|
Name |
Accession |
Description |
Interval |
E-value |
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-489 |
1.18e-115 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 346.48 E-value: 1.18e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 1 MAKPNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTK---- 75
Cdd:COG3119 21 AKRPNILFILADDLGYGDLGCYgNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGyngg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 76 LLEDRHTVGEDFAANGYRTALIGKAHFqplrdtdaypsveaypilqdlafwkqfngpfygfdhvelarnhtneahvgqhy 155
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALFGKWHL----------------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 156 alwmeekgclnwrdyflpptgtmdkqiehkwpipeqyHYNTWIAERSNALLEQYKANEEPFFLWSSFFDPHPDYLVPEPW 235
Cdd:COG3119 128 -------------------------------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 236 DTMYDPDRLTIPKavpgehdrnpphfrmtqeedpdfgawretgfgihgYHSHVQRSPEERKRQVATYYGMVSCMDQAIGR 315
Cdd:COG3119 171 LDKYDGKDIPLPP-----------------------------------NLAPRDLTEEELRRARAAYAAMIEEVDDQVGR 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 316 ILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGL 395
Cdd:COG3119 216 LLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 396 PVPSAMTGVNQSGVWLGEREAARDHAICEFRHEPttiHQKTYVDDRYKITVYYNQT-YGEIFDLAEDPDEVRNLWDDPNQ 474
Cdd:COG3119 296 PIPEDLDGRSLLPLLTGEKAEWRDYLYWEYPRGG---GNRAIRTGRWKLIRYYDDDgPWELYDLKNDPGETNNLAADYPE 372
|
490
....*....|....*..
gi 1805095636 475 --AALKTELLlkyAWAE 489
Cdd:COG3119 373 vvAELRALLE---AWLK 386
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
3-481 |
7.67e-101 |
|
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: 309.46 E-value: 7.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDR- 80
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYgNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDASq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 81 HTVGEDFAANGYRTALIGKAHFQPLRDTdaypsveaypilqdlafwkqfngPFYGFDHVElarnhtneAHVGQHyalwme 160
Cdd:cd16031 82 PTYPKLLRKAGYQTAFIGKWHLGSGGDL-----------------------PPPGFDYWV--------SFPGQG------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 161 ekgclnwrDYFLPPTGTMDKQIEHKWpipeqyHYNTWIAERSNALLEQYKANEePFFLWSSFFDPHPDYLVPEPWDTMYD 240
Cdd:cd16031 125 --------SYYDPEFIENGKRVGQKG------YVTDIITDKALDFLKERDKDK-PFCLSLSFKAPHRPFTPAPRHRGLYE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 241 PDRLTIPKAVPGEHDRNPPHFRmtqeedpdfgawRETGFGIHGYHSHVQRSPEERKRQVATYYGMVSCMDQAIGRILDKL 320
Cdd:cd16031 190 DVTIPEPETFDDDDYAGRPEWA------------REQRNRIRGVLDGRFDTPEKYQRYMKDYLRTVTGVDDNVGRILDYL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 321 DELGMADNTIVVFTTDHGHFFGQHGLqhkGG--FHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGLPVP 398
Cdd:cd16031 258 EEQGLADNTIIIYTSDNGFFLGEHGL---FDkrLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 399 SAMTGVNQSGVWLGEREAA-RDHAICEFRHE---PTTIHQKTYVDDRYKITVYYNQ-TYGEIFDLAEDPDEVRNLWDDPN 473
Cdd:cd16031 335 EDMQGRSLLPLLEGEKPVDwRKEFYYEYYEEpnfHNVPTHEGVRTERYKYIYYYGVwDEEELYDLKKDPLELNNLANDPE 414
|
....*...
gi 1805095636 474 QAALKTEL 481
Cdd:cd16031 415 YAEVLKEL 422
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-489 |
4.69e-99 |
|
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: 304.53 E-value: 4.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFNKDI-HTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWT-------LGTK 75
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNnvenagaYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 76 LLEDRHTVGEDFAANGYRTALIGKahfqplrdtdaypsveaypilqdlafWkqfngpfygfdhvelarnhtneaHVGQHY 155
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGK--------------------------W-----------------------HVGPEE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 156 alWMEEKGClnwrDYFLPPTGTMDkqiehkwpipeqyhynTWIAERSNALLEQYKANEEPFFLWSSFFDPHPDYLVPEPW 235
Cdd:cd16033 112 --TPLDYGF----DEYLPVETTIE----------------YFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 236 DTMYDPDRLTIPKAVPGEHDRNPPHFRMTQEEdpdFGAWRETgfgihgyhshvqrspEERKRQ-VATYYGMVSCMDQAIG 314
Cdd:cd16033 170 LDMYDPEDIPLPESFADDFEDKPYIYRRERKR---WGVDTED---------------EEDWKEiIAHYWGYITLIDDAIG 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 315 RILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAG 394
Cdd:cd16033 232 RILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFMYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 395 LPVPSAMTGvnQSGVWL---GEREAARDHAICEFR-HEPTTIhQKTYVDDRYKITvyYNQT-YGEIFDLAEDPDEVRNLW 469
Cdd:cd16033 312 VDVPPKVDG--RSLLPLlrgEQPEDWRDEVVTEYNgHEFYLP-QRMVRTDRYKYV--FNGFdIDELYDLESDPYELNNLI 386
|
490 500
....*....|....*....|.
gi 1805095636 470 DDPNQAALKTELLLK-YAWAE 489
Cdd:cd16033 387 DDPEYEEILREMRTRlYEWME 407
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-468 |
4.80e-98 |
|
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: 301.41 E-value: 4.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQqhWN--TIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLED 79
Cdd:cd16034 1 KPNILFIFADQ--HRaqALGCAgDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 80 RHTVGEDFAANGYRTALIGKAHFQ-PLRDTDAYpsveaypilqDLAFWkqfNGPF-YGFDHvelarnhtneahvgqhyal 157
Cdd:cd16034 79 APTIADVLKDAGYRTGYIGKWHLDgPERNDGRA----------DDYTP---PPERrHGFDY------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 158 WmeeKGCLNWRDYFLPPTGTMD---KQIEHKWPIpeqyhyntWIAERSNALLEQYKANEEPFFLWSSFFDPHPDY-LVPE 233
Cdd:cd16034 127 W---KGYECNHDHNNPHYYDDDgkrIYIKGYSPD--------AETDLAIEYLENQADKDKPFALVLSWNPPHDPYtTAPE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 234 PWDTMYDPDRLTIPKAVPGEHDRNpphfrmtqeedpdfgawretgfgihgyhshvqrspEERKRQVATYYGMVSCMDQAI 313
Cdd:cd16034 196 EYLDMYDPKKLLLRPNVPEDKKEE-----------------------------------AGLREDLRGYYAMITALDDNI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 314 GRILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFhYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLA 393
Cdd:cd16034 241 GRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVP-YEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLC 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 394 GLPVPSAMTGVNQSGVWLGEREAARDHA--ICEFR-HEPTTIHQKTY---VDDRYKITVYYNQTYgEIFDLAEDPDEVRN 467
Cdd:cd16034 320 GLPIPDTVEGRDLSPLLLGGKDDEPDSVllQCFVPfGGGSARDGGEWrgvRTDRYTYVRDKNGPW-LLFDNEKDPYQLNN 398
|
.
gi 1805095636 468 L 468
Cdd:cd16034 399 L 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
4-481 |
9.46e-97 |
|
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: 297.11 E-value: 9.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFNKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAW---TLGTKLLEDR 80
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHglrSRGFPLPDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 81 HTVGEDFAANGYRTALIGKAHFQPlrdtdaypsveaypilqdlafwkqfnGPFYGFDHVELARNHtneahvgQHYALWME 160
Cdd:cd16027 81 KTLPELLREAGYYTGLIGKTHYNP--------------------------DAVFPFDDEMRGPDD-------GGRNAWDY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 161 EKGCLNWRDYflpptgtmdkqiehkwpipeqyhyntwiaersnalleqyKANEEPFFLWSSFFDPHPDYLVPEPWDTMYD 240
Cdd:cd16027 128 ASNAADFLNR---------------------------------------AKKGQPFFLWFGFHDPHRPYPPGDGEEPGYD 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 241 PDRLTIPkavpgehdrnpPHFrmtqeedPDfgawretgfgihgyhshvqrSPEERKrQVATYYGMVSCMDQAIGRILDKL 320
Cdd:cd16027 169 PEKVKVP-----------PYL-------PD--------------------TPEVRE-DLADYYDEIERLDQQVGEILDEL 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 321 DELGMADNTIVVFTTDHGHFFgqhgLQHKGgFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGLPVPSA 400
Cdd:cd16027 210 EEDGLLDNTIVIFTSDHGMPF----PRAKG-TLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 401 MTGVNQSGVWLGEREAARDHAICEF-RHEPTTIHQKTYVDDRYKITVYYNqtYGEIFDLAEDPDEVRNLWDDPNQAALKT 479
Cdd:cd16027 285 LQGRSFLPLLKGEKDPGRDYVFAERdRHDETYDPIRSVRTGRYKYIRNYM--PEELYDLKNDPDELNNLADDPEYAEVLE 362
|
..
gi 1805095636 480 EL 481
Cdd:cd16027 363 EL 364
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
4-405 |
3.74e-93 |
|
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: 282.79 E-value: 3.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTL---GTKLLED 79
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYgNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNvgnGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 80 RHTVGEDFAANGYRTALIGKAHfqplrdtdaypsveaypilqdlafwkqfngpfygfdhvelarnhtneahvgqhyalwm 159
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGKWH---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 160 eekgclnwrdyflpptgtmDKQIEhkwpipeqyhyntWIAERsnalleqykANEEPFFLWSSFFDPHPdylvpePWdtmy 239
Cdd:cd16022 103 -------------------DEAID-------------FIERR---------DKDKPFFLYVSFNAPHP------PF---- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 240 dpdrltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrspeerkrqvaTYYGMVSCMDQAIGRILDK 319
Cdd:cd16022 132 -------------------------------------------------------------AYYAMVSAIDDQIGRILDA 150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 320 LDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGLPVPS 399
Cdd:cd16022 151 LEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPE 230
|
....*.
