|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
62-398 |
4.22e-163 |
|
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: 469.08 E-value: 4.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 GASGGLPTNETTFAKILKEKGYATGLI----------------------------------------------------- 168
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIgkwhlglhcesrndfchhplnhgfdyfyglpltnlkdcgdgsngeydlsfdpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 --------------------------------------------------------------------------------
Cdd:cd16159 161 fplltafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfncilmrnhevveqpmslenltqrltke 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 169 ----------------------------------------------------GRILDTLDVEGLSNSTLIYFTSDHGGSL 196
Cdd:cd16159 241 aisflernkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvGQILDALDELGLKDNTFVYFTSDNGGHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 197 ENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDRVIDGQDLL 276
Cdd:cd16159 321 EEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 277 PLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDLSR 356
Cdd:cd16159 401 PLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2462629488 357 DPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 398
Cdd:cd16159 480 DPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
62-362 |
1.35e-95 |
|
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: 292.54 E-value: 1.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRVLQWT 141
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 GASGGLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGkwhlghqpeflptrhgfdeyfgipysndmwpfplyrndppgplpplmeneev 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 ----------------------------------------------------------------------RILDTLDVEG 179
Cdd:cd16026 156 ieqpadqssltqrytdeavdfiernkdqpfflylahtmphvplfasekfkgrsgaglygdvveeldwsvgRILDALKELG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 180 LSNSTLIYFTSD---------HGGSleNQL-----GNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGE 245
Cdd:cd16026 236 LEENTLVIFTSDngpwleyggHGGS--AGPlrggkGTTWEGG-----------------VRVPFIAWWPGVIPAGTVSDE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 246 PTSLMDVFPTVVRLAGSEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPE 325
Cdd:cd16026 297 LASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGT 370
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462629488 326 GAGacygrkvcpcfGEKVVHHDPPLLFDLSRDPSETH 362
Cdd:cd16026 371 DPG-----------GLDPTKLEPPLLYDLEEDPGETY 396
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
44-362 |
9.70e-82 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 256.73 E-value: 9.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 123
Cdd:COG3119 5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 124 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGL------------------------------------ 167
Cdd:COG3119 85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALfgkwhlyltdlltdkaidflerqadkdkpfflylaf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 -------------------------------------------------------IGRILDTLDVEGLSNSTLIYFTSDH 192
Cdd:COG3119 158 naphapyqapeeyldkydgkdiplppnlaprdlteeelrraraayaamieevddqVGRLLDALEELGLADNTIVVFTSDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 193 GGSLENQlG-----NTQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQ 266
Cdd:COG3119 238 GPSLGEH-GlrggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 267 DrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhh 346
Cdd:COG3119 300 D--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------------YYDDD------------ 348
|
410
....*....|....*.
gi 2462629488 347 DPPLLFDLSRDPSETH 362
Cdd:COG3119 349 GPWELYDLKNDPGETN 364
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
62-379 |
1.10e-71 |
|
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: 232.32 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsiGYRV-LQW 140
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 141 TgaSGGLPTNETTFAKILKEKGYATGLIGR-------------------------------------------------- 170
Cdd:cd16160 79 D--IGGLPKTEVTMAEALKEAGYTTGMVGKwhlginennhsdgahlpshhgfdfvgtnlpftnswacddtgrhvdfpdrs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 --------------------------------------------------------------------------------
Cdd:cd16160 157 acflyyndtiveqpiqhehltetlvgdaksfiednqenpfflyfsfpqthtplfaskrfkgkskrgrygdninemswavg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 171 -ILDTLDVEGLSNSTLIYFTSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVL 237
Cdd:cd16160 237 eVLDTLVDTGLDQNTLVFFLSDHGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 238 PaGRVIGEPTSLMDVFPTVVRLAGSEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtmWKVHF 317
Cdd:cd16160 300 K-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHF 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462629488 318 VT---PVFQPEGAGACYGRKVCP------CFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMERV 379
Cdd:cd16160 372 KTqplPSQESLDPNCDGGGPLSDyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-365 |
1.73e-71 |
|
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: 229.34 E-value: 1.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssigYRVlQ 139
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 140 WTGASGGLPTNETTFAKILKEKGYATGL---------------------------------------------------- 167
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQfgkwhlgdedgrlptdhgfdefygnlyhtideeivdkaidfikrnakadkpf 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 ---------------------------------------IGRILDTLDVEGLSNSTLIYFTSDHG-----------GSLE 197
Cdd:cd16142 154 flyvnftkmhfptlpspefegkssgkgkyadsmvelddhVGQILDALDELGIADNTIVIFTTDNGpeqdvwpdggyTPFR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 198 NQLGNTQYGGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVP------QDRVID 271
Cdd:cd16142 234 GEKGTTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHID 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 272 GQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVtpVFQPEGAGACYGRKVCPCfgekvvhhdpPLL 351
Cdd:cd16142 297 GVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFYVLTF----------PLI 358
|
410
....*....|....
