|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-789 |
0e+00 |
|
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: 603.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFSTDLPTTPTIDEIAAQGIVFENLWVNPVCSPTRSTIFTGKYGTRTQVLAPGDELSLSET 501
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 502 SLPQALKNHPDTAEYASAKIGKWHLGGDSSHPAAFGL-DYYAGIFNGAVSDYYNWELTTNGQTLPQTEYATTVLTNLAID 580
Cdd:cd16154 81 TLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPNNPGGiPYYAGILGGGVQDYYNWNLTNNGQTTNSTEYATTKLTNLAID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 581 WLNQQTTPWFLWMGYNAPHTPFHLPPNELHSRNLSGDEADIEANPRAYYLAAVEALDSEINRLLNSLDQATRDNTVVIFI 660
Cdd:cd16154 161 WIDQQTKPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSADIEANPRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 661 GDNGTPTQARFRDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAGQEEVAIHDSLPFNNLL 740
Cdd:cd16154 241 GDNGTPGQVVDLPYTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 498244515 741 NDANATPlRETAFSQNEEAFTI----RNARYKLIEYLDGTRAFYDLQNDISEQ 789
Cdd:cd16154 321 SDVNAST-RQYNYTEYESPTTTgwatRNQYYKLIESENGQEELYDLINDPSEQ 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
408-794 |
2.31e-82 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 274.45 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 408 TFSVKVSAQVNTSKPNVLLIIADDLGQDSSNQYSFstDLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTR 486
Cdd:COG3119 10 ALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGN--PLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 487 TQVLAPG----DELSLSETSLPQALKNhpdtAEYASAKIGKWHLggdsshpaafgldyyagifngavsdyynwelttngq 562
Cdd:COG3119 88 TGVTDNGegynGGLPPDEPTLAELLKE----AGYRTALFGKWHL------------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 563 tlpqteYATTVLTNLAIDWLNQQTT---PWFLWMGYNAPHTPFHLPP---------NELHSRNLSGDEADIE--ANPRAY 628
Cdd:COG3119 128 ------YLTDLLTDKAIDFLERQADkdkPFFLYLAFNAPHAPYQAPEeyldkydgkDIPLPPNLAPRDLTEEelRRARAA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 629 YLAAVEALDSEINRLLNSLDQA-TRDNTVVIFIGDNGtptqARFRDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREA 707
Cdd:COG3119 202 YAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNG----PSLGEHGLRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 708 NVLNGTDFFSTILAIAGqeeVAIHDSLPFNNLLN--DANATPLRETAFSQNEEA---FTIRNARYKLIEYLDGTRA--FY 780
Cdd:COG3119 278 ALVSLIDLLPTLLDLAG---VPIPEDLDGRSLLPllTGEKAEWRDYLYWEYPRGggnRAIRTGRWKLIRYYDDDGPweLY 354
|
410
....*....|....
gi 498244515 781 DLQNDISEQTDLIS 794
Cdd:COG3119 355 DLKNDPGETNNLAA 368
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
422-724 |
4.04e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 173.76 E-value: 4.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFStdLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLA-PGDELSLS 499
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYP--RPTTPFLDRLAEEGLLFSNFYSGgTLTAPSRFALLTGLPPHNFGSYVsTPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 500 ETSLPQALKNhpdtAEYASAKIGKWHLGGDS-SHPAAFGLDYYAGiFNGAVSDYYNWELTTNgqTLPQTEYATTVLTNLA 578
Cdd:pfam00884 79 EPSLPDLLKR----AGYNTGAIGKWHLGWYNnQSPCNLGFDKFFG-RNTGSDLYADPPDVPY--NCSGGGVSDEALLDEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 579 IDWLNQQTTPWFLWMGYNAPHTPFHLPPNELHSRNLSGDEADIEANPRAYYLAAVEALDSEINRLLNSL-DQATRDNTVV 657
Cdd:pfam00884 152 LEFLDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLV 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 658 IFIGDNG---TPTQARFRDSElsgsKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAG 724
Cdd:pfam00884 232 VYTSDHGeslGEGGGYLHGGK----YDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
417-793 |
6.74e-30 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 125.17 E-value: 6.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 417 VNTSKPNVLLIIADDLGQD--SSNqysfSTDLPTTPTIDEIAAQGIVFENLW-VNPVCSPTRSTIFTGKYGTRTQVLAPG 493
Cdd:PRK13759 2 VQTKKPNIILIMVDQMRGDclGCN----GNKAVETPNLDMLASEGYNFENAYsAVPSCTPARAALLTGLSQWHHGRVGYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 494 DELSLS-ETSLPQALKNhpdtAEYASAKIGKWHLggdssHPAAFGLDYYA-----GIFNGA----------VSDYYNW-- 555
Cdd:PRK13759 78 DVVPWNyKNTLPQEFRD----AGYYTQCIGKMHV-----FPQRNLLGFHNvllhdGYLHSGrnedksqfdfVSDYLAWlr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 556 --------ELTTNG----------QTLPQTEYATTVLTNLAIDWLN--QQTTPWFLWMGYNAPHTPFHlPPNELHSRNLS 615
Cdd:PRK13759 149 ekapgkdpDLTDIGwdcnswvarpWDLEERLHPTNWVGSESIEFLRrrDPTKPFFLKMSFARPHSPYD-PPKRYFDMYKD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 616 GD------------------EADIEA-----------NPRAYYLAAVEALDSEINRLLNSL-DQATRDNTVVIFIGDNGt 665
Cdd:PRK13759 228 ADipdphigdweyaedqdpeGGSIDAlrgnlgeeyarRARAAYYGLITHIDHQIGRFLQALkEFGLLDNTIILFVSDHG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 666 ptqarfrdsELSGS-----KNNISEGGIRVPMIVS--GKNVT-RQGQREANVLNGTDFFSTILAIAGqeeVAIHDSLPFN 737
Cdd:PRK13759 307 ---------DMLGDhylfrKGYPYEGSAHIPFIIYdpGGLLAgNRGTVIDQVVELRDIMPTLLDLAG---GTIPDDVDGR 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498244515 738 NLLNDANATPLRETAFSQNEEAFTIRNARY---KLIEYL----DGTRAFYDLQNDISEQTDLI 793
Cdd:PRK13759 375 SLKNLIFGQYEGWRPYLHGEHALGYSSDNYltdGKWKYIwfsqTGEEQLFDLKKDPHELHNLS 437
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
37-414 |
1.74e-19 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 95.11 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 37 PVVTNQAPqLTTAITDQTTNQSQQYSFDlsqgGQTFTDPDGDTLTYSFStspQTN--DFTLNG----TVLSGTPE--QTE 108
Cdd:NF038112 1181 PGVCNRRP-VANAGPDQTVLERTTVTLN----GSGSFDPDGDPLTYAWT---QVSgpAVTLTGadtaTPSFTAPEvtADT 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 109 AITITVTASDPSGLTASDS---YLLTINGAPqTAKTIPDQSINLGENVSLDISQNrttfvDPDGDELTYA-FSTSPQ--- 181
Cdd:NF038112 1253 VLTFQLVVSDGTKTSAPDTvtvLVRNVNRAP-VAVAGAPATVDERSTVTLDGSGT-----DADGDALTYAwTQTSGPavt 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 182 -TNDFSLNGSVLSGTPALAQTITFTVTATDpNGLSANDSF---LLNINGAPkLTNSISNQSVNIGENynfdVTQNGSTfE 257
Cdd:NF038112 1327 lTGATTATATFTAPEVTADTQLTFTLTVSD-GTASATDTVtvtVRNVNRAP-VANAGADQTVDERST----VTLSGSA-T 1399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 258 DLDSEILIYS-VQITPTNDDLTFNGTHLSGM--PNQAGEYTIAVTATDDGGLFDSTSFVLYVVEPNENNSPiIANPIADQ 334
Cdd:NF038112 1400 DPDGDALTYAwTQTAGPTVTLTGADTATASFtaPEVAADTELTFQLTVSADGQASADVTVTVTVRNVNRAP-VAHAGESI 1478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 335 SATlnqdfNFDMSQNNTTFSDPDGDMLTF---QVAITP-TDSGLTSDGLIL-SGNPNQTGEINVTVTASDPAGLSVSDTF 409
Cdd:NF038112 1479 TVD-----EGSTVTLDASATDPDGDTLTYawtQVAGPSvTLTGADSAKLTFtAPEVSADTTLTFSLTVTDGSGSSGPVVV 1553
|
....*
gi 498244515 410 SVKVS 414
Cdd:NF038112 1554 TVTVK 1558
|
|
| YHYH |
pfam14240 |
YHYH protein; This domain family is found in bacteria, eukaryotes and viruses, and is ... |
931-1049 |
8.92e-14 |
|
YHYH protein; This domain family is found in bacteria, eukaryotes and viruses, and is typically between 141 and 198 amino acids in length. There is a conserved YHYH sequence motif.
Pssm-ID: 433802 Cd Length: 188 Bit Score: 70.94 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 931 TFPNNPTP-TQTECETGLGPVGLWVNGVPiYNWSDASSYNN--QDVWNNFAL-PFRSAAMDVCNGHSG-NGMYHHHSYNA 1005
Cdd:pfam14240 2 TIPLNPTLaTTTTTLNLPGPVGVALNGVP-FDPGTAESYNNdrDGGWRYDALgDVENLGLDCNNAHVQpTGAYHYHGLPS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 498244515 1006 CLKQQLGDeGKGHSPIYGYAGDGYPIHGPYHSKDVLAKSCWKKR 1049
Cdd:pfam14240 81 GLIKKLDG-GQHDMPLIGYAADGFPIYGPYGYTDALDATSGVKK 123
|
|
| CADG |
smart00736 |
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ... |
47-136 |
2.94e-11 |
|
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.
Pssm-ID: 214795 [Multi-domain] Cd Length: 97 Bit Score: 60.82 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 47 TTAITDQTTNQSQQYSFDLsqGGQTFTDPDGDTLTYSFSTSPQTND-----FTLNGTVLSGTP--EQTEAITITVTASDP 119
Cdd:smart00736 1 ANAIGDQTATEGESFSYTI--PSSTFTDADGDTLTYSATLSDGSALpswlsFDSDTGTLSGTPtnSDVGSLSLKVTATDS 78
|
90
....*....|....*..
gi 498244515 120 SGLTASDSYLLTINGAP 136
Cdd:smart00736 79 SGASASDTFTITVVNTN 95
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
41-229 |
1.04e-10 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 66.60 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 41 NQAPqLTTAITDQTTNQSQQYSFDLSQggqtfTDPDGDTLTYSFS-----TSPQTNDFTLNGTVLSGTPEQTEAITITVT 115
Cdd:NF038112 1373 NRAP-VANAGADQTVDERSTVTLSGSA-----TDPDGDALTYAWTqtagpTVTLTGADTATASFTAPEVAADTELTFQLT 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 116 ASDPSGLTASDSYLLTI---NGAPqTAKTIPDQSINLGENVSLDisqnrTTFVDPDGDELTYAFSTS--PQTNDFSLNGS 190
Cdd:NF038112 1447 VSADGQASADVTVTVTVrnvNRAP-VAHAGESITVDEGSTVTLD-----ASATDPDGDTLTYAWTQVagPSVTLTGADSA 1520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498244515 191 VLSGT-PALAQ--TITFTVTATDPNGLSANDSF---LLNINGAPK 229
Cdd:NF038112 1521 KLTFTaPEVSAdtTLTFSLTVTDGSGSSGPVVVtvtVKNVNRAPD 1565
|
|
| He_PIG |
pfam05345 |
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ... |
325-414 |
2.73e-06 |
|
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.
Pssm-ID: 398814 [Multi-domain] Cd Length: 95 Bit Score: 46.70 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 325 PIIANPIADQSATLNQDFNFDMSQNntTFSDPDGDMLTFQVAITPTD---SGLT--SDGLILSGNP--NQTGEINVTVTA 397
Cdd:pfam05345 1 PPVVTSPADQTATVGTPYSFTLSAS--GGSDPYGGSTVTYSTTATGGalpSGLTlnSSTGTISGTPtsVQPGTYTFTVTA 78
|
90
....*....|....*..
gi 498244515 398 SDPAGLSVSDTFSVKVS 414
Cdd:pfam05345 79 TDSSGLSSSTTFTLTVT 95
|
|
| Slr4-like |
cd22554 |
S (surface)-layer proteins similar to Pseudoalteromonas tunicata Slr4; Pseudoalteromonas ... |
71-314 |
6.88e-04 |
|
S (surface)-layer proteins similar to Pseudoalteromonas tunicata Slr4; Pseudoalteromonas tunicata D2 Slr4 (also known as EAR28894 protein) is an S-layer protein and the dominant protein within P. tunicata pellicle biofilm components. S-layers are self-assembling, paracrystalline proteinaceous lattices that form an interface between the cell and its extracellular environment; purified P. tunicata Slr4 protein is able to form square (p4 symmetry) paracrystalline lattices. Slr4 may protect cells and biofilm matrix components against stressors such as attack by viruses, bacteria or eukaryotes. The Slr4 family is widely distributed in gammaproteobacteria, including species of Pseudoalteromonas and Vibrio, and is found exclusively in marine metagenomes. It may play an important role in marine microbial physiology and ecology.
