|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
14-443 |
0e+00 |
|
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: 574.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 14 EKMNVLFLMADDMRPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPdRFVNYSAYASKDC 93
Cdd:cd16030 1 KKPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTT-GVYDNNSYFRKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 94 PTAIPISRWFTSHGYYTISNGKVFHHLS----DHANSWSEPPYRKHPDGYDVYWAEYNKwelwmneasarTINPKTMRGP 169
Cdd:cd16030 80 PDAVTLPQYFKENGYTTAGVGKIFHPGIpdgdDDPASWDEPPNPPGPEKYPPGKLCPGK-----------KGGKGGGGGP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 170 FCEWAEVPDTAYDDGKLALKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVaNNRFRPKDLPNEVK 249
Cdd:cd16030 149 AWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 250 N-STEIYAYART--------TTADDISFQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNF 320
Cdd:cd16030 228 NdLDDLPKYGDIpalnpgdpKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 321 LGKHNLMDRSTHVPLIVRVPGLKK--GKTKSMVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAKIKDQVYIQW- 397
Cdd:cd16030 308 WGKHTLFEEATRVPLIIRAPGVTKpgKVTDALVELVDIYPTLAELAGLPAPPC-LEGKSLVPLLKNPSAKWKDAAFSQYp 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1765882875 398 ---EGGDNAVSNRYNYAEWKQKEKIHSRMLFDHHIDPEENKNRVNERKY 443
Cdd:cd16030 387 rpsIMGYSIRTERYRYTEWVDFDKVGAEELYDHKNDPNEWKNLANDPEY 435
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-462 |
2.83e-113 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 338.78 E-value: 2.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 1 MLAFSSLSVFSQTEKMNVLFLMADDMRP-ELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPH-- 77
Cdd:COG3119 9 LALLAAAAAAAAAKRPNILFILADDLGYgDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHrt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 78 -YPDRFVNYSAYASKDCPTaipISRWFTSHGYYTISNGKVFHHLSDHanswseppyrkhpdgydvywaeynkwelwmnea 156
Cdd:COG3119 89 gVTDNGEGYNGGLPPDEPT---LAELLKEAGYRTALFGKWHLYLTDL--------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 157 sartinpktmrgpfcewaevpdtayddgkLALKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVAN 236
Cdd:COG3119 133 -----------------------------LTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 237 NrFRPKDLPNEVknsteiyayartttaddisfQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLG 316
Cdd:COG3119 184 N-LAPRDLTEEE--------------------LRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 317 EHNFLG-KHNLMDRSTHVPLIVRVPG-LKKGKT-KSMVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAKIKDQV 393
Cdd:COG3119 243 EHGLRGgKGTLYEGGIRVPLIVRWPGkIKAGSVsDALVSLIDLLPTLLDLAGVPIPED-LDGRSLLPLLTGEKAEWRDYL 321
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765882875 394 YIQ--WEGGDNAV-SNRYNYAEWKQKEKihSRMLFDHHIDPEENKNRVNErkYRSEINKLSSFLKAKKETLM 462
Cdd:COG3119 322 YWEypRGGGNRAIrTGRWKLIRYYDDDG--PWELYDLKNDPGETNNLAAD--YPEVVAELRALLEAWLKELG 389
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
16-456 |
3.25e-89 |
|
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: 276.31 E-value: 3.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMRPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPH----YPDRFVNYSAYasK 91
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHqngaHGLRSRGFPLP--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 92 DCPTaipISRWFTSHGYYTISNGKVfhhlsdHANSWSEPPyrkhpdgydvywaeynkWELWMNEASARTINPKTMRGPFC 171
Cdd:cd16027 79 GVKT---LPELLREAGYYTGLIGKT------HYNPDAVFP-----------------FDDEMRGPDDGGRNAWDYASNAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 172 EWaevpdtayddgklalkaiadLKRlKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVannrfrPKDLPNevkns 251
Cdd:cd16027 133 DF--------------------LNR-AKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV------PPYLPD----- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 252 TEIyayARTTTADdisfqkeakhgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWhlgehNFL-GKHNLMDRS 330
Cdd:cd16027 181 TPE---VREDLAD-----------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPrAKGTLYDSG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 331 THVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAKIKDQVYIQWEGGDNAV---- 404
Cdd:cd16027 242 LRVPLIVRWPGKIKPGSVSdaLVSFIDLAPTLLDLAGIEPPEY-LQGRSFLPLLKGEKDPGRDYVFAERDRHDETYdpir 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1765882875 405 ---SNRY----NYAEWkqkekihsrMLFDHHIDPEENKNRVNERKYRSEINKLSSFLKA 456
Cdd:cd16027 321 svrTGRYkyirNYMPE---------ELYDLKNDPDELNNLADDPEYAEVLEELRAALDA 370
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-455 |
3.38e-81 |
|
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: 255.95 E-value: 3.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 14 EKMNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGA----SRASLLTGvyphypdRFVnYSAY 88
Cdd:cd16155 1 KKPNILFILADDQRADtIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWSGAvcvpSRAMLMTG-------RTL-FHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 89 ASKDCPTAIPISRW---FTSHGYYTISNGKvFHhlSDHANswseppyrkhpdgydvywaeynkwelwmneasartinpkt 165
Cdd:cd16155 73 EGGKAAIPSDDKTWpetFKKAGYRTFATGK-WH--NGFAD---------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 166 mrgpfcewaevpdtayddgklalKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVANN--RFRPKD 243
Cdd:cd16155 110 -----------------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENflPQHPFD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 244 lPNEVKNSTEIYA-YARTTtaDDISFQKEAkhgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLG 322
Cdd:cd16155 167 -NGEGTVRDEQLApFPRTP--EAVRQHLAE---YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 323 KHNLMDRSTHVPLIVRVPGLKKGKT-KSMVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAKIKDQVYIQWEGGD 401
Cdd:cd16155 241 KQNLYEHSMRVPLIISGPGIPKGKRrDALVYLQDVFPTLCELAGIEIPES-VEGKSLLPVIRGEKKAVRDTLYGAYRDGQ 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1765882875 402 NAVSNRYNYAEWKQKEKIHSRmLFDHHIDPEENKNRVNERKYRSEINKLSSFLK 455
Cdd:cd16155 320 RAIRDDRWKLIIYVPGVKRTQ-LFDLKKDPDELNNLADEPEYQERLKKLLAELK 372
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
14-456 |
8.79e-80 |
|
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: 253.99 E-value: 8.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 14 EKMNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPH-----------YPDR 81
Cdd:cd16031 1 KRPNIIFILTDDHRYDaLGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHrhgvtdnngplFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 82 FVNYSAYASKdcptaipisrwftsHGYYTISNGKVfhhlsdHANSWSEPPyrkhPDGYDvYWAEYNKWelwmneASARTI 161
Cdd:cd16031 81 QPTYPKLLRK--------------AGYQTAFIGKW------HLGSGGDLP----PPGFD-YWVSFPGQ------GSYYDP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 162 NPKTMRGpfcewaEVPDTAYDDGKLALKAIADLKRLKEQgKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVANNrFRP 241
Cdd:cd16031 130 EFIENGK------RVGQKGYVTDIITDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPET-FDD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 242 KDLPN------EVKNSTEIYAYARTTTadDISFQKEAKHgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHL 315
Cdd:cd16031 202 DDYAGrpewarEQRNRIRGVLDGRFDT--PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 316 GEHNFLGKHNLMDRSTHVPLIVRVPGL-KKGKT-KSMVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAKI-KDQ 392
Cdd:cd16031 279 GEHGLFDKRLMYEESIRVPLIIRDPRLiKAGTVvDALVLNIDFAPTILDLAGVPIPED-MQGRSLLPLLEGEKPVDwRKE 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765882875 393 VYIQ--WEGGDNAV-------SNRYNYAEWKQKEKIHsrMLFDHHIDPEENKNRVNERKYRSEINKLSSFLKA 456
Cdd:cd16031 358 FYYEyyEEPNFHNVpthegvrTERYKYIYYYGVWDEE--ELYDLKKDPLELNNLANDPEYAEVLKELRKRLEE 428
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-444 |
1.02e-78 |
|
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: 250.60 E-value: 1.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHypdrfvnysayaskdcp 94
Cdd:cd16033 1 PNILFIMTDQQRYDtLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPH----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 taipisrwftSHGYYT--ISNGKVFHHLSDHANSWSEPPYRKhpdGYDVYWaeYNKWElwmneasARTINPKTMRGpFCE 172
Cdd:cd16033 64 ----------EHGVLNnvENAGAYSRGLPPGVETFSEDLREA---GYRNGY--VGKWH-------VGPEETPLDYG-FDE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 173 WaeVPDTAYDDGKLALKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVANNRFRP-KDLPNEVKNs 251
