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Conserved domains on  [gi|1720354692|ref|XP_030108828|]
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transforming growth factor beta-2 proprotein isoform X2 [Mus musculus]

Protein Classification

TGFb_propeptide domain-containing protein( domain architecture ID 10464559)

TGFb_propeptide domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TGFb_propeptide pfam00688
TGF-beta propeptide; This propeptide is known as latency associated peptide (LAP) in TGF-beta. ...
21-228 1.47e-44

TGF-beta propeptide; This propeptide is known as latency associated peptide (LAP) in TGF-beta. LAP is a homodimer which is disulfide linked to TGF-beta binding protein.


:

Pssm-ID: 459906  Cd Length: 239  Bit Score: 152.48  E-value: 1.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692  21 LSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPDEVPPE-VISIYNSTRDLLQEK----------ASRRAAAC 89
Cdd:pfam00688   1 NGTCQTVDHRRLKSKEKREIEHEILSLLGLPHRPRPSSGKHKSAPQfMLDLYNSTSGEEEEKerqsrlstrsEPLLTLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692  90 ERERSDEEYYAKEVYKIDMP--SHLPSENAIpptfyrpYFRivrFDVSTMEKNASnLVKAEFRVFRLQNPKARVA-EQRI 166
Cdd:pfam00688  81 SRAIDEADTVMSFVNKVENHhvPDLRHEEGK-------RFW---FNLSEIPEGEL-VTSAELRLYKDKVKARTSNeTFRI 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354692 167 ELYQILKSKDLTSPTQRYIDSKVVKTRAEGeWLSFDVTDAVQEWLHHKDRNLGFKISLHCPC 228
Cdd:pfam00688 150 EVYQVLKEHDGGDASLRLLDSRLVTASEEG-WLSFDVTEALNRWLANPEENLGLQLSVHCSC 210
 
Name Accession Description Interval E-value
TGFb_propeptide pfam00688
TGF-beta propeptide; This propeptide is known as latency associated peptide (LAP) in TGF-beta. ...
21-228 1.47e-44

TGF-beta propeptide; This propeptide is known as latency associated peptide (LAP) in TGF-beta. LAP is a homodimer which is disulfide linked to TGF-beta binding protein.


Pssm-ID: 459906  Cd Length: 239  Bit Score: 152.48  E-value: 1.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692  21 LSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPDEVPPE-VISIYNSTRDLLQEK----------ASRRAAAC 89
Cdd:pfam00688   1 NGTCQTVDHRRLKSKEKREIEHEILSLLGLPHRPRPSSGKHKSAPQfMLDLYNSTSGEEEEKerqsrlstrsEPLLTLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692  90 ERERSDEEYYAKEVYKIDMP--SHLPSENAIpptfyrpYFRivrFDVSTMEKNASnLVKAEFRVFRLQNPKARVA-EQRI 166
Cdd:pfam00688  81 SRAIDEADTVMSFVNKVENHhvPDLRHEEGK-------RFW---FNLSEIPEGEL-VTSAELRLYKDKVKARTSNeTFRI 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354692 167 ELYQILKSKDLTSPTQRYIDSKVVKTRAEGeWLSFDVTDAVQEWLHHKDRNLGFKISLHCPC 228
Cdd:pfam00688 150 EVYQVLKEHDGGDASLRLLDSRLVTASEEG-WLSFDVTEALNRWLANPEENLGLQLSVHCSC 210
DNRLRE_dom NF033679
DNRLRE domain; The DNRLRE domain, with a length of about 160 amino acids, appears typically in ...
129-222 1.08e-07

DNRLRE domain; The DNRLRE domain, with a length of about 160 amino acids, appears typically in large, repetitive surface proteins of bacteria and archaea, sometimes repeated several times. It occurs, notably, three times in the C-terminal region of the enzyme disaggregatase from the archaeal species Methanosarcina mazei, each time with the motif DNRLRE, for which the domain is named. Archaeal proteins within this family are described particularly well by the currently more narrowly defined Pfam model, PF06848. Note that the catalytic region of disaggregatase, in the N-terminal portion of the protein, is modeled by a different HMM, PF08480.