Pssm-ID: 412100 [Multi-domain] Cd Length: 400 Bit Score: 43.61 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 71 TFTDPDGDTLTY-----SFSTSPQTNDFTLNGTVLSGTPEQTEAITITVTASDPSGLTASDSYLLTINGAPQTAKTIPDQ 145
Cdd:cd22554 54 SVTATGATTVTFrvtlgNPAGANTATRTILGLTFDTDAVLAAGAVTVTYSAVTSTGTAIDGTSTATGTATLATVVDQFSA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 146 SINLGENVSLDISQNRTTFVDPDGDELTYAFSTSPQTNDFSLngsvlsGTPALAQTITFTVTATDPNGLSANDSFllnIN 225
Cdd:cd22554 134 SVTTKLDGVIDVEDDRKTFVGGTSDDTTTDLTVTTTTNTATL------ALAATATKVTVTLTGDFSGVDDDTDTT---GN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 226 GAPKLTNSISNQSVNIGENYNFD-VTQNGSTFEDLDSEILIYSVQITPTNDDLTFngthlsgmpnQAGEYTIAVTATDDG 304
Cdd:cd22554 205 DAAAATATAATAAATTGAAAAADtVTITSATAAAALATTAGTNAVGATAGGAVVL----------PAQSFTVDATVTYTD 274
|
250
....*....|
gi 498244515 305 GLFDSTSFVL 314
Cdd:cd22554 275 GATTTTTTLL 284
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
12-140 |
8.84e-04 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 43.88 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 12 SLLSVTLIGCGGGSSESNPDNDVTPPVVtNQAPQLTtAITDQTTNQSQQYSFDLSQggqtfTDPDGDTLTYSFSTS--PQ 89
Cdd:NF038112 1439 TELTFQLTVSADGQASADVTVTVTVRNV-NRAPVAH-AGESITVDEGSTVTLDASA-----TDPDGDTLTYAWTQVagPS 1511
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 498244515 90 TNDFTLNGTVLSGT-PE--QTEAITITVTASDPSGLTASDSYLLTINGAPQTAK 140
Cdd:NF038112 1512 VTLTGADSAKLTFTaPEvsADTTLTFSLTVTDGSGSSGPVVVTVTVKNVNRAPD 1565
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
6-437 |
1.51e-03 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 42.63 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 6 NSLFTISLLSVTLIGCGGGSSESNPDNDVTPPVVTNQAPQLTTAITDQTTNQSQQYSFDLSQGGQTFTDpDGDTLTYSFS 85
Cdd:COG3468 23 LGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGG-GGGNSGTGGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 86 TSPQTNDFTLNGTVLSGTPEQTEAITITVTASDPSGLTASDSYLLTINGAPQTAKTIPDQSINLGENVSLDISQNRTTfV 165
Cdd:COG3468 102 GGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAGGGGG-G 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 166 DPDGDELTYAFSTSPQTNDFSLNGSVLSGTPALAQTITFTVTATDPNGLSANDSFLLNINGA-----PKLTNSISNQSVN 240
Cdd:COG3468 181 GAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGgsaggTGGGGLTGGGAAG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 241 IGENYNFDVTQNGSTFEDLDSEILIYSVQITPTNDDLTFNGTHLSGMPNQAGEYTIAVTATDDGGLFDSTSFVLYVVEPN 320
Cdd:COG3468 261 TGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGGGGGG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 321 ENNSPIIANPIADQSATLNQDFNFDMSQNNTTFSDPDGDMLTFQVAITPTDSGLTSDGLILSGNPNQTGEINVTVTASDP 400
Cdd:COG3468 341 TTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGLTLTG 420
|
410 420 430
....*....|....*....|....*....|....*..
gi 498244515 401 AGLSVSDTFSVKvsaqvntskpNVLLIIADDLGQDSS 437
Cdd:COG3468 421 GTLTVNGNYTGN----------NGTLVLNTVLGDDNS 447
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-789 |
0e+00 |
|
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: 603.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFSTDLPTTPTIDEIAAQGIVFENLWVNPVCSPTRSTIFTGKYGTRTQVLAPGDELSLSET 501
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 502 SLPQALKNHPDTAEYASAKIGKWHLGGDSSHPAAFGL-DYYAGIFNGAVSDYYNWELTTNGQTLPQTEYATTVLTNLAID 580
Cdd:cd16154 81 TLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPNNPGGiPYYAGILGGGVQDYYNWNLTNNGQTTNSTEYATTKLTNLAID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 581 WLNQQTTPWFLWMGYNAPHTPFHLPPNELHSRNLSGDEADIEANPRAYYLAAVEALDSEINRLLNSLDQATRDNTVVIFI 660
Cdd:cd16154 161 WIDQQTKPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSADIEANPRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 661 GDNGTPTQARFRDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAGQEEVAIHDSLPFNNLL 740
Cdd:cd16154 241 GDNGTPGQVVDLPYTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 498244515 741 NDANATPlRETAFSQNEEAFTI----RNARYKLIEYLDGTRAFYDLQNDISEQ 789
Cdd:cd16154 321 SDVNAST-RQYNYTEYESPTTTgwatRNQYYKLIESENGQEELYDLINDPSEQ 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
408-794 |
2.31e-82 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 274.45 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 408 TFSVKVSAQVNTSKPNVLLIIADDLGQDSSNQYSFstDLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTR 486
Cdd:COG3119 10 ALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGN--PLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 487 TQVLAPG----DELSLSETSLPQALKNhpdtAEYASAKIGKWHLggdsshpaafgldyyagifngavsdyynwelttngq 562
Cdd:COG3119 88 TGVTDNGegynGGLPPDEPTLAELLKE----AGYRTALFGKWHL------------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 563 tlpqteYATTVLTNLAIDWLNQQTT---PWFLWMGYNAPHTPFHLPP---------NELHSRNLSGDEADIE--ANPRAY 628
Cdd:COG3119 128 ------YLTDLLTDKAIDFLERQADkdkPFFLYLAFNAPHAPYQAPEeyldkydgkDIPLPPNLAPRDLTEEelRRARAA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 629 YLAAVEALDSEINRLLNSLDQA-TRDNTVVIFIGDNGtptqARFRDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREA 707
Cdd:COG3119 202 YAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNG----PSLGEHGLRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 708 NVLNGTDFFSTILAIAGqeeVAIHDSLPFNNLLN--DANATPLRETAFSQNEEA---FTIRNARYKLIEYLDGTRA--FY 780
Cdd:COG3119 278 ALVSLIDLLPTLLDLAG---VPIPEDLDGRSLLPllTGEKAEWRDYLYWEYPRGggnRAIRTGRWKLIRYYDDDGPweLY 354
|
410
....*....|....
gi 498244515 781 DLQNDISEQTDLIS 794
Cdd:COG3119 355 DLKNDPGETNNLAA 368
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
422-795 |
1.46e-74 |
|
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: 253.62 E-value: 1.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLG-QDSSNQYSfstDLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLAPGD----- 494
Cdd:cd16144 1 PNIVLILVDDLGwADLGCYGS---KFYETPNIDRLAKEGMRFTQAYAAaPVCSPSRASILTGQYPARLGITDVIPgrrgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 495 -------------ELSLSETSLPQALKNhpdtAEYASAKIGKWHLGGDSSH-PAAFGLDYYAGIFN---GAVSDYYNWEL 557
Cdd:cd16144 78 pdntklipppsttRLPLEEVTIAEALKD----AGYATAHFGKWHLGGEGGYgPEDQGFDVNIGGTGnggPPSYYFPPGKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 558 TTNGQTLPQTEYATTVLTNLAIDWLNQQTT-PWFLWMGYNAPHTPFHLPPNEL-HSRNLSGDEADIEANPraYYLAAVEA 635
Cdd:cd16144 154 NPDLEDGPEGEYLTDRLTDEAIDFIEQNKDkPFFLYLSHYAVHTPIQARPELIeKYEKKKKGLRKGQKNP--VYAAMIES 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 636 LDSEINRLLNSLDQAT-RDNTVVIFIGDNGTPTQARFRDSE---LSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLN 711
Cdd:cd16144 232 LDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSnapLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 712 GTDFFSTILAIAGQEEVAIH--DSLPFNNLLNDANATPLRETAF-----SQNEEAF---TIRNARYKLIEYL-DGTRAFY 780
Cdd:cd16144 312 GTDLYPTFLELAGGPLPPPQhlDGVSLVPLLKGGEADLPRRALFwhfphYHGQGGRpasAIRKGDWKLIEFYeDGRVELY 391
|
410
....*....|....*
gi 498244515 781 DLQNDISEQTDLISA 795
Cdd:cd16144 392 NLKNDIGETNNLAAE 406
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
422-794 |
2.10e-68 |
|
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: 235.91 E-value: 2.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQdssNQYSF--STDLpTTPTIDEIAAQGIVFENLWVNPVCSPTRSTIFTGKYGTRT---QVLAPGDEL 496
Cdd:cd16146 1 PNVILILTDDQGY---GDLGFhgNPIL-KTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTgvwHTILGRERM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 497 SLSETSLPQALKNhpdtAEYASAKIGKWHLG-GDSSHPAAFGLDYYAGIFNGAVSDYYNWELTT--------NGQTLPQT 567
Cdd:cd16146 77 RLDETTLAEVFKD----AGYRTGIFGKWHLGdNYPYRPQDRGFDEVLGHGGGGIGQYPDYWGNDyfddtyyhNGKFVKTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 568 EYATTVLTNLAIDWLNQQTT-PWFLWMGYNAPHTPFHLPPNEL-HSRNLSGDEadieanPRAYYLAAVEALDSEINRLLN 645
Cdd:cd16146 153 GYCTDVFFDEAIDFIEENKDkPFFAYLATNAPHGPLQVPDKYLdPYKDMGLDD------KLAAFYGMIENIDDNVGRLLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 646 SLDQ-ATRDNTVVIFIGDNGT--PTQARFrDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAI 722
Cdd:cd16146 227 KLKElGLEENTIVIFMSDNGPagGVPKRF-NAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 723 AGqeeVAIHDSLPFN-----NLLNDANATPLRETAFSQN---------EEAFTIRNARYKLIEYLDGTRAFYDLQNDISE 788
Cdd:cd16146 306 CG---VKLPEGIKLDgrsllPLLKGESDPWPERTLFTHSgrwppppkkKRNAAVRTGRWRLVSPKGFQPELYDIENDPGE 382
|
....*.
gi 498244515 789 QTDLIS 794
Cdd:cd16146 383 ENDVAD 388
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
422-794 |
9.83e-62 |
|
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: 215.45 E-value: 9.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSnqySFSTDLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLA---PGDELS 497
Cdd:cd16027 1 PNILWIIADDLSPDLG---GYGGNVVKTPNLDRLAAEGVRFTNAFTTaPVCSPSRSALLTGLYPHQNGAHGlrsRGFPLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 498 LSETSLPQALKNhpdtAEYASAKIGKWHLGGDSSHPaafgldYYAGIFNGAVSDYYNWELTTNgqtlpqteyattvltnl 577
Cdd:cd16027 78 DGVKTLPELLRE----AGYYTGLIGKTHYNPDAVFP------FDDEMRGPDDGGRNAWDYASN----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 578 AIDWLNQ--QTTPWFLWMGYNAPHTPFHLPPNElhsrNLSGDEADIEA------NP-----RAYYLAAVEALDSEINRLL 644
Cdd:cd16027 131 AADFLNRakKGQPFFLWFGFHDPHRPYPPGDGE----EPGYDPEKVKVppylpdTPevredLADYYDEIERLDQQVGEIL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 645 NSLDQAT-RDNTVVIFIGDNGTPtqarfrdseLSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIA 723
Cdd:cd16027 207 DELEEDGlLDNTIVIFTSDHGMP---------FPRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 724 GqeeVAIHDSLPFNNLL--NDANATPLRETAFSQ---NEEAF----TIRNARYKLIEYLDgTRAFYDLQNDISEQTDLIS 794
Cdd:cd16027 278 G---IEPPEYLQGRSFLplLKGEKDPGRDYVFAErdrHDETYdpirSVRTGRYKYIRNYM-PEELYDLKNDPDELNNLAD 353
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
422-792 |
2.42e-58 |
|
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: 206.63 E-value: 2.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQdssNQYSF-STDLPTTPTIDEIAAQGIVFENLWVNPVCSPTRSTIFTGKYGTRT----QVLAPG--D 494
Cdd:cd16029 1 PHIVFILADDLGW---NDVGFhGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTgmqhGVILAGepY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 495 ELSLSETSLPQALKnhpdTAEYASAKIGKWHLG-GDSSH-PAAFGLDYYAGIFNGAVsDYYN---------WELTTNGQT 563
Cdd:cd16029 78 GLPLNETLLPQYLK----ELGYATHLVGKWHLGfYTWEYtPTNRGFDSFYGYYGGAE-DYYThtsggandyGNDDLRDNE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 564 LPQTE----YATTVLTNLAIDWLNQ--QTTPWFLWMGYNAPHTPFHLPPNelHSRNLSGDEADIEANPRAYYLAAVEALD 637
Cdd:cd16029 153 EPAWDyngtYSTDLFTDRAVDIIENhdPSKPLFLYLAFQAVHAPLQVPPE--YADPYEDKFAHIKDEDRRTYAAMVSALD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 638 SEINRLLNSLDQATR-DNTVVIFIGDNGTPTQARFRDSE--LSGSKNNISEGGIRVPMIVSGKNVTRQGQReanVLNG-- 712
Cdd:cd16029 231 ESVGNVVDALKAKGMlDNTLIVFTSDNGGPTGGGDGGSNypLRGGKNTLWEGGVRVPAFVWSPLLPPKRGT---VSDGlm 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 713 --TDFFSTILAIAGqeeVAIHDSLPFN-----NLLNDANATPlRETA------FSQNEEAFTIRNARYKLIEyldGTrAF 779
Cdd:cd16029 308 hvTDWLPTLLSLAG---GDPDDLPPLDgvdqwDALSGGAPSP-RTEIllniddITRTTGGAAIRVGDWKLIV---GK-PL 379
|
410
....*....|...
