGTTGHMMRELGYYTAYKGKWHLte 168
Cdd:cd16142   34 RLAKEGLRFtsFYVEPS---CTPGRAAFITGRHPIRTGLT-TVGLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHL-- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 169 klekplpdekdedidvGDIPE--PELHkimekyGFADYHGIgdiighskGGYFYDSTTTAQTINWLRckgqplnDQH--- 243
Cdd:cd16142  108 ----------------GDEDGrlPTDH------GFDEFYGN--------LYHTIDEEIVDKAIDFIK-------RNAkad 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 244 KPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlaptqppenelyqasWPNYPLPANRHQSfneqgrppahley 323
Cdd:cd16142  151 KPFFLYVNFTKMH-----------------------------------------FPTLPSPEFEGKS------------- 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 324 qTARaaleGQFPDedrrwrklldyyfnCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGE------LGGSHQMHGKGA 397
Cdd:cd16142  177 -SGK----GKYAD--------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGPeqdvwpDGGYTPFRGEKG 237
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555243212 398 SVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQALGNRK--GVNFSGLLK 462
Cdd:cd16142  238 TTWEGGVRVPAIVRWPGKiKPGRVSNEIVSHLDWFPTLAALAGAPDPKDKLLGKDRHidGVDQSPFLL 305
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
67-441 2.07e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 73.95  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  67 NILLVVTDQER---------FFPTFPFPVPGR------ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNl 131
Cdd:cd16153    3 NILWIITDDQRvdslscynnAHTGKSESRLGYvespniDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 132 glPWMPYDLDPALGTTGHMMRELGYYTAYKGKWHLTEklekplpdekdedidvgdipepelhkimekygFADYhgigdii 211
Cdd:cd16153   82 --EAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLEA--------------------------------FQRY------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 212 ghskggyfYDSTTTAQTINWLRCKGQPlnDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlAPTQPPEn 291
Cdd:cd16153  121 --------LKNANQSYKSFWGKIAKGA--DSDKPFFVRLSFLQPH---------------------------TPVLPPK- 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 292 elyqaswpnyplpanrhqsfneqgrppahleyqtaraalegqfpdedrRWRKLLDYYFNCirdcdTHLD----RILNELD 367
Cdd:cd16153  163 ------------------------------------------------EFRDRFDYYAFC-----AYGDaqvgRAVEAFK 189
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 368 ALKLT---DKTIVVFTADHGELGGSHQMHGKgASVYKEQIHVPMIISHP---AYPGNRKCQALTCHLDIAPTLVGLTGLP 441
Cdd:cd16153  190 AYSLKqdrDYTIVYVTGDHGWHLGEQGILAK-FTFWPQSHRVPLIVVSSdklKAPAGKVRHDFVEFVDLAPTLLAAAGVD 268
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
91-574 4.68e-14