gi 1805095636 400 AMTGVN 405
Cdd:cd16022 231 GLDGRS 236
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-482 |
6.05e-90 |
|
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: 279.45 E-value: 6.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPT----CTPSRASIITGMY----PSQHGAwtlg 73
Cdd:cd16155 2 KPNILFILADDQRADTIGALgNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTlfhaPEGGKA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 74 tKLLEDRHTVGEDFAANGYRTALIGKAHfqplrdtdaypsveaypilqdlafwkqfngpfygfdhvelarnhtneahvgQ 153
Cdd:cd16155 78 -AIPSDDKTWPETFKKAGYRTFATGKWH---------------------------------------------------N 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 154 HYAlwmeekgclnwrdyflpptgtmDKQIEHkwpipeqyhyntwiaersnalLEQYKANEEPFFLWSSFFDPHPDYLVPE 233
Cdd:cd16155 106 GFA----------------------DAAIEF---------------------LEEYKDGDKPFFMYVAFTAPHDPRQAPP 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 234 PWDTMYDPDRLTIPKAVPGEHDRNPPhfrMTQEEDPDFGAWRetgfgihgyhshvqRSPEERKRQVATYYGMVSCMDQAI 313
Cdd:cd16155 143 EYLDMYPPETIPLPENFLPQHPFDNG---EGTVRDEQLAPFP--------------RTPEAVRQHLAEYYAMITHLDAQI 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 314 GRILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFhYEDLIRLPFIVRYPSrVPAGRVSPAIQSLVDLAPTFLSLA 393
Cdd:cd16155 206 GRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNL-YEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELA 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 394 GLPVPSAMTGVNQSGVWLGEREAARDHAICEFRHepttiHQKTYVDDRYKITVYYNQT-YGEIFDLAEDPDEVRNLWDDP 472
Cdd:cd16155 284 GIEIPESVEGKSLLPVIRGEKKAVRDTLYGAYRD-----GQRAIRDDRWKLIIYVPGVkRTQLFDLKKDPDELNNLADEP 358
|
490
....*....|
gi 1805095636 473 NQAALKTELL 482
Cdd:cd16155 359 EYQERLKKLL 368
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
4-484 |
6.26e-78 |
|
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: 251.02 E-value: 6.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDRHT 82
Cdd:cd16028 1 RNVLFITADQWRADCLSCLgHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 83 VGEDFAANGYRTALIGKAHFQPlrDTDAYPSVEAYPILQDLAFwkqfngpfYGFDHVELARnhtneahvgqhyalwmeek 162
Cdd:cd16028 81 LALELRKAGYDPALFGYTDTSP--DPRGLAPLDPRLLSYELAM--------PGFDPVDRLD------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 163 gclnwrdyflpptgtmdkqiehkwPIPEQYHYNTWIAERSNALLEQYKanEEPFFLWSSFFDPHPDYLVPEPWDTMYDPD 242
Cdd:cd16028 132 ------------------------EYPAEDSDTAFLTDRAIEYLDERQ--DEPWFLHLSYIRPHPPFVAPAPYHALYDPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 243 RLTIP--KAVPGEHDRNPPHFRMTQEEDPDFGAWRetgfgihGYHSHVQRSPEERKRQVATYYGMVSCMDQAIGRILDKL 320
Cdd:cd16028 186 DVPPPirAESLAAEAAQHPLLAAFLERIESLSFSP-------GAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 321 DELGMADNTIVVFTTDHGHFFGQHGLQHKGGFhYEDLIRLPFIVRYPSR---VPAGRVSPAIQSLVDLAPTFLSLAGLPV 397
Cdd:cd16028 259 KETGQWDDTLIVFTSDHGEQLGDHWLWGKDGF-FDQAYRVPLIVRDPRReadATRGQVVDAFTESVDVMPTILDWLGGEI 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 398 PSAMTGVNQSGVWLGEREAA-RDHAICEF-----------RHEPTTIHQKTYV---DDRYKiTVYYNQTYGEIFDLAEDP 462
Cdd:cd16028 338 PHQCDGRSLLPLLAGAQPSDwRDAVHYEYdfrdvstrrpqEALGLSPDECSLAvirDERWK-YVHFAALPPLLFDLKNDP 416
|
490 500
....*....|....*....|..
gi 1805095636 463 DEVRNLWDDPNQAALKTELLLK 484
Cdd:cd16028 417 GELRDLAADPAYAAVVLRYAQK 438
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
1-481 |
6.56e-75 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 244.19 E-value: 6.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 1 MAKPNILLITSDQQHWNTIG-AFNKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLED 79
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDCLGcNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 80 -RHTVGEDFAANGYRTALIGKAHFQPLRDTDAYPSVeaypILQDlafwkqfngpfyGFDHVELARNHTNEAHVGQhYALW 158
Cdd:PRK13759 84 yKNTLPQEFRDAGYYTQCIGKMHVFPQRNLLGFHNV----LLHD------------GYLHSGRNEDKSQFDFVSD-YLAW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 159 MEEKGCLNWRDYFlpPTGTMDKQIEHK-WPIPEQYHYNTWIAERSNALLEQYKaNEEPFFLWSSFFDPHPDYLVPEPWDT 237
Cdd:PRK13759 147 LREKAPGKDPDLT--DIGWDCNSWVARpWDLEERLHPTNWVGSESIEFLRRRD-PTKPFFLKMSFARPHSPYDPPKRYFD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 238 MY-DPDrltIPKAVPGEhdrnpphFRMTQEEDPDFGAwRETGFGIHGyhshvqrsPEERKRQVATYYGMVSCMDQAIGRI 316
Cdd:PRK13759 224 MYkDAD---IPDPHIGD-------WEYAEDQDPEGGS-IDALRGNLG--------EEYARRARAAYYGLITHIDHQIGRF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 317 LDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKgGFHYEDLIRLPFIVRYPS---RVPAGRVSPAIQSLVDLAPTFLSLA 393
Cdd:PRK13759 285 LQALKEFGLLDNTIILFVSDHGDMLGDHYLFRK-GYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 394 GLPVPSAMTGVNQSGVWLGEREAARD-----HAICEFRHEPTTihqktyvDDRYKItVYYNQTYGE-IFDLAEDPDEVRN 467
Cdd:PRK13759 364 GGTIPDDVDGRSLKNLIFGQYEGWRPylhgeHALGYSSDNYLT-------DGKWKY-IWFSQTGEEqLFDLKKDPHELHN 435
|
490
....*....|....
gi 1805095636 468 LWDDPNQAALKTEL 481
Cdd:PRK13759 436 LSPSEKYQPRLREM 449
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
4-481 |
6.77e-74 |
|
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: 241.13 E-value: 6.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDRHT 82
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYgNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 83 VGEDFAANGYRTALIGKAHFqplrDTDAYPSVEAYPILQDLAFWkqfngpfygFDhvelARNHTNEahvgqhyalwMEEK 162
Cdd:cd16156 81 IGQRLSDNGIHTAYIGKWHL----DGGDYFGNGICPQGWDPDYW---------YD----MRNYLDE----------LTEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 163 GCLNWRDyflpPTGTMDKQiehkwPIPEQYHYNTWIAERSNALLEQYKanEEPFFLWSSFFDPHPDYLVPEPWDTMYDPD 242
Cdd:cd16156 134 ERRKSRR----GLTSLEAE-----GIKEEFTYGHRCTNRALDFIEKHK--DEDFFLVVSYDEPHHPFLCPKPYASMYKDF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 243 RLTIPKAVPGEHDRNPPHFRMtqeedpdfgaWretgfgiHGYHSHVQRspEERKRQVATYYGMVSCMDQAIGRILDKLDE 322
Cdd:cd16156 203 EFPKGENAYDDLENKPLHQRL----------W-------AGAKPHEDG--DKGTIKHPLYFGCNSFVDYEIGRVLDAADE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 323 LgmADNTIVVFTTDHGHFFGQHGLQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGLPVPSAMT 402
Cdd:cd16156 264 I--AEDAWVIYTSDHGDMLGAHKLWAKGPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 403 GVNQSGVWLGEREAARDHAICEF-RHEPTT------IHQKTYVDDRYKITVYYNQTyGEIFDLAEDPDEVRNLWDDPNQA 475
Cdd:cd16156 342 GESILATIEDPEIPENRGVFVEFgRYEVDHdgfggfQPVRCVVDGRYKLVINLLST-DELYDLEKDPYEMHNLIDDPDYA 420
|
....*.
gi 1805095636 476 ALKTEL 481
Cdd:cd16156 421 DVRDQL 426
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
3-472 |
3.30e-71 |
|
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: 233.23 E-value: 3.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQ-QHWntIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGT---KLL 77
Cdd:cd16030 2 KPNVLFIAVDDlRPW--LGCYgGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSyfrKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 78 EDRHTVGEDFAANGYRTALIGKAHFQPLRDTDAYPsveaypilqdlafwKQFNGPFYGfdhvelarnhtneAHVGQHYAL 157
Cdd:cd16030 80 PDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDDDP--------------ASWDEPPNP-------------PGPEKYPPG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 158 WMEEKGCLNWRDYFLPPTGTMDkqiehkwpIPEQYHYNTWIAERSNALLEQYKANEEPFFLWSSFFDPHPDYLVPEPWDT 237
Cdd:cd16030 133 KLCPGKKGGKGGGGGPAWEAAD--------VPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 238 MYDPDRLTIPKAVPgehDRNPPHFRMTQEEDpdFGAWRETGFGIHGYHSHVQrSPEERKRQVATYYGMVSCMDQAIGRIL 317
Cdd:cd16030 205 LYPLESIPLPNPFD---PIDLPEVAWNDLDD--LPKYGDIPALNPGDPKGPL-PDEQARELRQAYYASVSYVDAQVGRVL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 318 DKLDELGMADNTIVVFTTDHGHFFGQHGLQHKggfH--YEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGL 395
Cdd:cd16030 279 DALEELGLADNTIVVLWSDHGWHLGEHGHWGK---HtlFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 396 PVPSAMTGVNQSGVWLGEREAARDHAICEFRHEPTTIHqkTYVDDRYKITVYYNQTYG---EIFDLAEDPDEVRNLWDDP 472
Cdd:cd16030 356 PAPPCLEGKSLVPLLKNPSAKWKDAAFSQYPRPSIMGY--SIRTERYRYTEWVDFDKVgaeELYDHKNDPNEWKNLANDP 433
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-482 |
1.73e-68 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 225.58 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDRHT 82
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLgNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 83 VGEDFAANGYRTALIGKAHFqplrdtdaypsveaypilqdlafwkqfngpfygfdhveLARNHTNEAhvgqhYALWmeek 162
Cdd:cd16150 81 LLKTLKDAGYHVAWAGKNDD--------------------------------------LPGEFAAEA-----YCDS---- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 163 gclnwrDYflpptGTMDKQIEhkwpipeqyhyntWIAERSNalleqykanEEPFFLWSSFFDPHPDYLVPEPWDTMYDPD 242
Cdd:cd16150 114 ------DE-----ACVRTAID-------------WLRNRRP---------DKPFCLYLPLIFPHPPYGVEEPWFSMIDRE 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 243 rlTIPKAVPGEHD-RNPPHFRmtqeedpdfgawretgfGIHGYHsHVQRSPEERKRQV-ATYYGMVSCMDQAIGRILDKL 320
Cdd:cd16150 161 --KLPPRRPPGLRaKGKPSML-----------------EGIEKQ-GLDRWSEERWRELrATYLGMVSRLDHQFGRLLEAL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 321 DELGMADNTIVVFTTDHGHFFGQHGLQHK--GGFHyEDLIRLPFIVRYPSrVPAGRVSPAIQSLVDLAPTFLSLAGLPVP 398
Cdd:cd16150 221 KETGLYDDTAVFFFSDHGDYTGDYGLVEKwpNTFE-DCLTRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLS 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 399 SAMTGVNQSGVWLGEREAARDHAICE--FRHEPTTIHQKTYVDD-------------------------RYKitvYYNQT 451
Cdd:cd16150 299 HTHFGRSLLPVLAGETEEHRDAVFSEggRLHGEEQAMEGGHGPYdlkwprllqqeeppehtkavmirtrRYK---YVYRL 375
|
490 500 510
....*....|....*....|....*....|...