gi 498244515 780 YDLQNDISEQTDL 792
Cdd:cd16029 380 FNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
422-724 |
2.82e-57 |
|
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: 197.66 E-value: 2.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFSTDlpTTPTIDEIAAQGIVFENLWV-NPVCSPTRSTIFTGKYGTRTQV---LAPGDELS 497
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDI--KTPNLDRLAAEGVRFTNAYVaSPVCSPSRASLLTGRYPHRHGVrgnVGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 498 LSETSLPQALKNhpdtAEYASAKIGKWHlggdsshpaafgldyyagifngavsdyynwelttngqtlpqteyattvltNL 577
Cdd:cd16022 79 PDEPTLAELLKE----AGYRTALIGKWH--------------------------------------------------DE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 578 AIDWL--NQQTTPWFLWMGYNAPHTPFHlppnelhsrnlsgdeadieanprayYLAAVEALDSEINRLLNSLDQA-TRDN 654
Cdd:cd16022 105 AIDFIerRDKDKPFFLYVSFNAPHPPFA-------------------------YYAMVSAIDDQIGRILDALEELgLLDN 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 655 TVVIFIGDNGTPTQarfrDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAG 724
Cdd:cd16022 160 TLIVFTSDHGDMLG----DHGLRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAG 225
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
420-794 |
1.39e-56 |
|
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: 202.76 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 420 SKPNVLLIIADDLgqdssnqySFST------DLPTTPTIDEIAAQGIVFENLWV-NPVCSPTRSTIFTGKYGTRTQVLA- 491
Cdd:cd16031 1 KRPNIIFILTDDH--------RYDAlgcygnPIVKTPNIDRLAKEGVRFDNAFVtTSICAPSRASILTGQYSHRHGVTDn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 492 PGDELSLSETSLPQALKnhpdTAEYASAKIGKWHLGGDSSHPAAfGLDYYAGiFNGAvSDYYNWELTTNGQTLPQTEYAT 571
Cdd:cd16031 73 NGPLFDASQPTYPKLLR----KAGYQTAFIGKWHLGSGGDLPPP-GFDYWVS-FPGQ-GSYYDPEFIENGKRVGQKGYVT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 572 TVLTNLAIDWLNQQ--TTPWFLWMGYNAPHTPFHLPPNELH-------------------------------SRNLSGDE 618
Cdd:cd16031 146 DIITDKALDFLKERdkDKPFCLSLSFKAPHRPFTPAPRHRGlyedvtipepetfddddyagrpewareqrnrIRGVLDGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 619 ADIEANPRAY---YLAAVEALDSEINRLLNSLD-QATRDNTVVIFIGDNGtptqarFRDSE--LsGSKNNISEGGIRVPM 692
Cdd:cd16031 226 FDTPEKYQRYmkdYLRTVTGVDDNVGRILDYLEeQGLADNTIIIYTSDNG------FFLGEhgL-FDKRLMYEESIRVPL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 693 IVSGKNVTRQGQR-EANVLNgTDFFSTILAIAGQEEVAIHDSLPFNNLLNDANATPLR---------ETAFSQNEEAFTI 762
Cdd:cd16031 299 IIRDPRLIKAGTVvDALVLN-IDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPVDWRkefyyeyyeEPNFHNVPTHEGV 377
|
410 420 430
....*....|....*....|....*....|....
gi 498244515 763 RNARYKLIEY--LDGTRAFYDLQNDISEQTDLIS 794
Cdd:cd16031 378 RTERYKYIYYygVWDEEELYDLKKDPLELNNLAN 411
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
421-793 |
2.83e-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: 200.87 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLG-QDSSnqySFSTDLPTTPTIDEIAAQGIVFENLWV-NPVCSPTRSTIFTGKYGTRT----QVLAPGD 494
Cdd:cd16026 1 KPNIVVILADDLGyGDLG---CYGSPLIKTPNIDRLAAEGVRFTDFYAaAPVCSPSRAALLTGRYPVRVglpgVVGPPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 495 E--LSLSETSLPQALKNhpdtAEYASAKIGKWHLG-GDSSHPAAFGLDYYAGIFNGAVSDYYNWELTTNGQTLPQTEYAT 571
Cdd:cd16026 78 KggLPPDEITIAEVLKK----AGYRTALVGKWHLGhQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLPPLMENE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 572 TV-------------LTNLAIDWL-NQQTTPWFLWMGYNAPHTPFHLPPN-ELHSRN-LSGDeadieanprayylaAVEA 635
Cdd:cd16026 154 EVieqpadqssltqrYTDEAVDFIeRNKDQPFFLYLAHTMPHVPLFASEKfKGRSGAgLYGD--------------VVEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 636 LDSEINRLLNSLDQAT-RDNTVVIFIGDNGTPTQARFRDS---ELSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLN 711
Cdd:cd16026 220 LDWSVGRILDALKELGlEENTLVIFTSDNGPWLEYGGHGGsagPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELAS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 712 GTDFFSTILAIAG---QEEVAI--HDSLPfnnLLNDANATPlRETAF--SQNEEAFTIRNARYKLI---EYLDGTRAF-- 779
Cdd:cd16026 300 TMDLLPTLAALAGaplPEDRVIdgKDISP---LLLGGSKSP-PHPFFyyYDGGDLQAVRSGRWKLHlptTYRTGTDPGgl 375
|
410 420
....*....|....*....|....
gi 498244515 780 ----------YDLQNDISEQTDLI 793
Cdd:cd16026 376 dptkleppllYDLEEDPGETYNVA 399
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
421-792 |
1.37e-55 |
|
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: 198.95 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADdlgqdssnQYSFST-----DLPT-TPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLAPG 493
Cdd:cd16034 1 KPNILFIFAD--------QHRAQAlgcagDDPVkTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQYPLTNGVFGND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 494 DELSLSETSLPQALKNhpdtAEYASAKIGKWHL-GGDSSHPAA----------FGLDYYAGIFNGavSDYYN---WelTT 559
Cdd:cd16034 73 VPLPPDAPTIADVLKD----AGYRTGYIGKWHLdGPERNDGRAddytppperrHGFDYWKGYECN--HDHNNphyY--DD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 560 NGQTLPQTEYATTVLTNLAIDWLNQQ---TTPWFLWMGYNAPHTPFHLPPNELHSR-----NLSGDEADIEANPR----- 626
Cdd:cd16034 145 DGKRIYIKGYSPDAETDLAIEYLENQadkDKPFALVLSWNPPHDPYTTAPEEYLDMydpkkLLLRPNVPEDKKEEaglre 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 627 --AYYLAAVEALDSEINRLLNSLDQA-TRDNTVVIFIGDNGtptqarfrdsELSGS-----KNNISEGGIRVPMIVSGKN 698
Cdd:cd16034 225 dlRGYYAMITALDDNIGRLLDALKELgLLENTIVVFTSDHG----------DMLGShglmnKQVPYEESIRVPFIIRYPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 699 VTRQGQREANVLNGTDFFSTILAIAGQEevaIHDSLPFNNL----LNDANAT----------PLRETAFSQNEEAFTIRN 764
Cdd:cd16034 295 KIKAGRVVDLLINTVDIMPTLLGLCGLP---IPDTVEGRDLspllLGGKDDEpdsvllqcfvPFGGGSARDGGEWRGVRT 371
|
410 420
....*....|....*....|....*...
gi 498244515 765 ARYKLIEYLDGTRAFYDLQNDISEQTDL 792
Cdd:cd16034 372 DRYTYVRDKNGPWLLFDNEKDPYQLNNL 399
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
421-792 |
4.61e-55 |
|
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: 197.28 E-value: 4.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLGqdssnqysFStDLPT------TPTIDEIAAQGIVFENLWVNPVCSPTRSTIFTGKY------GTRTQ 488
Cdd:cd16025 2 RPNILLILADDLG--------FS-DLGCfggeipTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNhhqvgmGTMAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 489 VLA--PGDELSLSETS--LPQALKNhpdtAEYASAKIGKWHLGGDsshpaafglDYyagifngavsdyynwelttngqtl 564
Cdd:cd16025 73 LATgkPGYEGYLPDSAatIAEVLKD----AGYHTYMSGKWHLGPD---------DY------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 565 pqteYATTVLTNLAIDWLNQQTT---PWFLWMGYNAPHTPFH---------------------------------LPPN- 607
Cdd:cd16025 116 ----YSTDDLTDKAIEYIDEQKApdkPFFLYLAFGAPHAPLQapkewidkykgkydagwdalreerlerqkelglIPADt 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 608 ELHSRN--------LSGDEADIEANPRAYYLAAVEALDSEINRLLNSLDQA-TRDNTVVIFIGDNG------------TP 666
Cdd:cd16025 192 KLTPRPpgvpawdsLSPEEKKLEARRMEVYAAMVEHMDQQIGRLIDYLKELgELDNTLIIFLSDNGasaepgwanasnTP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 667 tqarFRdselsGSKNNISEGGIRVPMIVSG-KNVTRQGQREANVLNGTDFFSTILAIAGQEEVAIHDSLP--------FN 737
Cdd:cd16025 272 ----FR-----LYKQASHEGGIRTPLIVSWpKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPqlpldgvsLL 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 738 NLLNDANATPLRETAFSQNEEAFTIRNARYKLI----EYLDGTR-AFYDLQNDISEQTDL 792
Cdd:cd16025 343 PTLDGAAAPSRRRTQYFELFGNRAIRKGGWKAValhpPPGWGDQwELYDLAKDPSETHDL 402
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
422-794 |
1.97e-54 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 195.89 E-value: 1.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQ-DSSnqySFSTDLPTTPTIDEIAAQGIVFENLWV-NPVCSPTRSTIFTGKYGTRTQV---LAPGDEL 496
Cdd:cd16145 1 PNIIFILADDLGYgDLG---CYGQKKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLHTGHTRVrgnSEPGGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 497 SL--SETSLPQALKNhpdtAEYASAKIGKWHLG--GDSSHPAAFGLDYYAGIFNGAVS-DYYNWELTTNGQTLP------ 565
Cdd:cd16145 78 PLppDDVTLAEVLKK----AGYATAAFGKWGLGgpGTPGHPTKQGFDYFYGYLDQVHAhNYYPEYLWRNGEKVPlpnnvi 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 566 ------------QTEYATTVLTNLAIDWL-NQQTTPWFLWMGYNAPHTPFHLP---PNELHSRNLSGDEADIEANPRAYY 629
Cdd:cd16145 154 ppldegnnagggGGTYSHDLFTDEALDFIrENKDKPFFLYLAYTLPHAPLQVPddgPYKYKPKDPGIYAYLPWPQPEKAY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 630 LAAVEALDSEINRLLNSL-DQATRDNTVVIFIGDNG------TPTQARFRDS--ELSGSKNNISEGGIRVPMIVSGKNVT 700
Cdd:cd16145 234 AAMVTRLDRDVGRILALLkELGIDENTLVVFTSDNGphseggSEHDPDFFDSngPLRGYKRSLYEGGIRVPFIARWPGKI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 701 RQGQREANVLNGTDFFSTILAIAGQEEVAIHDSLPFNNLLNDANATPLRET---AFSQNEEAFTIRNARYKLIEYLDGTR 777
Cdd:cd16145 314 PAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKPQQQQHDYlywEFYEGGGAQAVRMGGWKAVRHGKKDG 393
|
410
....*....|....*....