Cdd:cd16033 121 Y--LPVETTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDfEDKPYIYRR- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 252 teiYAYARTTTADDISFQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLM-DRS 330
Cdd:cd16033 198 ---ERKRWGVDTEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFMyEET 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 331 THVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAK-IKDQVYIQWEGGDnavSNR 407
Cdd:cd16033 275 YRIPLIIKWPGVIAAGQVVdeFVSLLDLAPTILDLAGVDVPPK-VDGRSLLPLLRGEQPEdWRDEVVTEYNGHE---FYL 350
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1765882875 408 YNYAEWKQKEKI----HSR-MLFDHHIDPEENKNRVNERKYR 444
Cdd:cd16033 351 PQRMVRTDRYKYvfngFDIdELYDLESDPYELNNLIDDPEYE 392
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-436 |
1.34e-74 |
|
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: 239.78 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYsAYASKDCPT 95
Cdd:cd16034 3 NILFIFADQHRAQaLGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGND-VPLPPDAPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 96 aipISRWFTSHGYYTISNGKVfhHL-------SDHANSWSEPPYRKhpdGYDvYWAEYNKWELWMNeaSARTINpktmRG 168
Cdd:cd16034 82 ---IADVLKDAGYRTGYIGKW--HLdgperndGRADDYTPPPERRH---GFD-YWKGYECNHDHNN--PHYYDD----DG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 169 PFCEWAEvpdtaYDDGKLALKAIADLKRLKEQGKPFFMACGFWKPHLPF-NAPKKYWDLYDREKIPVannrfrPKDLPNE 247
Cdd:cd16034 147 KRIYIKG-----YSPDAETDLAIEYLENQADKDKPFALVLSWNPPHDPYtTAPEEYLDMYDPKKLLL------RPNVPED 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 248 VKNSTEIYAYARtttaddisfqkeakhGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLM 327
Cdd:cd16034 216 KKEEAGLREDLR---------------GYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVPY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 328 DRSTHVPLIVRVPG-LKKGKTKS-MVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAKIKDQVYIQW---EGGDN 402
Cdd:cd16034 281 EESIRVPFIIRYPGkIKAGRVVDlLINTVDIMPTLLGLCGLPIPDT-VEGRDLSPLLLGGKDDEPDSVLLQCfvpFGGGS 359
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1765882875 403 AVSN---------RYNYAEWKQKEKihsrMLFDHHIDPEENKN 436
Cdd:cd16034 360 ARDGgewrgvrtdRYTYVRDKNGPW----LLFDNEKDPYQLNN 398
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-432 |
2.43e-70 |
|
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: 225.89 E-value: 2.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYSAYASkDCP 94
Cdd:cd16037 1 PNILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-DVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 TaipISRWFTSHGYYTISNGKVfhhlsdHANSWSEPpyrkHPDGYDVYWAEynkwelwmneasartinpktmrgpfcewa 174
Cdd:cd16037 80 S---WGHALRAAGYETVLIGKL------HFRGEDQR----HGFRYDRDVTE----------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 175 evpdtayddgklalKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREkipvannrfrpkdlpnevknstei 254
Cdd:cd16037 118 --------------AAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLYVRR------------------------ 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 255 yayartttaddisfqkeAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLMDRSTHVP 334
Cdd:cd16037 160 -----------------ARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVRVP 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 335 LIVRVPGLKKGKT-KSMVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILtNLKAKIKDQVYIQWEGGDNAVSNR-YNYAE 412
Cdd:cd16037 223 MIISGPGIPAGKRvKTPVSLVDLAPTILEAAGAPPPPD-LDGRSLLPLA-EGPDDPDRVVFSEYHAHGSPSGAFmLRKGR 300
|
410 420
....*....|....*....|....
gi 1765882875 413 WKQkekIH----SRMLFDHHIDPE 432
Cdd:cd16037 301 WKY---IYyvgyPPQLFDLENDPE 321
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
17-377 |
1.85e-69 |
|
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: 220.77 E-value: 1.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHypdRF--VNYSAYASKDC 93
Cdd:cd16022 2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPH---RHgvRGNVGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 94 PTAIPISRWFTSHGYYTISNGKvfhhlsdhanswseppyrkhpdgydvywaeynkwelWMNEAsartinpktmrgpfCEW 173
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGK------------------------------------WHDEA--------------IDF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 174 aevpdtayddgklalkaiadLKRLKeQGKPFFMACGFWKPHLPFNapkkywdlydrekipvannrfrpkdlpnevknste 253
Cdd:cd16022 109 --------------------IERRD-KDKPFFLYVSFNAPHPPFA----------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 254 iyayartttaddisfqkeakhgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLG-KHNLMDRSTH 332
Cdd:cd16022 133 ----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGkKGSLYEGGIR 190
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1765882875 333 VPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPKnQLDGTS 377
Cdd:cd16022 191 VPFIVRWPGKIPAGQVSdaLVSLLDLLPTLLDLAGIEPPE-GLDGRS 236
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-450 |
4.39e-68 |
|
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: 223.27 E-value: 4.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHypdrfvnysayaskdcp 94
Cdd:cd16150 1 PNIVIFVADQLRADsLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPH----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 taipisrwftSHGYYTIsngkvFHHLSDHanswsEPPYRK--HPDGYDVYWAEYNkwELWMNEASArtinpktmrGPFCE 172
Cdd:cd16150 64 ----------VNGHRTL-----HHLLRPD-----EPNLLKtlKDAGYHVAWAGKN--DDLPGEFAA---------EAYCD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 173 WaevpDTAYDDGklalkAIADLKRlKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVannRFRPKDLPNEVKNST 252
Cdd:cd16150 113 S----DEACVRT-----AIDWLRN-RRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPP---RRPPGLRAKGKPSML 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 253 EIYAYARTTTADDISFQkEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGK-HNLMDRS- 330
Cdd:cd16150 180 EGIEKQGLDRWSEERWR-ELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKwPNTFEDCl 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 331 THVPLIVRVPGLKKGKT-KSMVEFVDLYPTLCELCHLPIPKNQLdGTSFVPILTNLKAKIKDQVYIqwEGGDNAVSNR-- 407
Cdd:cd16150 259 TRVPLIIKPPGGPAGGVsDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGETEEHRDAVFS--EGGRLHGEEQam 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765882875 408 ----YNYAEWKQKEKIHSRM-------------------------LFDHHIDPEENKNRVNERKYRSEINKL 450
Cdd:cd16150 336 egghGPYDLKWPRLLQQEEPpehtkavmirtrrykyvyrlyepdeLYDLEADPLELHNLIGDPAYAEIIAEM 407
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
12-450 |
1.30e-63 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 213.38 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 12 QTEKMNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRfVNYSAYAS 90
Cdd:PRK13759 3 QTKKPNIILIMVDQMRGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR-VGYGDVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 91 KDCPTAIPisRWFTSHGYYTISNGKV----------FHHLSDHaNSWSEPPYRKHPDGYDvYWAEYNKWeLWM------- 153
Cdd:PRK13759 82 WNYKNTLP--QEFRDAGYYTQCIGKMhvfpqrnllgFHNVLLH-DGYLHSGRNEDKSQFD-FVSDYLAW-LREkapgkdp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 154 ---------NEASARTINPKTMRGPfCEWaeVPDTAyddgklalkaiADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYW 224
Cdd:PRK13759 157 dltdigwdcNSWVARPWDLEERLHP-TNW--VGSES-----------IEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 225 DLYDREKIP---VANNRFRPKDLPNevknSTEIYAyARTTTADDisFQKEAKHGYYACLSYVDAQIGKVLDALDELGLAN 301
Cdd:PRK13759 223 DMYKDADIPdphIGDWEYAEDQDPE----GGSIDA-LRGNLGEE--YARRARAAYYGLITHIDHQIGRFLQALKEFGLLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 302 NTIVVLLGDHGWHLGEHNFLGKHNLMDRSTHVPLIVRVPG----LKKGKT-KSMVEFVDLYPTLCELCHLPIPkNQLDGT 376
Cdd:PRK13759 296 NTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGgllaGNRGTViDQVVELRDIMPTLLDLAGGTIP-DDVDGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 377 SFVPILTNLKAKIKDQV---YIQWEGGDNAVSN-RYNYAEWKQ--KEKihsrmLFDHHIDPEENKNRVNERKYRSEINKL 450
Cdd:PRK13759 375 SLKNLIFGQYEGWRPYLhgeHALGYSSDNYLTDgKWKYIWFSQtgEEQ-----LFDLKKDPHELHNLSPSEKYQPRLREM 449
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
17-399 |
7.87e-63 |
|
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: 206.66 E-value: 7.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYSAYASkDCPT 95
Cdd:cd16032 2 NILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPA-DIPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 96 aipISRWFTSHGYYTISNGKVfhhlsdhanswseppyrkH---PD---GYDvywaeynkwelwmneasartinpktmrgp 169
