NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720356375|ref|XP_030111510|]
View 

tomoregulin-2 isoform X1 [Mus musculus]

Protein Classification

KAZAL_FS and PHA02887 domain-containing protein( domain architecture ID 12883870)

KAZAL_FS and PHA02887 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
95-135 2.18e-10

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


:

Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 55.35  E-value: 2.18e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720356375  95 CNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
181-227 4.60e-08

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 48.83  E-value: 4.60e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720356375  181 VCNIDCSQtNFNPLCASDGKSYDNACQIKEASCQKQEKIEVMSLGRC 227
Cdd:smart00280   1 DCPEACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
PHA02887 super family cl31518
EGF-like protein; Provisional
236-301 2.39e-06

EGF-like protein; Provisional


The actual alignment was detected with superfamily member PHA02887:

Pssm-ID: 165214  Cd Length: 126  Bit Score: 46.46  E-value: 2.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720356375 236 KSEDGHYARTDYAENANKLEESAREHHI--PCPEHYNGFCMHGKCEHSINMQEPSCRCDAGYTGQHCE 301
Cdd:PHA02887   55 RNFESHISKFNYKENANAQNFKRKNSMFfeKCKNDFNDFCINGECMNIIDLDEKFCICNKGYTGIRCD 122
 
Name Accession Description Interval E-value
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
95-135 2.18e-10

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 55.35  E-value: 2.18e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720356375  95 CNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
90-135 4.24e-10

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 54.61  E-value: 4.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1720356375   90 VCQFKCNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:smart00280   1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
181-227 4.60e-08

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 48.83  E-value: 4.60e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720356375  181 VCNIDCSQtNFNPLCASDGKSYDNACQIKEASCQKQEKIEVMSLGRC 227
Cdd:smart00280   1 DCPEACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
PHA02887 PHA02887
EGF-like protein; Provisional
236-301 2.39e-06

EGF-like protein; Provisional


Pssm-ID: 165214  Cd Length: 126  Bit Score: 46.46  E-value: 2.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720356375 236 KSEDGHYARTDYAENANKLEESAREHHI--PCPEHYNGFCMHGKCEHSINMQEPSCRCDAGYTGQHCE 301
Cdd:PHA02887   55 RNFESHISKFNYKENANAQNFKRKNSMFfeKCKNDFNDFCINGECMNIIDLDEKFCICNKGYTGIRCD 122
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
189-227 4.79e-06

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 43.03  E-value: 4.79e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720356375 189 TNFNPLCASDGKSYDNACQIKEASCQKQEKIEVMSLGRC 227
Cdd:cd00104     3 KEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
95-135 3.59e-04

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 38.03  E-value: 3.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720356375  95 CNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:pfam00050   9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
182-227 1.22e-03

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 36.70  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720356375 182 CNIDCSQTNFNPLCASDGKSYDNACQIKEASCQKQEKIE---VMSLGRC 227
Cdd:pfam07648   2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
 
Name Accession Description Interval E-value
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
95-135 2.18e-10

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 55.35  E-value: 2.18e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720356375  95 CNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
90-135 4.24e-10

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 54.61  E-value: 4.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1720356375   90 VCQFKCNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:smart00280   1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
181-227 4.60e-08

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 48.83  E-value: 4.60e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720356375  181 VCNIDCSQtNFNPLCASDGKSYDNACQIKEASCQKQEKIEVMSLGRC 227
Cdd:smart00280   1 DCPEACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
92-135 1.58e-06

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 44.58  E-value: 1.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720356375  92 QFKCNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:cd01327     2 VFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
PHA02887 PHA02887
EGF-like protein; Provisional
236-301 2.39e-06

EGF-like protein; Provisional


Pssm-ID: 165214  Cd Length: 126  Bit Score: 46.46  E-value: 2.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720356375 236 KSEDGHYARTDYAENANKLEESAREHHI--PCPEHYNGFCMHGKCEHSINMQEPSCRCDAGYTGQHCE 301
Cdd:PHA02887   55 RNFESHISKFNYKENANAQNFKRKNSMFfeKCKNDFNDFCINGECMNIIDLDEKFCICNKGYTGIRCD 122
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
189-227 4.79e-06

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 43.03  E-value: 4.79e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720356375 189 TNFNPLCASDGKSYDNACQIKEASCQKQEKIEVMSLGRC 227
Cdd:cd00104     3 KEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
95-135 3.59e-04

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 38.03  E-value: 3.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720356375  95 CNSDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSC 135
Cdd:pfam00050   9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
91-135 3.72e-04

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 37.86  E-value: 3.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720356375  91 CQFKC-NSDYVPVCGSNGESYQNECYLRQAACKQQSEI---LVVSEGSC 135
Cdd:pfam07648   2 CNCQCpKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVkeeKVKYDGSC 50
PHA03099 PHA03099
epidermal growth factor-like protein (EGF-like protein); Provisional
247-301 9.71e-04

epidermal growth factor-like protein (EGF-like protein); Provisional


Pssm-ID: 165381  Cd Length: 139  Bit Score: 39.24  E-value: 9.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720356375 247 YAENANKLEESARE-----HHIP----CPEHYNGFCMHGKCEHSINMQEPSCRCDAGYTGQHCE 301
Cdd:PHA03099   18 FADSGNAIETTSPEitnatTDIPairlCGPEGDGYCLHGDCIHARDIDGMYCRCSHGYTGIRCQ 81
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
182-227 1.22e-03

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 36.70  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720356375 182 CNIDCSQTNFNPLCASDGKSYDNACQIKEASCQKQEKIE---VMSLGRC 227
Cdd:pfam07648   2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
 
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