gi 498244515 778 AF--YDLQNDISEQTDLIS 794
Cdd:cd16145 394 PFelYDLSTDPGETNNLAA 412
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-792 |
3.61e-53 |
|
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: 190.89 E-value: 3.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQY---SFSTdlpttPTIDEIAAQGIVFENLWVNPVCSPTRSTIFTGKYGTRTQVlAPGDeLSL 498
Cdd:cd16151 1 PNIILIMADDLGYECIGCYggeSYKT-----PNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYV-VFGY-LDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 499 SETSLPQALKNhpdtAEYASAKIGKWHLGG---DSSHPAAFGLDYYAgIF--NGAVSDYYNWELTT----NGQTLPQT-- 567
Cdd:cd16151 74 KQKTFGHLLKD----AGYATAIAGKWQLGGgrgDGDYPHEFGFDEYC-LWqlTETGEKYSRPATPTfnirNGKLLETTeg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 568 EYATTVLTNLAIDWL-NQQTTPWFLWMGYNAPHTPF-HLPPNELHSRnlsgDEADIEANPRaYYLAAVEALDSEINRLLN 645
Cdd:cd16151 149 DYGPDLFADFLIDFIeRNKDQPFFAYYPMVLVHDPFvPTPDSPDWDP----DDKRKKDDPE-YFPDMVAYMDKLVGKLVD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 646 SLDQA-TRDNTVVIFIGDNGTPTQ--ARFRDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAI 722
Cdd:cd16151 224 KLEELgLRENTIIIFTGDNGTHRPitSRTNGREVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAEL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498244515 723 AGQE--EVAIHDSLPFNNLLNDANATPLRETAF--SQNEEAFT----IRNARYKLieYLDGTraFYDLQNDISEQTDL 792
Cdd:cd16151 304 AGAPlpEDYPLDGRSFAPQLLGKTGSPRREWIYwyYRNPHKKFgsrfVRTKRYKL--YADGR--FFDLREDPLEKNPL 377
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
422-793 |
1.74e-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: 189.72 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFSTDLPTtPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQ---VLAPGDELS 497
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKIPT-PNIDRLAAEGMRFTDAHSPsSVCTPSRYGLLTGRYPWRSRlkgGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 498 L---SETSLPQALKNhpdtAEYASAKIGKWHLGGD----SSHPAAFG----LDYYAGIFNGAVS---DYYnwelttngQT 563
Cdd:cd16143 80 LiepDRVTLAKMLKQ----AGYRTAMVGKWHLGLDwkkkDGKKAATGtgkdVDYSKPIKGGPLDhgfDYY--------FG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 564 LPQTEYATTvLTNLAIDWLNQQ---TTPWFLWMGYNAPHTPfHLPPNELHSRnlSGdeadieANPrayYLAAVEALDSEI 640
Cdd:cd16143 148 IPASEVLPT-LTDKAVEFIDQHakkDKPFFLYFALPAPHTP-IVPSPEFQGK--SG------AGP---YGDFVYELDWVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 641 NRLLNSLD-QATRDNTVVIFIGDNGTPTQARFRDSE---------LSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVL 710
Cdd:cd16143 215 GRILDALKeLGLAENTLVIFTSDNGPSPYADYKELEkfghdpsgpLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 711 NGTDFFSTILAIAGQ---EEVAIhDSLPFNNLLNDANATPLRETAFSQ-NEEAFTIRNARYKLIEYLDGTR--------- 777
Cdd:cd16143 295 SLTDLFATLAAIVGQklpDNAAE-DSFSFLPALLGPKKQEVRESLVHHsGNGSFAIRKGDWKLIDGTGSGGfsyprgkek 373
|
410 420
....*....|....*....|..
gi 498244515 778 ------AFYDLQNDISEQTDLI 793
Cdd:cd16143 374 lglppgQLYNLSTDPGESNNLY 395
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
422-724 |
4.04e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 173.76 E-value: 4.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFStdLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLA-PGDELSLS 499
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYP--RPTTPFLDRLAEEGLLFSNFYSGgTLTAPSRFALLTGLPPHNFGSYVsTPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 500 ETSLPQALKNhpdtAEYASAKIGKWHLGGDS-SHPAAFGLDYYAGiFNGAVSDYYNWELTTNgqTLPQTEYATTVLTNLA 578
Cdd:pfam00884 79 EPSLPDLLKR----AGYNTGAIGKWHLGWYNnQSPCNLGFDKFFG-RNTGSDLYADPPDVPY--NCSGGGVSDEALLDEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 579 IDWLNQQTTPWFLWMGYNAPHTPFHLPPNELHSRNLSGDEADIEANPRAYYLAAVEALDSEINRLLNSL-DQATRDNTVV 657
Cdd:pfam00884 152 LEFLDNNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLV 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 658 IFIGDNG---TPTQARFRDSElsgsKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAG 724
Cdd:pfam00884 232 VYTSDHGeslGEGGGYLHGGK----YDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
422-748 |
6.91e-43 |
|
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: 161.16 E-value: 6.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFSTDLPT-TPTIDEIAAQGIVFENLWVNPVCSPTRSTIFTGKYGTRT---QVLAPGDELS 497
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRGApTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTgltTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 498 LS--ETSLPQALKnhpdTAEYASAKIGKWHLGG-DSSHPAAFGLDYYAGIFNGAVSDYynwelttngqtlpqteyattvL 574
Cdd:cd16142 81 LPpwEPTLAELLK----DAGYATAQFGKWHLGDeDGRLPTDHGFDEFYGNLYHTIDEE---------------------I 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 575 TNLAIDWLNQQT---TPWFLWMGYNAPHTPFHLPPnelHSRNLSGDEADieanprayYLAAVEALDSEINRLLNSLDQA- 650
Cdd:cd16142 136 VDKAIDFIKRNAkadKPFFLYVNFTKMHFPTLPSP---EFEGKSSGKGK--------YADSMVELDDHVGQILDALDELg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 651 TRDNTVVIFIGDNGtPTQARFRDSE---LSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAGqEE 727
Cdd:cd16142 205 IADNTIVIFTTDNG-PEQDVWPDGGytpFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAG-AP 282
|
330 340
....*....|....*....|.
gi 498244515 728 VAIHDSLPFNNLLNDANATPL 748
Cdd:cd16142 283 DPKDKLLGKDRHIDGVDQSPF 303
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
420-794 |
7.06e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 158.11 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 420 SKPNVLLIIADDLGQDSSNQYsfstDLPT--TPTIDEIAAQGIVFENL-----WVNPVCSPTRSTIFTGKYGTRTQVlAP 492
Cdd:cd16155 1 KKPNILFILADDQRADTIGAL----GNPEiqTPNLDRLARRGTSFTNAynmggWSGAVCVPSRAMLMTGRTLFHAPE-GG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 493 GDELSLSETSLPQALKNhpdtAEYASAKIGKWHLGgdsshpaafgldyyagifngavsdyynwelttngqtlpqteyatt 572
Cdd:cd16155 76 KAAIPSDDKTWPETFKK----AGYRTFATGKWHNG--------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 573 vLTNLAIDWLNQQTT---PWFLWMGYNAPHTP------FH---------LPPNELHSRNLSGDEADI-----EANPR--- 626
Cdd:cd16155 107 -FADAAIEFLEEYKDgdkPFFMYVAFTAPHDPrqappeYLdmyppetipLPENFLPQHPFDNGEGTVrdeqlAPFPRtpe 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 627 ------AYYLAAVEALDSEINRLLNSLDQA-TRDNTVVIFIGDNGtptqarfrdseLS-GS-----KNNISEGGIRVPMI 693
Cdd:cd16155 186 avrqhlAEYYAMITHLDAQIGRILDALEASgELDNTIIVFTSDHG-----------LAvGShglmgKQNLYEHSMRVPLI 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 694 VSGKNVTRQGQREANV-LNgtDFFSTILAIAGqeeVAIHDSLPFNNLLN--DANATPLRET---AFSQNEEAftIRNARY 767
Cdd:cd16155 255 ISGPGIPKGKRRDALVyLQ--DVFPTLCELAG---IEIPESVEGKSLLPviRGEKKAVRDTlygAYRDGQRA--IRDDRW 327
|
410 420
....*....|....*....|....*....
gi 498244515 768 KLIEYLDGTR--AFYDLQNDISEQTDLIS 794
Cdd:cd16155 328 KLIIYVPGVKrtQLFDLKKDPDELNNLAD 356
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
420-793 |
2.98e-40 |
|
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: 155.04 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 420 SKPNVLLIIADDLgqdsSNQYSFSTDLPT-TPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVL---APGD 494
Cdd:cd16030 1 KKPNVLFIAVDDL----RPWLGCYGGHPAkTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVYdnnSYFR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 495 ELSLSETSLPQALKNHpdtaEYASAKIGK-WHLGGDSS------------HPAAFGLDYYAGIFNGAVSDYYNWELTTNG 561
Cdd:cd16030 77 KVAPDAVTLPQYFKEN----GYTTAGVGKiFHPGIPDGdddpaswdeppnPPGPEKYPPGKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 562 QTLPQTEYATTVLTNLAIDWLNQ---QTTPWFLWMGYNAPHTPFH------------------------LPPNELHSRNL 614
Cdd:cd16030 153 ADVPDEAYPDGKVADEAIEQLRKlkdSDKPFFLAVGFYKPHLPFVapkkyfdlyplesiplpnpfdpidLPEVAWNDLDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 615 SGDEADIEANPRAY----------------YLAAVEALDSEINRLLNSLDQAT-RDNTVVIFIGDNGtptqarFRDSELS 677
Cdd:cd16030 233 LPKYGDIPALNPGDpkgplpdeqarelrqaYYASVSYVDAQVGRVLDALEELGlADNTIVVLWSDHG------WHLGEHG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 678 G-SKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAGQEEVAIHDSLPFNNLLNDANATPlRETAFSQ- 755
Cdd:cd16030 307 HwGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAKW-KDAAFSQy 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 498244515 756 ---NEEAFTIRNARYKLIEYLD----GTRAFYDLQNDISEQTDLI 793
Cdd:cd16030 386 prpSIMGYSIRTERYRYTEWVDfdkvGAEELYDHKNDPNEWKNLA 430
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
421-793 |
1.63e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 151.23 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLGQDSSNQYSfsTDLPTTPTIDEIAAQGIVFENLW-VNPVCSPTRSTIFTGKYGTRTQVLAPGDELSLS 499
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYG--QPLDLTPNLDALAEEGVLFENAFtPQPVCGPARACLQTGLYPTETGCFRNGIPLPAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 500 ETSLPQALKNhpdtAEYASAKIGKWHLGGdsshpaafgldyyagifngavsdyynwelttngqtlpqteYATTVLTNLAI 579
Cdd:cd16152 79 EKTLAHYFRD----AGYETGYVGKWHLAG----------------------------------------YRVDALTDFAI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 580 DWLNQQTT--PWFLWMGYNAPHtpfHlpPNELHS-------------RNLSGDEADIEANPRAY---YLAAVEALDSEIN 641
Cdd:cd16152 115 DYLDNRQKdkPFFLFLSYLEPH---H--QNDRDRyvapegsaerfanFWVPPDLAALPGDWAEElpdYLGCCERLDENVG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 642 RLLNSL-DQATRDNTVVIFIGDNGtpTQARFRDSELsgsKNNISEGGIRVPMIVSGKNVTRqGQREANVLNGTDFFSTIL 720
Cdd:cd16152 190 RIRDALkELGLYDNTIIVFTSDHG--CHFRTRNAEY---KRSCHESSIRVPLVIYGPGFNG-GGRVEELVSLIDLPPTLL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 721 AIAGqeeVAIHDSLPFNNLLN--DANATPLRETAFSQNEEAFT---IRNARYKLIEY---LDGTRAF----------YDL 782
Cdd:cd16152 264 DAAG---IDVPEEMQGRSLLPlvDGKVEDWRNEVFIQISESQVgraIRTDRWKYSVAapdKDGWKDSgsdvyvedylYDL 340
|
410
....*....|.
gi 498244515 783 QNDISEQTDLI 793
Cdd:cd16152 341 EADPYELVNLI 351
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-793 |
1.91e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 151.99 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSfsTDLPTTPTIDEIAAQGIVFENLW-VNPVCSPTRSTIFTGKYGTRTQVL-------APG 493
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYG--NPIVKTPNIDRLAAEGVRFTNAYtPSPVCCPARASLLTGLYPHEHGVLnnvenagAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 494 DELSLSETSLPQALKNhpdtAEYASAKIGKWHLGGDSShPAAFGLDYYagifngavsdyynwelttngqtLPQTEYATTV 573
Cdd:cd16033 79 RGLPPGVETFSEDLRE----AGYRNGYVGKWHVGPEET-PLDYGFDEY----------------------LPVETTIEYF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 574 LTNLAIDWLNQ---QTTPWFLWMGYNAPHTPF---------------HLPPN---------ELH---SRNLSGDEADIE- 622
Cdd:cd16033 132 LADRAIEMLEElaaDDKPFFLRVNFWGPHDPYippepyldmydpediPLPESfaddfedkpYIYrreRKRWGVDTEDEEd 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 623 -ANPRAYYLAAVEALDSEINRLLNSLDQ-ATRDNTVVIFIGDNGtptqarfrdsELSGSKNNISEGGI------RVPMIV 694
Cdd:cd16033 212 wKEIIAHYWGYITLIDDAIGRILDALEElGLADDTLVIFTSDHG----------DALGAHRLWDKGPFmyeetyRIPLII 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 695 SGKNVTRQGQREANVLNGTDFFSTILAIAGQEEVAIHDSLPFNNLLNDANATPLRETAFSQ---NEEAFT---IRNARYK 768
Cdd:cd16033 282 KWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPEDWRDEVVTEyngHEFYLPqrmVRTDRYK 361
|
410 420
....*....|....*....|....*
gi 498244515 769 LIEYLDGTRAFYDLQNDISEQTDLI 793
Cdd:cd16033 362 YVFNGFDIDELYDLESDPYELNNLI 386
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
421-789 |
1.05e-38 |
|
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: 149.16 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLG-QDSSNQYSFSTDLptTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTR---TQVLAPGDE 495
Cdd:cd16161 1 KPNFLLLFADDLGwGDLGANWAPNAIL--TPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRngvGHNFLPTSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 496 --LSLSETSLPQALKnhpdTAEYASAKIGKWHLG-GDSSHPAAFGLDYYAGI-FngavsdyynweltTNGQTLPQ--TEY 569
Cdd:cd16161 79 ggLPLNETTLAEVLR----QAGYATGMIGKWHLGqREAYLPNSRGFDYYFGIpF-------------SHDSSLADryAQF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 570 ATTVLTNLAidwlnQQTTPWFLWMGYNAPHTPFHLPPNELHSRNLSGDeadieanprayYLAAVEALDSEINRLLNSLDQ 649
Cdd:cd16161 142 ATDFIQRAS-----AKDRPFFLYAALAHVHVPLANLPRFQSPTSGRGP-----------YGDALQEMDDLVGQIMDAVKH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 650 AT-RDNTVVIFIGDNGTPTQ-----------ARFRDSELSGSKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFFS 717
Cdd:cd16161 206 AGlKDNTLTWFTSDNGPWEVkcelavgpgtgDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 718 TILAIAGQE--EVAIHDSLPFNNLLNDANATPLR-----ETAFSQNEEAFTIRNARYKLIEYLDGTRA------------ 778
Cdd:cd16161 286 TVVALAGASlpPGRIYDGKDLSPVLFGGSKTGHRclfhpNSGAAGAGALSAVRCGDYKAHYATGGALAccgstgpklyhd 365
|
410
....*....|....