gi 2462629488 352 FDLSRDPSETHILT 365
Cdd:cd16142 359 FNLRRDPKERYDVT 372
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
63-274 |
3.13e-71 |
|
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: 224.24 E-value: 3.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssigyrVLQWTG 142
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 ASGGLPTNETTFAKILKEKGYATGL----------------------------------------------IGRILDTLD 176
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALigkwhdeaidfierrdkdkpfflyvsfnaphppfayyamvsaiddqIGRILDALE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 177 VEGLSNSTLIYFTSDHGGSLENqlGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTV 256
Cdd:cd16022 153 ELGLLDNTLIVFTSDHGDMLGD--HGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTL 220
|
250
....*....|....*...
gi 2462629488 257 VRLAGSEVPQDrvIDGQD 274
Cdd:cd16022 221 LDLAGIEPPEG--LDGRS 236
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
286-420 |
2.86e-60 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 191.76 E-value: 2.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 286 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 365
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462629488 366 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 420
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-362 |
1.77e-59 |
|
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: 199.69 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 A-------SGGLPTNETTFAKILKEKGYATGLIG---------------------------------------------- 169
Cdd:cd16144 81 TklipppsTTRLPLEEVTIAEALKDAGYATAHFGkwhlggeggygpedqgfdvniggtgnggppsyyfppgkpnpdledg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 -----------------------------------------------------------------------------RIL 172
Cdd:cd16144 161 pegeyltdrltdeaidfieqnkdkpfflylshyavhtpiqarpeliekyekkkkglrkgqknpvyaamiesldesvgRIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 173 DTLDVEGLSNSTLIYFTSDHGG-SLENQLGNTQY-----------GGwngiykggkgmggweggIRVPGIFRWPGVLPAG 240
Cdd:cd16144 241 DALEELGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRWPGVIKPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 241 RVIGEPTSLMDVFPTVVRLAGSEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYcerFLHAARWHQRDRGTM----WK-V 315
Cdd:cd16144 304 SVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWH---FPHYHGQGGRPASAIrkgdWKlI 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462629488 316 HFvtpvfqpegagacygrkvcpcfgekvvHHDPPL-LFDLSRDPSETH 362
Cdd:cd16144 381 EF---------------------------YEDGRVeLYNLKNDIGETN 401
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
62-365 |
3.02e-59 |
|
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: 198.08 E-value: 3.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRvlqw 140
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 141 tgASGGLPTNETTFAKILKEKGYATG------------------------------------------------------ 166
Cdd:cd16161 77 --SVGGLPLNETTLAEVLRQAGYATGmigkwhlgqreaylpnsrgfdyyfgipfshdssladryaqfatdfiqrasakdr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 167 ----------------------------------------LIGRILDTLDVEGLSNSTLIYFTSDHG-----GSLENQLG 201
Cdd:cd16161 155 pfflyaalahvhvplanlprfqsptsgrgpygdalqemddLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkCELAVGPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 202 NTQY---GGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDRVIDGQDLLPL 278
Cdd:cd16161 235 TGDWqgnLGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 279 LLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtmWKVHFVTpvfqpEGAGACygrkvCPCFGEKvVHHDPPLLFD 353
Cdd:cd16161 310 LFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALAC-----CGSTGPK-LYHDPPLLFD 371
|
410
....*....|..
gi 2462629488 354 LSRDPSETHILT 365
Cdd:cd16161 372 LEVDPAESFPLT 383
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
63-420 |
2.06e-57 |
|
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: 195.74 E-value: 2.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqwTG 142
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 ASGGLPTNETTFAKILKEKGYATGLIGR---------------------------------------------------- 170
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKwhlgvglngtylpthqgfdhylgipyshdqgpcqnltcfppnipcfggcdqg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 --------------------------------------------------------------------------------
Cdd:cd16158 157 evpcplfynesivqqpvdlltleeryakfakdfiadnakegkpfflyyashhthypqfagqkfagrssrgpfgdalaeld 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 171 -----ILDTLDVEGLSNSTLIYFTSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRW 233
Cdd:cd16158 237 gsvgeLLQTLKENGIDNNTLVFFTSDNGpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 234 PGVLPAGRVIgEPTSLMDVFPTVVRLAGSEVPqDRVIDGQDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdr 309
Cdd:cd16158 300 PGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK--- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 310 gtmWKVHFVT---PVFQPEGAGACYGRKvcpcfgeKVVHHDPPLLFDLSRDPSETHILTpaSEPVFYQVMERVQQAVWEH 386
Cdd:cd16158 375 ---YKAHFYTqgaAHSGTTPDKDCHPSA-------ELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERF 442
|
490 500 510
....*....|....*....|....*....|....*...
gi 2462629488 387 QRTLSPVPLQLDRLGNiwrPWLQPC----CGPFPLCWC 420
Cdd:cd16158 443 EASMKFGESEINKGED---PALEPCckpgCTPKPSCCQ 477
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-362 |
6.16e-54 |
|
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: 184.33 E-value: 6.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssiGYRVLQWT 141
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL----KGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 GASGgLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16143 77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGkwhlgldwkkkdgkkaatgtgkdvdyskpikggpldhgfdyyfgipasevlp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 ------------------------------------------------------------RILDTLDVEGLSNSTLIYFT 189
Cdd:cd16143 156 tltdkavefidqhakkdkpfflyfalpaphtpivpspefqgksgagpygdfvyeldwvvgRILDALKELGLAENTLVIFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 190 SDHGGSLENQLGNTQ-----------------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMD 251
Cdd:cd16143 236 SDNGPSPYADYKELEkfghdpsgplrgmkadiYeGG-----------------HRVPFIVRWPGKIPAGSVSDQLVSLTD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 252 VFPTVVRLAGSEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTMWKVhfvtpVFQPEGAGACY 331
Cdd:cd16143 299 LFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL-----IDGTGSGGFSY 367
|
410 420 430
....*....|....*....|....*....|..