gi 1805095636 452 YG--EIFDLAEDPDEVRNLWDDPNQAALKTELL 482
Cdd:cd16150 376 YEpdELYDLEADPLELHNLIGDPAYAEIIAEMK 408
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-468 |
4.98e-68 |
|
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: 224.34 E-value: 4.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFNKDIH-TPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWT---------LG 73
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYeTPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipgrrgppDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 74 TKLLEDRH---------TVGEDFAANGYRTALIGKAHfqpLRDTDAYpsveaYPILQdlafwkqfngpfyGFDHVElarN 144
Cdd:cd16144 81 TKLIPPPSttrlpleevTIAEALKDAGYATAHFGKWH---LGGEGGY-----GPEDQ-------------GFDVNI---G 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 145 HTNEAHVGQHYALWmeekgclnWRDYFLPPTGTMDKQIEHKwpipeqyhyntwIAERSNALLEQYKanEEPFFLWSSFFD 224
Cdd:cd16144 137 GTGNGGPPSYYFPP--------GKPNPDLEDGPEGEYLTDR------------LTDEAIDFIEQNK--DKPFFLYLSHYA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 225 PHpdylvpEPWDTmyDPDRLTipkavpgehdrnppHFRmtqeedpdfgawretgfgihgyhshvQRSPEERKRQV-ATYY 303
Cdd:cd16144 195 VH------TPIQA--RPELIE--------------KYE--------------------------KKKKGLRKGQKnPVYA 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 304 GMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHGHFFGQHG-------LQHKGGFHYEDLIRLPFIVRYPSRVPAGRVS 376
Cdd:cd16144 227 AMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGpptsnapLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVS 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 377 --PAIQslVDLAPTFLSLAGLPVPSAMT--GVNQSGVWLGEREAARDHAIceFRHEPTTIHQKT-----YVDDRYKITVY 447
Cdd:cd16144 307 dvPVIG--TDLYPTFLELAGGPLPPPQHldGVSLVPLLKGGEADLPRRAL--FWHFPHYHGQGGrpasaIRKGDWKLIEF 382
|
490 500
....*....|....*....|.
gi 1805095636 448 YNQTYGEIFDLAEDPDEVRNL 468
Cdd:cd16144 383 YEDGRVELYNLKNDIGETNNL 403
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-463 |
5.36e-67 |
|
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: 218.57 E-value: 5.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDRHT 82
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYgHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 83 VGEDFAANGYRTALIGKAHFqplRDTDAYpsveaypilqdlafwkqfngpfYGFDHvelarnhtneahvgqhyalwmeek 162
Cdd:cd16037 81 WGHALRAAGYETVLIGKLHF---RGEDQR----------------------HGFRY------------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 163 gclnwrdyflpptgtmDKQIehkwpipeqyhyntwiAERSNALLEQYKANEEPFFLWSSFFDPHPDYLVPEPWDTMYdpd 242
Cdd:cd16037 112 ----------------DRDV----------------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY--- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 243 rltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrspeeRKRQVATYYGMVSCMDQAIGRILDKLDE 322
Cdd:cd16037 157 ----------------------------------------------------VRRARAAYYGLVEFLDENIGRVLDALEE 184
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 323 LGMADNTIVVFTTDHGHFFGQHGLQHKGGFhYEDLIRLPFIVRYPsRVPAGRVSPAIQSLVDLAPTFLSLAGLPVPSAMT 402
Cdd:cd16037 185 LGLLDNTLIIYTSDHGDMLGERGLWGKSTM-YEESVRVPMIISGP-GIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLD 262
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805095636 403 GVnqSGVWLGEREAARDH-AICEF-RHEPTTIHqKTYVDDRYKItVYYNQTYGEIFDLAEDPD 463
Cdd:cd16037 263 GR--SLLPLAEGPDDPDRvVFSEYhAHGSPSGA-FMLRKGRWKY-IYYVGYPPQLFDLENDPE 321
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
3-472 |
1.74e-61 |
|
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: 206.25 E-value: 1.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQhwntigafnkDIHTPSLD-------RLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLG-- 73
Cdd:cd16147 1 RPNIVLILTDDQ----------DVELGSMDpmpktkkLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSpp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 74 -------TKLLEDRHTVGEDFAANGYRTALIGKAhfqpLRDTDAYPSVEAYPilqdLAF--WKQFNGPFYGFDHveLARN 144
Cdd:cd16147 71 gggypkfWQNGLERSTLPVWLQEAGYRTAYAGKY----LNGYGVPGGVSYVP----PGWdeWDGLVGNSTYYNY--TLSN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 145 HTNEAHVGQHyalwmeekgclnwrdyflpptgtmdkqiehkwpiPEQYhYNTWIAERSNALLEQYKANEEPFFLWSSFFD 224
Cdd:cd16147 141 GGNGKHGVSY----------------------------------PGDY-LTDVIANKALDFLRRAAADDKPFFLVVAPPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 225 PHPDYLVPEPWDTMYDPDRLTIPKAvPGEHDRNP-PHFRMTQEEDPDfgawretgfgihgyhSHVQRSPEERKRQVATyy 303
Cdd:cd16147 186 PHGPFTPAPRYANLFPNVTAPPRPP-PNNPDVSDkPHWLRRLPPLNP---------------TQIAYIDELYRKRLRT-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 304 gMVScMDQAIGRILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFHYEDLIRLPFIVRYPSrVPAGRVSPAIQSLV 383
Cdd:cd16147 248 -LQS-VDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNI 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 384 DLAPTFLSLAGLPVPSAMTGVNQSGVWLGEREAARdhaicefrhepttihqktYVDDRYKiTVYYNQTYG--EIFDLAED 461
Cdd:cd16147 325 DLAPTILDLAGAPPPSDMDGRSCGDSNNNTYKCVR------------------TVDDTYN-LLYFEWCTGfrELYDLTTD 385
|
490
....*....|.
gi 1805095636 462 PDEVRNLWDDP 472
Cdd:cd16147 386 PYQLTNLAGDL 396
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-468 |
4.23e-61 |
|
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: 205.91 E-value: 4.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQ-----HGAWTLGTKLL 77
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYgQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHtrvrgNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 78 EDRHTVGEDFAANGYRTALIGKAHFQPlRDTDAYPSveaypilqdlafwKQfngpfyGFDHVELARNHTNeAHvgQHYA- 156
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGG-PGTPGHPT-------------KQ------GFDYFYGYLDQVH-AH--NYYPe 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 157 -LWMEEKgclnwrdYFLPPTGTMDKQIEHKWPIPEQYHYNT-WIAERSNALLEQYKanEEPFFLWSSFFDPHPDYLVPEP 234
Cdd:cd16145 138 yLWRNGE-------KVPLPNNVIPPLDEGNNAGGGGGTYSHdLFTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPDD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 235 WdtmydpdrltipkavpgehdrnpphfrmtqeEDPDFGAWRETGfgihGYHSHvqrsPEERKRqvatYYGMVSCMDQAIG 314
Cdd:cd16145 209 G-------------------------------PYKYKPKDPGIY----AYLPW----PQPEKA----YAAMVTRLDRDVG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 315 RILDKLDELGMADNTIVVFTTDHGH-----------FFgqhglQHKGGFH------YEDLIRLPFIVRYPSRVPAGRVSP 377
Cdd:cd16145 246 RILALLKELGIDENTLVVFTSDNGPhseggsehdpdFF-----DSNGPLRgykrslYEGGIRVPFIARWPGKIPAGSVSD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 378 AIQSLVDLAPTFLSLAGLPVPSAMTGVNQSGVWLGEREAAR-DHAICEFrHEPttIHQKTYVDDRYKItVYYNQTYG--E 454
Cdd:cd16145 321 HPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKPQQQQhDYLYWEF-YEG--GGAQAVRMGGWKA-VRHGKKDGpfE 396
|
490
....*....|....
gi 1805095636 455 IFDLAEDPDEVRNL 468
Cdd:cd16145 397 LYDLSTDPGETNNL 410
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
4-471 |
5.95e-61 |
|
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: 205.48 E-value: 5.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCpNPTCTPSRASIITGMYPSQHGAWTL---GTKLLED 79
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHgNPILKTPNLDRLAAESVRFTNFHV-SPVCAPTRAALLTGRYPFRTGVWHTilgRERMRLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 80 RHTVGEDFAANGYRTALIGKAHfqpLRDTDAY-PsveaypilqdlafWKQfngpfyGFDHVELARNhtneAHVGQHYALW 158
Cdd:cd16146 80 ETTLAEVFKDAGYRTGIFGKWH---LGDNYPYrP-------------QDR------GFDEVLGHGG----GGIGQYPDYW 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 159 MEekgclnwrDYFLPptgtmdkQIEHKwPIPEQYH-YNT---------WIAERSnalleqykanEEPFFLWSSFFDPHPD 228
Cdd:cd16146 134 GN--------DYFDD-------TYYHN-GKFVKTEgYCTdvffdeaidFIEENK----------DKPFFAYLATNAPHGP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 229 YLVPEPWDTMYdpdrltipkavpgehdrnpphfrmtqeedpdfgawRETGFGIHgyhshvqrspeerkrqVATYYGMVSC 308
Cdd:cd16146 188 LQVPDKYLDPY-----------------------------------KDMGLDDK----------------LAAFYGMIEN 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 309 MDQAIGRILDKLDELGMADNTIVVFTTDHGHFFGQH-----GLQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLV 383
Cdd:cd16146 217 IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPkrfnaGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHI 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 384 DLAPTFLSLAGLPVPS--AMTGVNQSGVWLGEREAARDHAICEFRHEPTTIHQKTY----VDDRYKITVYYNQTYgEIFD 457
Cdd:cd16146 297 DLLPTLLDLCGVKLPEgiKLDGRSLLPLLKGESDPWPERTLFTHSGRWPPPPKKKRnaavRTGRWRLVSPKGFQP-ELYD 375
|
490
....*....|....