Pssm-ID: 468137 [Multi-domain]  Cd Length: 164  Bit Score: 50.84  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692 129 IVRFDVSTMEKNASnLVKAEFRVF--RLQNPKARVAEQRIELYQIL----------KSKDLTSPTQRYIDSKVVKTraeG 196
Cdd:NF033679   34 YLKFDLSSLPAGAT-ITSATLRLYvyYSYSTDSGTSPTTVEVYRVTsdwsestvtwNNAPAAAYASITITVSSVPD---G 109
                          90       100
                  ....*....|....*....|....*.
gi 1720354692 197 EWLSFDVTDAVQEWLHHKDRNLGFKI 222
Cdd:NF033679  110 GWVEIDVTDLVQAWVSGTYPNYGFLL 135
 
Name Accession Description Interval E-value
TGFb_propeptide pfam00688
TGF-beta propeptide; This propeptide is known as latency associated peptide (LAP) in TGF-beta. ...
21-228 1.47e-44

TGF-beta propeptide; This propeptide is known as latency associated peptide (LAP) in TGF-beta. LAP is a homodimer which is disulfide linked to TGF-beta binding protein.


Pssm-ID: 459906  Cd Length: 239  Bit Score: 152.48  E-value: 1.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692  21 LSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPDEVPPE-VISIYNSTRDLLQEK----------ASRRAAAC 89
Cdd:pfam00688   1 NGTCQTVDHRRLKSKEKREIEHEILSLLGLPHRPRPSSGKHKSAPQfMLDLYNSTSGEEEEKerqsrlstrsEPLLTLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692  90 ERERSDEEYYAKEVYKIDMP--SHLPSENAIpptfyrpYFRivrFDVSTMEKNASnLVKAEFRVFRLQNPKARVA-EQRI 166
Cdd:pfam00688  81 SRAIDEADTVMSFVNKVENHhvPDLRHEEGK-------RFW---FNLSEIPEGEL-VTSAELRLYKDKVKARTSNeTFRI 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354692 167 ELYQILKSKDLTSPTQRYIDSKVVKTRAEGeWLSFDVTDAVQEWLHHKDRNLGFKISLHCPC 228
Cdd:pfam00688 150 EVYQVLKEHDGGDASLRLLDSRLVTASEEG-WLSFDVTEALNRWLANPEENLGLQLSVHCSC 210
DNRLRE_dom NF033679
DNRLRE domain; The DNRLRE domain, with a length of about 160 amino acids, appears typically in ...
129-222 1.08e-07

DNRLRE domain; The DNRLRE domain, with a length of about 160 amino acids, appears typically in large, repetitive surface proteins of bacteria and archaea, sometimes repeated several times. It occurs, notably, three times in the C-terminal region of the enzyme disaggregatase from the archaeal species Methanosarcina mazei, each time with the motif DNRLRE, for which the domain is named. Archaeal proteins within this family are described particularly well by the currently more narrowly defined Pfam model, PF06848. Note that the catalytic region of disaggregatase, in the N-terminal portion of the protein, is modeled by a different HMM, PF08480.


Pssm-ID: 468137 [Multi-domain]  Cd Length: 164  Bit Score: 50.84  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354692 129 IVRFDVSTMEKNASnLVKAEFRVF--RLQNPKARVAEQRIELYQIL----------KSKDLTSPTQRYIDSKVVKTraeG 196
Cdd:NF033679   34 YLKFDLSSLPAGAT-ITSATLRLYvyYSYSTDSGTSPTTVEVYRVTsdwsestvtwNNAPAAAYASITITVSSVPD---G 109
                          90       100
                  ....*....|....*....|....*.
gi 1720354692 197 EWLSFDVTDAVQEWLHHKDRNLGFKI 222
Cdd:NF033679  110 GWVEIDVTDLVQAWVSGTYPNYGFLL 135
 
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.
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