gi 498244515 779 ---FYDLQNDISEQ 789
Cdd:cd16161 366 pplLFDLEVDPAES 379
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-785 |
2.52e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 146.15 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADdlgQDSSNQYSFSTDLPT-TPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLAPGDELSLS 499
Cdd:cd16037 1 PNILIIMSD---EHNPDAMGCYGHPVVrTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETGVWDNADPYDGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 500 ETSLPQALKNhpdtAEYASAKIGKWH-LGGDSSHpaafGLDYyagifngavsDYYNwelttngqtlpqteyattvlTNLA 578
Cdd:cd16037 78 VPSWGHALRA----AGYETVLIGKLHfRGEDQRH----GFRY----------DRDV--------------------TEAA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 579 IDWLN---QQTTPWFLWMGYNAPHTPFHLPPN--ELHSRNLsgdeadieanpRAYYLAAVEALDSEINRLLNSLDQA-TR 652
Cdd:cd16037 120 VDWLReeaADDKPWFLFVGFVAPHFPLIAPQEfyDLYVRRA-----------RAAYYGLVEFLDENIGRVLDALEELgLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 653 DNTVVIFIGDNGtptqarfrdsELSGS-----KNNISEGGIRVPMIVSGKNVTRQGQREANVlNGTDFFSTILAIAGQEE 727
Cdd:cd16037 189 DNTLIIYTSDHG----------DMLGErglwgKSTMYEESVRVPMIISGPGIPAGKRVKTPV-SLVDLAPTILEAAGAPP 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498244515 728 VAIHDSLPFNNLLNDANatPLRETAFSQ------NEEAFTIRNARYKLIEYLDGTRAFYDLQND 785
Cdd:cd16037 258 PPDLDGRSLLPLAEGPD--DPDRVVFSEyhahgsPSGAFMLRKGRWKYIYYVGYPPQLFDLEND 319
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
421-724 |
3.78e-35 |
|
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: 138.84 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDlgQDSSnqySFSTDlPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKY----GTRTQVLAPG-- 493
Cdd:cd16147 1 RPNIVLILTDD--QDVE---LGSMD-PMPKTKKLLADQGTTFTNAFVTtPLCCPSRASILTGQYahnhGVTNNSPPGGgy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 494 ---DELSLSETSLPQALKNhpdtAEYASAKIGK----WHLGGDSSHPAAfGLDYYAGIFNGAVSDYYNWELTTNGQTL-- 564
Cdd:cd16147 75 pkfWQNGLERSTLPVWLQE----AGYRTAYAGKylngYGVPGGVSYVPP-GWDEWDGLVGNSTYYNYTLSNGGNGKHGvs 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 565 PQTEYATTVLTNLAIDWLN---QQTTPWFLWMGYNAPHTPF-------HLPPNELHSRNLSGDEADIEANPR-------- 626
Cdd:cd16147 150 YPGDYLTDVIANKALDFLRraaADDKPFFLVVAPPAPHGPFtpapryaNLFPNVTAPPRPPPNNPDVSDKPHwlrrlppl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 627 ---------AYY---LAAVEALDSEINRLLNSLDQATR-DNTVVIFIGDNGTPT-QarFRdseLSGSKNNISEGGIRVPM 692
Cdd:cd16147 230 nptqiayidELYrkrLRTLQSVDDLVERLVNTLEATGQlDNTYIIYTSDNGYHLgQ--HR---LPPGKRTPYEEDIRVPL 304
|
330 340 350
....*....|....*....|....*....|..
gi 498244515 693 IVSGKNVTRQGQREANVLNgTDFFSTILAIAG 724
Cdd:cd16147 305 LVRGPGIPAGVTVDQLVSN-IDLAPTILDLAG 335
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-724 |
1.89e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 132.75 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSsnQYSFSTDLPTTPTIDEIAAQGIVFENLW-VNPVCSPTRSTIFTGKY-----------GTRTQV 489
Cdd:cd16149 1 PNILFILTDDQGPWA--LGCYGNSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRMpsqhgihdwivEGSHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 490 LAPGDELSLSETSLPQALKNhpdtAEYASAKIGKWHLGGDsshpaafgldyyAGIFngavsdyynwelttngqtlpqtey 569
Cdd:cd16149 79 TKKPEGYLEGQTTLPEVLQD----AGYRCGLSGKWHLGDD------------AADF------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 570 attvltnlaIDWLNQQTTPWFLWMGYNAPHTPFHlppnelhsrnlsgdeadieanprayYLAAVEALDSEINRLLNSLD- 648
Cdd:cd16149 119 ---------LRRRAEAEKPFFLSVNYTAPHSPWG-------------------------YFAAVTGVDRNVGRLLDELEe 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 649 QATRDNTVVIFIGDNGtptqarfrdseLS-------GSKN-----NISEGGIRVPMIVSGKNVTRQGQREANVLNGTDFF 716
Cdd:cd16149 165 LGLTENTLVIFTSDNG-----------FNmghhgiwGKGNgtfplNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFF 233
|
....*...
gi 498244515 717 STILAIAG 724
Cdd:cd16149 234 PTLLELAG 241
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-726 |
1.59e-31 |
|
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: 124.97 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFstDLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLapGDELSLSE 500
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGY--DRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVW--GGPLEPDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 501 TSLPQALKNhpdtAEYASAKIgkwhlggdSSHPAAFGL-DYYAGIfngavsDYYNWELTTNGQTLPQTEYATTVLTNLAI 579
Cdd:cd16148 77 PTLAEILRK----AGYYTAAV--------SSNPHLFGGpGFDRGF------DTFEDFRGQEGDPGEEGDERAERVTDRAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 580 DWLNQQTT--PWFLWMGYNAPHTPFHlppnelhsrnlsgdeadieanprayYLAAVEALDSEINRLLNSLDQA-TRDNTV 656
Cdd:cd16148 139 EWLDRNADddPFFLFLHYFDPHEPYL-------------------------YDAEVRYVDEQIGRLLDKLKELgLLEDTL 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498244515 657 VIFIGDNGTptqarfrdsELSGSKNNISEGG------IRVPMIVSGKNVTRQGQREANVLNgTDFFSTILAIAGQE 726
Cdd:cd16148 194 VIVTSDHGE---------EFGEHGLYWGHGSnlydeqLHVPLIIRWPGKEPGKRVDALVSH-IDIAPTLLDLLGVE 259
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
417-793 |
6.74e-30 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 125.17 E-value: 6.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 417 VNTSKPNVLLIIADDLGQD--SSNqysfSTDLPTTPTIDEIAAQGIVFENLW-VNPVCSPTRSTIFTGKYGTRTQVLAPG 493
Cdd:PRK13759 2 VQTKKPNIILIMVDQMRGDclGCN----GNKAVETPNLDMLASEGYNFENAYsAVPSCTPARAALLTGLSQWHHGRVGYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 494 DELSLS-ETSLPQALKNhpdtAEYASAKIGKWHLggdssHPAAFGLDYYA-----GIFNGA----------VSDYYNW-- 555
Cdd:PRK13759 78 DVVPWNyKNTLPQEFRD----AGYYTQCIGKMHV-----FPQRNLLGFHNvllhdGYLHSGrnedksqfdfVSDYLAWlr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 556 --------ELTTNG----------QTLPQTEYATTVLTNLAIDWLN--QQTTPWFLWMGYNAPHTPFHlPPNELHSRNLS 615
Cdd:PRK13759 149 ekapgkdpDLTDIGwdcnswvarpWDLEERLHPTNWVGSESIEFLRrrDPTKPFFLKMSFARPHSPYD-PPKRYFDMYKD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 616 GD------------------EADIEA-----------NPRAYYLAAVEALDSEINRLLNSL-DQATRDNTVVIFIGDNGt 665
Cdd:PRK13759 228 ADipdphigdweyaedqdpeGGSIDAlrgnlgeeyarRARAAYYGLITHIDHQIGRFLQALkEFGLLDNTIILFVSDHG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 666 ptqarfrdsELSGS-----KNNISEGGIRVPMIVS--GKNVT-RQGQREANVLNGTDFFSTILAIAGqeeVAIHDSLPFN 737
Cdd:PRK13759 307 ---------DMLGDhylfrKGYPYEGSAHIPFIIYdpGGLLAgNRGTVIDQVVELRDIMPTLLDLAG---GTIPDDVDGR 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498244515 738 NLLNDANATPLRETAFSQNEEAFTIRNARY---KLIEYL----DGTRAFYDLQNDISEQTDLI 793
Cdd:PRK13759 375 SLKNLIFGQYEGWRPYLHGEHALGYSSDNYltdGKWKYIwfsqTGEEQLFDLKKDPHELHNLS 437
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
421-769 |
1.58e-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: 123.31 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLGQDSSNQYSFSTDLPTTptIDEIAAQGIVFENLWV-NPVCSPTRSTIFTGKYGTRTQVLAP------- 492
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGP--IDDMAAEGIRFTQAYSaDSVCTPSRAALLTGRLPIRSGMYGGtrvflpw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 493 -GDELSLSETSLPQALKNhpdtAEYASAKIGKWHLG------GDSSH-PAAFGLDYYAGI----FNGAVSD--------- 551
Cdd:cd16160 79 dIGGLPKTEVTMAEALKE----AGYTTGMVGKWHLGinennhSDGAHlPSHHGFDFVGTNlpftNSWACDDtgrhvdfpd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 552 ------YYNWELTtngQTLPQTEYATTVLTNLAIDWL-NQQTTPWFLWMGYNAPHTPFhlppneLHSRNLSGdeadieAN 624
Cdd:cd16160 155 rsacflYYNDTIV---EQPIQHEHLTETLVGDAKSFIeDNQENPFFLYFSFPQTHTPL------FASKRFKG------KS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 625 PRAYYLAAVEALDSEINRLLNSL-DQATRDNTVVIFIGDNGTPTQARFRD---SELSGSKNNISEGGIRVPMIV--SGkn 698
Cdd:cd16160 220 KRGRYGDNINEMSWAVGEVLDTLvDTGLDQNTLVFFLSDHGPHVEYCLEGgstGGLKGGKGNSWEGGIRVPFIAywPG-- 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498244515 699 vTRQGQREANVLNGTDFFSTILAIAGQE--EVAIHDSLPFNNLLNDANATPLRETAFSQNEEAFTIRNARYKL 769
Cdd:cd16160 298 -TIKPRVSHEVVSTMDIFPTFVDLAGGTlpTDRIYDGLSITDLLLGEADSPHDDILYYCCSRLMAVRYGSYKI 369
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
422-793 |
4.43e-29 |
|
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: 122.49 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSfSTDLpTTPTIDEIAAQGIVFENLW-VNPVCSPTRSTIFTGKY----GTRTQVLAPGDEL 496
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYG-NKAM-KTPNLDRLAAEGVRFDSAYtTQPVCGPARSGLFTGLYphtnGSWTNCMALGDNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 497 SlsetSLPQALKNhpdtAEYASAKIGKWHL-GGDSshpaaFGLdyyaGIF-NGAVSDY------YNWELT-------TNG 561
Cdd:cd16156 79 K----TIGQRLSD----NGIHTAYIGKWHLdGGDY-----FGN----GICpQGWDPDYwydmrnYLDELTeeerrksRRG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 562 QTLPQTE-------YATTVlTNLAIDWLNQ-QTTPWFLWMGYNAPHTPFHLPP-------------NELHSRNLS----- 615
Cdd:cd16156 142 LTSLEAEgikeeftYGHRC-TNRALDFIEKhKDEDFFLVVSYDEPHHPFLCPKpyasmykdfefpkGENAYDDLEnkplh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 616 ------------GDEADIEAnprAYYLAAVEALDSEINRLLNSLDQaTRDNTVVIFIGDNGtptqarfrdsELSGSKNNI 683
Cdd:cd16156 221 qrlwagakphedGDKGTIKH---PLYFGCNSFVDYEIGRVLDAADE-IAEDAWVIYTSDHG----------DMLGAHKLW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 684 SEGG------IRVPMIVSGKNVTRQGQREANVLNGTDFFSTILAIAGqeeVAIHDSLPFNNLLNDANA--TPLRETAFSQ 755
Cdd:cd16156 287 AKGPavydeiTNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG---IPQPKVLEGESILATIEDpeIPENRGVFVE 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 498244515 756 ------NEEAF----TIRNA---RYKLIEYLDGTRAFYDLQNDISEQTDLI 793
Cdd:cd16156 364 fgryevDHDGFggfqPVRCVvdgRYKLVINLLSTDELYDLEKDPYEMHNLI 414
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