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: 74.40  E-value: 4.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSnVCTPSRSVLYTGLHMPQTkmfdnlGLPWMPYDLDPALGTTGH----------MMRELGYYTAY 160
Cdd:cd16025   32 ALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQV------GMGTMAELATGKPGYEGYlpdsaatiaeVLKDAGYHTYM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 161 KGKWHLteklekplpdekdedidvgdipepelhkimekyGFADYHgigdiighskggyfydSTT--TAQTINWLRcKGQp 238
Cdd:cd16025  105 SGKWHL---------------------------------GPDDYY----------------STDdlTDKAIEYID-EQK- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 239 lnDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlAPTQPPENEL------YQASWPNypLPANRHQSFN 312
Cdd:cd16025  134 --APDKPFFLYLAFGAPH---------------------------APLQAPKEWIdkykgkYDAGWDA--LREERLERQK 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 313 EQGRPPAHLEYqTARAALE---GQFPDEDRRW--RK------LLDYyfncirdCDTHLDRILNELDALKLTDKTIVVFTA 381
Cdd:cd16025  183 ELGLIPADTKL-TPRPPGVpawDSLSPEEKKLeaRRmevyaaMVEH-------MDQQIGRLIDYLKELGELDNTLIIFLS 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 382 DHG---ELG----GS-------HQMHGKGasvykeqIHVPMIISHPAY--PGNRKCQALTcHL-DIAPTLVGLTGLPEEK 444
Cdd:cd16025  255 DNGasaEPGwanaSNtpfrlykQASHEGG-------IRTPLIVSWPKGikAKGGIRHQFA-HViDIAPTILELAGVEYPK 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 445 QHqalgnrkgvnfsgllknpEGVAVNAVRNASLycygmiLYT----DAHYLHRVIAlqrdkqktvaqikqeishlhpdFS 520
Cdd:cd16025  327 TV------------------NGVPQLPLDGVSL------LPTldgaAAPSRRRTQY----------------------FE 360
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 555243212 521 HrSGTRMINDGRYKfaryfsLREHNTPETWEDlikynDLELYDLKNDPDENHNL 574
Cdd:cd16025  361 L-FGNRAIRKGGWK------AVALHPPPGWGD-----QWELYDLAKDPSETHDL 402
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
334-447 1.28e-13

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 73.92  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 334 FPDEDRRW----RKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHqmhgKGASVYKEQIHVPMI 409
Cdd:COG1368  401 LPEEDKKIpdygKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGK----TDYENPLERYRVPLL 476
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 555243212 410 ISHPAYPGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQ 447
Cdd:COG1368  477 IYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYA 514
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
93-441 5.33e-13

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: 70.65  E-value: 5.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  93 MKT-GVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGlpwmpyDLDPALGTTGHMMRELGYYTAYKGK-------- 163
Cdd:cd16171   32 MKQhGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYK------GLDPNYPTWMDRLEKHGYHTQKYGKldytsghh 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 164 --------WhlTEKLEKPLPDEKDEDID-VGDIPEPelhKIMEKygfadyhgigdiighskggyfyDSTTTAQTINWLRC 234
Cdd:cd16171  106 svsnrveaW--TRDVPFLLRQEGRPTVNlVGDRSTV---RVMLK----------------------DWQNTDKAVHWIRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 235 KGQplnDQHKPWFLAVNLVNPHDvmfidtdkegekvqwrgeldqddntlaptqppenelyqaswpnYPLPAnrhqsfneQ 314
Cdd:cd16171  159 EAP---NLTQPFALYLGLNLPHP-------------------------------------------YPSPS--------M 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 315 GRPPAHLeyqtaraalegqfpdedrrwRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHG 394
Cdd:cd16171  185 GENFGSI--------------------RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFY 244
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 555243212 395 KgASVYKEQIHVPMIISHPAYPGNRKCQALTCHLDIAPTLVGLTGLP 441
Cdd:cd16171  245 K-MSMYEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVP 290
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
90-580 1.30e-12

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


Pssm-ID: 293779 [Multi-domain]  Cd Length: 445  Bit Score: 70.15  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLG--LPWMPYDLDPALGTTGHMMRELGYYTAYKGKWHLT 167
Cdd:cd16160   31 DDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRvfLPWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 168 EKLEKP-----LPDEKDEDIdVGDIPEPELHKimekygFADYHGIGDIIGHSKGGYFYDSTT-TAQTINWLRCKGQPLND 241
Cdd:cd16160  111 INENNHsdgahLPSHHGFDF-VGTNLPFTNSW------ACDDTGRHVDFPDRSACFLYYNDTiVEQPIQHEHLTETLVGD 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 242 --------QHKPWFLAVNLVNPHDVMFIDTDKEGEKVqwRGELdqDDNTlaptqppeNELyqaSWpnyplpanrhqsfne 313
Cdd:cd16160  184 aksfiednQENPFFLYFSFPQTHTPLFASKRFKGKSK--RGRY--GDNI--------NEM---SW--------------- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 314 qgrppahleyqtaraALEgqfpdedrrwrklldyyfncirdcdthldRILNELDALKLTDKTIVVFTADHG------ELG 387
Cdd:cd16160  234 ---------------AVG-----------------------------EVLDTLVDTGLDQNTLVFFLSDHGphveycLEG 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 388 GSHQMH--GKGASvYKEQIHVPMIISHPAYPGNRKCQALTCHLDIAPTLVGLTG--LPEEkqhqalGNRKGVNFSGLLKn 463
Cdd:cd16160  270 GSTGGLkgGKGNS-WEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGgtLPTD------RIYDGLSITDLLL- 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 464 peGVAVNAVRNaslycygmILYtdaHYLHRVIALQRDKQKTvaqikqeisHLHpdfSHRSGTRMINDGRykfARYFSLRE 543
Cdd:cd16160  342 --GEADSPHDD--------ILY---YCCSRLMAVRYGSYKI---------HFK---TQPLPSQESLDPN---CDGGGPLS 393
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 555243212 544 HNTpeTWED-----LIKYNDLELYDLKNDPDENHNLAADKQK 580
Cdd:cd16160  394 DYI--VCYDcedecVTKHNPPLIFDVEKDPGEQYPLQPSVYE 433
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
343-439 2.74e-12

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: 67.71  E-value: 2.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 343 KLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMhgKGASVYKEQIHVPMIISHPAYPGNRKCQ 422
Cdd:cd16015  189 TELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYD--ETDEDPLDLYRTPLLIYSPGLKKPKKID 266
                         90
                 ....*....|....*..
gi 555243212 423 ALTCHLDIAPTLVGLTG 439
Cdd:cd16015  267 RVGSQIDIAPTLLDLLG 283
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
91-411 5.04e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 67.76  E-value: 5.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQNTSnVCTPSRSVLYTGLHMPQTkmfdnlGLPWMPydlDPALGTTGHMMREL-------GYYTAYKGK 163
Cdd:cd16154   33 SLANSGIVFDNLWATP-ACSPTRATILTGKYGFRT------GVLAVP---DELLLSEETLLQLLikdattaGYSSAVIGK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 164 WHLTeklekplpdekdedidvGDIPEPelhkiMEKYGFADYHGIgdIIGHSKGGYFYDSTTTAQT--------------- 228
Cdd:cd16154  103 WHLG-----------------GNDNSP-----NNPGGIPYYAGI--LGGGVQDYYNWNLTNNGQTtnsteyattkltnla 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 229 INWLrckgqplNDQHKPWFLavnlvnphdvmfidtdkegekvqWrgeldqddntLAptqppenelYQAswPNYPLPAnrh 308
Cdd:cd16154  159 IDWI-------DQQTKPWFL-----------------------W----------LA---------YNA--PHTPFHL--- 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 309 qsfneqgrPPAHLEYQTaraaLEGQFPDEDRRWRkllDYYFNCIRDCDTHLDRILNELDALKLtDKTIVVFTADHGELGG 388
Cdd:cd16154  185 --------PPAELHSRS----LLGDSADIEANPR---PYYLAAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDNGTPGQ 248
                        330       340
                 ....*....|....*....|....*...
gi 555243212 389 SHQM-----HGKGaSVYKEQIHVPMIIS 411
Cdd:cd16154  249 VVDLpytrnHAKG-SLYEGGINVPLIVS 275
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
361-590 9.89e-11

Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.