Cdd:cd16032 81 ---FAHYLRAAGYRTALSGKM------------------HfvgPDqlhGFD----------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 170 fcewaevpdtaYDD--GKLALKAIADLKRlKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREkipvannrfrpkdlpne 247
Cdd:cd16032 111 -----------YDEevAFKAVQKLYDLAR-GEDGRPFFLTVSFTHPHDPYVIPQEYWDLYVRR----------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 248 vknsteiyayartttaddisfqkeAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLM 327
Cdd:cd16032 162 ------------------------ARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFF 217
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765882875 328 DRSTHVPLIVRVPGLKKGKT-KSMVEFVDLYPTLCEL--CHLPIPKNQLDGTSFVPILTNLKAKIKDQVYIQWEG 399
Cdd:cd16032 218 EGSARVPLIISAPGRFAPRRvAEPVSLVDLLPTLVDLagGGTAPHVPPLDGRSLLPLLEGGDSGGEDEVISEYLA 292
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
16-454 |
9.94e-61 |
|
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: 204.80 E-value: 9.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHypdrfvNYSAYASKDcp 94
Cdd:cd16028 1 RNVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM------NHRSVWNGT-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 taiPISRWFTShgyytisngkvfhhLSDHAnswseppyRKHpdGYDVYWAEYNkwelwmnEASA--RTINPKTMRG---- 168
Cdd:cd16028 73 ---PLDARHLT--------------LALEL--------RKA--GYDPALFGYT-------DTSPdpRGLAPLDPRLlsye 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 169 -------PFCEWAEVP----DTAYddgkLALKAIADLKrlKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVANN 237
Cdd:cd16028 119 lampgfdPVDRLDEYPaedsDTAF----LTDRAIEYLD--ERQDEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPIR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 238 RFRPKDL----PnevknsteIYAYARTTTADDISFQKEAKHG-------------YYACLSYVDAQIGKVLDALDELGLA 300
Cdd:cd16028 193 AESLAAEaaqhP--------LLAAFLERIESLSFSPGAANAAdlddeevaqmratYLGLIAEVDDHLGRLFDYLKETGQW 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 301 NNTIVVLLGDHGWHLGEHNFLGKHNLMDRSTHVPLIVRVPGLKKGKTKS-----MVEFVDLYPTLCELCHLPIPKnQLDG 375
Cdd:cd16028 265 DDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREADATRGqvvdaFTESVDVMPTILDWLGGEIPH-QCDG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 376 TSFVPILTNLKAKI-KDQVYIQWEGGD-------------------NAV-SNRYNYAEWKQkekiHSRMLFDHHIDPEEN 434
Cdd:cd16028 344 RSLLPLLAGAQPSDwRDAVHYEYDFRDvstrrpqealglspdecslAVIrDERWKYVHFAA----LPPLLFDLKNDPGEL 419
|
490 500
....*....|....*....|
gi 1765882875 435 KNRVNERKYRSEINKLSSFL 454
Cdd:cd16028 420 RDLAADPAYAAVVLRYAQKL 439
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-384 |
1.22e-60 |
|
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: 203.93 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDM-RPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYP-------------HYPDRF 82
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYParlgitdvipgrrGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 83 VNYSAYASKDCPT-AIPISRWFTSHGYYTISNGKvfHHLSDHANSWSEppyrKHpdGYDVywaeynkwelwmNEASARTI 161
Cdd:cd16144 82 KLIPPPSTTRLPLeEVTIAEALKDAGYATAHFGK--WHLGGEGGYGPE----DQ--GFDV------------NIGGTGNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 162 NPKTMRGPFCEWAEVPDTAYDDGK----LALKAIADLKrlKEQGKPFFMACGFWKPHLPFNAPKKYWDLYdrekipvann 237
Cdd:cd16144 142 GPPSYYFPPGKPNPDLEDGPEGEYltdrLTDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKY---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 238 RFRPKDLPNEVKNSTeiYAyartttaddisfqkeakhgyyACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGE 317
Cdd:cd16144 210 EKKKKGLRKGQKNPV--YA---------------------AMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTR 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765882875 318 HNFL--------GKHNLMDRSTHVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPKNQ-LDGTSFVPILTN 384
Cdd:cd16144 267 GGPPtsnaplrgGKGSLYEGGIRVPLIVRWPGVIKPGSVSdvPVIGTDLYPTFLELAGGPLPPPQhLDGVSLVPLLKG 344
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-380 |
1.30e-60 |
|
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: 198.93 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYpdrfvnYSAYASKDCP 94
Cdd:cd16148 1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY------HGVWGGPLEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 TAIPISRWFTSHGYYTisngkvfHHLSDHANSWSEPPYRKhpdGYDVYwaeynkwelwmneasartinpktMRGPFCEWA 174
Cdd:cd16148 75 DDPTLAEILRKAGYYT-------AAVSSNPHLFGGPGFDR---GFDTF-----------------------EDFRGQEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 175 EVPDTAYDDGKLALKAIADLKRLKeQGKPFFMACGFWKPHLPFnapkkywdLYDrekipvannrfrpkdlpnevknstei 254
Cdd:cd16148 122 PGEEGDERAERVTDRALEWLDRNA-DDDPFFLFLHYFDPHEPY--------LYD-------------------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 255 yayartttaddisfqkeakhgyyACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKH--NLMDRSTH 332
Cdd:cd16148 167 -----------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHgsNLYDEQLH 223
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1765882875 333 VPLIVRVPGLKKGKTKS-MVEFVDLYPTLCELCHLPIPKnQLDGTSFVP 380
Cdd:cd16148 224 VPLIIRWPGKEPGKRVDaLVSHIDIAPTLLDLLGVEPPD-YSDGRSLLP 271
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-379 |
1.00e-54 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 184.12 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 15 KMNVLFLMADDMRPE-LGCYG----------VKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFV 83
Cdd:cd16153 1 KPNILWIITDDQRVDsLSCYNnahtgksesrLGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 84 N-YSAYASKDCPTAIPISrwFTSHGYYTISNGKvfhhlsdhanswseppyrkhpDGYDvywaEYNKWelwmneasarTIN 162
Cdd:cd16153 81 FeAAHPALDHGLPTFPEV--LKKAGYQTASFGK---------------------SHLE----AFQRY----------LKN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 163 P-KTMRGPFCEWAEVPDTAyddgklalkaiadlkrlkeqgKPFFMACGFWKPHLPFNAPKKYWDLYDrekipvannrfrp 241
Cdd:cd16153 124 AnQSYKSFWGKIAKGADSD---------------------KPFFVRLSFLQPHTPVLPPKEFRDRFD------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 242 kdlpnevknsteiyayartttaddisfqkeakhgYYACLSYVDAQIGKVLDALDELGLAN---NTIVVLLGDHGWHLGEH 318
Cdd:cd16153 170 ----------------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQ 215
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1765882875 319 NFLGKHNLMDRSTHVPLIVRVPGLKK----GKTKSMVEFVDLYPTLCELCHLPIPK-NQLDGTSFV 379
Cdd:cd16153 216 GILAKFTFWPQSHRVPLIVVSSDKLKapagKVRHDFVEFVDLAPTLLAAAGVDVDApDYLDGRDLF 281
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-436 |
1.08e-50 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 177.40 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRP-ELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYP-HYPDRFVNYSAYASKDCP 94
Cdd:cd16145 2 NIIFILADDLGYgDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTgHTRVRGNSEPGGQDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 TAIPISRWFTSHGYYTISNGKVfhHLSDHAnsWSEPPYRKHPD---GYDV------YWAEYnkweLWMNEASARTINPKT 165
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGKW--GLGGPG--TPGHPTKQGFDyfyGYLDqvhahnYYPEY----LWRNGEKVPLPNNVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 166 MRGPFCEWAEVPDTAYDDGKLALKAIADLKRLKEqgKPFFMacgfwkpHLPFNAPKKYWDLydrekipvannrfrPKDLP 245
Cdd:cd16145 154 PPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKD--KPFFL-------YLAYTLPHAPLQV--------------PDDGP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 246 NEVKNS-TEIYAYArtttaddisFQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLgEHNFLGKH 324
Cdd:cd16145 211 YKYKPKdPGIYAYL---------PWPQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHS-EGGSEHDP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 325 NLMD---------RSTH-----VPLIVRVPGL-KKGKT-KSMVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTNLKAK 388
Cdd:cd16145 281 DFFDsngplrgykRSLYeggirVPFIARWPGKiPAGSVsDHPSAFWDFMPTLADLAGAEPPED-IDGISLLPTLLGKPQQ 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1765882875 389 IKDQvYIQWE----GGDNAVSNrynyAEWK------QKEKIhsrMLFDHHIDPEENKN 436
Cdd:cd16145 360 QQHD-YLYWEfyegGGAQAVRM----GGWKavrhgkKDGPF---ELYDLSTDPGETNN 409
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
17-454 |
2.15e-50 |
|
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: 177.96 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYSAYASKdcpt 95
Cdd:cd16156 2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDN---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 96 AIPISRWFTSHGYYTISNGKvfHHLSDHanswsepPYRKH---PDGYDV-YWAEYNKW--ELWMNEASARTINPKTMRGP 169