gi 2462629488 332 GRKvcpcfgeKVVHHDPP-LLFDLSRDPSETH 362
Cdd:cd16143 368 PRG-------KEKLGLPPgQLYNLSTDPGESN 392
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
62-398 |
6.33e-50 |
|
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: 175.73 E-value: 6.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 GAS--GGLPTNETTFAKILKEKGYATGLIGR------------------------------------------------- 170
Cdd:cd16157 81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKwhlghrpqyhplkhgfdewfgapnchfgpydnkaypnipvyrdwemigr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 171 -------------------------------------------------------------------------------I 171
Cdd:cd16157 161 yyeefkidkktgesnltqiylqealefiekqhdaqkpfflywapdathapvyaskpflgtsqrglygdavmeldssvgkI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 172 LDTLDVEGLSNSTLIYFTSDHGGSLenqLGNTQYGGWNGIYKGGKGMGGWEGgIRVPGIFRWPGVLPAGRVIGEPTSLMD 251
Cdd:cd16157 241 LESLKSLGIENNTFVFFSSDNGAAL---ISAPEQGGSNGPFLCGKQTTFEGG-MREPAIAWWPGHIKPGQVSHQLGSLMD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 252 VFPTVVRLAGSEVPQDRVIDGQDLLPLLLgtAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVT----PVFQPEGA 327
Cdd:cd16157 317 LFTTSLALAGLPIPSDRAIDGIDLLPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGI 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462629488 328 GACYGRKVCPCFGEKVVHH-DPPLLFDLSRDPSETHILTPASePVFYQVMERVQQAVWEHQRTLSPVPLQLD 398
Cdd:cd16157 389 NFCPGQNVPGVTTHNQTDHtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
63-388 |
1.74e-49 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 171.92 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssIGYRVLQWTg 142
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 asggLPTNETTFAKILKEKGYATGL------------------------------------------------------- 167
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLigkthynpdavfpfddemrgpddggrnawdyasnaadflnrakkgqpfflwfgfh 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 --------------------------------------------------IGRILDTLDVEGLSNSTLIYFTSDHGGSLE 197
Cdd:cd16027 152 dphrpyppgdgeepgydpekvkvppylpdtpevredladyydeierldqqVGEILDELEEDGLLDNTIVIFTSDHGMPFP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 198 NQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLP 277
Cdd:cd16027 232 RAKGTLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 278 LLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtmwkvhfvtpvfqpegagacYgrkvcpcfgekVVHHDPP 349
Cdd:cd16027 293 LLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y-----------IRNYMPE 336
|
410 420 430
....*....|....*....|....*....|....*....
gi 2462629488 350 LLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 388
Cdd:cd16027 337 ELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
63-385 |
3.79e-49 |
|
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: 171.96 E-value: 3.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSIGYRVLqwt 141
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 gasggLPTNETTFAKILKEKGYATGL------------------------------------------------------ 167
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIfgkwhlgdnypyrpqdrgfdevlghggggigqypdywgndyfddtyyhngkfvk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 ----------------------------------------------------------------------IGRILDTLDV 177
Cdd:cd16146 151 tegyctdvffdeaidfieenkdkpffaylatnaphgplqvpdkyldpykdmglddklaafygmieniddnVGRLLAKLKE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 178 EGLSNSTLIYFTSDHGGSLENQLGN---------TQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPT 247
Cdd:cd16146 231 LGLEENTIVIFMSDNGPAGGVPKRFnagmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 248 SLMDVFPTVVRLAGSEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTMWKVHFVtpVFQPEga 327
Cdd:cd16146 294 AHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-- 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462629488 328 gacYgRKVCPcfgekvvHHDPPLLFDLSRDPSETHILTpASEPVFYQVMERVQQAVWE 385
Cdd:cd16146 361 ---W-RLVSP-------KGFQPELYDIENDPGEENDVA-DEHPEVVKRLKAAYEAWWD 406
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-362 |
8.25e-49 |
|
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: 171.24 E-value: 8.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyRVLQWTG 142
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 ASGGLPTNETTFAKILKEKGYATGLIG----------------------------------------------------- 169
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGkwglggpgtpghptkqgfdyfygyldqvhahnyypeylwrngekvplpnnvip 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 --------------------------------------------------------------------------------
Cdd:cd16145 155 pldegnnagggggtyshdlftdealdfirenkdkpfflylaytlphaplqvpddgpykykpkdpgiyaylpwpqpekaya 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 -----------RILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQY--------------------GGwngiykggkgm 218
Cdd:cd16145 235 amvtrldrdvgRILALLKELGIDENTLVVFTSDNGPHSE---GGSEHdpdffdsngplrgykrslyeGG----------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 219 ggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLPLLLGTAQHSDHEFLmhYCERF 298
Cdd:cd16145 301 ------IRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFY 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462629488 299 LH----AARWHQrdrgtmWKVhfvtpVFQPEGAGacygrkvcpcfgekvvhhdPPLLFDLSRDPSETH 362
Cdd:cd16145 371 EGggaqAVRMGG------WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
62-362 |
6.56e-45 |
|
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: 160.69 E-value: 6.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEDGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSIGYRVLQW 140
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 141 TGASGGLPTNETTFAKILKEKGYAT------------------------------------------------------- 165
Cdd:cd16025 78 PGYEGYLPDSAATIAEVLKDAGYHTymsgkwhlgpddyystddltdkaieyideqkapdkpfflylafgaphaplqapke 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 166 ---------------------------GL---------------------------------------------IGRILD 173
Cdd:cd16025 158 widkykgkydagwdalreerlerqkelGLipadtkltprppgvpawdslspeekklearrmevyaamvehmdqqIGRLID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 174 TLDVEGLSNSTLIYFTSDHGGSLEN---QLGNTQY---------GGwngiykggkgmggweggIRVPGIFRWP-GVLPAG 240