421-776 |
2.92e-27 |
|
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: 117.16 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLGQDSSNQYSFSTDlpTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRT----QVLAPGDE 495
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSS--STPNLDRLAANGLRFTDFYSSsPVCSPSRAALLTGRYQVRSgvypGVFYPGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 496 --LSLSETSLPQALKNHpdtaEYASAKIGKWHLG---GDSSHPAAFGLDYYAGI--------------FNGAVSDY---- 552
Cdd:cd16158 79 ggLPLNETTIAEVLKTV----GYQTAMVGKWHLGvglNGTYLPTHQGFDHYLGIpyshdqgpcqnltcFPPNIPCFggcd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 553 ---------YNWELTTNGQTLPQTEYATTVLTNLAIDWLNQQTTPWFLWMGYNAPHTPfhlppnelhsrNLSGDEADiEA 623
Cdd:cd16158 155 qgevpcplfYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYP-----------QFAGQKFA-GR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 624 NPRAYYLAAVEALDSEINRLLNSLDQ-ATRDNTVVIFIGDNGTPTQARFRDSE---LSGSKNNISEGGIRVPMIVSGKNV 699
Cdd:cd16158 223 SSRGPFGDALAELDGSVGELLQTLKEnGIDNNTLVFFTSDNGPSTMRKSRGGNaglLKCGKGTTYEGGVREPAIAYWPGR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 700 TRQGqREANVLNGTDFFSTILAIAGQ--EEVAIhDSLPFNNLLNDANATPlRETAF------SQNEEAFTIRNARYKLIE 771
Cdd:cd16158 303 IKPG-VTHELASTLDILPTIAKLAGAplPNVTL-DGVDMSPILFEQGKSP-RQTFFyyptspDPDKGVFAVRWGKYKAHF 379
|
....*
gi 498244515 772 YLDGT 776
Cdd:cd16158 380 YTQGA 384
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
422-785 |
1.06e-26 |
|
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: 112.29 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSsnqysfstdLPT-------TPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLAPG 493
Cdd:cd16032 1 PNILLIMADQLTAAA---------LPAygntvvkTPNLDRLAARGVVFDNAYCNsPLCAPSRASMMTGRLPSRIGAYDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 494 DELSLSETSLPQALKNhpdtAEYASAKIGKWHL-GGDSSHpaafGLDYyagifngavsDyynwelttngqtlPQTEYATT 572
Cdd:cd16032 72 AEFPADIPTFAHYLRA----AGYRTALSGKMHFvGPDQLH----GFDY----------D-------------EEVAFKAV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 573 V-LTNLAidwLNQQTTPWFLWMGYNAPHTPFHLPPN--ELHSRNLSgdeadieanpRAYYlAAVEALDSEINRLLNSLDQ 649
Cdd:cd16032 121 QkLYDLA---RGEDGRPFFLTVSFTHPHDPYVIPQEywDLYVRRAR----------RAYY-GMVSYVDDKVGQLLDTLER 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 650 A-TRDNTVVIFIGDNGtptqarfrdsELSGS-----KNNISEGGIRVPMIVSGKNVTRQGQREANVLNgTDFFSTILAIA 723
Cdd:cd16032 187 TgLADDTIVIFTSDHG----------DMLGErglwyKMSFFEGSARVPLIISAPGRFAPRRVAEPVSL-VDLLPTLVDLA 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498244515 724 GQEEVAIHDSLPFNNLLndanatPLRETAFSQNEE--------------AFTIRNARYKLIeYLDGTRA-FYDLQND 785
Cdd:cd16032 256 GGGTAPHVPPLDGRSLL------PLLEGGDSGGEDeviseylaegavapCVMIRRGRWKFI-YCPGDPDqLFDLEAD 325
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
421-734 |
1.59e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 110.54 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLGQDS----SNQYSFSTDLPT----TPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLa 491
Cdd:cd16153 1 KPNILWIITDDQRVDSlscyNNAHTGKSESRLgyveSPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 492 pGDELSLSETS-----LPQALKNHpdtaEYASAKIGKwhlggdsSHPAAFgLDYYagifngavsdyynwelttngqtlpQ 566
Cdd:cd16153 80 -GFEAAHPALDhglptFPEVLKKA----GYQTASFGK-------SHLEAF-QRYL------------------------K 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 567 TEYATTVLTNLAIDWLNQQTTPWFLWMGYNAPHTPFhLPPNELHSrnlsgdeadieanpRAYYLAAVEALDSEINRLLNS 646
Cdd:cd16153 123 NANQSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPV-LPPKEFRD--------------RFDYYAFCAYGDAQVGRAVEA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 647 LDQA----TRDNTVVIFIGDNGtptqARFRDSELSgSKNNISEGGIRVPMIVSGKNVTR--QGQREANVLNGTDFFSTIL 720
Cdd:cd16153 188 FKAYslkqDRDYTIVYVTGDHG----WHLGEQGIL-AKFTFWPQSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLL 262
|
330
....*....|....
gi 498244515 721 AIAGQeEVAIHDSL 734
Cdd:cd16153 263 AAAGV-DVDAPDYL 275
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
422-792 |
2.00e-26 |
|
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: 113.89 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFStdLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLAPGDELSLSE 500
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHP--LVKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRYLMNHRSVWNGTPLDARH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 501 TSLPQALKNhpdtAEYASAKIGKWHLGGD-----SSHPAAFGLDYYAGIFN-GAVSDYYNWELTTngqtlpqteyaTTVL 574
Cdd:cd16028 79 LTLALELRK----AGYDPALFGYTDTSPDprglaPLDPRLLSYELAMPGFDpVDRLDEYPAEDSD-----------TAFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 575 TNLAIDWL-NQQTTPWFLWMGYNAPHTPFHLP--------PNEL---------------H-----------SRNLSGDEA 619
Cdd:cd16028 144 TDRAIEYLdERQDEPWFLHLSYIRPHPPFVAPapyhalydPADVpppiraeslaaeaaqHpllaaflerieSLSFSPGAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 620 DIEANP-------RAYYLAAVEALDSEINRLLNSLDQATR-DNTVVIFIGDNGtptqarfrdsELSGS-----KNNISEG 686
Cdd:cd16028 224 NAADLDdeevaqmRATYLGLIAEVDDHLGRLFDYLKETGQwDDTLIVFTSDHG----------EQLGDhwlwgKDGFFDQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 687 GIRVPMIVSG----KNVTRqGQREANVLNGTDFFSTILAIAGQEEVAIHDSLPFNNLLNDANATPLRETAFS-------- 754
Cdd:cd16028 294 AYRVPLIVRDprreADATR-GQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSDWRDAVHYeydfrdvs 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 498244515 755 ----------QNEEA--FTIRNARYKLIEYLDGTRAFYDLQNDISEQTDL 792
Cdd:cd16028 373 trrpqealglSPDECslAVIRDERWKYVHFAALPPLLFDLKNDPGELRDL 422
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
421-724 |
4.58e-26 |
|
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: 113.33 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLGQdsSNQYSFSTDLPTTPTIDEIAAQGIVFENLW-VNPVCSPTRSTIFTGKYGTRT------------ 487
Cdd:cd16157 1 KPNIILMLMDDMGW--GDLGVFGEPSRETPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNgfyttnaharna 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 488 ---QVLAPGdeLSLSETSLPQALKNhpdtAEYASAKIGKWHLGGDSS-HPAAFGLDYYAGIFN---GAVSD--------Y 552
Cdd:cd16157 79 ytpQNIVGG--IPDSEILLPELLKK----AGYRNKIVGKWHLGHRPQyHPLKHGFDEWFGAPNchfGPYDNkaypnipvY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 553 YNWELT-----------TNGQTlpqteYATTVLTNLAIDWLNQQTT---PWFLWMGYNAPHTPFHLPPNELHSRNlsgde 618
Cdd:cd16157 153 RDWEMIgryyeefkidkKTGES-----NLTQIYLQEALEFIEKQHDaqkPFFLYWAPDATHAPVYASKPFLGTSQ----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 619 adieanpRAYYLAAVEALDSEINRLLNSL-DQATRDNTVVIFIGDNGTPTQARfrdSELSGS-------KNNISEGGIRV 690
Cdd:cd16157 223 -------RGLYGDAVMELDSSVGKILESLkSLGIENNTFVFFSSDNGAALISA---PEQGGSngpflcgKQTTFEGGMRE 292
|
330 340 350
....*....|....*....|....*....|....
gi 498244515 691 PMIVSGKNVTRQGQREANVLNGTDFFSTILAIAG 724
Cdd:cd16157 293 PAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAG 326
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-775 |
5.53e-25 |
|
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: 106.91 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADdlgqdssnQYSFSTDLPTT------PTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQV---LA 491
Cdd:cd16035 1 PNILLILTD--------QERYPPPWPAGwaalnlPARERLAANGLSFENHYTAaCMCSPSRSTLYTGLHPQQTGVtdtLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 492 PGDELSLSeTSLPQ---ALKNhpdtAEYASAKIGKWHLggdsshpaafgldyyagifNGAVSDYYNWELTTNGQtlpqte 568
Cdd:cd16035 73 SPMQPLLS-PDVPTlghMLRA----AGYYTAYKGKWHL-------------------SGAAGGGYKRDPGIAAQ------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 569 yattvltnlAIDWL------NQQTTPWFLWMGYNAPHTpFHLPPnelhsrnlsgDEADIEANPRAYYLAAVEALDSEINR 642
Cdd:cd16035 123 ---------AVEWLrergakNADGKPWFLVVSLVNPHD-IMFPP----------DDEERWRRFRNFYYNLIRDVDRQIGR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 643 LLNSLDQAT-RDNTVVIFIGDNGtptqarfrdsELSGSK------NNISEGGIRVPMIVSGKNVTRQGQREANVLNGTDF 715
Cdd:cd16035 183 VLDALDASGlADNTIVVFTSDHG----------EMGGAHglrgkgFNAYEEALHVPLIISHPDLFGTGQTTDALTSHIDL 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498244515 716 FSTILAIAG---QEEVAIHDSLP---FNNLLNDANATPLRETAFsqneeaFTirNARYKLIEYLDG 775
Cdd:cd16035 253 LPTLLGLAGvdaEARATEAPPLPgrdLSPLLTDADADAVRDGIL------FT--YDRYKFARYFDP 310
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
421-724 |
6.93e-25 |
|
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: 110.46 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 421 KPNVLLIIADDLGqdssnqY----SFSTDLPTTPTIDEIAAQGIVFE-NLWVNPVCSPTRSTIFTGKYGTRTQVLAPGDE 495
Cdd:cd16159 1 KPNIVLFMADDLG------IgdvgCFGNDTIRTPNIDRLAKEGVKLThHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 496 -----------LSLSETSLPQALKnhpdTAEYASAKIGKWHLG-------GDSSHPAAFGLDYYAGI------------- 544
Cdd:cd16159 75 rvilftassggLPPNETTFAEVLK----QQGYSTALIGKWHLGlhcesrnDFCHHPLNHGFDYFYGLpltnlkdcgdgsn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 545 -----------------------------FNGAVS-------------------------DYYNWELTTNGQTLPQ---T 567
Cdd:cd16159 151 geydlsfdplfplltafvlitaltiflllYLGAVSkrffvfllilsllfislfflllitnRYFNCILMRNHEVVEQpmsL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 568 EYATTVLTNLAIDWLNQQT-TPWFLWMGYNAPHTPFHLPPN----ELHSRnlsgdeadieanprayYLAAVEALDSEINR 642
Cdd:cd16159 231 ENLTQRLTKEAISFLERNKeRPFLLVMSFLHVHTALFTSKKfkgrSKHGR----------------YGDNVEEMDWSVGQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 643 LLNSLDQA-TRDNTVVIFIGDNGTPTQARFRDSELSG--------SKNNISEGGIRVPMIVSGKNVTRQGQREANVLNGT 713
Cdd:cd16159 295 ILDALDELgLKDNTFVYFTSDNGGHLEEISVGGEYGGgnggiyggKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLM 374
|
410
....*....|.