gi 1805095636 458 LAEDPDEVRNLWDD 471
Cdd:cd16146 376 IENDPGEENDVADE 389
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-485 |
3.73e-58 |
|
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: 197.07 E-value: 3.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAF--NKDIhTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDR 80
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYgqPLDL-TPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 81 HTVGEDFAANGYRTALIGKAHFQPLRdTDAypsveaypiLQDLAfwkqfngpfygfdhvelarnhtneahvgqhyalwme 160
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGKWHLAGYR-VDA---------LTDFA------------------------------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 161 ekgclnwrdyflpptgtmdkqIEhkwpipeqyhyntWIAERSnalleqykaNEEPFFLWSSFFDPH-----PDYLVP--- 232
Cdd:cd16152 114 ---------------------ID-------------YLDNRQ---------KDKPFFLFLSYLEPHhqndrDRYVAPegs 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 233 -EPWDTMYDPDRLtipKAVPGEhdrnpphfrmTQEEDPDfgawretgfgihgyhshvqrspeerkrqvatYYGMVSCMDQ 311
Cdd:cd16152 151 aERFANFWVPPDL---AALPGD----------WAEELPD-------------------------------YLGCCERLDE 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 312 AIGRILDKLDELGMADNTIVVFTTDHG-HFFGQHGlQHKGGFHyEDLIRLPFIVRYPsRVPAGRVSPAIQSLVDLAPTFL 390
Cdd:cd16152 187 NVGRIRDALKELGLYDNTIIVFTSDHGcHFRTRNA-EYKRSCH-ESSIRVPLVIYGP-GFNGGGRVEELVSLIDLPPTLL 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 391 SLAGLPVPSAMTGVNQSGVWLGEREAARDHA---ICEFR--------------HEPTTIHQKTYVDDRYkitvyynqTYG 453
Cdd:cd16152 264 DAAGIDVPEEMQGRSLLPLVDGKVEDWRNEVfiqISESQvgrairtdrwkysvAAPDKDGWKDSGSDVY--------VED 335
|
490 500 510
....*....|....*....|....*....|....*
gi 1805095636 454 EIFDLAEDPDEVRNLWDDPNQAALKTEL---LLKY 485
Cdd:cd16152 336 YLYDLEADPYELVNLIGRPEYREVAAELrerLLAR 370
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
4-463 |
1.01e-56 |
|
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: 191.64 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDRHT 82
Cdd:cd16032 1 PNILLIMADQLTAAALPAYgNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 83 VGEDFAANGYRTALIGKAHFQplrdtdaypsveaypilqdlafwkqfnGP--FYGFDHvelarnhtneahvgqhyalwme 160
Cdd:cd16032 81 FAHYLRAAGYRTALSGKMHFV---------------------------GPdqLHGFDY---------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 161 ekgclnwrdyflpptgtmDKQIEHKwpiPEQYHYNtwIAERsnalleqykANEEPFFLWSSFFDPHPDYLVPEP-WDtMY 239
Cdd:cd16032 112 ------------------DEEVAFK---AVQKLYD--LARG---------EDGRPFFLTVSFTHPHDPYVIPQEyWD-LY 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 240 dpdrltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshVQRSpeerkRQvaTYYGMVSCMDQAIGRILDK 319
Cdd:cd16032 159 ------------------------------------------------VRRA-----RR--AYYGMVSYVDDKVGQLLDT 183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 320 LDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFhYEDLIRLPFIVRYPSRVPAGRVSPAIqSLVDLAPTFLSLAG---LP 396
Cdd:cd16032 184 LERTGLADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPV-SLVDLLPTLVDLAGggtAP 261
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 397 VPSAMTGVNQSGVWLGEREAARDHAICEFRHEPTTIHQKTYVDDRYKitvyYNQTYGE---IFDLAEDPD 463
Cdd:cd16032 262 HVPPLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVAPCVMIRRGRWK----FIYCPGDpdqLFDLEADPL 327
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
3-468 |
1.65e-56 |
|
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: 193.16 E-value: 1.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTL------GTK 75
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYgSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvgppgsKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 76 LLEDRHTVGEDFAANGYRTALIGKAH------FQPLRdtdaypsveaypilqdlafwkqfngpfYGFDHvelarnhtnea 149
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHlghqpeFLPTR---------------------------HGFDE----------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 150 HVGQHYALWMEEKGCLNWRDYFLPPTGTMDKQIEhKWPiPEQYHYNTWIAERSNALLEqyKANEEPFFLWSSFFDPHpdy 229
Cdd:cd16026 123 YFGIPYSNDMWPFPLYRNDPPGPLPPLMENEEVI-EQP-ADQSSLTQRYTDEAVDFIE--RNKDQPFFLYLAHTMPH--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 230 lvpepwdtmydpdrltIPKAVPgehdrnpPHFRmtqeedpdfgawretgfgihgyhSHVQRSPeerkrqvatyYG-MVSC 308
Cdd:cd16026 196 ----------------VPLFAS-------EKFK-----------------------GRSGAGL----------YGdVVEE 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 309 MDQAIGRILDKLDELGMADNTIVVFTTDHG---HFFGQHG----LQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQS 381
Cdd:cd16026 220 LDWSVGRILDALKELGLEENTLVIFTSDNGpwlEYGGHGGsagpLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELAS 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 382 LVDLAPTFLSLAGLPVPSAMT--GVNQSGVWLGEREAARD-----------HAICEFRHEPTTIHQKTYVDDRYKiTVYY 448
Cdd:cd16026 300 TMDLLPTLAALAGAPLPEDRVidGKDISPLLLGGSKSPPHpffyyydggdlQAVRSGRWKLHLPTTYRTGTDPGG-LDPT 378
|
490 500
....*....|....*....|
gi 1805095636 449 NQTYGEIFDLAEDPDEVRNL 468
Cdd:cd16026 379 KLEPPLLYDLEEDPGETYNV 398
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-405 |
3.50e-56 |
|
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: 188.53 E-value: 3.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFNKD-IHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWtlGTKLLEDRHT 82
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDrVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW--GGPLEPDDPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 83 VGEDFAANGYRTALIgkahfqplrdTDAYPSVEAYPILQdlafwkqfngpfyGFDHVELARNHTNEAHVGQHYalwmeek 162
Cdd:cd16148 79 LAEILRKAGYYTAAV----------SSNPHLFGGPGFDR-------------GFDTFEDFRGQEGDPGEEGDE------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 163 gclnwrdyflPPTGTMDKQIEhkwpipeqyhyntWIAERsnalleqykANEEPFFLWSSFFDPHPDYLvpepwdtmydpd 242
Cdd:cd16148 129 ----------RAERVTDRALE-------------WLDRN---------ADDDPFFLFLHYFDPHEPYL------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 243 rltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrspeerkrqvatYYGMVSCMDQAIGRILDKLDE 322
Cdd:cd16148 165 -----------------------------------------------------------YDAEVRYVDEQIGRLLDKLKE 185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 323 LGMADNTIVVFTTDHGHFFGQHGLQHKGGFH-YEDLIRLPFIVRYPSRVPAGRVSpAIQSLVDLAPTFLSLAGLPVPSAM 401
Cdd:cd16148 186 LGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEPGKRVD-ALVSHIDIAPTLLDLLGVEPPDYS 264
|
....
gi 1805095636 402 TGVN 405
Cdd:cd16148 265 DGRS 268
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-400 |
1.96e-52 |
|
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: 178.20 E-value: 1.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLI-TSDQQHWNTIGAFNKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGA--W---------T 71
Cdd:cd16149 1 PNILFIlTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdWivegshgktK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 72 LGTKLLEDRHTVGEDFAANGYRTALIGKahfqplrdtdaypsveaypilqdlafWkqfngpfygfdhvelarnhtneaHV 151
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGK--------------------------W-----------------------HL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 152 GqhyalwmeekgclnwrdyflpptgtmDKQIEHkwpipeqyhyntwiaersnalLEQYKANEEPFFLWSSFFDPHpdylv 231
Cdd:cd16149 112 G--------------------------DDAADF---------------------LRRRAEAEKPFFLSVNYTAPH----- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 232 pEPWDtmydpdrltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrspeerkrqvatYYGMVSCMDQ 311
Cdd:cd16149 140 -SPWG-----------------------------------------------------------------YFAAVTGVDR 153
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 312 AIGRILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFH-----YEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLA 386
Cdd:cd16149 154 NVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKGNGTfplnmYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFF 233
|
410
....*....|....
gi 1805095636 387 PTFLSLAGLPVPSA 400
Cdd:cd16149 234 PTLLELAGVDPPAD 247
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-449 |
2.66e-52 |
|
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: 179.71 E-value: 2.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQ-HWNTIGAFNKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAW-TLG----TKLL 77
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTdTLGspmqPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 78 EDRHTVGEDFAANGYRTALIGKAHFQplrdtdaypsveaypilqdlafwkqfngpfygfdhvelarNHTNEAhvgqhyal 157
Cdd:cd16035 81 PDVPTLGHMLRAAGYYTAYKGKWHLS----------------------------------------GAAGGG-------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 158 wmeekgclnwrdyflpptgtmdkqiehkwpipeqYHYNTWIAERSNALLEQ---YKANEEPFFLWSSFFDPHpdylvpep 234
Cdd:cd16035 113 ----------------------------------YKRDPGIAAQAVEWLRErgaKNADGKPWFLVVSLVNPH-------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 235 wDTMYDPDrltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrsPEERKRQVATYYG-MVSCMDQAI 313
Cdd:cd16035 151 -DIMFPPD-------------------------------------------------DEERWRRFRNFYYnLIRDVDRQI 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 314 GRILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLA 393
Cdd:cd16035 181 GRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLA 260
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805095636 394 GLPVPSAMT------GVNQSGVWLGEREAARDHAICeFrhepttihqkTYvdDRYKITVYYN 449
Cdd:cd16035 261 GVDAEARATeapplpGRDLSPLLTDADADAVRDGIL-F----------TY--DRYKFARYFD 309
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-469 |
6.96e-52 |
|
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: 180.86 E-value: 6.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFNKD--IHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYP--SQHGAWTLGTK---- 75
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDskIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPwrSRLKGGVLGGFsppl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 76 LLEDRHTVGEDFAANGYRTALIGKAHFQpLRDTDAYPSVEAYPILQDLAFWKQF-NGPF-YGFDHvelarnhtneahvgq 153
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWHLG-LDWKKKDGKKAATGTGKDVDYSKPIkGGPLdHGFDY--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 154 hyalwmeekgclnwrdYFLPPTGTMDKQIehkwpipeqyhyntwiAERSNALLEQYKANEEPFFLWSSFFDPHpdylvpE 233
Cdd:cd16143 145 ----------------YFGIPASEVLPTL----------------TDKAVEFIDQHAKKDKPFFLYFALPAPH------T 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 234 PWdtmydpdrltipkaVPgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrSPEERKRQVATYYG-MVSCMDQA 312
Cdd:cd16143 187 PI--------------VP---------------------------------------SPEFQGKSGAGPYGdFVYELDWV 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 313 IGRILDKLDELGMADNTIVVFTTDHG----HFFG---QHGLQHKGGFH------YEDLIRLPFIVRYPSRVPAGRVSPAI 379
Cdd:cd16143 214 VGRILDALKELGLAENTLVIFTSDNGpspyADYKeleKFGHDPSGPLRgmkadiYEGGHRVPFIVRWPGKIPAGSVSDQL 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 380 QSLVDLAPTFLSLAGLPVPS--AMTGVNQSGVWLGEREAARDHAIceFRHEPTT------------IHQKTYVDDRYKIT 445
Cdd:cd16143 294 VSLTDLFATLAAIVGQKLPDnaAEDSFSFLPALLGPKKQEVRESL--VHHSGNGsfairkgdwkliDGTGSGGFSYPRGK 371
|
490 500
....*....|....*....|....