Cdd:cd16025 238 YLKELGELDNTLIIFLSDNGASAEPgwaNASNTPFrlykqasheGG-----------------IRTPLIVSWPkGIKAKG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 241 RVIGEPTSLMDVFPTVVRLAGSEVPQDRV------IDGQDLLPLLLGTAQHSDHEFLmhYCERFLHAARWHQRdrgtmWK 314
Cdd:cd16025 301 GIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ--YFELFGNRAIRKGG-----WK 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462629488 315 VhfvtpvfqpegagacygrkvcpcfgekVVHHDPPL------LFDLSRDPSETH 362
Cdd:cd16025 374 A---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-277 |
1.08e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 150.85 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 ASGGLPTNETTFAKILKEKGYATGL-------------------------------------------------IGRILD 173
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLsgkwhlgddaadflrrraeaekpfflsvnytaphspwgyfaavtgvdrnVGRLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 174 TLDVEGLSNSTLIYFTSDHGGSLenqlgnTQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIG 244
Cdd:cd16149 161 ELEELGLTENTLVIFTSDNGFNM------GHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVD 224
|
250 260 270
....*....|....*....|....*....|...
gi 2462629488 245 EPTSLMDVFPTVVRLAGSEVPQDRVIDGQDLLP 277
Cdd:cd16149 225 SLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-304 |
7.65e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 151.60 E-value: 7.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqwtg 142
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 aSGGLPTNETTFAKILKEKGYATG-------------------------------------------------------- 166
Cdd:cd16151 68 -FGYLDPKQKTFGHLLKDAGYATAiagkwqlgggrgdgdyphefgfdeyclwqltetgekysrpatptfnirngkllett 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 167 ----------------------------------------------------------------------LIGRILDTLD 176
Cdd:cd16151 147 egdygpdlfadflidfiernkdqpffayypmvlvhdpfvptpdspdwdpddkrkkddpeyfpdmvaymdkLVGKLVDKLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 177 VEGLSNSTLIYFTSDHG--GSLENQLGNTQY-GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVF 253
Cdd:cd16151 227 ELGLRENTIIIFTGDNGthRPITSRTNGREVrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFL 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462629488 254 PTVVRLAGSEVPQDRVIDGQDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 304
Cdd:cd16151 298 PTLAELAGAPLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-358 |
2.84e-40 |
|
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: 146.15 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRsgmvssIGYrvlqWTG 142
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 ASgGLPTNETTFAKILKEKGYAT--------------------------------------------------------- 165
Cdd:cd16037 71 AD-PYDGDVPSWGHALRAAGYETvligklhfrgedqrhgfrydrdvteaavdwlreeaaddkpwflfvgfvaphfpliap 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 166 ----------------GL-------IGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLG-------NTQYggwngiykgg 215
Cdd:cd16037 150 qefydlyvrraraayyGLvefldenIGRVLDALEELGLLDNTLIIYTSDHG----DMLGerglwgkSTMY---------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 216 kgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGseVPQDRVIDGQDLLPLLLGTAQHSDHEFlmhyC 295
Cdd:cd16037 216 ------EESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAG--APPPPDLDGRSLLPLAEGPDDPDRVVF----S 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462629488 296 ErfLHAARwhQRDRGTM-----WK-VHFVtpvfqpegagacygrkvcpcfgekvvhHDPPLLFDLSRDP 358
Cdd:cd16037 283 E--YHAHG--SPSGAFMlrkgrWKyIYYV---------------------------GYPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
62-364 |
1.52e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 143.48 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVsSIGYRvlqwt 141
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 gasggLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGkwhldgperndgraddytppperrhgfdywkgyecnhdhnnphyydddgkri 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 --------------------------------------------------------------------------------
Cdd:cd16034 150 yikgyspdaetdlaieylenqadkdkpfalvlswnpphdpyttapeeyldmydpkklllrpnvpedkkeeaglredlrgy 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 ------------RILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQYGGwngiykggkgmggwegGIRVPGIFRWP 234
Cdd:cd16034 230 yamitalddnigRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 235 GVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTM-- 312
Cdd:cd16034 294 GKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrt 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462629488 313 --WKvhFVtpvfqpegagacygrkvcpcfgekVVHHDPPLLFDLSRDPSETHIL 364
Cdd:cd16034 372 drYT--YV------------------------RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
63-358 |
2.38e-38 |
|
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: 141.18 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 ASGgLPTNETTFAKILKEKGYATGL------------------------------------------------------- 167
Cdd:cd16032 71 AAE-FPADIPTFAHYLRAAGYRTALsgkmhfvgpdqlhgfdydeevafkavqklydlargedgrpffltvsfthphdpyv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 ---------------------------IGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGntQYGGWngiykggKGMGG 220
Cdd:cd16032 150 ipqeywdlyvrrarrayygmvsyvddkVGQLLDTLERTGLADDTIVIFTSDHG----DMLG--ERGLW-------YKMSF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 221 WEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDRV-IDGQDLLPLLLGTAQHSDHEFLMHYCErfl 299
Cdd:cd16032 217 FEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGEDEVISEYLA--- 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462629488 300 haarwhqrdrgtmwkvhfvtpvfqpEGAGAcygrkvcPCF-----GEKVVH--HDPPLLFDLSRDP 358
Cdd:cd16032 293 -------------------------EGAVA-------PCVmirrgRWKFIYcpGDPDQLFDLEADP 326
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
61-381 |
9.04e-38 |
|
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: 141.90 E-value: 9.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqw 140
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 141 TGASGGLPTNETTFAKILKEKGYATGLIG--------------------------------------------------- 169
