NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|194381358|dbj|BAG58633|]
View 

unnamed protein product [Homo sapiens]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 3-143 3.47e-24

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.


The actual alignment was detected with superfamily member cd16030:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 435  Bit Score: 96.49  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358   3 LVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKNLLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwns 80
Cdd:cd16030  339 LVELVDIYPTLAELAGLPAPP-----------CLEGKSLV-----------PLLknPSAKWKDAAFSQYPRPS------- 389

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194381358  81 dkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFSDIHAGELYFVDSDPLQDHNMYNDSQ 143
Cdd:cd16030  390 ---------IMGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPE 434
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 3-143 3.47e-24

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: 96.49  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358   3 LVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKNLLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwns 80
Cdd:cd16030  339 LVELVDIYPTLAELAGLPAPP-----------CLEGKSLV-----------PLLknPSAKWKDAAFSQYPRPS------- 389

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194381358  81 dkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFSDIHAGELYFVDSDPLQDHNMYNDSQ 143
Cdd:cd16030  390 ---------IMGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPE 434
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
2-141 1.10e-07

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 49.49  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358   2 DLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPsdipqwnsd 81
Cdd:COG3119  278 ALVSLIDLLPTLLDLAGVPIPEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRG--------- 328

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358  82 kpslkdikIMGYSIRTIDYRYTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 141
Cdd:COG3119  329 --------GGNRAIRTGRWKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 3-143 3.47e-24

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: 96.49  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358   3 LVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKNLLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwns 80
Cdd:cd16030  339 LVELVDIYPTLAELAGLPAPP-----------CLEGKSLV-----------PLLknPSAKWKDAAFSQYPRPS------- 389

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194381358  81 dkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFSDIHAGELYFVDSDPLQDHNMYNDSQ 143
Cdd:cd16030  390 ---------IMGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPE 434
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
2-141 1.10e-07

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 49.49  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358   2 DLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPsdipqwnsd 81
Cdd:COG3119  278 ALVSLIDLLPTLLDLAGVPIPEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRG--------- 328

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358  82 kpslkdikIMGYSIRTIDYRYTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 141
Cdd:COG3119  329 --------GGNRAIRTGRWKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 2-143 6.75e-06

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: 44.53  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358   2 DLVELVSLFPTLAGLAGLQVPPrcpvPSFhvelcreGKNLLKHFRFRDLEEDPY-------LPGNPReliAYSQYPRPSD 74
Cdd:cd16150  278 ALVELVDIPPTLLDLAGIPLSH----THF-------GRSLLPVLAGETEEHRDAvfseggrLHGEEQ---AMEGGHGPYD 343

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194381358  75 IPQWNSDKPSLKDIKIMGYSIRTIDYRYtVWVGFNPDeflanfsdihagELYFVDSDPLQDHNMYNDSQ 143
Cdd:cd16150  344 LKWPRLLQQEEPPEHTKAVMIRTRRYKY-VYRLYEPD------------ELYDLEADPLELHNLIGDPA 399
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 11-151 3.66e-04

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: 39.43  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358  11 PTLAGLAGLQVPPRCpvpsfhvelcrEGKNLLKHFRFRDleedpylPGNPRE--LIAYSQYPRPSDIPQWnsdkpslkdi 88
Cdd:cd16031  323 PTILDLAGVPIPEDM-----------QGRSLLPLLEGEK-------PVDWRKefYYEYYEEPNFHNVPTH---------- 374

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194381358  89 kimgYSIRTIDYRYTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYNDSQGGDLFQLL 151
Cdd:cd16031  375 ----EGVRTERYKYIYYYGVWDEE-----------ELYDLKKDPLELNNLANDPEYAEVLKEL 422
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 9-137 1.51e-03

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: 37.53  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381358   9 LFPTLAGLAGLQVPPrcpvpsfHVELcrEGKNLLKhfrfrdLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSdkpslkdi 88
Cdd:cd16146  298 LLPTLLDLCGVKLPE-------GIKL--DGRSLLP------LLKGESDPWPERTLFTHSGRWPPPPKKKRNA-------- 354

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 194381358  89 kimgySIRTIDYRYTVWVGFNPdeflanfsdihagELYFVDSDPLQDHN 137
Cdd:cd16146  355 -----AVRTGRWRLVSPKGFQP-------------ELYDIENDPGEEND 385
 
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