gi 1805095636 446 VYYNQTYGEIFDLAEDPDEVRNLW 469
Cdd:cd16143 372 EKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
3-468 |
5.40e-50 |
|
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: 176.09 E-value: 5.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAFNKDIHTPSLDRLAREGTTFTRAYCpNPTCTPSRASIITGMYPSQHG----AWTLGTK--- 75
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHHQVGmgtmAELATGKpgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 76 --LLEDRH-TVGEDFAANGYRTALIGKahfqplrdtdaypsveaypilqdlafWkqfngpfygfdhvelarnhtneaHVG 152
Cdd:cd16025 81 egYLPDSAaTIAEVLKDAGYHTYMSGK--------------------------W-----------------------HLG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 153 qhyalwmeekgclnwrdyflpptgtmdkqiehkwpiPEQYHYNTWIAERSNALLEQYKANEEPFFLWSSFFDPHPDYLVP 232
Cdd:cd16025 112 ------------------------------------PDDYYSTDDLTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 233 EPW--------DTMYDP---DRLT-------IPKAVPgehdrNPPHfrmtqeeDPDFGAWREtgfgihgyhshvqRSPEE 294
Cdd:cd16025 156 KEWidkykgkyDAGWDAlreERLErqkelglIPADTK-----LTPR-------PPGVPAWDS-------------LSPEE 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 295 RK---RQVATYYGMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHG-------------HFFGQHGLQHKGGfhyedlI 358
Cdd:cd16025 211 KKleaRRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwanasntPFRLYKQASHEGG------I 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 359 RLPFIVRYPSRVPA-GRVSPAIQSLVDLAPTFLSLAGLPVPSAMTGVNQ---SGV-----WLGEREAARDHAICeFRHEp 429
Cdd:cd16025 285 RTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPQlplDGVsllptLDGAAAPSRRRTQY-FELF- 362
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1805095636 430 ttiHQKTYVDDRYKItVYYNQTYG-----EIFDLAEDPDEVRNL 468
Cdd:cd16025 363 ---GNRAIRKGGWKA-VALHPPPGwgdqwELYDLAKDPSETHDL 402
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-469 |
9.83e-50 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 174.64 E-value: 9.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFNKDIH----TPSLDRLAREGTTFTRAYCpNPTCTPSRASIITGMYPSQHGAWTLGTK---- 75
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGrgapTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGLTTVGLPgspg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 76 -LLEDRHTVGEDFAANGYRTALIGKAHfqpLRDTDaypsvEAYPILQdlafwkqfngpfyGFDhvelarnhtneahvgqh 154
Cdd:cd16142 80 gLPPWEPTLAELLKDAGYATAQFGKWH---LGDED-----GRLPTDH-------------GFD----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 155 yalwmEEKGCLNwrdyflpptGTMDKQIEhkwpipeqyhyntwiaERSNALLEQYKANEEPFFLWSSFFDPHPDylvpep 234
Cdd:cd16142 122 -----EFYGNLY---------HTIDEEIV----------------DKAIDFIKRNAKADKPFFLYVNFTKMHFP------ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 235 wdtmydpdrlTIPKavpgehdrnpphfrmtqeedPDFGAwRETGFGIhgYHShvqrspeerkrqvatyyGMVScMDQAIG 314
Cdd:cd16142 166 ----------TLPS--------------------PEFEG-KSSGKGK--YAD-----------------SMVE-LDDHVG 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 315 RILDKLDELGMADNTIVVFTTDHGH------------FFGQHGLQHKGGFhyedliRLPFIVRYPSRVPAGRVSPAIQSL 382
Cdd:cd16142 195 QILDALDELGIADNTIVIFTTDNGPeqdvwpdggytpFRGEKGTTWEGGV------RVPAIVRWPGKIKPGRVSNEIVSH 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 383 VDLAPTFLSLAGLPVPSAMT--------GVNQSGVWLGEREAARDHAIceFRHEPTT----------IHQKTYVDDRY-K 443
Cdd:cd16142 269 LDWFPTLAALAGAPDPKDKLlgkdrhidGVDQSPFLLGKSEKSRRSEF--FYFGEGElgavrwknwkVHFKAQEDTGGpT 346
|
490 500
....*....|....*....|....*.
gi 1805095636 444 ITVYYNQTYGEIFDLAEDPDEVRNLW 469
Cdd:cd16142 347 GEPFYVLTFPLIFNLRRDPKERYDVT 372
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
4-395 |
2.11e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 168.76 E-value: 2.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWT-LGTKLLEDRH 81
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYgYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVsTPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 82 TVGEDFAANGYRTALIGKAHfqplrdtdaypsveaypilqdLAFWKQFNGPFYGFDHVeLARNHTNEAHVGQHYalwmee 161
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWH---------------------LGWYNNQSPCNLGFDKF-FGRNTGSDLYADPPD------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 162 kgclnwRDYFLPPTGTMDKQIehkwpipeqyhyntwiAERSNALLEQykaNEEPFFLWSSFFDPHPDYLVPEPWDTMYdp 241
Cdd:pfam00884 133 ------VPYNCSGGGVSDEAL----------------LDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKY-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 242 drltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhSHVQRSPEERKRQVATYYGMVSCMDQAIGRILDKLD 321
Cdd:pfam00884 186 --------------------------------------------ATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLE 221
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805095636 322 ELGMADNTIVVFTTDHG--HFFGQHGLQ-HKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGL 395
Cdd:pfam00884 222 ENGLLDNTLVVYTSDHGesLGEGGGYLHgGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-468 |
6.53e-45 |
|
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: 161.61 E-value: 6.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCpNPTCTPSRASIITGMYPSQHGAWTlgtKLLEDR-H 81
Cdd:cd16151 1 PNIILIMADDLGYECIGCYgGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNYVVF---GYLDPKqK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 82 TVGEDFAANGYRTALIGKAHFQPLRDTDAYPsveaypilQDLafwkqfngpfyGFDHvelarnhtneahvgqhYALW--- 158
Cdd:cd16151 77 TFGHLLKDAGYATAIAGKWQLGGGRGDGDYP--------HEF-----------GFDE----------------YCLWqlt 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 159 -MEEKGCLNWRDYFLPPTGtmdkqiEHKWPIPEQYHYNTWiaerSNALLEQYKAN-EEPFFLWssffdpHPDYLVPEPWD 236
Cdd:cd16151 122 eTGEKYSRPATPTFNIRNG------KLLETTEGDYGPDLF----ADFLIDFIERNkDQPFFAY------YPMVLVHDPFV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 237 TMYDPDRltiPKAVPGEHDRNPPHFRmtqeedpdfgawretgfgihgyhshvqrspeerkrqvatyyGMVSCMDQAIGRI 316
Cdd:cd16151 186 PTPDSPD---WDPDDKRKKDDPEYFP-----------------------------------------DMVAYMDKLVGKL 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 317 LDKLDELGMADNTIVVFTTDHGHFFGQHGLQHKG------GFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFL 390
Cdd:cd16151 222 VDKLEELGLRENTIIIFTGDNGTHRPITSRTNGRevrggkGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLA 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 391 SLAGLPVPS--AMTGVNQSGVWLGEREAARDHAICeFRHEPTTIHQKTYV--DDRYKitvYYNqtYGEIFDLAEDPDEVR 466
Cdd:cd16151 302 ELAGAPLPEdyPLDGRSFAPQLLGKTGSPRREWIY-WYYRNPHKKFGSRFvrTKRYK---LYA--DGRFFDLREDPLEKN 375
|
..
gi 1805095636 467 NL 468
Cdd:cd16151 376 PL 377
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-405 |
1.18e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 158.31 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAFNK-----------DIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWT 71
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlgYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 72 LG---TKLLEDRHTVGEDFAANGYRTALIGKAHFQPLRDtdaypsveaypilqdlaFWKQFNGPFYGFdhvelarnhtne 148
Cdd:cd16153 81 FEaahPALDHGLPTFPEVLKKAGYQTASFGKSHLEAFQR-----------------YLKNANQSYKSF------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 149 ahvgqhyalwmeekgclnwrdyflpptgtmdkqiehkwpipeqYHYNTWIAERSnalleqykaneEPFFLWSSFFDPHPD 228
Cdd:cd16153 132 -------------------------------------------WGKIAKGADSD-----------KPFFVRLSFLQPHTP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 229 YLVPEPWDTMYDpdrltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrspeerkrqvatYYGMVSC 308
Cdd:cd16153 158 VLPPKEFRDRFD-------------------------------------------------------------YYAFCAY 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 309 MDQAIGRILDKLDELGMA---DNTIVVFTTDHGHFFGQHGLQHKGGFHYEDlIRLPFIVRYP--SRVPAGRVSPAIQSLV 383
Cdd:cd16153 177 GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGILAKFTFWPQS-HRVPLIVVSSdkLKAPAGKVRHDFVEFV 255
|
410 420
....*....|....*....|....