Cdd:cd16031 71 DNNGPLFDASQPTYPKLLRKAGYQTAFIGkwhlgsggdlpppgfdywvsfpgqgsyydpefiengkrvgqkgyvtdiitd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 --------------------------------------------------------------------------------
Cdd:cd16031 151 kaldflkerdkdkpfclslsfkaphrpftpaprhrglyedvtipepetfddddyagrpewareqrnrirgvldgrfdtpe 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 ---------------------RILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGG-WNgiykggkgmgGWEGGIRV 227
Cdd:cd16031 231 kyqrymkdylrtvtgvddnvgRILDYLEEQGLADNTIIIYTSDNG----FFLGEHGLFDkRL----------MYEESIRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 228 PGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARW 304
Cdd:cd16031 297 PLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 305 H--QRDRgtmWK-VHFvtpvfqpegagacygrkvcpcfgekvvHHDPPL--LFDLSRDPSETH--ILTPASEPVFYQVME 377
Cdd:cd16031 375 EgvRTER---YKyIYY---------------------------YGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRK 424
|
....
gi 2462629488 378 RVQQ 381
Cdd:cd16031 425 RLEE 428
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-277 |
3.43e-37 |
|
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: 136.52 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyrvLQWT 141
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 GASGGLPTNETTFAKILKEKGYATGL------------------------------------------------------ 167
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAvssnphlfggpgfdrgfdtfedfrgqegdpgeegderaervtdralewldrnad 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 -----------------------------IGRILDTLDVEGLSNSTLIYFTSDHGGSLeNQLGNTQYGGWNgiykggkgm 218
Cdd:cd16148 147 ddpfflflhyfdphepylydaevryvdeqIGRLLDKLKELGLLEDTLVIVTSDHGEEF-GEHGLYWGHGSN--------- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462629488 219 gGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLP 277
Cdd:cd16148 217 -LYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
63-362 |
1.85e-36 |
|
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: 137.68 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssiGYRVLqWTG 142
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 ASGGLPTNETTFAKILKEKGYATGLIG----------------------------------------------------- 169
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGkwhlgfytweytptnrgfdsfygyyggaedyythtsggandygnddlrdneep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 --------------------------------------------------------------------------------
Cdd:cd16029 155 awdyngtystdlftdravdiienhdpskplflylafqavhaplqvppeyadpyedkfahikdedrrtyaamvsaldesvg 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 RILDTLDVEGLSNSTLIYFTSDHGGSLENQLG----------NTQY-GGwngiykggkgmggweggIRVPGiFRWPGVLP 238
Cdd:cd16029 235 NVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsnyplrggkNTLWeGG-----------------VRVPA-FVWSPLLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 239 --AGRVIGEPTSLMDVFPTVVRLAGSEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRgtmwkvh 316
Cdd:cd16029 297 pkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDD------- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2462629488 317 fvtPVFQPEGAGACYGRKvcpcfgeKVVHHDPplLFDLSRDPSETH 362
Cdd:cd16029 357 ---ITRTTGGAAIRVGDW-------KLIVGKP--LFNIENDPCERN 390
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-385 |
1.17e-34 |
|
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: 133.12 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqWTG 142
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 A-SGGLPTNETTFAKILKEKGYATG------------------------------------------------------- 166
Cdd:cd16033 76 AySRGLPPGVETFSEDLREAGYRNGyvgkwhvgpeetpldygfdeylpvettieyfladraiemleelaaddkpfflrvn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 167 -------------------------------------------------------------------------LIGRILD 173
Cdd:cd16033 156 fwgphdpyippepyldmydpediplpesfaddfedkpyiyrrerkrwgvdtedeedwkeiiahywgyitliddAIGRILD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 174 TLDVEGLSNSTLIYFTSDHGGSLENQlgntqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVF 253
Cdd:cd16033 236 ALEELGLADDTLVIFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 254 PTVVRLAGSEVPQDrvIDGQDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWHQrdrgtmwkvhfvtpVFQ 323
Cdd:cd16033 304 PTILDLAGVDVPPK--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYKY--------------VFN 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462629488 324 PEGagacygrkvcpcFGEkvvhhdpplLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWE 385
Cdd:cd16033 366 GFD------------IDE---------LYDLESDPYELNNL--IDDPEYEEILREMRTRLYE 404
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
63-262 |
4.17e-33 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 126.38 E-value: 4.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 142
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 143 asGGLPTNETTFAKILKEKGYATG-------------------------------------------------------- 166
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGaigkwhlgwynnqspcnlgfdkffgrntgsdlyadppdvpyncsgggvsdeallde 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 167 -------------------------------------------------------------LIGRILDTLDVEGLSNSTL 185
Cdd:pfam00884 151 alefldnndkpfflvlhtlgshgppyypdrypekyatfkpsscseeqllnsydntllytddAIGRVLDKLEENGLLDNTL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462629488 186 IYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGS 262
Cdd:pfam00884 231 VVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
63-260 |
5.66e-33 |
|
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: 124.07 E-value: 5.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQwT 141
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPEL-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 GASGGLPTNETTFAKILKEKGYATGL-------------------------------------------------IGRIL 172
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVigllkaidetskekpfvlflhfdgpdgpghaygpntpeyydaveeiderIGKVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 173 DTLDVEGLSNSTLIYFTSDHGGSLENqLGNTqyggwngiYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDV 252
Cdd:cd00016 160 DALKKAGDADDTVIIVTADHGGIDKG-HGGD--------PKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDI 229
|
....*...
