NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|498244515|ref|WP_010558671|]
View 

sulfatase-like hydrolase/transferase [Pseudoalteromonas spongiae]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

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
myxo_dep_M36 super family cl45606
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.


The actual alignment was detected with superfamily member NF038112:

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 super family cl16738
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.


The actual alignment was detected with superfamily member pfam14240:

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH