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Conserved domains on  [gi|21313152|ref|NP_083844|]
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microfibril-associated glycoprotein 4 isoform 2 precursor [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 ...
38-256 7.55e-116

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: 330.74  E-value: 7.55e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152  38 QQPLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQ 117
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152 118 NLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISPnaisaEEDGYTLYVAGFEdGGAGDSLSYHSGQKFSTFDRDQDLF 197
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGS-----ESEGYRLTLGGYS-GTAGDALSYHNGMKFSTFDRDNDGA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152 198 VQNCAALSSGAFWFRSCHFANLNGFYLGGSH-LSYANGINWAQWKGFYYSLKRTEMKIRR 256
Cdd:cd00087 155 SGNCAESYSGGWWYNSCHASNLNGRYYSGGHrNEYDNGINWATWKGSTYSLKFTEMKIRP 214
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
38-256 7.55e-116

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: 330.74  E-value: 7.55e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152  38 QQPLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQ 117
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152 118 NLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISPnaisaEEDGYTLYVAGFEdGGAGDSLSYHSGQKFSTFDRDQDLF 197
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGS-----ESEGYRLTLGGYS-GTAGDALSYHNGMKFSTFDRDNDGA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152 198 VQNCAALSSGAFWFRSCHFANLNGFYLGGSH-LSYANGINWAQWKGFYYSLKRTEMKIRR 256
Cdd:cd00087 155 SGNCAESYSGGWWYNSCHASNLNGRYYSGGHrNEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
39-257 3.17e-111

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: 318.84  E-value: 3.17e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152     39 QPLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQN 118
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152    119 LHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISPnaisaEEDGYTLYVAGFEdGGAGD-SLSYHSGQKFSTFDRDQDLF 197
Cdd:smart00186  81 IHLLTSQGKYELRIDLEDWEGNTAYALYDSFKVAD-----EADGYRLHIGGYS-GTAGDaSLTYHNGMQFSTYDRDNDKY 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152    198 VQNCAALSSGAFWFRSCHFANLNGFYlgGSHLSYANGINWAQWKGFYYSLKRTEMKIRRA 257
Cdd:smart00186 155 SGNCAEEYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
40-255 2.23e-77

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


Pssm-ID: 395095  Cd Length: 221  Bit Score: 233.18  E-value: 2.23e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152    40 PLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFG-RADGEYWLGLQN 118
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152   119 LHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISpnaisAEEDGYTLYVAGF------EDGGAGDSLSYHSGQKFSTFDR 192
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVT-----NENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21313152   193 DQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSHLSYANGINWAQWKGFYYSLKRTEMKIR 255
Cdd:pfam00147 157 DNDSPDGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
38-256 7.55e-116

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: 330.74  E-value: 7.55e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152  38 QQPLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQ 117
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152 118 NLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISPnaisaEEDGYTLYVAGFEdGGAGDSLSYHSGQKFSTFDRDQDLF 197
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGS-----ESEGYRLTLGGYS-GTAGDALSYHNGMKFSTFDRDNDGA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152 198 VQNCAALSSGAFWFRSCHFANLNGFYLGGSH-LSYANGINWAQWKGFYYSLKRTEMKIRR 256
Cdd:cd00087 155 SGNCAESYSGGWWYNSCHASNLNGRYYSGGHrNEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
39-257 3.17e-111

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: 318.84  E-value: 3.17e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152     39 QPLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQN 118
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152    119 LHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISPnaisaEEDGYTLYVAGFEdGGAGD-SLSYHSGQKFSTFDRDQDLF 197
Cdd:smart00186  81 IHLLTSQGKYELRIDLEDWEGNTAYALYDSFKVAD-----EADGYRLHIGGYS-GTAGDaSLTYHNGMQFSTYDRDNDKY 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152    198 VQNCAALSSGAFWFRSCHFANLNGFYlgGSHLSYANGINWAQWKGFYYSLKRTEMKIRRA 257
Cdd:smart00186 155 SGNCAEEYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
40-255 2.23e-77

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


Pssm-ID: 395095  Cd Length: 221  Bit Score: 233.18  E-value: 2.23e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152    40 PLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFG-RADGEYWLGLQN 118
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313152   119 LHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISpnaisAEEDGYTLYVAGF------EDGGAGDSLSYHSGQKFSTFDR 192
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVT-----NENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21313152   193 DQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSHLSYANGINWAQWKGFYYSLKRTEMKIR 255
Cdd:pfam00147 157 DNDSPDGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 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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