Cdd:cd16156 78 VKTIGQRLSDNGIHTAYIGK--WHLDGG-------DYFGNgicPQGWDPdYWYDMRNYldELTEEERRKSRRGLTSLEAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 170 fcEWAEVPDTAYDDGKLALKAIAdlkrlKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPVANNRFrpKDLPNEVK 249
Cdd:cd16156 149 --GIKEEFTYGHRCTNRALDFIE-----KHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAY--DDLENKPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 250 NStEIYAYARTTTADDiSFQKEAKhGYYACLSYVDAQIGKVLDALDElgLANNTIVVLLGDHGWHLGEHNFLGKHNLM-D 328
Cdd:cd16156 220 HQ-RLWAGAKPHEDGD-KGTIKHP-LYFGCNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLWAKGPAVyD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 329 RSTHVPLIVRVPG-LKKGKTKSM-VEFVDLYPTLCELCHLPIPKnQLDGTSFVPILTNLKAKIKDQVYIQWeggdnavsN 406
Cdd:cd16156 295 EITNIPLIIRGKGgEKAGTVTDTpVSHIDLAPTILDYAGIPQPK-VLEGESILATIEDPEIPENRGVFVEF--------G 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765882875 407 RY-----NYAEW---------KQKEKIH---SRMLFDHHIDPEENKNRVNERKYRSEINKLSSFL 454
Cdd:cd16156 366 RYevdhdGFGGFqpvrcvvdgRYKLVINllsTDELYDLEKDPYEMHNLIDDPDYADVRDQLHDEL 430
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-380 |
4.51e-49 |
|
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: 168.57 E-value: 4.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMRP-ELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPhypdrfvnySAYASKDcp 94
Cdd:cd16149 1 PNILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMP---------SQHGIHD-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 taipisrWFTSHGYytiSNGKVFHHLSDHANSWSEppyRKHPDGYdvYWAEYNKWELwmneasartinpktmrGpfcewa 174
Cdd:cd16149 70 -------WIVEGSH---GKTKKPEGYLEGQTTLPE---VLQDAGY--RCGLSGKWHL----------------G------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 175 evpdtayDDgklalkAIADLKRLKEQGKPFFMACGFWKPHLPfnapkkywdlydrekipvannrfrpkdlpnevknstei 254
Cdd:cd16149 113 -------DD------AADFLRRRAEAEKPFFLSVNYTAPHSP-------------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 255 yayartttaddisfqkeakHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGK------HNLMD 328
Cdd:cd16149 142 -------------------WGYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtfpLNMYD 202
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1765882875 329 RSTHVPLIVRVPGLKKG--KTKSMVEFVDLYPTLCELCHLPIPKNQ-LDGTSFVP 380
Cdd:cd16149 203 NSVKVPFIIRWPGVVPAgrVVDSLVSAYDFFPTLLELAGVDPPADPrLPGRSFAD 257
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-436 |
4.15e-48 |
|
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: 169.32 E-value: 4.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNiPVSGASRASLLTGVYPHypdRfvNYSAYASKDcPT 95
Cdd:cd16151 2 NIILIMADDLGYEcIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNF---R--NYVVFGYLD-PK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 96 AIPISRWFTSHGYYTISNGKvfhhlsdhansW---SEPPYRKHPdgYDVYWAEYNKWELW-MNEASARTINPKtmrgPFC 171
Cdd:cd16151 75 QKTFGHLLKDAGYATAIAGK-----------WqlgGGRGDGDYP--HEFGFDEYCLWQLTeTGEKYSRPATPT----FNI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 172 EWAEVPDTAYDD-G-KLALKAIAD-LKRLKEQgkPFF----MACgfwkPHLPFNapkkywdlydrekipvannrfrpkDL 244
Cdd:cd16151 138 RNGKLLETTEGDyGpDLFADFLIDfIERNKDQ--PFFayypMVL----VHDPFV------------------------PT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 245 PNevknsteiyayarTTTADDISFQKEAKHGYY-ACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFL-- 321
Cdd:cd16151 188 PD-------------SPDWDPDDKRKKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTng 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 322 -----GKHNLMDRSTHVPLIVRVPGLKKGK--TKSMVEFVDLYPTLCELCHLPIPKN-QLDGTSFVPILTNLKAKIKDQV 393
Cdd:cd16151 255 revrgGKGKTTDAGTHVPLIVNWPGLIPAGgvSDDLVDFSDFLPTLAELAGAPLPEDyPLDGRSFAPQLLGKTGSPRREW 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1765882875 394 YIQWEGGDNAVSNRY--NYAEWKQKEKIHsrmLFDHHIDPEENKN 436
Cdd:cd16151 335 IYWYYRNPHKKFGSRfvRTKRYKLYADGR---FFDLREDPLEKNP 376
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
17-436 |
1.26e-47 |
|
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: 168.88 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDM-RPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNiPVSGASRASLLTGVYPH-------YPDRfvnysAY 88
Cdd:cd16146 2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFrtgvwhtILGR-----ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 89 ASKDCPTaipISRWFTSHGYYTISNGKvfHHLSDhanswsEPPYRKHPDGYD-VYWAEYNKWE----LWMNEASARTIN- 162
Cdd:cd16146 76 MRLDETT---LAEVFKDAGYRTGIFGK--WHLGD------NYPYRPQDRGFDeVLGHGGGGIGqypdYWGNDYFDDTYYh 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 163 ---PKTMRGpFCewaevPDTAYDDgklALKAIAdlkrlKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKIPvannrf 239
Cdd:cd16146 145 ngkFVKTEG-YC-----TDVFFDE---AIDFIE-----ENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLD------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 240 rpkdlpnevknsteiyayarTTTAddisfqkeakhGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHG-WHLGEH 318
Cdd:cd16146 205 --------------------DKLA-----------AFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGpAGGVPK 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 319 NFLG-----KHNLMDRSTHVPLIVRVPG--LKKGKTKSMVEFVDLYPTLCELCHLPIPKN-QLDGTSFVPILTNLKAKIK 390
Cdd:cd16146 254 RFNAgmrgkKGSVYEGGHRVPFFIRWPGkiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEGiKLDGRSLLPLLKGESDPWP 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1765882875 391 DQV-YIQWEGGDNAVSNRYNYAEWKQK-----EKIHSRMLFDHHIDPEENKN 436
Cdd:cd16146 334 ERTlFTHSGRWPPPPKKKRNAAVRTGRwrlvsPKGFQPELYDIENDPGEEND 385
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
17-439 |
5.47e-45 |
|
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: 161.56 E-value: 5.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPELGCYgvkEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPH-------------YPdrfv 83
Cdd:cd16147 3 NIVLILTDDQDVELGSM---DPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHnhgvtnnsppgggYP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 84 nySAYASKDCPTAIPIsrWFTSHGYYTISNGKVFhhlsdhaNSWSEPPYRKH-PDGYDvYWA------EYNKWELWMNEA 156
Cdd:cd16147 76 --KFWQNGLERSTLPV--WLQEAGYRTAYAGKYL-------NGYGVPGGVSYvPPGWD-EWDglvgnsTYYNYTLSNGGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 157 SARTINPktmrgpfcewaevpDTAYDDGKLALKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYWDLY--DREKIPV 234
Cdd:cd16147 144 GKHGVSY--------------PGDYLTDVIANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFpnVTAPPRP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 235 ANNRFRPKDLPNEVKNSTeiyayarTTTADDISFQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWH 314
Cdd:cd16147 210 PPNNPDVSDKPHWLRRLP-------PLNPTQIAYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 315 LGEHNFL-GKHNLMDRSTHVPLIVRVPGLKKGKT-KSMVEFVDLYPTLCELCHLPIPkNQLDGTSfvpiltnlkakikdq 392
Cdd:cd16147 283 LGQHRLPpGKRTPYEEDIRVPLLVRGPGIPAGVTvDQLVSNIDLAPTILDLAGAPPP-SDMDGRS--------------- 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1765882875 393 vyiqWEGGDNA-------VSNRYN--YAEWKQKEkihsRMLFDHHIDPEENKNRVN 439
Cdd:cd16147 347 ----CGDSNNNtykcvrtVDDTYNllYFEWCTGF----RELYDLTTDPYQLTNLAG 394
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-414 |
2.56e-43 |
|
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: 154.67 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 16 MNVLFLMADDMR-PELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYSAYASKDCP 94
Cdd:cd16035 1 PNILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 TAIP-ISRWFTSHGYYTISNGKvfHHLSDHAnswseppyrkhpdgydvyWAEYNKWELWMNEAsartinpktmrgpfCEW 173
Cdd:cd16035 81 PDVPtLGHMLRAAGYYTAYKGK--WHLSGAA------------------GGGYKRDPGIAAQA--------------VEW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 174 aevpdtayddgklalkaIADLKRLKEQGKPFFMACGFWKPH---LPFNAPKKYWDLydrekipvanNRFrpkdlpnevkn 250
Cdd:cd16035 127 -----------------LRERGAKNADGKPWFLVVSLVNPHdimFPPDDEERWRRF----------RNF----------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 251 steiyayartttaddisfqkeakhgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLM-DR 329
Cdd:cd16035 169 -------------------------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAyEE 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 330 STHVPLIVRVPGLKKG--KTKSMVEFVDLYPTLCELCHLPIPKNQ-----LDGTSFVPILTNLKAK-IKDQVYiqweggd 401
Cdd:cd16035 224 ALHVPLIISHPDLFGTgqTTDALTSHIDLLPTLLGLAGVDAEARAteappLPGRDLSPLLTDADADaVRDGIL------- 296
|
410
....*....|...
