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Conserved domains on  [gi|1720367883|ref|XP_030102271|]
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microfibril-associated glycoprotein 4 isoform X1 [Mus musculus]

Protein Classification

fibrinogen-related domain-containing protein (domain architecture ID 10053370)

fibrinogen-related domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
1-183 3.78e-96

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


:

Pssm-ID: 238040  Cd Length: 215  Bit Score: 277.58  E-value: 3.78e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883   1 MTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISP 80
Cdd:cd00087    37 MDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883  81 naisaEEDGYTLYVAGFEdGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSH-LSYA 159
Cdd:cd00087   117 -----ESEGYRLTLGGYS-GTAGDALSYHNGMKFSTFDRDNDGASGNCAESYSGGWWYNSCHASNLNGRYYSGGHrNEYD 190
                         170       180
                  ....*....|....*....|....
gi 1720367883 160 NGINWAQWKGFYYSLKRTEMKIRR 183
Cdd:cd00087   191 NGINWATWKGSTYSLKFTEMKIRP 214
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
1-183 3.78e-96

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040  Cd Length: 215  Bit Score: 277.58  E-value: 3.78e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883   1 MTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISP 80
Cdd:cd00087    37 MDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883  81 naisaEEDGYTLYVAGFEdGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSH-LSYA 159
Cdd:cd00087   117 -----ESEGYRLTLGGYS-GTAGDALSYHNGMKFSTFDRDNDGASGNCAESYSGGWWYNSCHASNLNGRYYSGGHrNEYD 190
                         170       180
                  ....*....|....*....|....
gi 1720367883 160 NGINWAQWKGFYYSLKRTEMKIRR 183
Cdd:cd00087   191 NGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
1-184 1.14e-90

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548  Cd Length: 212  Bit Score: 263.75  E-value: 1.14e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883    1 MTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISP 80
Cdd:smart00186  36 METDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIHLLTSQGKYELRIDLEDWEGNTAYALYDSFKVAD 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883   81 naisaEEDGYTLYVAGFEdGGAGD-SLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYlgGSHLSYA 159
Cdd:smart00186 116 -----EADGYRLHIGGYS-GTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEEYGGGWWYNNCHAANLNGRY--YPNNNYD 187
                          170       180
                   ....*....|....*....|....*
gi 1720367883  160 NGINWAQWKGFYYSLKRTEMKIRRA 184
Cdd:smart00186 188 NGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
1-182 4.20e-63

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095  Cd Length: 221  Bit Score: 193.89  E-value: 4.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883   1 MTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFG-RADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSIS 79
Cdd:pfam00147  36 METDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDKIHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883  80 pnaisAEEDGYTLYVAGF------EDGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGG 153
Cdd:pfam00147 116 -----NENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSPDGNCALSYGGGWWYNNCHAANLNGVYYYG 190
                         170       180
                  ....*....|....*....|....*....
gi 1720367883 154 SHLSYANGINWAQWKGFYYSLKRTEMKIR 182
Cdd:pfam00147 191 GTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
1-183 3.78e-96

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040  Cd Length: 215  Bit Score: 277.58  E-value: 3.78e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883   1 MTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISP 80
Cdd:cd00087    37 MDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883  81 naisaEEDGYTLYVAGFEdGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSH-LSYA 159
Cdd:cd00087   117 -----ESEGYRLTLGGYS-GTAGDALSYHNGMKFSTFDRDNDGASGNCAESYSGGWWYNSCHASNLNGRYYSGGHrNEYD 190
                         170       180
                  ....*....|....*....|....
gi 1720367883 160 NGINWAQWKGFYYSLKRTEMKIRR 183
Cdd:cd00087   191 NGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
1-184 1.14e-90

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548  Cd Length: 212  Bit Score: 263.75  E-value: 1.14e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883    1 MTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISP 80
Cdd:smart00186  36 METDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIHLLTSQGKYELRIDLEDWEGNTAYALYDSFKVAD 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883   81 naisaEEDGYTLYVAGFEdGGAGD-SLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYlgGSHLSYA 159
Cdd:smart00186 116 -----EADGYRLHIGGYS-GTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEEYGGGWWYNNCHAANLNGRY--YPNNNYD 187
                          170       180
                   ....*....|....*....|....*
gi 1720367883  160 NGINWAQWKGFYYSLKRTEMKIRRA 184
Cdd:smart00186 188 NGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
1-182 4.20e-63

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095  Cd Length: 221  Bit Score: 193.89  E-value: 4.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883   1 MTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFG-RADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSIS 79
Cdd:pfam00147  36 METDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDKIHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367883  80 pnaisAEEDGYTLYVAGF------EDGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGG 153
Cdd:pfam00147 116 -----NENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSPDGNCALSYGGGWWYNNCHAANLNGVYYYG 190
                         170       180
                  ....*....|....*....|....*....
gi 1720367883 154 SHLSYANGINWAQWKGFYYSLKRTEMKIR 182
Cdd:pfam00147 191 GTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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