gi 1805095636 384 DLAPTFLSLAGLPV--PSAMTGVN 405
Cdd:cd16153 256 DLAPTLLAAAGVDVdaPDYLDGRD 279
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
4-469 |
6.75e-38 |
|
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: 143.07 E-value: 6.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFNKD-IHTPSLDRLAREGTTFTRAYCpNPTCTPSRASIITGMYPS----QHGA--WTLGTKL 76
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIhtgmQHGVilAGEPYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 77 LEDRHTVGEDFAANGYRTALIGKAHfqplrdtdaypsveaypilqdLAFWKQFNGPFY-GFDHvelarnhtneaHVGQ-- 153
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWH---------------------LGFYTWEYTPTNrGFDS-----------FYGYyg 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 154 ----HYALWMEEkGCLNWRDYFLPPTGTMDKQIEHkwpipeqyhYNTWI-AERSNALLEQYKAnEEPFFLWSSFFDPH-- 226
Cdd:cd16029 128 gaedYYTHTSGG-ANDYGNDDLRDNEEPAWDYNGT---------YSTDLfTDRAVDIIENHDP-SKPLFLYLAFQAVHap 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 227 ----PDYLVPEPWDTMYDPDrltipkavpgeHDRnpphfrmtqeedpdfgawretgfgihgyhshvqrspeerkrqvATY 302
Cdd:cd16029 197 lqvpPEYADPYEDKFAHIKD-----------EDR-------------------------------------------RTY 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 303 YGMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHGhffGQHGLQH-------KGGFH--YEDLIRLPFIVRYPSRVP-A 372
Cdd:cd16029 223 AAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG---GPTGGGDggsnyplRGGKNtlWEGGVRVPAFVWSPLLPPkR 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 373 GRVSPAIQSLVDLAPTFLSLAGLPVPS--AMTGVNQSGVWLGEREAARDHAICEFRHEPTTIHQKTYVDDRYKITVyyNQ 450
Cdd:cd16029 300 GTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQWDALSGGAPSPRTEILLNIDDITRTTGGAAIRVGDWKLIV--GK 377
|
490
....*....|....*....
gi 1805095636 451 TygeIFDLAEDPDEVRNLW 469
Cdd:cd16029 378 P---LFNIENDPCERNDLA 393
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
3-413 |
4.94e-34 |
|
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: 132.21 E-value: 4.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAFNK--DIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGA-------WTLG 73
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApnAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVghnflptSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 74 TKLLEDrhTVGEDFAANGYRTALIGKAHfqpLRDTDAY-PSveaypilqdlafwkqfngpFYGFDHVeLARNHTNEAHVG 152
Cdd:cd16161 81 LPLNET--TLAEVLRQAGYATGMIGKWH---LGQREAYlPN-------------------SRGFDYY-FGIPFSHDSSLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 153 QHYAlwmeekgclnwrdyflpptgtmdkqiehkwpipeqyhyntwiaERSNALLEQYKANEEPFFLWSSFFDPHpdylVP 232
Cdd:cd16161 136 DRYA-------------------------------------------QFATDFIQRASAKDRPFFLYAALAHVH----VP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 233 EPwdtmydpdrltipkavpgehdrNPPHFRMTQEEDPDFGAwretgfgihgyhshvqrspeerkrqvatyygMVSCMDQA 312
Cdd:cd16161 169 LA----------------------NLPRFQSPTSGRGPYGD-------------------------------ALQEMDDL 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 313 IGRILDKLDELGMADNTIVVFTTD---------------HGHFFGQHGLQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSP 377
Cdd:cd16161 196 VGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSA 275
|
410 420 430
....*....|....*....|....*....|....*...
gi 1805095636 378 AIQSLVDLAPTFLSLAGLPVPSA--MTGVNQSGVWLGE 413
Cdd:cd16161 276 ALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVLFGG 313
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
3-464 |
1.43e-29 |
|
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: 120.61 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAFNKDIHTPS-LDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHG---------AWTl 72
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGpIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGmyggtrvflPWD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 73 GTKLLEDRHTVGEDFAANGYRTALIGKAHF--QPLRDTDAY--PSveaypilqdlafwkqfngpFYGFDHVELARNHTNE 148
Cdd:cd16160 80 IGGLPKTEVTMAEALKEAGYTTGMVGKWHLgiNENNHSDGAhlPS-------------------HHGFDFVGTNLPFTNS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 149 ---AHVGQHYALWMEEKGCLNWRDyflpptgTMDKQiehkwPIPEQYHYNTWIAERSNALLEQYkanEEPFFLWSSFFDP 225
Cdd:cd16160 141 wacDDTGRHVDFPDRSACFLYYND-------TIVEQ-----PIQHEHLTETLVGDAKSFIEDNQ---ENPFFLYFSFPQT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 226 HPdylvpepwdTMYdpdrltipkavpgehdrNPPHFRMTQEEdpdfgawretgfGIHGYHshvqrspeerkrqvatyygm 305
Cdd:cd16160 206 HT---------PLF-----------------ASKRFKGKSKR------------GRYGDN-------------------- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 306 VSCMDQAIGRILDKLDELGMADNTIVVFTTDHG-HF-FGQHG-----LQHKGGFHYEDLIRLPFIVRYPSRVPaGRVSPA 378
Cdd:cd16160 228 INEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGpHVeYCLEGgstggLKGGKGNSWEGGIRVPFIAYWPGTIK-PRVSHE 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 379 IQSLVDLAPTFLSLAG--LPVPSAMTGVNQSGVWLGEREAARDHAI--CE-----FRHEPTTIHQKT-----------YV 438
Cdd:cd16160 307 VVSTMDIFPTFVDLAGgtLPTDRIYDGLSITDLLLGEADSPHDDILyyCCsrlmaVRYGSYKIHFKTqplpsqesldpNC 386
|
490 500 510
....*....|....*....|....*....|....*..
gi 1805095636 439 DDRYKITVYYNQTYGE-----------IFDLAEDPDE 464
Cdd:cd16160 387 DGGGPLSDYIVCYDCEdecvtkhnpplIFDVEKDPGE 423
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-464 |
3.90e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 118.22 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIGAFN--KDI-HTPSLDRLAREGTTFTRAYCpNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDR 80
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSlsSDLpVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 81 HTV----GEDFAANGYRTALIGKAHFQplrdtdaypsveaypilqdlafwkqfNGPfygfdhvelarNHTNEAHVGQHYA 156
Cdd:cd16154 80 ETLlqllIKDATTAGYSSAVIGKWHLG--------------------------GND-----------NSPNNPGGIPYYA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 157 lwmeekGCL--NWRDYFLPPTGTMDKQIEHKwpipeqyHYNT---------WIAERSnalleqykaneEPFFLWSSFFDP 225
Cdd:cd16154 123 ------GILggGVQDYYNWNLTNNGQTTNST-------EYATtkltnlaidWIDQQT-----------KPWFLWLAYNAP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 226 HPDYLVPepwdtmydPDRLtipkavpgeHDRNPphfrmtqeedpdfgawretgfgihgyhSHVQRSPEERKRqvATYYGM 305
Cdd:cd16154 179 HTPFHLP--------PAEL---------HSRSL---------------------------LGDSADIEANPR--PYYLAA 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 306 VSCMDQAIGRILDKLDElGMADNTIVVFTTDHG--------HFFGQHGlqhKGGFhYEDLIRLPFIVrYPSRVP-AGRVS 376
Cdd:cd16154 213 IEAMDTEIGRLLASIDE-EERENTIIIFIGDNGtpgqvvdlPYTRNHA---KGSL-YEGGINVPLIV-SGAGVErANERE 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 377 PAIQSLVDLAPTFLSLAGLPVP---------SAMTGVNQSgvwlgereaARDHAICEFRHEPTTIHqkTYVDDRYKITVY 447
Cdd:cd16154 287 SALVNATDLYATIAELAGVDAAeihdsvsfkPLLSDVNAS---------TRQYNYTEYESPTTTGW--ATRNQYYKLIES 355
|
490
....*....|....*..
gi 1805095636 448 YNQTYgEIFDLAEDPDE 464
Cdd:cd16154 356 ENGQE-ELYDLINDPSE 371
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
3-399 |
8.46e-28 |
|
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: 116.23 E-value: 8.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYP--SQHGAWTLGTKLL-- 77
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFgNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirSGMASSHGMRVILft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 78 -------EDRHTVGEDFAANGYRTALIGKAHFQPLRDTdaypsveaypiLQDLAFwkqfnGPF-YGFDHvelarnhtnea 149
Cdd:cd16159 81 assgglpPNETTFAEVLKQQGYSTALIGKWHLGLHCES-----------RNDFCH-----HPLnHGFDY----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 150 hvgqHYALWMEekgclNWRDYFLPPTGTMDKQIEHKWPIPEQYHYNTWIAERsnALLEQYKANEEPFF-----------L 218
Cdd:cd16159 134 ----FYGLPLT-----NLKDCGDGSNGEYDLSFDPLFPLLTAFVLITALTIF--LLLYLGAVSKRFFVfllilsllfisL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 219 WSSFFDPHPDY---------LVPEPwdtmYDPDRLT---IPKAVpgehdrnppHFRMTQEEDP--DFGAWretgfgiHGY 284
Cdd:cd16159 203 FFLLLITNRYFncilmrnheVVEQP----MSLENLTqrlTKEAI---------SFLERNKERPflLVMSF-------LHV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 285 HSHVQRSPEERKRQVATYYG-MVSCMDQAIGRILDKLDELGMADNTIVVFTTDHG----------HFFGQHGLQHKGGFH 353
Cdd:cd16159 263 HTALFTSKKFKGRSKHGRYGdNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGghleeisvggEYGGGNGGIYGGKKM 342
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1805095636 354 --YEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAPTFLSLAGLPVPS 399
Cdd:cd16159 343 ggWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPS 390
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
3-420 |
1.35e-27 |
|
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: 115.26 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAF-NKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTK------ 75
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFgEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHarnayt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 76 -------LLEDRHTVGEDFAANGYRTALIGKAHfqpLRDTDAYpsveaYPILQDLAFWkqFNGP---FYGFDHVELAR-- 143
Cdd:cd16157 81 pqnivggIPDSEILLPELLKKAGYRNKIVGKWH---LGHRPQY-----HPLKHGFDEW--FGAPnchFGPYDNKAYPNip 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 144 NHTNEAHVGQHYAlwmeekgclnwrdyflpptgtmDKQIEHKwpIPEQYHYNTWIaERSNALLEQYKANEEPFFLWssff 223
Cdd:cd16157 151 VYRDWEMIGRYYE----------------------EFKIDKK--TGESNLTQIYL-QEALEFIEKQHDAQKPFFLY---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 224 dphpdylvpepwdtmydpdrltipkavpgehdrnpphfrmtqeedpdfgawretgFGIHGYHSHVQRSPEER-KRQVATY 302
Cdd:cd16157 202 -------------------------------------------------------WAPDATHAPVYASKPFLgTSQRGLY 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 303 YGMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHG---HFFGQHGlQHKGGF------HYEDLIRLPFIVRYPSRVPAG 373
Cdd:cd16157 227 GDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQG-GSNGPFlcgkqtTFEGGMREPAIAWWPGHIKPG 305
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1805095636 374 RVSPAIQSLVDLAPTFLSLAGLPVPS--AMTGVNQSGVWLGEREAARDH 420
Cdd:cd16157 306 QVSHQLGSLMDLFTTSLALAGLPIPSdrAIDGIDLLPVLLNGKEKDRPI 354
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
3-486 |
1.55e-23 |
|
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: 103.29 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAFNkdiH----TPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAW-------- 70
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYG---HpsssTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpgvfypgs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 71 TLGTKLLEDrhTVGEDFAANGYRTALIGKAHfqplrdtdaypsveaypilqdLAFWKqfNGPF----YGFDHVeLARNHT 146
Cdd:cd16158 78 RGGLPLNET--TIAEVLKTVGYQTAMVGKWH---------------------LGVGL--NGTYlpthQGFDHY-LGIPYS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 147 NEAHVGQHYALWMEEKGCLNWRDYFLPPTGTMDKQIehkwpIPEQYHYNTWIAERSNALLEQYKAN----EEPFFLWSSF 222
Cdd:cd16158 132 HDQGPCQNLTCFPPNIPCFGGCDQGEVPCPLFYNES-----IVQQPVDLLTLEERYAKFAKDFIADnakeGKPFFLYYAS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 223 FDPHpdylvpepwdtmydpdrltipkavpgehdrnpphfrmtqeeDPDFGAWRETGFGIHGyhshvqrspeerkrqvaTY 302
Cdd:cd16158 207 HHTH-----------------------------------------YPQFAGQKFAGRSSRG-----------------PF 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 303 YGMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHGHFF------GQHGLQHKG-GFHYEDLIRLPFIVRYPSRVPAGRV 375
Cdd:cd16158 229 GDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKCGkGTTYEGGVREPAIAYWPGRIKPGVT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 376 SpAIQSLVDLAPTFLSLAGLPVPS-AMTGVNQSGVWLGEREAARDhaicEFRHEPTTIHQKTYV----DDRYKITvYYNQ 450
Cdd:cd16158 309 H-ELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPRQ----TFFYYPTSPDPDKGVfavrWGKYKAH-FYTQ 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805095636 451 -------------------TYGE---IFDLAEDPDEVRNLWDDPNQAALKTELLLKYA 486
Cdd:cd16158 383 gaahsgttpdkdchpsaelTSHDpplLFDLSQDPSENYNLLGLPEYNQVLKQIQQVKE 440
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
4-463 |
2.32e-21 |
|
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: 95.69 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSDQQHWNTIG-AFNKDIHTPSLDRLAREGTTFTRAYCPNPTCTPSRASIITGMYPSQHGAWTLGTKLLEDRHT 82
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFrPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 83 VGEDFAANGYRTALIGKAHFqplrdTDAYPS----VEAYPilQDLAFwkqfngpfygfdhvelarnhtneahvgqhyALW 158
Cdd:cd16171 81 WMDRLEKHGYHTQKYGKLDY-----TSGHHSvsnrVEAWT--RDVPF------------------------------LLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 159 MEEKGCLNwrdyfLPPTGTMDKQIEHKWPIPEQYhyNTWIAERSNALleqykanEEPFFLWSSFFDPHPdylvpEPWDTM 238
Cdd:cd16171 124 QEGRPTVN-----LVGDRSTVRVMLKDWQNTDKA--VHWIRKEAPNL-------TQPFALYLGLNLPHP-----YPSPSM 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 239 ydpdrltipkavpgehdrnpphfrmtqeeDPDFGAWREtgfgIHGYhshvqrspeerkrqvatYYGMVSCMDQAIGRILD 318
Cdd:cd16171 185 -----------------------------GENFGSIRN----IRAF-----------------YYAMCAETDAMLGEIIS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 319 KLDELGMADNTIVVFTTDHGHFFGQHGLQHKGGFhYEDLIRLPFIVRYPsRVPAGRVSPAIQSLVDLAPTFLSLAGLPVP 398
Cdd:cd16171 215 ALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGP-GIKAGQQVSDVVSLVDIYPTMLDIAGVPQP 292
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805095636 399 SAMTGV-------NQSGVWLGEREAARDHAICEFrhEPTTIHQKTYV--DDRYKITVYY--NQTYGEIFDLAEDPD 463
Cdd:cd16171 293 QNLSGYsllpllsESSIKESPSRVPHPDWVLSEF--HGCNVNASTYMlrTNSWKYIAYAdgNSVPPQLFDLSKDPD 366
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
3-399 |
1.37e-19 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 92.02 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 3 KPNILLITSDQQHWNTIGAFNKDIH-TPSLDRLAREGTTFTRAYcpNPTCTPSRA--SIITGMYPSQHGAWTLgTKLLED 79
Cdd:COG1368 234 KPNVVVILLESFSDFFIGALGNGKDvTPFLDSLAKESLYFGNFY--SQGGRTSRGefAVLTGLPPLPGGSPYK-RPGQNN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 80 RHTVGEDFAANGYRTALIgkahfqplrdtdaYPSveaypilqDLAFWKQFNgpFY---GFDHVelarnhtneahVGQhya 156
Cdd:COG1368 311 FPSLPSILKKQGYETSFF-------------HGG--------DGSFWNRDS--FYknlGFDEF-----------YDR--- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 157 lwmeekgclnwrdyflpptGTMDKQIEHKWPIPEQYHYNtwiaersnALLEQYKANEEPFFlwsSFF---DPHPDYLVPE 233
Cdd:COG1368 354 -------------------EDFDDPFDGGWGVSDEDLFD--------KALEELEKLKKPFF---AFLitlSNHGPYTLPE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 234 pwdtmydpdrltipkavpgehdrnpphfrmtqeEDPDFgawretgfgihgyhshvqrsPEERKRQVATYYGMVSCMDQAI 313
Cdd:COG1368 404 ---------------------------------EDKKI--------------------PDYGKTTLNNYLNAVRYADQAL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 314 GRILDKLDELGMADNTIVVFTTDHGHFFGQHGLQHkggfHYEDLIRLPFIVRYPSrVPAGRVSPAIQSLVDLAPTFLSLA 393
Cdd:COG1368 431 GEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYE----NPLERYRVPLLIYSPG-LKKPKVIDTVGSQIDIAPTLLDLL 505
|
....*.
gi 1805095636 394 GLPVPS 399
Cdd:COG1368 506 GIDYPS 511
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
260-393 |
1.31e-18 |
|
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: 84.78 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 260 HFRMTQEEDPDFGAWRETGFGiHGYHSHVQRSPEerkrqvatYYGMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHGH 339
Cdd:cd00016 111 AIDETSKEKPFVLFLHFDGPD-GPGHAYGPNTPE--------YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1805095636 340 FFGQHGLQHKGGFH---YEDLIRLPFIVRYPsRVPAGRVSPAIQSLVDLAPTFLSLA 393
Cdd:cd00016 182 IDKGHGGDPKADGKadkSHTGMRVPFIAYGP-GVKKGGVKHELISQYDIAPTLADLL 237
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
4-394 |
1.09e-17 |
|
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: 83.12 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 4 PNILLITSD--QQHWNTIGAFNKDIhTPSLDRLAREGTTFTRAYCPNPTCTPSRA--SIITGMYPSQHGAWTLGTKLLED 79
Cdd:cd16015 1 PNVIVILLEsfSDPYIDKDVGGEDL-TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 80 RHTVGEDFAANGYRTALIgkahfqplrdtdaYPSveaypilqDLAFWKQFNgpFY---GFDHVElarnhtneahvgqhya 156
Cdd:cd16015 80 LPSLPSILKEQGYETIFI-------------HGG--------DASFYNRDS--VYpnlGFDEFY---------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 157 lwmeekgclnWRDYFlpptgTMDKQIEHKWPIPEQYHYntwiaERSNALLEQYKanEEPFFLwssFF---DPHPDYLVPE 233
Cdd:cd16015 121 ----------DLEDF-----PDDEKETNGWGVSDESLF-----DQALEELEELK--KKPFFI---FLvtmSNHGPYDLPE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 234 PWDTMYDPDrltipkavpgehdrnpphfrmtqeedpdfgawretgfgihgyhshvqrspEERKRQVATYYGMVSCMDQAI 313
Cdd:cd16015 176 EKKDEPLKV--------------------------------------------------EEDKTELENYLNAIHYTDKAL 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 314 GRILDKLDELGMADNTIVVFTTDHGHFFGQHglQHKGGFHYEDLIRLPFIVRYPSRVPAGRVSPAIqSLVDLAPTFLSLA 393
Cdd:cd16015 206 GEFIEKLKKSGLYENTIIVIYGDHLPSLGSD--YDETDEDPLDLYRTPLLIYSPGLKKPKKIDRVG-SQIDIAPTLLDLL 282
|
.
gi 1805095636 394 G 394
Cdd:cd16015 283 G 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-339 |
6.91e-11 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 64.00 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 1 MAKPNILLITSDQQHWNTIGAFnkdiHTPSLDRLAREGTTFTRAYCPNPTCT-PSRASIITGMYPSQHGawtlgtklled 79
Cdd:COG1524 21 PPAKKVVLILVDGLRADLLERA----HAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYPGEHG----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 80 rhtvgedfaangyrtaLIGKAHFQPLRDTDAYPSVEAYPILQDLAFWKQfnGPFYgfdhvELARNHtneahvGQHYAlwm 159
Cdd:COG1524 86 ----------------IVGNGWYDPELGRVVNSLSWVEDGFGSNSLLPV--PTIF-----ERARAA------GLTTA--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 160 eekgCLNWRDYFLPP--TGTMDKQIEHKWPIPEQYHYNTWIAERSNALLEQYKaneePFFLWSSFfdPHPDYLvpepwdt 237
Cdd:COG1524 134 ----AVFWPSFEGSGliDAARPYPYDGRKPLLGNPAADRWIAAAALELLREGR----PDLLLVYL--PDLDYA------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 238 mydpdrltipkavpgEHDrnpphfrmtqeedpdfgawretgfgiHGYHShvqrspEERKRQVATyygmvscMDQAIGRIL 317
Cdd:COG1524 197 ---------------GHR--------------------------YGPDS------PEYRAALRE-------VDAALGRLL 222
|
330 340
....*....|....*....|..