Pssm-ID: 293778 [Multi-domain]  Cd Length: 521  Bit Score: 64.62  E-value: 9.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 361 RILNELDALKLTDKTIVVFTADHG---ELGGSHQMH---------GKGASVYKEQIHVPMIISHPAY-PGNRKCQALTCH 427
Cdd:cd16159  294 QILDALDELGLKDNTFVYFTSDNGghlEEISVGGEYgggnggiygGKKMGGWEGGIRVPTIVRWPGViPPGSVIDEPTSL 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 428 LDIAPTLVGLTG--LPEEKQHQalgnrkGVNFSGLLKNPEgvavnavrNASLYCYgMILYTDAHyLHRVialqrdkqktv 505
Cdd:cd16159  374 MDIFPTVAALAGapLPSDRIID------GRDLMPLLTGQE--------KRSPHEF-LFHYCGAE-LHAV----------- 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 506 aqikqeisHLHPdfshRSGTRMindgrYKfARYFSLREHNTPETW----------EDLIKYNDLELYDLKNDPDENHNLA 575
Cdd:cd16159  427 --------RYRP----RDGGAV-----WK-AHYFTPNFYPGTEGCcgtllcrcfgDSVTHHDPPLLFDLSADPSESNPLD 488
                        250
                 ....*....|....*
gi 555243212 576 ADKQKYQDLILTMNE 590
Cdd:cd16159  489 PTDEPYQEIIKKILE 503
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
91-574 2.53e-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: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 62.62  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFcNHQNTSNVCTPSRSVLYTGLHMpqtkmFDNLglpWMPYDLDPALGTTGHMMRELGYYTAYKGKWHLT-EK 169
Cdd:cd16151   31 ALAAEGVRF-NNAYAQPLCTPSRVQLMTGKYN-----FRNY---VVFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGgGR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 170 LEKPLPdekdedidvgdipepelhkimEKYGFADY---HGIGDIIGHSKGGYFY-------DSTTTAQT----------I 229
Cdd:cd16151  102 GDGDYP---------------------HEFGFDEYclwQLTETGEKYSRPATPTfnirngkLLETTEGDygpdlfadflI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 230 NWLRckgqplNDQHKPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlaptqppenelyqasWPNYPLPANRHQ 309
Cdd:cd16151  161 DFIE------RNKDQPFFAYYPMVLVH-----------------------------------------DPFVPTPDSPDW 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 310 SfneqgrppahleyqtaraalegqfpDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHG-ELGG 388
Cdd:cd16151  194 D-------------------------PDDKRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGtHRPI 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 389 SHQMHGKGASVYKEQ-----IHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTGLPEEKQHQalgnRKGVNFSGLLK 462
Cdd:cd16151  249 TSRTNGREVRGGKGKttdagTHVPLIVNWPGLiPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYP----LDGRSFAPQLL 324
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 463 NPEGvavnAVRNASLYCYGmilytdahylhrvialqrdkqktvaqikqeishlhPDFSHRSGTRMINDGRYKFaryfslr 542
Cdd:cd16151  325 GKTG----SPRREWIYWYY-----------------------------------RNPHKKFGSRFVRTKRYKL------- 358
                        490       500       510
                 ....*....|....*....|....*....|..
gi 555243212 543 ehntpetwedlikYNDLELYDLKNDPDENHNL 574
Cdd:cd16151  359 -------------YADGRFFDLREDPLEKNPL 377
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
348-437 1.55e-08

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: 55.89  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 348 YFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHqmHGKGASVYKE-----QIHVPMIISHPAYPGNRKCQ 422
Cdd:cd00016  144 YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGH--GGDPKADGKAdkshtGMRVPFIAYGPGVKKGGVKH 221
                         90
                 ....*....|....*
gi 555243212 423 ALTCHLDIAPTLVGL 437
Cdd:cd00016  222 ELISQYDIAPTLADL 236
DUF4976 pfam16347
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ...
528-598 4.94e-08

Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.


Pssm-ID: 406689 [Multi-domain]  Cd Length: 103  Bit Score: 51.10  E-value: 4.94e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555243212  528 INDGRYKFARYFslrehNTPETWEdlikyndleLYDLKNDPDENHNLAADKQkYQDLILTMNEKLNKIIKD 598
Cdd:pfam16347  45 VRTERYKLIHFY-----NDIDEWE---------LYDLQKDPKEMNNVYGDPE-YAEVQAELKEELEELRKQ 100
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
90-574 2.86e-07

Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.


Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 53.22  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPYDLDPALGTTGHMMRELGYYTAYKGKWHLTEK 169
Cdd:cd16158   31 DRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 170 LE-KPLPdekdedidvgdipepelhkimEKYGFADYHGIgdiighskggyfydstttaqtinwlrckgqPLNDQHKPwfl 248
Cdd:cd16158  111 LNgTYLP---------------------THQGFDHYLGI------------------------------PYSHDQGP--- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 249 AVNLVN-PHDVMFIDTDKEGE---KVQWRGELDQddntlaptQPPE----NELYQASwpnyplpANRHQSFNEQGRPPAH 320
Cdd:cd16158  137 CQNLTCfPPNIPCFGGCDQGEvpcPLFYNESIVQ--------QPVDlltlEERYAKF-------AKDFIADNAKEGKPFF 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 321 LEYQTARAALEgQFPDEDRRWRKLLDYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHG------ELGGSHQMH- 393
Cdd:cd16158  202 LYYASHHTHYP-QFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGpstmrkSRGGNAGLLk 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 394 -GKGaSVYKEQIHVPMIISHPAY--PGnrKCQALTCHLDIAPTLVGLTG--LPEekqhQALgnrKGVNFSGLLKNPEgva 468
Cdd:cd16158  281 cGKG-TTYEGGVREPAIAYWPGRikPG--VTHELASTLDILPTIAKLAGapLPN----VTL---DGVDMSPILFEQG--- 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 469 vNAVRNASLYcygmiLYTDAHYLHRVIALQRDKQKtvaqikqeiSHLHPDFSHRSGTRMINDGRYKfaryFSLREHNTPe 548
Cdd:cd16158  348 -KSPRQTFFY-----YPTSPDPDKGVFAVRWGKYK---------AHFYTQGAAHSGTTPDKDCHPS----AELTSHDPP- 407
                        490       500
                 ....*....|....*....|....*.
gi 555243212 549 twedlikyndlELYDLKNDPDENHNL 574
Cdd:cd16158  408 -----------LLFDLSQDPSENYNL 422
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
342-440 4.51e-07

Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 51.86  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 342 RKLLDYYFNCIRdcdtHLDRILNEL-DALKLTDK-TIVVFTADHGE-LGGS-HQMHGKGASVyKEQIHVPMII-----SH 412
Cdd:cd16017  182 EELINAYDNSIL----YTDYVLSQIiERLKKKDKdAALIYFSDHGEsLGENgLYLHGAPYAP-KEQYHVPFIIwssdsYK 256
                         90       100       110
                 ....*....|....*....|....*....|..
gi 555243212 413 PAYPGNR----KCQALTcHLDIAPTLVGLTGL 440
Cdd:cd16017  257 QRYPVERlranKDRPFS-HDNLFHTLLGLLGI 287
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
90-461 1.31e-06

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: 50.93  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  90 ERLMKTGVTFCNHQNTSNVCTPSRSVLYTGLHMPQTKMFDNL------GLPwmpydLDPAlgTTGHMMRELGYYTAYKGK 163
Cdd:cd16161   32 DKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFlptsvgGLP-----LNET--TLAEVLRQAGYATGMIGK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 164 WHLTEKlEKPLPDEKdedidvgdipepelhkimekyGFADYHGIGdiighskggYFYDSTTTAQTINWLRCKGQPLNDQH 243
Cdd:cd16161  105 WHLGQR-EAYLPNSR---------------------GFDYYFGIP---------FSHDSSLADRYAQFATDFIQRASAKD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 244 KPWFLAVNLVNPHdvmfidtdkegekvqwrgeldqddntlaptqppenelyqASWPNYPLPANrhqsfNEQGRPPahley 323
Cdd:cd16161  154 RPFFLYAALAHVH---------------------------------------VPLANLPRFQS-----PTSGRGP----- 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 324 qtaraalegqfpdedrrwrklldyYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHG------ELGGSH---QMHG 394
Cdd:cd16161  185 ------------------------YGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcELAVGPgtgDWQG 240
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555243212 395 KG------ASVYKEQIHVPMIISHPAY-PGNRKCQALTCHLDIAPTLVGLTG--LPEEKQHQalgnrkGVNFSGLL 461
Cdd:cd16161  241 NLggsvakASTWEGGHREPAIVYWPGRiPANSTSAALVSTLDIFPTVVALAGasLPPGRIYD------GKDLSPVL 310
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
91-439 5.85e-06

N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.


Pssm-ID: 293753 [Multi-domain]  Cd Length: 393  Bit Score: 49.09  E-value: 5.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212  91 RLMKTGVTFCNHQnTSNVCTPSRSVLYTGLHMPQTKMFDNLGLPWMPYDLDPALGTTGHMMRELGYYTAYKGKWHL---T 167
Cdd:cd16029   31 ALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLgfyT 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 168 EKLekpLPDEKdedidvgdipepelhkimekyGFaDYHgigdiIGHSKGGYFYDSTTTAQTINW----LRCKGQPLNDQH 243
Cdd:cd16029  110 WEY---TPTNR---------------------GF-DSF-----YGYYGGAEDYYTHTSGGANDYgnddLRDNEEPAWDYN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 244 KPW--FL----AVNLVNPHDV---MFIdtdkegekvqwrgeldqddnTLAptqppenelYQAswPNYPLPAnrhqsfneq 314
Cdd:cd16029  160 GTYstDLftdrAVDIIENHDPskpLFL--------------------YLA---------FQA--VHAPLQV--------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 315 grPPahlEYQTARAALEGQFPDEDRRwrklldYYFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGelGGSHQMHG 394
Cdd:cd16029  200 --PP---EYADPYEDKFAHIKDEDRR------TYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG--GPTGGGDG 266
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 555243212 395 ------KG--ASVYKEQIHVPMIISHPAYPGNR--KCQALTCHLDIAPTLVGLTG 439
Cdd:cd16029  267 gsnyplRGgkNTLWEGGVRVPAFVWSPLLPPKRgtVSDGLMHVTDWLPTLLSLAG 321
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
348-410 7.37e-05

Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 45.62  E-value: 7.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555243212 348 YFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHGELGGSHQMHGKGASvY----KEQIHVPMII 410
Cdd:COG2194  414 YDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTP-YaiapDEQTHVPMIM 479
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
361-441 2.04e-04

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 43.71  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 361 RILNELDALKLTDKTIVVFTADHG--ELGGshqmHGkGASvyKEQIHVPMIISHPAY-PGNRKCQALTCHL------DIA 431
Cdd:cd16024  182 RIYESLEEQSSNNPTLLVVCGDHGmtDAGN----HG-GSS--PGETSVPLLFISPKFsSKPSNADGELSYYetvqqvDLA 254
                         90
                 ....*....|
gi 555243212 432 PTLVGLTGLP 441
Cdd:cd16024  255 PTLALLLGLP 264
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
352-439 5.43e-04

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 42.19  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555243212 352 IRDCDTHLDRILNELDALKLTDKTIVVFTADHGELG-GSHqmhgkGASVYKEQIHVPMIISHPAYPGNRKCQalTCHL-D 429
Cdd:cd16018  185 LKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDvGTH-----GYDNELPDMRAIFIARGPAFKKGKKLG--PFRNvD 257
                         90
                 ....*....|
gi 555243212 430 IAPTLVGLTG 439
Cdd:cd16018  258 IYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
348-384 8.12e-04

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 42.04  E-value: 8.12e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 555243212 348 YFNCIRDCDTHLDRILNELDALKLTDKTIVVFTADHG 384
Cdd:COG1524  207 YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
 
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.
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