gi 498244515 714 DFFSTILAIAG 724
Cdd:cd16159 375 DIFPTVAALAG 385
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-793 |
1.33e-23 |
|
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: 105.01 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDS----SNQYSFstdlptTPTIDEIAAQGIVFENLWV-NPVCSPTRSTIFTGKY----GTRTQV-LA 491
Cdd:cd16150 1 PNIVIFVADQLRADSlghlGNPAAV------TPNLDALAAEGVRFSNAYCqNPVCSPSRCSFLTGWYphvnGHRTLHhLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 492 PGDELSLSETslpqaLKNHpdtaEYASAKIGKwhlggdsshpaafgldyyagifNGAVSDYYNWElttngqtlpQTEYAT 571
Cdd:cd16150 75 RPDEPNLLKT-----LKDA----GYHVAWAGK----------------------NDDLPGEFAAE---------AYCDSD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 572 TVLTNLAIDWLNQQTT--PWFLWMGYNAPHTPF-------------HLPPN-----------------ELHSRNLSGDEA 619
Cdd:cd16150 115 EACVRTAIDWLRNRRPdkPFCLYLPLIFPHPPYgveepwfsmidreKLPPRrppglrakgkpsmlegiEKQGLDRWSEER 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 620 DIEAnpRAYYLAAVEALDSEINRLLNSLDQAT-RDNTVVIFIGDNGTPTQarfrDSELSgSK--NNISEGGIRVPMIVSG 696
Cdd:cd16150 195 WREL--RATYLGMVSRLDHQFGRLLEALKETGlYDDTAVFFFSDHGDYTG----DYGLV-EKwpNTFEDCLTRVPLIIKP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 697 KNVTRQGQREANV-LngTDFFSTILAIAGQEEVAIHDSLPFNNLLNDANATPlRETAFS--------------------- 754
Cdd:cd16150 268 PGGPAGGVSDALVeL--VDIPPTLLDLAGIPLSHTHFGRSLLPVLAGETEEH-RDAVFSeggrlhgeeqamegghgpydl 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 498244515 755 ------QNEE------AFTIRNARYKLIEYLDGTRAFYDLQNDISEQTDLI 793
Cdd:cd16150 345 kwprllQQEEppehtkAVMIRTRRYKYVYRLYEPDELYDLEADPLELHNLI 395
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
37-414 |
1.74e-19 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 95.11 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 37 PVVTNQAPqLTTAITDQTTNQSQQYSFDlsqgGQTFTDPDGDTLTYSFStspQTN--DFTLNG----TVLSGTPE--QTE 108
Cdd:NF038112 1181 PGVCNRRP-VANAGPDQTVLERTTVTLN----GSGSFDPDGDPLTYAWT---QVSgpAVTLTGadtaTPSFTAPEvtADT 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 109 AITITVTASDPSGLTASDS---YLLTINGAPqTAKTIPDQSINLGENVSLDISQNrttfvDPDGDELTYA-FSTSPQ--- 181
Cdd:NF038112 1253 VLTFQLVVSDGTKTSAPDTvtvLVRNVNRAP-VAVAGAPATVDERSTVTLDGSGT-----DADGDALTYAwTQTSGPavt 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 182 -TNDFSLNGSVLSGTPALAQTITFTVTATDpNGLSANDSF---LLNINGAPkLTNSISNQSVNIGENynfdVTQNGSTfE 257
Cdd:NF038112 1327 lTGATTATATFTAPEVTADTQLTFTLTVSD-GTASATDTVtvtVRNVNRAP-VANAGADQTVDERST----VTLSGSA-T 1399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 258 DLDSEILIYS-VQITPTNDDLTFNGTHLSGM--PNQAGEYTIAVTATDDGGLFDSTSFVLYVVEPNENNSPiIANPIADQ 334
Cdd:NF038112 1400 DPDGDALTYAwTQTAGPTVTLTGADTATASFtaPEVAADTELTFQLTVSADGQASADVTVTVTVRNVNRAP-VAHAGESI 1478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 335 SATlnqdfNFDMSQNNTTFSDPDGDMLTF---QVAITP-TDSGLTSDGLIL-SGNPNQTGEINVTVTASDPAGLSVSDTF 409
Cdd:NF038112 1479 TVD-----EGSTVTLDASATDPDGDTLTYawtQVAGPSvTLTGADSAKLTFtAPEVSADTTLTFSLTVTDGSGSSGPVVV 1553
|
....*
gi 498244515 410 SVKVS 414
Cdd:NF038112 1554 TVTVK 1558
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
422-723 |
3.46e-19 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 88.25 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFSTdlPTTPTIDEIAAQGIVFENLWVNPVCS--PTRSTIFTGKYGTRTQVLAPGdelsls 499
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPA--PTTPNLKRLASEGATFNFRSVSPPTSsaPNHAALLTGAYPTLHGYTGNG------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 500 etslpqalknhpdtaeyasakigkWHLGGDSSHPAAfgldyyagifngavsdyynweLTTNGQTLP----QTEYATTVLT 575
Cdd:cd00016 73 ------------------------SADPELPSRAAG---------------------KDEDGPTIPellkQAGYRTGVIG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 576 NL-AIDWlNQQTTPWFLWMGYNAPHTPFHlppnelhsrnlsgdeaDIEANPRAYYlAAVEALDSEINRLLNSLDQATR-D 653
Cdd:cd00016 108 LLkAIDE-TSKEKPFVLFLHFDGPDGPGH----------------AYGPNTPEYY-DAVEEIDERIGKVLDALKKAGDaD 169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 654 NTVVIFIGDNGTPTQARFRDSELSGSKNNiSEGGIRVPMIVSGKNVtRQGQREANVLNGTDFFSTILAIA 723
Cdd:cd00016 170 DTVIIVTADHGGIDKGHGGDPKADGKADK-SHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| YHYH |
pfam14240 |
YHYH protein; This domain family is found in bacteria, eukaryotes and viruses, and is ... |
931-1049 |
8.92e-14 |
|
YHYH protein; This domain family is found in bacteria, eukaryotes and viruses, and is typically between 141 and 198 amino acids in length. There is a conserved YHYH sequence motif.
Pssm-ID: 433802 Cd Length: 188 Bit Score: 70.94 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 931 TFPNNPTP-TQTECETGLGPVGLWVNGVPiYNWSDASSYNN--QDVWNNFAL-PFRSAAMDVCNGHSG-NGMYHHHSYNA 1005
Cdd:pfam14240 2 TIPLNPTLaTTTTTLNLPGPVGVALNGVP-FDPGTAESYNNdrDGGWRYDALgDVENLGLDCNNAHVQpTGAYHYHGLPS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 498244515 1006 CLKQQLGDeGKGHSPIYGYAGDGYPIHGPYHSKDVLAKSCWKKR 1049
Cdd:pfam14240 81 GLIKKLDG-GQHDMPLIGYAADGFPIYGPYGYTDALDATSGVKK 123
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
422-785 |
2.22e-13 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 73.34 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLgqDSSNQYSFSTDLPTTPTIDEIAAQGIVFENLWVN-PVCSPTRSTIFTGKYGTRTQVLAPGDELSLSE 500
Cdd:cd16171 1 PNVVMVMSDSF--DGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSGLFTHLTESWNNYKGLDPNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 501 TSLPQALKNHpdtaEYASAKIGKwhlggdsshpaafgLDYYAGifNGAVSDYY-------NWELTTNGQTLPQ-TEYATT 572
Cdd:cd16171 79 PTWMDRLEKH----GYHTQKYGK--------------LDYTSG--HHSVSNRVeawtrdvPFLLRQEGRPTVNlVGDRST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 573 V--------LTNLAIDWLNQ----QTTPWFLWMGYNAPHtPFhlpPNELHSRNLSGDEadieaNPRAYYL---AAVEALD 637
Cdd:cd16171 139 VrvmlkdwqNTDKAVHWIRKeapnLTQPFALYLGLNLPH-PY---PSPSMGENFGSIR-----NIRAFYYamcAETDAML 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 638 SEINRLLNSLDQAtrDNTVVIFIGDNGtptqarfrdsELSGS-----KNNISEGGIRVPMIVSGKNVtRQGQREANVLNG 712
Cdd:cd16171 210 GEIISALKDTGLL--DKTYVFFTSDHG----------ELAMEhrqfyKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 713 TDFFSTILAIAG---QEEVAIHDSLP-----FNNLLNDANATPlrETAFSQ------NEEAFTIRNARYKLIEYLDGTRA 778
Cdd:cd16171 277 VDIYPTMLDIAGvpqPQNLSGYSLLPllsesSIKESPSRVPHP--DWVLSEfhgcnvNASTYMLRTNSWKYIAYADGNSV 354
|
410
....*....|
gi 498244515 779 ---FYDLQND 785
Cdd:cd16171 355 ppqLFDLSKD 364
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
414-786 |
3.06e-12 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 70.84 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 414 SAQVNTSKPNVLLIIADDLGQDSSNQYSFSTDLptTPTIDEIAAQGIVFENLWvnpvcSPTRST------IFTGKYGTrt 487
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDV--TPFLDSLAKESLYFGNFY-----SQGGRTsrgefaVLTGLPPL-- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 488 qvlaPGDELSLSE-----TSLPQALKNHpdtaEYASAKIgkwHlGGDSS-------HPAA-----FGLDYYAGIFNGA-- 548
Cdd:COG1368 298 ----PGGSPYKRPgqnnfPSLPSILKKQ----GYETSFF---H-GGDGSfwnrdsfYKNLgfdefYDREDFDDPFDGGwg 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 549 VSDYYnwelttngqtlpqteyattvLTNLAIDWLNQQTTPWFLwmgY-----NapHTPFHLPPNElhsrnlsGDEADIEA 623
Cdd:COG1368 366 VSDED--------------------LFDKALEELEKLKKPFFA---FlitlsN--HGPYTLPEED-------KKIPDYGK 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 624 NPRAYYLAAVEALDSEINRLLNSLDQATR-DNTVVIFIGDNGTPtqarfrdseLSGSKN-NISEGGIRVPMIVSGKNVTr 701
Cdd:COG1368 414 TTLNNYLNAVRYADQALGEFIEKLKKSGWyDNTIFVIYGDHGPR---------SPGKTDyENPLERYRVPLLIYSPGLK- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 702 QGQREANVLNGTDFFSTILAIAGQEevaiHDSLPF--NNLLN-DANATPLRETAFSQNEEAFTIRNARYKLI--EYLDGT 776
Cdd:COG1368 484 KPKVIDTVGSQIDIAPTLLDLLGID----YPSYYAfgRDLLSpDTDPFAFRNGGFITDDYVYVLKTGELTEEdkELEEEA 559
|
410
....*....|
gi 498244515 777 RAFYDLQNDI 786
Cdd:COG1368 560 LAYLQLSDYL 569
|
|
| CADG |
smart00736 |
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ... |
47-136 |
2.94e-11 |
|
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.
Pssm-ID: 214795 [Multi-domain] Cd Length: 97 Bit Score: 60.82 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 47 TTAITDQTTNQSQQYSFDLsqGGQTFTDPDGDTLTYSFSTSPQTND-----FTLNGTVLSGTP--EQTEAITITVTASDP 119
Cdd:smart00736 1 ANAIGDQTATEGESFSYTI--PSSTFTDADGDTLTYSATLSDGSALpswlsFDSDTGTLSGTPtnSDVGSLSLKVTATDS 78
|
90
....*....|....*..
gi 498244515 120 SGLTASDSYLLTINGAP 136
Cdd:smart00736 79 SGASASDTFTITVVNTN 95
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
41-229 |
1.04e-10 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 66.60 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 41 NQAPqLTTAITDQTTNQSQQYSFDLSQggqtfTDPDGDTLTYSFS-----TSPQTNDFTLNGTVLSGTPEQTEAITITVT 115
Cdd:NF038112 1373 NRAP-VANAGADQTVDERSTVTLSGSA-----TDPDGDALTYAWTqtagpTVTLTGADTATASFTAPEVAADTELTFQLT 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 116 ASDPSGLTASDSYLLTI---NGAPqTAKTIPDQSINLGENVSLDisqnrTTFVDPDGDELTYAFSTS--PQTNDFSLNGS 190
Cdd:NF038112 1447 VSADGQASADVTVTVTVrnvNRAP-VAHAGESITVDEGSTVTLD-----ASATDPDGDTLTYAWTQVagPSVTLTGADSA 1520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498244515 191 VLSGT-PALAQ--TITFTVTATDPNGLSANDSF---LLNINGAPK 229
Cdd:NF038112 1521 KLTFTaPEVSAdtTLTFSLTVTDGSGSSGPVVVtvtVKNVNRAPD 1565
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
422-724 |
3.15e-09 |
|
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: 59.62 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 422 PNVLLIIADDLGQDSSNQYSFSTDLptTPTIDEIAAQGIVFENLWVNPVCSPTRSTIF---TG----KYGTRTQVLAPGD 494
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDL--TPNLNKLAKEGLYFGNFYSPGFGGGTANGEFevlTGlpplPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 495 ELslseTSLPQALKN--------HPDTAEYASAKIGKWHLGGDSSHPA-AFGLDYYAGIFNGaVSDYYnwelttngqtlp 565
Cdd:cd16015 79 PL----PSLPSILKEqgyetifiHGGDASFYNRDSVYPNLGFDEFYDLeDFPDDEKETNGWG-VSDES------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 566 qteyattvLTNLAIDWLNQQT-TPWFLWM--GYNapHTPFHLPPNELHSRNLSGDEADIEANprayYLAAVEALDSEINR 642
Cdd:cd16015 142 --------LFDQALEELEELKkKPFFIFLvtMSN--HGPYDLPEEKKDEPLKVEEDKTELEN----YLNAIHYTDKALGE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 643 LLNSLDQATR-DNTVVIFIGDNGTPTQARFRDSELSGSKNNiseggiRVPMIVSGKNVTrQGQREANVLNGTDFFSTILA 721
Cdd:cd16015 208 FIEKLKKSGLyENTIIVIYGDHLPSLGSDYDETDEDPLDLY------RTPLLIYSPGLK-KPKKIDRVGSQIDIAPTLLD 280
|
...
gi 498244515 722 IAG 724
Cdd:cd16015 281 LLG 283
|
|
| CADG |
smart00736 |
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ... |
328-415 |
8.96e-09 |
|
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.