gi 1765882875 402 navsnrYNYAEWK 414
Cdd:cd16035 297 ------FTYDRYK 303
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
17-436 |
7.07e-43 |
|
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: 156.06 E-value: 7.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRP-ELGCYGvKEVKTPNIDRFAASGLLFQNAYcNIPVSGASRASLLTGVYPH---------YPDRFVNYS 86
Cdd:cd16025 4 NILLILADDLGFsDLGCFG-GEIPTPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHqvgmgtmaeLATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 87 AYASKDCPTaipISRWFTSHGYYTISNGKvfHHLSdhanswseppyrkhPDGYdvywaeYNkwelwmneasartinpktm 166
Cdd:cd16025 82 GYLPDSAAT---IAEVLKDAGYHTYMSGK--WHLG--------------PDDY------YS------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 167 rgpfcewaevpDTAYDDgklalKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYWDLYD----------RE------ 230
Cdd:cd16025 118 -----------TDDLTD-----KAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKgkydagwdalREerlerq 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 231 ----------KIPVANNRFRP-KDLPNEVKNST----EIYAyartttaddisfqkeakhgyyACLSYVDAQIGKVLDALD 295
Cdd:cd16025 182 kelglipadtKLTPRPPGVPAwDSLSPEEKKLEarrmEVYA---------------------AMVEHMDQQIGRLIDYLK 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 296 ELGLANNTIVVLLGD------HGW-HLGEHNF-LGKHNLMDRSTHVPLIVRVPGLKK---GKTKSMVEFVDLYPTLCELC 364
Cdd:cd16025 241 ELGELDNTLIIFLSDngasaePGWaNASNTPFrLYKQASHEGGIRTPLIVSWPKGIKakgGIRHQFAHVIDIAPTILELA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 365 HLPIPKN-------QLDGTSFVPILTNLKAKIKDQVYIqWEGGDN---------AVSNRYNYAEWKQKEkihsrmLFDHH 428
Cdd:cd16025 321 GVEYPKTvngvpqlPLDGVSLLPTLDGAAAPSRRRTQY-FELFGNrairkggwkAVALHPPPGWGDQWE------LYDLA 393
|
....*...
gi 1765882875 429 IDPEENKN 436
Cdd:cd16025 394 KDPSETHD 401
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-457 |
1.31e-42 |
|
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: 154.69 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 15 KMNVLFLMADDMRPE-LGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNysayaskdc 93
Cdd:cd16152 1 KPNVIVFFTDQQRWDtLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 94 ptAIPISRwftshGYYTISngkvfHHLSDhanswseppyrkhpDGYDVywAEYNKWELwmneASARTinpktmrgpfcew 173
Cdd:cd16152 72 --GIPLPA-----DEKTLA-----HYFRD--------------AGYET--GYVGKWHL----AGYRV------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 174 aevpDTAYDdgkLALKAIADlkrlKEQGKPFFMACGFWKPHLP-----FNAPKKYwdlydREKIPvanNRFRPKDLPNEV 248
Cdd:cd16152 107 ----DALTD---FAIDYLDN----RQKDKPFFLFLSYLEPHHQndrdrYVAPEGS-----AERFA---NFWVPPDLAALP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 249 KNSTEIYAyartttaddisfqkeakhGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLMD 328
Cdd:cd16152 168 GDWAEELP------------------DYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAEYKRSCHE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 329 RSTHVPLIVRVPGLKKGKT-KSMVEFVDLYPTLCELCHLPIPkNQLDGTSFVPILTNLKAKIKDQVYIQ----WEGgdNA 403
Cdd:cd16152 230 SSIRVPLVIYGPGFNGGGRvEELVSLIDLPPTLLDAAGIDVP-EEMQGRSLLPLVDGKVEDWRNEVFIQisesQVG--RA 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765882875 404 V-SNRYNYA-------EWKQK--EKIHSRMLFDHHIDPEENKNRVNERKYRSEINKLSSFLKAK 457
Cdd:cd16152 307 IrTDRWKYSvaapdkdGWKDSgsDVYVEDYLYDLEADPYELVNLIGRPEYREVAAELRERLLAR 370
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
17-436 |
5.71e-42 |
|
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: 153.49 E-value: 5.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDM-RPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHypdRFVNYSAYASKDCPT 95
Cdd:cd16026 3 NIVVILADDLgYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPV---RVGLPGVVGPPGSKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 96 AIP-----ISRWFTSHGYYTISNGKvfHHLSDHANSWsepPYRkHpdGYDVYW-AEYNkweLWMNEASARTINPKTMRGP 169
Cdd:cd16026 80 GLPpdeitIAEVLKKAGYRTALVGK--WHLGHQPEFL---PTR-H--GFDEYFgIPYS---NDMWPFPLYRNDPPGPLPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 170 FCEWAEVPDTAYDDGKL----ALKAIADLKRlkEQGKPFFMACGFWKPHLPFNAPKKywdlydrekipvannrfrpkdlp 245
Cdd:cd16026 149 LMENEEVIEQPADQSSLtqryTDEAVDFIER--NKDQPFFLYLAHTMPHVPLFASEK----------------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 246 nevknsteiyayartttaddisFQKEAKHGYY-ACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLG-- 322
Cdd:cd16026 204 ----------------------FKGRSGAGLYgDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGGsa 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 323 ------KHNLMDRSTHVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPKNQ-LDGTSFVPILTNlKAKIKDQV 393
Cdd:cd16026 262 gplrggKGTTWEGGVRVPFIAWWPGVIPAGTVSdeLASTMDLLPTLAALAGAPLPEDRvIDGKDISPLLLG-GSKSPPHP 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1765882875 394 YIQWEGGD--NAV-SNRYNYAEWKQKEKIHSR-----------MLFDHHIDPEENKN 436
Cdd:cd16026 341 FFYYYDGGdlQAVrSGRWKLHLPTTYRTGTDPggldptkleppLLYDLEEDPGETYN 397
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
17-363 |
3.36e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 143.33 E-value: 3.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMR-PELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYSAYASKDCPT 95
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRTEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 96 aipISRWFTSHGYYTISNGKvFHhlsdhaNSWSEppyRKHP--DGYDvYWAEYNKWELWMNEasartinpKTMRGPFCEW 173
Cdd:pfam00884 82 ---LPDLLKRAGYNTGAIGK-WH------LGWYN---NQSPcnLGFD-KFFGRNTGSDLYAD--------PPDVPYNCSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 174 AEVPDTAYddgklaLKAIADLkrLKEQGKPFFMACGFWKPHLPFNAPKKYWDLYDREKipvannrfrpkdlpnevknste 253
Cdd:pfam00884 140 GGVSDEAL------LDEALEF--LDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFK---------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 254 iyayartttaDDISFQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNF---LGKHNLMDRS 330
Cdd:pfam00884 190 ----------PSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGylhGGKYDNAPEG 259
|
330 340 350
....*....|....*....|....*....|....*.
gi 1765882875 331 -THVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCEL 363
Cdd:pfam00884 260 gYRVPLLIWSPGGKAKGQKSeaLVSHVDLFPTILDL 295
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-436 |
5.36e-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: 293762 [Multi-domain] Cd Length: 395 Bit Score: 145.42 E-value: 5.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRP-ELGCYGVKE-VKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHypdRFVNYSAYASKDCP 94
Cdd:cd16143 2 NIVIILADDLGYgDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPW---RSRLKGGVLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 95 TAIP-----ISRWFTSHGYYTISNGKVfhHLS-DHANSWSEPPYRKHPDGYDvywaeYNKWELwmneasartinpktmRG 168
Cdd:cd16143 79 PLIEpdrvtLAKMLKQAGYRTAMVGKW--HLGlDWKKKDGKKAATGTGKDVD-----YSKPIK---------------GG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 169 P----FCEWAEVPDTAYDDgKLALKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKYwdlydrekipvannrfrpkdl 244
Cdd:cd16143 137 PldhgFDYYFGIPASEVLP-TLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEF--------------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 245 pnevKNSTEIYAYArtttadDisFQKEakhgyyaclsyVDAQIGKVLDALDELGLANNTIVVLLGDHG-------WHLGE 317
Cdd:cd16143 195 ----QGKSGAGPYG------D--FVYE-----------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEK 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 318 HN------FLG-KHNLMDRSTHVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPKNQ-LDGTSFVPILTNLK- 386
Cdd:cd16143 252 FGhdpsgpLRGmKADIYEGGHRVPFIVRWPGKIPAGSVSdqLVSLTDLFATLAAIVGQKLPDNAaEDSFSFLPALLGPKk 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765882875 387 AKIKDQVYIQWEGGDNAV------------SNRYNYAEWKQKEKIHSRMLFDHHIDPEENKN 436
Cdd:cd16143 332 QEVRESLVHHSGNGSFAIrkgdwklidgtgSGGFSYPRGKEKLGLPPGQLYNLSTDPGESNN 393
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-414 |
2.21e-32 |
|
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: 126.49 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDM-RPELGCYG---VKEVKTPNIDRFAASGLLFQNAY----CNipvsgASRASLLTGvypHYPDRFVNYSA- 87
Cdd:cd16142 2 NILVILGDDIgWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYvepsCT-----PGRAAFITG---RHPIRTGLTTVg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 88 ------YASKDCPTaipISRWFTSHGYYTISNGKvfHHLSDHanswsePPYRKHPDGYDVYWaeYNKWelwmneasarti 161
Cdd:cd16142 74 lpgspgGLPPWEPT---LAELLKDAGYATAQFGK--WHLGDE------DGRLPTDHGFDEFY--GNLY------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 162 npktmrgpfcewaevpdtAYDDGKLALKAIADLKRLKEQGKPFFMACGFWKPHLPfNAPKKywdlydrekipvannRFRP 241
Cdd:cd16142 129 ------------------HTIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFP-TLPSP---------------EFEG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 242 KdlpnevknSTEIYAYArtttaddisfqkeakhgyyACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHL------ 315
Cdd:cd16142 175 K--------SSGKGKYA-------------------DSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQdvwpdg 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 316 GEHNFLG-KHNLMDRSTHVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCEL--CHLPIPKNQ-----LDGTSFVPILTnL 385
Cdd:cd16142 228 GYTPFRGeKGTTWEGGVRVPAIVRWPGKIKPGRVSneIVSHLDWFPTLAALagAPDPKDKLLgkdrhIDGVDQSPFLL-G 306
|
410 420
....*....|....*....|....*....