gi 1805095636 318 DKLDELGMADNTIVVFTTDHGH 339
Cdd:COG1524 223 DALKARGLYEGTLVIVTADHGM 244
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
179-390 |
3.96e-10 |
|
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: 62.23 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 179 DKQIEHKWpipeqyhyNTWIAERSNalleqykanEEPFFLWSSFFDPHpDYLVPEPWDTMYDPDRltipkavpgehdrNP 258
Cdd:COG3083 363 DRQITAQW--------LQWLDQRDS---------DRPWFSYLFLDAPH-AYSFPADYPKPFQPSE-------------DC 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 259 PHFRMTQEEDPDfgawretgfgihgyhshvqrsPEERKRQVATYYgmvscMDQAIGRILDKLDELGMADNTIVVFTTDHG 338
Cdd:COG3083 412 NYLALDNESDPT---------------------PFKNRYRNAVHY-----VDSQIGRVLDTLEQRGLLENTIVIITADHG 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1805095636 339 HFFGQHGLQHKGGFHY--EDLIRLPFIVRYPSRvPAGRVSpAIQSLVDLAPTFL 390
Cdd:COG3083 466 EEFNENGQNYWGHNSNfsRYQLQVPLVIHWPGT-PPQVIS-KLTSHLDIVPTLM 517
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
22-394 |
8.94e-10 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 59.52 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 22 FNKDIHTPSLDRLAREGTTFTRAYCPNPTCT-PSRASIITGMYPSQHGawtlgtklledrhtvgedFAANGYrtaligka 100
Cdd:cd16018 16 LDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTfPNHYSIVTGLYPESHG------------------IVGNYF-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 101 hFQPLRDTdaypsveaypilqdlAFWKQFNGPFYGFDHVE--LARNHTNEAHVGQHYalWmeeKGCL-NWRDYFLPPtgt 177
Cdd:cd16018 70 -YDPKTNE---------------EFSDSDWVWDPWWIGGEpiWVTAEKAGLKTASYF--W---PGSEvAIIGYNPTP--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 178 mdkqiEHKWPIPEQYHYNTWIAERSNALLEqykaneepfflwssffdphpdylvpepWDTMYDPDRLTIpkavpgehdrn 257
Cdd:cd16018 126 -----IPLGGYWQPYNDSFPFEERVDTILE---------------------------WLDLERPDLILL----------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 258 ppHFrmtqeEDPDFgawretgFG-IHGYHShvqrspEERKRQVATyygmvscMDQAIGRILDKLDELGMADNTIVVFTTD 336
Cdd:cd16018 163 --YF-----EEPDS-------AGhKYGPDS------PEVNEALKR-------VDRRLGYLIEALKERGLLDDTNIIVVSD 215
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805095636 337 HGHF-FGQHglqhkGGFHYEDLIRLPFIVRYPSRVPAGRVSPAiqSLVDLAPTFLSLAG 394
Cdd:cd16018 216 HGMTdVGTH-----GYDNELPDMRAIFIARGPAFKKGKKLGPF--RNVDIYPLMCNLLG 267
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
7-387 |
4.59e-09 |
|
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: 58.20 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 7 LLITSDQQHWNTIGAFNkdiHTPSLDRLAREGTTFTRAYCPNPTCT-PSRASIITGMYPSQHGawtlgtklledrhtvge 85
Cdd:pfam01663 2 LVISLDGFRADYLDRFE---LTPNLAALAKEGVSAPNLTPVFPTLTfPNHYTLVTGLYPGSHG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 86 dFAANGYRTALIGKAHFQPLRDTDAYPSVEAYPILQDLAFwkqfngpfygfdhvelARNHTneahvgqhyalwmeekGCL 165
Cdd:pfam01663 62 -IVGNTFYDPKTGEYLVFVISDPEDPRWWQGEPIWDTAAK----------------AGVRA----------------AAL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 166 NWrdyflpPTGtmdkqiehKWPIPEQYHYntwiaersnalleqykaneEPFFLwssffdpHPDYLVPEPWDTMYDPDRLT 245
Cdd:pfam01663 109 FW------PGS--------EVDYSTYYGT-------------------PPRYL-------KDDYNNSVPFEDRVDTAVLQ 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 246 IPKAVPGEHDRnpphfrmtqEEDPDFGAWRETGFGIHGyHSHVQRSPEerkrqVATYYGMVscmDQAIGRILDKLDELGM 325
Cdd:pfam01663 149 TWLDLPFADVA---------AERPDLLLVYLEEPDYAG-HRYGPDSPE-----VEDALRRV---DRAIGDLLEALDERGL 210
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805095636 326 ADNTIVVFTTDHGHffgQHGLQHKgGFHYEDLIRLPFIVRYPSRVPAGRVSPAIQSLVDLAP 387
Cdd:pfam01663 211 FEDTNVIVVSDHGM---TPVSDDK-VIFLNDYLREKGLLHLVDGGPVVAIYPKARELGHVPP 268
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
306-403 |
6.69e-06 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 48.57 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 306 VSCMDQAIGRILDKLDELGmadnTIVVFTTDHGH----FFGQHGLQHKGgfHyeDLIRLPFIVRYPSRVPAGRVSPaiqS 381
Cdd:cd16010 409 VEAVDECLGRIVEAVLENG----GTLLITADHGNaeemIDPETGGPHTA--H--TTNPVPFIIVDPGLKRKLLKDG---G 477
|
90 100
....*....|....*....|..
gi 1805095636 382 LVDLAPTFLSLAGLPVPSAMTG 403
Cdd:cd16010 478 LADVAPTILDLLGIEKPKEMTG 499
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
438-482 |
9.36e-06 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 44.55 E-value: 9.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1805095636 438 VDDRYK-ITVYYNQTYGEIFDLAEDPDEVRNLWDDPN----QAALKTELL 482
Cdd:pfam16347 46 RTERYKlIHFYNDIDEWELYDLQKDPKEMNNVYGDPEyaevQAELKEELE 95
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
309-404 |
3.17e-05 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 45.63 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 309 MDQAIGRILDKLDELGMADNTIVVFTTDHG------HffgqhglqhkGGFHYEDlIRLPFIV------RYPSRVPAGRVS 376
Cdd:cd16024 176 MDDVIKRIYESLEEQSSNNPTLLVVCGDHGmtdagnH----------GGSSPGE-TSVPLLFispkfsSKPSNADGELSY 244
|
90 100
....*....|....*....|....*...
gi 1805095636 377 PAIQSLVDLAPTFLSLAGLPVPSAMTGV 404
Cdd:cd16024 245 YETVQQVDLAPTLALLLGLPIPKNSVGV 272
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
302-367 |
4.78e-05 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 45.80 E-value: 4.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805095636 302 YYGMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHGHFFGQHgLQHKGGFHYEdliRLPFIV-RYP 367
Cdd:pfam02995 306 DFNYASALDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKL-RRTSQGMLEE---RLPLMSiRYP 368
|
|
| pgm_bpd_ind |
TIGR01307 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ... |
306-403 |
5.07e-05 |
|
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in length of, and devoid of homology to the form of phosphoglycerate mutase that uses 2,3-bisphosphoglycerate as a cofactor. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130374 [Multi-domain] Cd Length: 501 Bit Score: 45.83 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 306 VSCMDQAIGRILDKLDELGmadntIVVF-TTDHGHffGQHGLQHKGGFHYEDLI-RLPFIVrypsrVPAGRVSpAIQ--- 380
Cdd:TIGR01307 408 VEALDVCLGRIVEACKKVG-----GTLFlTADHGN--AEEMIDENGNPHTAHTTnPVPFVC-----VGAKNVK-LIRegg 474
|
90 100
....*....|....*....|...
gi 1805095636 381 SLVDLAPTFLSLAGLPVPSAMTG 403
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTG 497
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
306-403 |
9.56e-05 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 44.71 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 306 VSCMDQAIGRILDKLDELGMAdntiVVFTTDHGH----FFGQHGLQHKGgfHYEDLIrlPFIV--RYPSRVPAGRvspai 379
Cdd:PRK05434 414 VEAVDECLGRVVDAVLKVGGT----LLITADHGNaeqmIDPETGQPHTA--HTTNPV--PFILvgGKALRLEGGK----- 480
|
90 100
....*....|....*....|....
gi 1805095636 380 qsLVDLAPTFLSLAGLPVPSAMTG 403
Cdd:PRK05434 481 --LADIAPTILDLLGLEQPAEMTG 502
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
309-360 |
2.74e-04 |
|
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 43.29 E-value: 2.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1805095636 309 MDQAIGRILDKLDELGMADNTIVVFTTDHG-----HFFGQHGLQHkGGFHYEDLIRL 360
Cdd:cd16016 238 LDRDLARLLDALDKKVGKGNYLVFLTADHGaadnpEFLKDHKIPA-GRFDPKRLKAL 293
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
302-367 |
1.28e-03 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 40.58 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805095636 302 YYGMVSCMDQAIGRILDKLDELGMADNTIVVFTTDHGHFFGQHgLQHKGGFhYEDliRLPF-IVRYP 367
Cdd:cd16021 178 YLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKI-RETLQGK-LEE--RLPFlSISLP 240
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
310-403 |
1.43e-03 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 41.19 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 310 DQAIGRILDKLDELGMAdntiVVFTTDHG-------HFFGQHGLQHkggfhyeDLIRLPFIV---RYPSRV-PAGRvspa 378
Cdd:COG0696 419 DECLGRVVDAVLAAGGT----LLITADHGnaeqmidPDTGGPHTAH-------TTNPVPFILvggDKGVKLrEDGR---- 483
|
90 100
....*....|....*....|....*
gi 1805095636 379 iqsLVDLAPTFLSLAGLPVPSAMTG 403
Cdd:COG0696 484 ---LADIAPTILELMGLPQPAEMTG 505
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
309-398 |
2.86e-03 |
|
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293747 Cd Length: 289 Bit Score: 39.85 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805095636 309 MDQAIGRILDKLDelgmaDNTIVVFTTDHG---HffGQHG------------LQHKGGFHYEDLIRLPFIVRYPSRVPag 373
Cdd:cd16023 191 MDQFIRDIIERLD-----DDTLLLVFGDHGmteT--GDHGgdsdeevdaalfAYSKRPFNNSDEPIESNGPGDPSKVR-- 261
|
90 100
....*....|....*....|....*
gi 1805095636 374 RVSpaiQslVDLAPTFLSLAGLPVP 398
Cdd:cd16023 262 SVP---Q--IDLVPTLSLLLGLPIP 281
|
|
| |