gi 2462629488 253 FPTVVRLA 260
Cdd:cd00016 230 APTLADLL 237
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
62-381 |
7.02e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 118.87 E-value: 7.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRvlqwt 141
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 142 gASGGLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16152 71 -NGIPLPADEKTLAHYFRDAGYETGYVGkwhlagyrvdaltdfaidyldnrqkdkpfflflsylephhqndrdryvapeg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 170 ----------------------------------------RILDTLDVEGLSNSTLIYFTSDHGGSLENQlgNTQYggwn 209
Cdd:cd16152 150 saerfanfwvppdlaalpgdwaeelpdylgccerldenvgRIRDALKELGLYDNTIIVFTSDHGCHFRTR--NAEY---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 210 giykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLPLLLGTAQHSDHE 289
Cdd:cd16152 224 -------KRSCHESSIRVPLVIYGPGFN-GGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 290 FLMHYCE----RFLHAARW----HQRDRGtmWKVHFVTPVFQPEgagacygrkvcpcfgekvvhhdppLLFDLSRDPSET 361
Cdd:cd16152 294 VFIQISEsqvgRAIRTDRWkysvAAPDKD--GWKDSGSDVYVED------------------------YLYDLEADPYEL 347
|
410 420
....*....|....*....|
gi 2462629488 362 HILtpASEPVFYQVMERVQQ 381
Cdd:cd16152 348 VNL--IGRPEYREVAAELRE 365
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
63-388 |
1.92e-29 |
|
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: 119.29 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMV------------ 130
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwngtpldarhlt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 131 ------------SSIGY---------------RVLQWTGASGGLPTN-----------ETTFA-----KILKEKG----- 162
Cdd:cd16028 81 lalelrkagydpALFGYtdtspdprglapldpRLLSYELAMPGFDPVdrldeypaedsDTAFLtdraiEYLDERQdepwf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 163 ---------------------------------------------YAT-------------------------------- 165
Cdd:cd16028 161 lhlsyirphppfvapapyhalydpadvpppiraeslaaeaaqhplLAAflerieslsfspgaanaadlddeevaqmraty 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 166 -GLI-------GRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGGwngiykggkGMGGWEGGIRVPGIFRWPGVL 237
Cdd:cd16028 241 lGLIaevddhlGRLFDYLKETGQWDDTLIVFTSDHG----EQLGDHWLWG---------KDGFFDQAYRVPLIVRDPRRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 238 ---PAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQR 307
Cdd:cd16028 308 adaTRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 308 DRGTmwkvhfvtpvfQPEGAGACYGRkvcpcfGE--KVVHHD--PPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAV 383
Cdd:cd16028 379 ALGL-----------SPDECSLAVIR------DErwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKL 439
|
....*
gi 2462629488 384 WEHQR 388
Cdd:cd16028 440 LSWRM 444
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
61-378 |
2.03e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 117.67 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssigy 135
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 136 rvlqwtGASGGLPTNETTFAKILKEKGY---ATG---------------------------------------------- 166
Cdd:cd16155 74 ------GGKAAIPSDDKTWPETFKKAGYrtfATGkwhngfadaaiefleeykdgdkpffmyvaftaphdprqappeyldm 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 167 --------------------------------------------------------LIGRILDTLDVEGLSNSTLIYFTS 190
Cdd:cd16155 148 yppetiplpenflpqhpfdngegtvrdeqlapfprtpeavrqhlaeyyamithldaQIGRILDALEASGELDNTIIVFTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 191 DHG------GSLENQlgNTQYGGWngiykggkgmggweggiRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGSEV 264
Cdd:cd16155 228 DHGlavgshGLMGKQ--NLYEHSM-----------------RVPLIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 265 PQDrvIDGQDLLPLLLG-TAQHSDHEFLMhycerFLHAARWHQRDRgtmWKVHFVTPvfqpegagacygrkvcpcfGEKV 343
Cdd:cd16155 288 PES--VEGKSLLPVIRGeKKAVRDTLYGA-----YRDGQRAIRDDR---WKLIIYVP-------------------GVKR 338
|
410 420 430
....*....|....*....|....*....|....*
gi 2462629488 344 VhhdppLLFDLSRDPSETHILtpASEPVFYQVMER 378
Cdd:cd16155 339 T-----QLFDLKKDPDELNNL--ADEPEYQERLKK 366
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
62-275 |
2.69e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 115.55 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM-- 129