gi 1765882875 386 KAKIKDQVYIQWEGGDNAVSNRYNyaEWK 414
Cdd:cd16142 307 KSEKSRRSEFFYFGEGELGAVRWK--NWK 333
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
17-384 |
1.74e-29 |
|
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: 118.41 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPELGCY-GVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYSAYaSKDCPT 95
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGL-DPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 96 AIPISRwftSHGYYTISNGKVFHHLSDHANSwseppyrkhpdgydvywaeyNKWELWMNEAS------AR-----TINPK 164
Cdd:cd16171 81 WMDRLE---KHGYHTQKYGKLDYTSGHHSVS--------------------NRVEAWTRDVPfllrqeGRptvnlVGDRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 165 TMRGPFCEWAEVpdtayddgKLALKAIadLKRLKEQGKPFFMACGFWKPHlPFNAPKkywdlydrekipvANNRFrpkdl 244
Cdd:cd16171 138 TVRVMLKDWQNT--------DKAVHWI--RKEAPNLTQPFALYLGLNLPH-PYPSPS-------------MGENF----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 245 pNEVKNsteIYAYartttaddisfqkeakhgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKH 324
Cdd:cd16171 189 -GSIRN---IRAF------------------YYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKM 246
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1765882875 325 NLMDRSTHVPLIVRVPGLKKGKTKS-MVEFVDLYPTLCELCHLPIPKNqLDGTSFVPILTN 384
Cdd:cd16171 247 SMYEGSSHVPLLIMGPGIKAGQQVSdVVSLVDIYPTMLDIAGVPQPQN-LSGYSLLPLLSE 306
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-434 |
1.96e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 118.61 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDM-RPELGCYGVKEVK--TPNIDRFAASGLLFQNAYCNiPVSGASRASLLTGVYP-HYPDRFVNYSAYASkd 92
Cdd:cd16154 2 NILLIIADDQgLDSSAQYSLSSDLpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGfRTGVLAVPDELLLS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 93 cPTAIPISRW--FTSHGYYTISNGKvfHHLSDHANSWSEPPYRKH-----PDGYDVYWAeynkWELwmneasarTINPKT 165
Cdd:cd16154 79 -EETLLQLLIkdATTAGYSSAVIGK--WHLGGNDNSPNNPGGIPYyagilGGGVQDYYN----WNL--------TNNGQT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 166 MrgpfcewaevPDTAYDDGKLALKAIadlKRLKEQGKPFFMACGFWKPHLPFNAPkkywdlydrekipvannrfrpkdlP 245
Cdd:cd16154 144 T----------NSTEYATTKLTNLAI---DWIDQQTKPWFLWLAYNAPHTPFHLP------------------------P 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 246 NEVknsteiyaYARTTTADDISFQKEAKHGYYACLSYVDAQIGKVLDALDELGLaNNTIVVLLGDHG--------WHLGE 317
Cdd:cd16154 187 AEL--------HSRSLLGDSADIEANPRPYYLAAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDNGtpgqvvdlPYTRN 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 318 HnflGKHNLMDRSTHVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPkNQLDGTSFVPILTNLKAKIKDQVYI 395
Cdd:cd16154 258 H---AKGSLYEGGINVPLIVSGAGVERANEREsaLVNATDLYATIAELAGVDAA-EIHDSVSFKPLLSDVNASTRQYNYT 333
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1765882875 396 QWEGGD---NAVSNRYNYaeWKQKEKiHSRMLFDHHIDPEEN 434
Cdd:cd16154 334 EYESPTttgWATRNQYYK--LIESEN-GQEELYDLINDPSEQ 372
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
17-463 |
2.83e-24 |
|
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: 105.22 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDM-RPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPH----YPDRFVNYSayaSK 91
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVrsgvYPGVFYPGS---RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 92 DCP-TAIPISRWFTSHGYYTISNGKvfHHLSDHANSWSEPPYRkhpdGYDVYWA-EY--------NKWELWMNEASARTI 161
Cdd:cd16158 80 GLPlNETTIAEVLKTVGYQTAMVGK--WHLGVGLNGTYLPTHQ----GFDHYLGiPYshdqgpcqNLTCFPPNIPCFGGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 162 NPKTMRGPFC-------EWAEVPDTAYDDGKLALKAIADLKRlkeQGKPFFMACGFWKPHLPFNAPKKYwdlydrekipv 234
Cdd:cd16158 154 DQGEVPCPLFynesivqQPVDLLTLEERYAKFAKDFIADNAK---EGKPFFLYYASHHTHYPQFAGQKF----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 235 annrfrpkdlpnevKNSTeiyayARTTTADdisfqkeakhgyyaCLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWH 314
Cdd:cd16158 220 --------------AGRS-----SRGPFGD--------------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPS 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 315 L------GEHNFL--GKHNLMDRSTHVPLIVRVPG-LKKGKTKSMVEFVDLYPTLCELCHLPIPKNQLDGTSFVPILTNL 385
Cdd:cd16158 267 TmrksrgGNAGLLkcGKGTTYEGGVREPAIAYWPGrIKPGVTHELASTLDILPTIAKLAGAPLPNVTLDGVDMSPILFEQ 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 386 KAKIKDQV-----YIQWEGGDNAVSNRYNYAEWKQKEKIHSR-------------------MLFDHHIDPEENKNRVNER 441
Cdd:cd16158 347 GKSPRQTFfyyptSPDPDKGVFAVRWGKYKAHFYTQGAAHSGttpdkdchpsaeltshdppLLFDLSQDPSENYNLLGLP 426
|
490 500
....*....|....*....|..
gi 1765882875 442 KYRSEINKLSSfLKAKKETLMK 463
Cdd:cd16158 427 EYNQVLKQIQQ-VKERFEASMK 447
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
40-363 |
4.13e-23 |
|
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: 98.52 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 40 TPNIDRFAASGLLFQNAYCNIPVSGASRA--SLLTGVYPhYPDRFVNYSAYASKDCPTaipISRWFTSHGYYTISngkvF 117
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPP-LPLGSGSYTLYKLNPLPS---LPSILKEQGYETIF----I 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 118 HhlSDHANSWSeppyRK--HPD-GYDVYWAEYNkwelwMNEASARTINPKtmrgpfcewaevpdtaYDDGKLALKAIADL 194
Cdd:cd16015 98 H--GGDASFYN----RDsvYPNlGFDEFYDLED-----FPDDEKETNGWG----------------VSDESLFDQALEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 195 KRLKEQgkPFF-----MAcgfwkPHLPFNAPKKYWDLYdrekipvannrFRPKDLPNEVKNsteiyayartttaddisfq 269
Cdd:cd16015 151 EELKKK--PFFiflvtMS-----NHGPYDLPEEKKDEP-----------LKVEEDKTELEN------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 270 keakhgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLMDRStHVPLIVRVPGLKKGKTKS 349
Cdd:cd16015 194 ------YLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY-RTPLLIYSPGLKKPKKID 266
|
330
....*....|....*
gi 1765882875 350 MV-EFVDLYPTLCEL 363
Cdd:cd16015 267 RVgSQIDIAPTLLDL 281
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
15-384 |
1.86e-21 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 96.97 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 15 KMNVLFLMADDMR-PELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYP-------HYPDRFVNYS 86
Cdd:cd16159 1 KPNIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmasSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 87 AYASKDCPTAIPISRWFTSHGYYTISNGKvfHHLSDHANSWSEPPYrkHPD--GYDVYWA-------EYNKWELWMNEAS 157
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGK--WHLGLHCESRNDFCH--HPLnhGFDYFYGlpltnlkDCGDGSNGEYDLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 158 ARTINPKTMrgpfcewAEVPdtayddgkLALKAIADLKRLKEQGKPFFMAC-----GFWKPHLPFNAPKKYWD--LYDRE 230
Cdd:cd16159 157 FDPLFPLLT-------AFVL--------ITALTIFLLLYLGAVSKRFFVFLlilslLFISLFFLLLITNRYFNciLMRNH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 231 KI---PVANNRFRPKdLPNE----VKNSTE-----IYAYARTTTADDIS--FQKEAKHGYY-ACLSYVDAQIGKVLDALD 295
Cdd:cd16159 222 EVveqPMSLENLTQR-LTKEaisfLERNKErpfllVMSFLHVHTALFTSkkFKGRSKHGRYgDNVEEMDWSVGQILDALD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 296 ELGLANNTIVVLLGDHGWHLGE---------HNFL----GKHNLMDRSTHVPLIVRVPG-LKKGK-----TKSMvefvDL 356
Cdd:cd16159 301 ELGLKDNTFVYFTSDNGGHLEEisvggeyggGNGGiyggKKMGGWEGGIRVPTIVRWPGvIPPGSvidepTSLM----DI 376
|
410 420
....*....|....*....|....*....