Pssm-ID: 214795 [Multi-domain] Cd Length: 97 Bit Score: 53.89 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 328 ANPIADQSATLNQDFNFDMSQnnTTFSDPDGDMLTFQVAIT-----PTDSGLTSDGLILSGNP--NQTGEINVTVTASDP 400
Cdd:smart00736 1 ANAIGDQTATEGESFSYTIPS--STFTDADGDTLTYSATLSdgsalPSWLSFDSDTGTLSGTPtnSDVGSLSLKVTATDS 78
|
90
....*....|....*
gi 498244515 401 AGLSVSDTFSVKVSA 415
Cdd:smart00736 79 SGASASDTFTITVVN 93
|
|
| CADG |
smart00736 |
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ... |
141-228 |
6.23e-08 |
|
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.
Pssm-ID: 214795 [Multi-domain] Cd Length: 97 Bit Score: 51.57 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 141 TIPDQSINLGENVSLDIsqNRTTFVDPDGDELTYAFSTSPQTND---FSLNGS--VLSGTPAL--AQTITFTVTATDPNG 213
Cdd:smart00736 3 AIGDQTATEGESFSYTI--PSSTFTDADGDTLTYSATLSDGSALpswLSFDSDtgTLSGTPTNsdVGSLSLKVTATDSSG 80
|
90
....*....|....*
gi 498244515 214 LSANDSFLLNINGAP 228
Cdd:smart00736 81 ASASDTFTITVVNTN 95
|
|
| CADG |
smart00736 |
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ... |
231-322 |
2.51e-07 |
|
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.
Pssm-ID: 214795 [Multi-domain] Cd Length: 97 Bit Score: 49.65 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 231 TNSISNQSVNIGENYNFDVtqNGSTFEDLDSEILIYSVQITPTNDD---LTFNG-TH-LSGMP--NQAGEYTIAVTATDD 303
Cdd:smart00736 1 ANAIGDQTATEGESFSYTI--PSSTFTDADGDTLTYSATLSDGSALpswLSFDSdTGtLSGTPtnSDVGSLSLKVTATDS 78
|
90
....*....|....*....
gi 498244515 304 GGLFDSTSFVLYVVEPNEN 322
Cdd:smart00736 79 SGASASDTFTITVVNTNDA 97
|
|
| He_PIG |
pfam05345 |
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ... |
325-414 |
2.73e-06 |
|
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.
Pssm-ID: 398814 [Multi-domain] Cd Length: 95 Bit Score: 46.70 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 325 PIIANPIADQSATLNQDFNFDMSQNntTFSDPDGDMLTFQVAITPTD---SGLT--SDGLILSGNP--NQTGEINVTVTA 397
Cdd:pfam05345 1 PPVVTSPADQTATVGTPYSFTLSAS--GGSDPYGGSTVTYSTTATGGalpSGLTlnSSTGTISGTPtsVQPGTYTFTVTA 78
|
90
....*....|....*..
gi 498244515 398 SDPAGLSVSDTFSVKVS 414
Cdd:pfam05345 79 TDSSGLSSSTTFTLTVT 95
|
|
| He_PIG |
pfam05345 |
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ... |
46-133 |
4.19e-06 |
|
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.
Pssm-ID: 398814 [Multi-domain] Cd Length: 95 Bit Score: 46.31 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 46 LTTAITDQTTNQSQQYSFDLSQGGQTFTDPdGDTLTYSFSTSPQT--NDFTLNGT--VLSGTPEQTEA--ITITVTASDP 119
Cdd:pfam05345 3 VVTSPADQTATVGTPYSFTLSASGGSDPYG-GSTVTYSTTATGGAlpSGLTLNSStgTISGTPTSVQPgtYTFTVTATDS 81
|
90
....*....|....
gi 498244515 120 SGLTASDSYLLTIN 133
Cdd:pfam05345 82 SGLSSSTTFTLTVT 95
|
|
| He_PIG |
pfam05345 |
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ... |
230-314 |
3.73e-04 |
|
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.
Pssm-ID: 398814 [Multi-domain] Cd Length: 95 Bit Score: 40.92 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 230 LTNSISNQSVNIGENYNFDVTQNGSTFEDLDSeiliySVQITPTNDD------LTFNGT--HLSGMP--NQAGEYTIAVT 299
Cdd:pfam05345 3 VVTSPADQTATVGTPYSFTLSASGGSDPYGGS-----TVTYSTTATGgalpsgLTLNSStgTISGTPtsVQPGTYTFTVT 77
|
90
....*....|....*
gi 498244515 300 ATDDGGLFDSTSFVL 314
Cdd:pfam05345 78 ATDSSGLSSSTTFTL 92
|
|
| Slr4-like |
cd22554 |
S (surface)-layer proteins similar to Pseudoalteromonas tunicata Slr4; Pseudoalteromonas ... |
71-314 |
6.88e-04 |
|
S (surface)-layer proteins similar to Pseudoalteromonas tunicata Slr4; Pseudoalteromonas tunicata D2 Slr4 (also known as EAR28894 protein) is an S-layer protein and the dominant protein within P. tunicata pellicle biofilm components. S-layers are self-assembling, paracrystalline proteinaceous lattices that form an interface between the cell and its extracellular environment; purified P. tunicata Slr4 protein is able to form square (p4 symmetry) paracrystalline lattices. Slr4 may protect cells and biofilm matrix components against stressors such as attack by viruses, bacteria or eukaryotes. The Slr4 family is widely distributed in gammaproteobacteria, including species of Pseudoalteromonas and Vibrio, and is found exclusively in marine metagenomes. It may play an important role in marine microbial physiology and ecology.
Pssm-ID: 412100 [Multi-domain] Cd Length: 400 Bit Score: 43.61 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 71 TFTDPDGDTLTY-----SFSTSPQTNDFTLNGTVLSGTPEQTEAITITVTASDPSGLTASDSYLLTINGAPQTAKTIPDQ 145
Cdd:cd22554 54 SVTATGATTVTFrvtlgNPAGANTATRTILGLTFDTDAVLAAGAVTVTYSAVTSTGTAIDGTSTATGTATLATVVDQFSA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 146 SINLGENVSLDISQNRTTFVDPDGDELTYAFSTSPQTNDFSLngsvlsGTPALAQTITFTVTATDPNGLSANDSFllnIN 225
Cdd:cd22554 134 SVTTKLDGVIDVEDDRKTFVGGTSDDTTTDLTVTTTTNTATL------ALAATATKVTVTLTGDFSGVDDDTDTT---GN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 226 GAPKLTNSISNQSVNIGENYNFD-VTQNGSTFEDLDSEILIYSVQITPTNDDLTFngthlsgmpnQAGEYTIAVTATDDG 304
Cdd:cd22554 205 DAAAATATAATAAATTGAAAAADtVTITSATAAAALATTAGTNAVGATAGGAVVL----------PAQSFTVDATVTYTD 274
|
250
....*....|
gi 498244515 305 GLFDSTSFVL 314
Cdd:cd22554 275 GATTTTTTLL 284
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
12-140 |
8.84e-04 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 43.88 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 12 SLLSVTLIGCGGGSSESNPDNDVTPPVVtNQAPQLTtAITDQTTNQSQQYSFDLSQggqtfTDPDGDTLTYSFSTS--PQ 89
Cdd:NF038112 1439 TELTFQLTVSADGQASADVTVTVTVRNV-NRAPVAH-AGESITVDEGSTVTLDASA-----TDPDGDTLTYAWTQVagPS 1511
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 498244515 90 TNDFTLNGTVLSGT-PE--QTEAITITVTASDPSGLTASDSYLLTINGAPQTAK 140
Cdd:NF038112 1512 VTLTGADSAKLTFTaPEvsADTTLTFSLTVTDGSGSSGPVVVTVTVKNVNRAPD 1565
|
|
| He_PIG |
pfam05345 |
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ... |
141-225 |
1.18e-03 |
|
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.
Pssm-ID: 398814 [Multi-domain] Cd Length: 95 Bit Score: 39.38 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 141 TIPDQSINLGENVSLDISQNRTTFVDPdGDELTYAFSTSPQT--NDFSLNGS--VLSGTPALAQ--TITFTVTATDPNGL 214
Cdd:pfam05345 6 SPADQTATVGTPYSFTLSASGGSDPYG-GSTVTYSTTATGGAlpSGLTLNSStgTISGTPTSVQpgTYTFTVTATDSSGL 84
|
90
....*....|.
gi 498244515 215 SANDSFLLNIN 225
Cdd:pfam05345 85 SSSTTFTLTVT 95
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
6-437 |
1.51e-03 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 42.63 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 6 NSLFTISLLSVTLIGCGGGSSESNPDNDVTPPVVTNQAPQLTTAITDQTTNQSQQYSFDLSQGGQTFTDpDGDTLTYSFS 85
Cdd:COG3468 23 LGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGG-GGGNSGTGGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 86 TSPQTNDFTLNGTVLSGTPEQTEAITITVTASDPSGLTASDSYLLTINGAPQTAKTIPDQSINLGENVSLDISQNRTTfV 165
Cdd:COG3468 102 GGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAGGGGG-G 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 166 DPDGDELTYAFSTSPQTNDFSLNGSVLSGTPALAQTITFTVTATDPNGLSANDSFLLNINGA-----PKLTNSISNQSVN 240
Cdd:COG3468 181 GAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGgsaggTGGGGLTGGGAAG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 241 IGENYNFDVTQNGSTFEDLDSEILIYSVQITPTNDDLTFNGTHLSGMPNQAGEYTIAVTATDDGGLFDSTSFVLYVVEPN 320
Cdd:COG3468 261 TGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGGGGGG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 321 ENNSPIIANPIADQSATLNQDFNFDMSQNNTTFSDPDGDMLTFQVAITPTDSGLTSDGLILSGNPNQTGEINVTVTASDP 400
Cdd:COG3468 341 TTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGLTLTG 420
|
410 420 430
....*....|....*....|....*....|....*..
gi 498244515 401 AGLSVSDTFSVKvsaqvntskpNVLLIIADDLGQDSS 437
Cdd:COG3468 421 GTLTVNGNYTGN----------NGTLVLNTVLGDDNS 447
|
|
| COG1470 |
COG1470 |
Uncharacterized membrane protein [Function unknown]; |
24-460 |
8.38e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 441079 [Multi-domain] Cd Length: 475 Bit Score: 40.23 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 24 GSSESNPDNDVTPPVVTNQAPQLTTAITDQTTNQSQQYSFDLS-QGGQTFTDPDGDTLTYSFSTSPQTNDFTLNGTVLSG 102
Cdd:COG1470 29 GSTVALTSTASALSGERTTLAALAATGGLVTATPVSPTSATLTlSVEVPSNATVGTYLPITVTVAPYGLTLSVESPSLEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 103 TPEQTEAITITVTASDPSgltaSDSYLLTINGAPqtaktipdqsinlgENVSLDISQNRTTFVDPdGDELTYAFSTSPQT 182
Cdd:COG1470 109 APGETVTYTVTLTNTGDE----PDTVSLSAEGLP--------------EGWTVTFTPDTSVSLAP-GESKTVTLEVTPPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 183 NdfslngsvlsgtpALAQTITFTVTATDPN-GLSANDSFLLNINGAPKLTNSI--SNQSVNIGENYNFDVT-QNGSTFED 258
Cdd:COG1470 170 N-------------AEPGTYPVTVTATSGEdSSSASLTLTLTVTGSYELELSStpTGRTVTPGESATFTVTvTNTGNGAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 259 LdseiliYSVQIT---PTNDDLTFNGTHLSG-MPNQ---------------AGEYTIAVTATDDGGlfDSTSFVLYVVEP 319
Cdd:COG1470 237 L------TNVTLSasaPSGWTVSFEPETIPSlAPGEsatvtltvtvpadatAGDYTVTVTATSDET--ASATLRLTVETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 320 N------------------------ENNSPIIANPIADQSATLNQDFNFDMSQNNTTFSDPDGDMLTFQVAITPTDSGLT 375
Cdd:COG1470 309 SlwgwigylirkygglgatgsllvaSVSLVVGAVVGTLTTPLLLTGFAGNGLLSAATAPLLLLLGLTLSLLSDVLVFTVG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498244515 376 SDGLILSGNPNQTGEINVTVTASDPAGLSVSDTFSVKVSAQVNTSKPNVLLIIADDLGQDSSNQYSFSTDLPTTPTIDEI 455
Cdd:COG1470 389 SAGVSAAAATAETSALTALGVGATGAVGSGSASASVKVTGGAAVATGLTDATTLPGAGSTATLALPGGGGITSTLSLGTL 468
|
....*
gi 498244515 456 AAQGI 460
Cdd:COG1470 469 PLGGS 473
|
|
| |