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 130 -------------------------VSSIG-------YRVLQ---------WTGASGGLPTNETTFAKI---------LK 159
Cdd:cd16153 81 feaahpaldhglptfpevlkkagyqTASFGkshleafQRYLKnanqsyksfWGKIAKGADSDKPFFVRLsflqphtpvLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 160 EKGYAT------------GLIGRILDTLDVEGLSN---STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmggweGG 224
Cdd:cd16153 161 PKEFRDrfdyyafcaygdAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QS 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462629488 225 IRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTVVRLAGSEVPQDRVIDGQDL 275
Cdd:cd16153 228 HRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
61-288 |
8.60e-29 |
|
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: 116.90 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 61 SRPNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM----------- 129
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVydnnsyfrkva 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 130 --VSSI-------GYRVL------------------QWT------------------------GASGGLPTNETTF---- 154
Cdd:cd16030 80 pdAVTLpqyfkenGYTTAgvgkifhpgipdgdddpaSWDeppnppgpekyppgklcpgkkggkGGGGGPAWEAADVpdea 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 155 ----------AKILKEKG-------------------------------------------------------------- 162
Cdd:cd16030 160 ypdgkvadeaIEQLRKLKdsdkpfflavgfykphlpfvapkkyfdlyplesiplpnpfdpidlpevawndlddlpkygdi 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 163 -----------------------------YATGLIGRILDTLDVEGLSNSTLIYFTSDHGGslenQLGntQYGGW----- 208
Cdd:cd16030 240 palnpgdpkgplpdeqarelrqayyasvsYVDAQVGRVLDALEELGLADNTIVVLWSDHGW----HLG--EHGHWgkhtl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 209 ----NgiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGseVPQDRVIDGQDLLPLLLGTAQ 284
Cdd:cd16030 314 feeaT----------------RVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSA 375
|
....
gi 2462629488 285 HSDH 288
Cdd:cd16030 376 KWKD 379
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-362 |
7.52e-26 |
|
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: 108.48 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSG-------------- 128
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGhrtlhhllrpdepn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 129 MVSSI---GYRVlQWTGASGGLPTNETTFA-------------------------------------------------- 155
Cdd:cd16150 81 LLKTLkdaGYHV-AWAGKNDDLPGEFAAEAycdsdeacvrtaidwlrnrrpdkpfclylplifphppygveepwfsmidr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 156 --------KILKEKGYATGLI---------------------------------GRILDTLDVEGLSNSTLIYFTSDHG- 193
Cdd:cd16150 160 eklpprrpPGLRAKGKPSMLEgiekqgldrwseerwrelratylgmvsrldhqfGRLLEALKETGLYDDTAVFFFSDHGd 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 194 ------------GSLENQLgntqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAG 261
Cdd:cd16150 240 ytgdyglvekwpNTFEDCL------------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 262 seVPQDRVIDGQDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHqrdrgtMWKVHFVTPVFQPEG----AGACYGRKV 335
Cdd:cd16150 295 --IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQA------MEGGHGPYDLKWPRLlqqeEPPEHTKAV 362
|
410 420 430
....*....|....*....|....*....|....*.
gi 2462629488 336 cpcfgeKVVHHD---------PPLLFDLSRDPSETH 362
Cdd:cd16150 363 ------MIRTRRykyvyrlyePDELYDLEADPLELH 392
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-294 |
3.00e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 87.65 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSI--- 133
Cdd:cd16035 1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLgsp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 134 -------------------GYRVlQW------TGASGGLPTNETTFA----KILKEKG---------------------- 162
Cdd:cd16035 75 mqpllspdvptlghmlraaGYYT-AYkgkwhlSGAAGGGYKRDPGIAaqavEWLRERGaknadgkpwflvvslvnphdim 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 163 ---------------------YATGLIGRILDTLDVEGLSNSTLIYFTSDHG------GSLENqlGNTQYGgwngiykgg 215
Cdd:cd16035 154 fppddeerwrrfrnfyynlirDVDRQIGRVLDALDASGLADNTIVVFTSDHGemggahGLRGK--GFNAYE--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 216 kgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDRVID----GQDLLPLLLGTAQHSDHE-F 290
Cdd:cd16035 223 -------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAVRDgI 295
|
....