gi 1765882875 357 YPTLCELCHLPIPKNQL-DGTSFVPILTN 384
Cdd:cd16159 377 FPTVAALAGAPLPSDRIiDGRDLMPLLTG 405
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
15-465 |
3.68e-21 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 95.61 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 15 KMNVLFLMADDMR-PELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYP----HYPDRFVNYSAYA 89
Cdd:cd16157 1 KPNIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPirngFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 90 SKDCPTAIP-----ISRWFTSHGYYTISNGK-------VFHHLSDHANSWSEPPyRKHPDGYDvywaeynkwelwmneas 157
Cdd:cd16157 81 PQNIVGGIPdseilLPELLKKAGYRNKIVGKwhlghrpQYHPLKHGFDEWFGAP-NCHFGPYD----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 158 artiNPKTMRGPFCEWAEVPDTAYDDGKLALK-------------AIADLKRLKEQGKPFFMacgFWKP---HLPFNAPK 221
Cdd:cd16157 143 ----NKAYPNIPVYRDWEMIGRYYEEFKIDKKtgesnltqiylqeALEFIEKQHDAQKPFFL---YWAPdatHAPVYASK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 222 KYWDLYDREKipvannrfrpkdlpnevknsteiyayartttaddisfqkeakhgYYACLSYVDAQIGKVLDALDELGLAN 301
Cdd:cd16157 216 PFLGTSQRGL--------------------------------------------YGDAVMELDSSVGKILESLKSLGIEN 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 302 NTIVVLLGDHGWHL------GEHN--FL-GKHNLMDRSTHVPLIVRVPG-LKKGKTKSMV-EFVDLYPTLCELCHLPIPK 370
Cdd:cd16157 252 NTFVFFSSDNGAALisapeqGGSNgpFLcGKQTTFEGGMREPAIAWWPGhIKPGQVSHQLgSLMDLFTTSLALAGLPIPS 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 371 N-QLDGTSFVPILTNLKAKIKDQVYIQ------------------WEGGDNAVSNRYNYAEWKQKEKIHSRMLFDH---- 427
Cdd:cd16157 332 DrAIDGIDLLPVLLNGKEKDRPIFYYRgdelmavrlgqykahfwtWSNSWEEFRKGINFCPGQNVPGVTTHNQTDHtklp 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1765882875 428 ---HI--DPEEN-KNRVNERKYRSEINKLSSFLKAKKETLMKSQ 465
Cdd:cd16157 412 llfHLgrDPGEKyPISFKSAEYKQAMPRISKVVQQHQKTLVPGE 455
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
8-377 |
6.06e-21 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 95.49 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 8 SVFSQTEKMNVLFLMADDM-RPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNipVSGASRA--SLLTGVYPhyPDRFVN 84
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQ--GGRTSRGefAVLTGLPP--LPGGSP 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 85 YSAYASKDCPTaipISRWFTSHGYYTIsngkVFHhlSDHANSWSEPPYRKHpDGYDVYWAEYNkwelwMNEASARTinpk 164
Cdd:COG1368 303 YKRPGQNNFPS---LPSILKKQGYETS----FFH--GGDGSFWNRDSFYKN-LGFDEFYDRED-----FDDPFDGG---- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 165 tmrgpfceWAevpdtaYDDGKLALKAIadlKRLKEQGKPFF-----MAcgfwkPHLPFNAPKKYWDLYDREKIPVANnrf 239
Cdd:COG1368 364 --------WG------VSDEDLFDKAL---EELEKLKKPFFaflitLS-----NHGPYTLPEEDKKIPDYGKTTLNN--- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 240 rpkdlpnevknsteiyayartttaddisfqkeakhgYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDH-GWHLGEH 318
Cdd:COG1368 419 ------------------------------------YLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHgPRSPGKT 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 319 NFLGKHNLMdrstHVPLIVRVPGLKKGKT-KSMVEFVDLYPTLCELCHLPIPKNQLDGTS 377
Cdd:COG1368 463 DYENPLERY----RVPLLIYSPGLKKPKViDTVGSQIDIAPTLLDLLGIDYPSYYAFGRD 518
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
15-439 |
1.29e-19 |
|
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: 90.95 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 15 KMNVLFLMADDM-RPELGCYGVKEVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPH----YPDRFVNYsAYA 89
Cdd:cd16160 1 KPNIVLFFADDMgYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIrsgmYGGTRVFL-PWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 90 SKDCP-TAIPISRWFTSHGYYTISNGKvFH------------HLSDH------------ANSWSEPPYRKHPDGYDVywa 144
Cdd:cd16160 80 IGGLPkTEVTMAEALKEAGYTTGMVGK-WHlginennhsdgaHLPSHhgfdfvgtnlpfTNSWACDDTGRHVDFPDR--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 145 eyNKWELWMN-EASARTINPKTMrgpfcewaevPDTAYDDGKlalKAIADlkrlkEQGKPFFMACGFWKPHLP-FNAPkk 222
Cdd:cd16160 156 --SACFLYYNdTIVEQPIQHEHL----------TETLVGDAK---SFIED-----NQENPFFLYFSFPQTHTPlFASK-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 223 ywdlydrekipvannRFRPKDLpnevknsteiyayaRTTTADDISFQKEAkhgyyaclsyvdaqIGKVLDALDELGLANN 302
Cdd:cd16160 214 ---------------RFKGKSK--------------RGRYGDNINEMSWA--------------VGEVLDTLVDTGLDQN 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 303 TIVVLLGDHGWHL------GEHNFL--GKHNLMDRSTHVPLIVRVPG-LKKGKTKSMVEFVDLYPTLCELC--HLPIPKN 371
Cdd:cd16160 251 TLVFFLSDHGPHVeyclegGSTGGLkgGKGNSWEGGIRVPFIAYWPGtIKPRVSHEVVSTMDIFPTFVDLAggTLPTDRI 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765882875 372 qLDGTSFVPILTNLKAKIKDQVYIQWEGGDNAVsnRYNyaewkqKEKIHsrmLFDHHIdPEENKNRVN 439
Cdd:cd16160 331 -YDGLSITDLLLGEADSPHDDILYYCCSRLMAV--RYG------SYKIH---FKTQPL-PSQESLDPN 385
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
17-363 |
1.42e-19 |
|
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: 87.48 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRP-ELGCYGVKEVKTPNIDRFAASGLLFQnAYCNIPVSG--ASRASLLTGVYPHYpdrfvnysayaskdc 93
Cdd:cd00016 2 HVVLIVLDGLGAdDLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTSsaPNHAALLTGAYPTL--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 94 ptaipisrwftsHGYYTisngkvfhhlsdhaNSWSEPPYRKHPDGYDvyWAEYNKWELwMNEASARTINpktmrgpfcew 173
Cdd:cd00016 66 ------------HGYTG--------------NGSADPELPSRAAGKD--EDGPTIPEL-LKQAGYRTGV----------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 174 aevpdtayddgkLALKAIADLKRLKeqgKPFFMACGFWKPHLPFnapkkywdlydrekipvannrfrpkdlpnevknste 253
Cdd:cd00016 106 ------------IGLLKAIDETSKE---KPFVLFLHFDGPDGPG------------------------------------ 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 254 iYAYARTTTaddisfqkeakhGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEHNFLGKHNLMDRSTH- 332
Cdd:cd00016 135 -HAYGPNTP------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHt 201
|
330 340 350
....*....|....*....|....*....|....*
gi 1765882875 333 ---VPLIVRVPGLKKGKTKS-MVEFVDLYPTLCEL 363
Cdd:cd00016 202 gmrVPFIAYGPGVKKGGVKHeLISQYDIAPTLADL 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
17-438 |
1.70e-19 |
|
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: 89.92 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDM--------RPELgcygvkeVKTPNIDRFAASGLLFQNAYCNiPVSGASRASLLTGVYPH----------- 77
Cdd:cd16029 2 HIVFILADDLgwndvgfhGSDQ-------IKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIhtgmqhgvila 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 78 ------------YPDRF--VNYS----------AYASKDCPTAipisRWFTSH-GYYtisNGKV--FHHLSDHANSWSEP 130
Cdd:cd16029 74 gepyglplnetlLPQYLkeLGYAthlvgkwhlgFYTWEYTPTN----RGFDSFyGYY---GGAEdyYTHTSGGANDYGND 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 131 PYRkhpDGYDVYWAEYNKW--ELWMNEAsARTINpktmrgpfcewaevpdtAYDdgklalkaiadlkrlkeQGKPFFMAC 208
Cdd:cd16029 147 DLR---DNEEPAWDYNGTYstDLFTDRA-VDIIE-----------------NHD-----------------PSKPLFLYL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 209 GFWKPHLPFNAPKKYWDLYDREKIPVAN-NRfrpkdlpnevknsteiyayaRTttaddisfqkeakhgYYACLSYVDAQI 287
Cdd:cd16029 189 AFQAVHAPLQVPPEYADPYEDKFAHIKDeDR--------------------RT---------------YAAMVSALDESV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 288 GKVLDALDELGLANNTIVVLLGDHGwhlGEHNFL----------GKHNLMDRSTHVPLIVRVPGLKKGK---TKSMVEFV 354
Cdd:cd16029 234 GNVVDALKAKGMLDNTLIVFTSDNG---GPTGGGdggsnyplrgGKNTLWEGGVRVPAFVWSPLLPPKRgtvSDGLMHVT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 355 DLYPTLCELC-HLPIPKNQLDGTSFVPILTNLKAKIKDQVYIQ----WEGGDNAVsnrYNYAEWKQkekIHSRMLFDHHI 429
Cdd:cd16029 311 DWLPTLLSLAgGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNiddiTRTTGGAA---IRVGDWKL---IVGKPLFNIEN 384
|
....*....