gi 2462629488 291 LMHY 294
Cdd:cd16035 296 LFTY 299
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
61-369 |
3.99e-19 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 89.34 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 61 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVS-------- 131
Cdd:PRK13759 5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGygdvvpwn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 132 -----------------SIG---------------------------------------YRVLQWTGASG--------GL 147
Cdd:PRK13759 84 ykntlpqefrdagyytqCIGkmhvfpqrnllgfhnvllhdgylhsgrnedksqfdfvsdYLAWLREKAPGkdpdltdiGW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 148 -----------------PTNET---------------------TFAK--------------------------------- 156
Cdd:PRK13759 164 dcnswvarpwdleerlhPTNWVgsesieflrrrdptkpfflkmSFARphspydppkryfdmykdadipdphigdweyaed 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 157 -------------ILKEK-------GYaTGL-------IGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ----- 204
Cdd:PRK13759 244 qdpeggsidalrgNLGEEyarraraAY-YGLithidhqIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 205 --YGGwngiykggkgmggwegGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLPLL 279
Cdd:PRK13759 319 ypYEG----------------SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 280 LG-TAQHSDHEFLMH-YCERFLHaarWHQRDRGT-MWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSR 356
Cdd:PRK13759 381 FGqYEGWRPYLHGEHaLGYSSDN---YLTDGKWKyIW--FSQTGEEQ---------------------------LFDLKK 428
|
490
....*....|...
gi 2462629488 357 DPSETHILTPASE 369
Cdd:PRK13759 429 DPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
63-170 |
4.11e-18 |
|
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: 86.28 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
|
90 100
....*....|....*....|....*...
gi 2462629488 143 aSGGLPTNETTFAKILKEKGYATGLIGR 170
Cdd:cd16156 71 -CMALGDNVKTIGQRLSDNGIHTAYIGK 97
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
62-169 |
8.87e-15 |
|
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: 75.66 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 62 RPNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSIGYRV 137
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPK 76
|
90 100 110
....*....|....*....|....*....|..
gi 2462629488 138 LQWTGAsgglptNETTFAKILKEKGYATGLIG 169
Cdd:cd16147 77 FWQNGL------ERSTLPVWLQEAGYRTAYAG 102
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-170 |
2.97e-14 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 73.54 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSIGYRVLQw 140
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
|
90 100 110
....*....|....*....|....*....|...
gi 2462629488 141 tgasgglpTNETTFAKILKE---KGYATGLIGR 170
Cdd:cd16154 78 --------SEETLLQLLIKDattAGYSSAVIGK 102
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
148-359 |
1.21e-11 |
|
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: 65.64 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 148 PTNETTFAKILKEKGY-------ATGLIGRILDTLDVEGLSNSTLIYFTSDHGgslENQLGNTQYggwngiykggKGMGG 220
Cdd:cd16171 182 PSMGENFGSIRNIRAFyyamcaeTDAMLGEIISALKDTGLLDKTYVFFTSDHG---ELAMEHRQF----------YKMSM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 221 WEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGSEVPQDrvIDGQDLLPLLLGTAQHSDH-----------E 289
Cdd:cd16171 249 YEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSIKESPsrvphpdwvlsE 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 290 FlmHYCErfLHAARWHQRDrgTMWKvhFVTpvfqpegagacYGRkvcpcfGEKVvhhdPPLLFDLSRDPS 359
Cdd:cd16171 326 F--HGCN--VNASTYMLRT--NSWK--YIA-----------YAD------GNSV----PPQLFDLSKDPD 366
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
163-276 |
4.39e-08 |
|
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: 55.30 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 163 YATGLIGRILDTLDVEGLSNSTLIYFTSDHGGSL----ENQLG-NTQYGGWNgiykggkgmggweggIRVPGIFRWPGVL 237
Cdd:COG3083 435 YVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGhNSNFSRYQ---------------LQVPLVIHWPGTP 499
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462629488 238 PagRVIGEPTSLMDVFPTVV-RLAGSEVPqdrVID---GQDLL 276
Cdd:COG3083 500 P--QVISKLTSHLDIVPTLMqRLLGVQNP---ASDysqGEDLF 537
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
168-276 |
1.82e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 50.04 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 IGRILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQYggwngiykggkgmGGWEGGIRVPGIFRWPGvLPAGRVIGEPT 247
Cdd:COG1368 430 LGEFIEKLKKSGWYDNTIFVIYGDHGPRSP---GKTDY-------------ENPLERYRVPLLIYSPG-LKKPKVIDTVG 492
|
90 100
....*....|....*....|....*....
gi 2462629488 248 SLMDVFPTVVRLAGSEVPQDRVIdGQDLL 276
Cdd:COG1368 493 SQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
44-169 |
8.78e-06 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 47.44 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGR 122
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462629488 123 YPVRSGMVSSIGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIG 169
Cdd:COG1524 80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVF 136
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
63-165 |
4.33e-04 |
|
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: 41.90 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 63 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSIGYRvl 138
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
|
90 100
....*....|....*....|....*..
gi 2462629488 139 qwtgasgglPTNETTFAKILKEKGYAT 165
Cdd:cd16015 77 ---------LNPLPSLPSILKEQGYET 94
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
168-261 |
5.87e-04 |
|
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: 41.51 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462629488 168 IGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPaGRVIGEPT 247
Cdd:cd16015 205 LGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVG 269
|
90
....*....|....
gi 2462629488 248 SLMDVFPTVVRLAG 261
Cdd:cd16015 270 SQIDIAPTLLDLLG 283
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
87-131 |
1.83e-03 |
|
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: 40.10 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2462629488 87 RTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVS 131
Cdd:pfam01663 19 LTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
|
|
| |