gi 1765882875 430 DPEENKNRV 438
Cdd:cd16029 385 DPCERNDLA 393
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
17-360 |
4.30e-19 |
|
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: 89.96 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 17 NVLFLMADDMRPELgcygVKEVKTPNIDRFAASGLLFQNAYcnipvSGASRA-----SLLTGVYPHYPDrfvnySAYASK 91
Cdd:COG3083 246 NILLIVVDSLRADM----LDPEVMPNLYAFAQRSLRFTNHY-----SSGNSTraglfGLFYGLPGNYWD-----SILAER 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 92 DCPTAIPIsrwFTSHGYytisngkVFHHLSdhANSWSEPPYRKhpdgydvywaeynkwelwmneASARTINPKTMRGPFC 171
Cdd:COG3083 312 TPPVLIDA---LQQQGY-------QFGLFS--SAGFNSPLFRQ---------------------TIFSDVSLPRLHTPGG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 172 EWaeVPDTayddgklalKAIADLKR-LKEQ--GKPFFmacGFwkphLPFNAPKKYWDLYDrekipvannrFRPKDLPNEV 248
Cdd:COG3083 359 PA--QRDR---------QITAQWLQwLDQRdsDRPWF---SY----LFLDAPHAYSFPAD----------YPKPFQPSED 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 249 KNsteiyaYARTTTADDisfQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWHLGEH--NFLGKHNL 326
Cdd:COG3083 411 CN------YLALDNESD---PTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENgqNYWGHNSN 481
|
330 340 350
....*....|....*....|....*....|....*
gi 1765882875 327 MDRS-THVPLIVRVPGLKKGKTKSMVEFVDLYPTL 360
Cdd:COG3083 482 FSRYqLQVPLVIHWPGTPPQVISKLTSHLDIVPTL 516
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
15-403 |
5.10e-16 |
|
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: 79.44 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 15 KMNVLFLMADDMR-PELGCYGVK-EVKTPNIDRFAASGLLFQNAYCNIPVSGASRASLLTGVYPHYPDRFVNYSAYASKD 92
Cdd:cd16161 1 KPNFLLLFADDLGwGDLGANWAPnAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 93 CP-TAIPISRWFTSHGYYTISNGKvfHHLSDHANswseppYRKHPDGYDVYWAEynkwelwmneasartinpktmrgPFC 171
Cdd:cd16161 81 LPlNETTLAEVLRQAGYATGMIGK--WHLGQREA------YLPNSRGFDYYFGI-----------------------PFS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 172 EWAEVPDtayddgKLALKAIADLKRLKEQGKPFFMACGFWKPHLPFNAPKKywdlydrekipvannrfrpkdlpnevKNS 251
Cdd:cd16161 130 HDSSLAD------RYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPR--------------------------FQS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 252 TeiyayartttaddisfqKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHG-W-----------HLGEHN 319
Cdd:cd16161 178 P-----------------TSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWevkcelavgpgTGDWQG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 320 FLG----KHNLMDRSTHVPLIVRVPGLKKGKTKS--MVEFVDLYPTLCELCHLPIPKNQL-DGTSFVPILTNlKAKIKDQ 392
Cdd:cd16161 241 NLGgsvaKASTWEGGHREPAIVYWPGRIPANSTSaaLVSTLDIFPTVVALAGASLPPGRIyDGKDLSPVLFG-GSKTGHR 319
|
410
....*....|.
gi 1765882875 393 VYIQWEGGDNA 403
Cdd:cd16161 320 CLFHPNSGAAG 330
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-367 |
2.16e-12 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 68.24 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 1 MLAFSSLSVFS--------QTEKMNVLFLMADDMRPELgcygVKEVKTPNIDRFAASGLLFQNAYCNIP-VSGASRASLL 71
Cdd:COG1524 1 MKRGLSLLLASllaaaaaaAPPAKKVVLILVDGLRADL----LERAHAPNLAALAARGVYARPLTSVFPsTTAPAHTTLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 72 TGVYPhypdrfvnysayaskdcptaipisrwfTSHGyytisngkVFhhlsdhanswseppyrkhpdGYDVYWAEYNKWEL 151
Cdd:COG1524 77 TGLYP---------------------------GEHG--------IV--------------------GNGWYDPELGRVVN 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 152 WMNEASARTINPKTMRGPfcewaevpdTAYDdgklalkaiadlkRLKEQGKPffMACGFWKphlPFNAPKkywdLYDREK 231
Cdd:COG1524 102 SLSWVEDGFGSNSLLPVP---------TIFE-------------RARAAGLT--TAAVFWP---SFEGSG----LIDAAR 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 232 IPVANNRFRPKDLPNEVKNSTEIYAYARTTTADDISF----------QkeaKHG-----YYACLSYVDAQIGKVLDALDE 296
Cdd:COG1524 151 PYPYDGRKPLLGNPAADRWIAAAALELLREGRPDLLLvylpdldyagH---RYGpdspeYRAALREVDAALGRLLDALKA 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 297 LGLANNTIVVLLGDHG---------------------------------------------------------WHLGEH- 318
Cdd:COG1524 228 RGLYEGTLVIVTADHGmvdvppdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaGHFGPHr 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1765882875 319 ----------------NFLGKH-NLMDRSTHVPLIVRVPGLKKGktksmVEFVDLYPTLCELCHLP 367
Cdd:COG1524 308 igdlvlvakpgwaldaPLKGSHgGLPDEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
271-363 |
3.52e-12 |
|
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: 66.45 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 271 EAKHGY-------YACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWH-LGEHNFLGKHNLMdrstHVPLIVRVPGL 342
Cdd:cd16018 169 SAGHKYgpdspevNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHGYDNELPDM----RAIFIARGPAF 244
|
90 100
....*....|....*....|.
gi 1765882875 343 KKGKTKSMVEFVDLYPTLCEL 363
Cdd:cd16018 245 KKGKKLGPFRNVDIYPLMCNL 265
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
280-371 |
1.21e-06 |
|
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: 49.87 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 280 LSYVDAQIGKVLDALDELGLANNTIVVLLGDHGWhlgehNFLGKH-NLMDRSTHVPLIVRVPGLKKGKTKSMVEF----- 353
Cdd:cd16024 173 LKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGM-----TDAGNHgGSSPGETSVPLLFISPKFSSKPSNADGELsyyet 247
|
90 100
....*....|....*....|.
gi 1765882875 354 ---VDLYPTLCELCHLPIPKN 371
Cdd:cd16024 248 vqqVDLAPTLALLLGLPIPKN 268
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
275-378 |
1.94e-04 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 43.59 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 275 GYYACLSYVDAQIGKVLDALDElglanNTIVVLLGDHG----WHLGEHnflgkhnlmdrsT--HVPLIVRVPGLKKG--- 345
Cdd:cd16009 293 GYAEALEEFDRRLPELLAKLKE-----DDLLIITADHGndptIGGTDH------------TreYVPLLVYGKGLKGVnlg 355
|
90 100 110
....*....|....*....|....*....|....*
gi 1765882875 346 --KTksmveFVDLYPTLCELCHLPIPKNqldGTSF 378
Cdd:cd16009 356 trET-----FADIGATIADNFGVEPPEN---GTSF 382
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
280-312 |
2.78e-04 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 42.79 E-value: 2.78e-04
10 20 30
....*....|....*....|....*....|...
gi 1765882875 280 LSYVDAQIGKVLDALDELGLANNTIVVLLGDHG 312
Cdd:pfam01663 191 LRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
331-369 |
6.14e-04 |
|
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 42.13 E-value: 6.14e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1765882875 331 THVPLIVRVPGLKKGKTKSMVEFVDLYPTLCELCHLPIP 369
Cdd:cd16016 409 THVPLLFYGWGIKPGEIPRPVEITDIAPTLAALLGIQPP 447
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
267-312 |
2.45e-03 |
|
uncharacterized Alkaline phosphatase subfamily; 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.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 39.81 E-value: 2.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1765882875 267 SFQKEAKHGYYACLSYVDAQIGKVLDALDELGLANNTIVVLLGDHG 312
Cdd:cd16021 169 FWLSELTHDYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHG 214
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
278-377 |
3.72e-03 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 39.71 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765882875 278 AClSYVDAQIGKVLDALDElglaNNTIVVLLGDHG-----WHLGEHNFLGKHnlmdrSTH-VPLIV-----RVPGLKKGK 346
Cdd:cd16010 408 AV-EAVDECLGRIVEAVLE----NGGTLLITADHGnaeemIDPETGGPHTAH-----TTNpVPFIIvdpglKRKLLKDGG 477
|
90 100 110
....*....|....*....|....*....|.
gi 1765882875 347 TKsmvefvDLYPTLCELCHLPIPKnQLDGTS 377
Cdd:cd16010 478 LA------DVAPTILDLLGIEKPK-EMTGKS 501
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
282-337 |
4.40e-03 |
|
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: 39.14 E-value: 4.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1765882875 282 YVDAQIGKVLDALDELGlaNNTIVVLLGDHGWHLGEHNFLGkHNLMDRS---THVPLIV 337
Cdd:cd16017 194 YTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYL-HGAPYAPkeqYHVPFII 249
|
|
| |
