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Conserved domains on  [gi|2217263034|ref|XP_047280386|]
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angiopoietin-related protein 7 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FReD super family cl00085
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 129-224 4.64e-50

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.


The actual alignment was detected with superfamily member smart00186:

Pssm-ID: 412152 [Multi-domain]  Cd Length: 212  Bit Score: 162.83  E-value: 4.64e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034  129 YDCSSLYQKNYRISGVYKLPPDDFlgSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEH 208
Cdd:smart00186   3 RDCSDVLQNGGKTSGLYTIYPDGS--SRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80

                           90
                   ....*....|....*..
gi 2217263034  209 IHRLSRQ-PTRLRVEME 224
Cdd:smart00186  81 IHLLTSQgKYELRIDLE 97
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 37-109 3.92e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 3.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217263034  37 QPQLKAANccEEVKELKAQVANLSSLLSELNKKQERDWVSVVMQvmELESNSKRM---ESRLTDAESKYSEMNNQI 109
Cdd:TIGR04523 273 QKELEQNN--KKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS--ELKNQEKKLeeiQNQISQNNKIISQLNEQI 344
 
Name Accession Description Interval E-value
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 129-224 4.64e-50

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 [Multi-domain]  Cd Length: 212  Bit Score: 162.83  E-value: 4.64e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034  129 YDCSSLYQKNYRISGVYKLPPDDFlgSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEH 208
Cdd:smart00186   3 RDCSDVLQNGGKTSGLYTIYPDGS--SRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80

                           90
                   ....*....|....*..
gi 2217263034  209 IHRLSRQ-PTRLRVEME 224
Cdd:smart00186  81 IHLLTSQgKYELRIDLE 97
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 129-224 8.77e-49

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 [Multi-domain]  Cd Length: 215  Bit Score: 159.71  E-value: 8.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034 129 YDCSSLYQKNYRISGVYKLPPDDFlgSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEH 208
Cdd:cd00087     4 RDCSEVLQRGGRTSGVYTIQPPGS--NEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEK 81

                          90
                  ....*....|....*..
gi 2217263034 209 IHRLSRQ-PTRLRVEME 224
Cdd:cd00087    82 IHLLTSQgPYELRIDLE 98
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
130-224 1.30e-36

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 128.79  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034 130 DCSSLYQKNYRISGVYKLPPDDFLGSpeLEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSI-RGDFWLGNEH 208
Cdd:pfam00147   4 DCSDVYNKGAKTSGLYTIRPDGATKP--FEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90
                  ....*....|....*..
gi 2217263034 209 IHRLSRQ-PTRLRVEME 224
Cdd:pfam00147  82 IHLLTKQgPYVLRIDLE 98
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 131-174 4.41e-10

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 53.72  E-value: 4.41e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217263034 131 CSSLYQKNYRI-SGVYKLPPDDFLGSPELEVFCDMETSGGGWTII 174
Cdd:NF040941    2 CWEILQAGPSApSGVYWIDPDGMGGLAPFQVYCDMTTDGGGWTLV 46
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 37-109 3.92e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 3.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217263034  37 QPQLKAANccEEVKELKAQVANLSSLLSELNKKQERDWVSVVMQvmELESNSKRM---ESRLTDAESKYSEMNNQI 109
Cdd:TIGR04523 273 QKELEQNN--KKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS--ELKNQEKKLeeiQNQISQNNKIISQLNEQI 344
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
26-130 1.03e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034  26 LQKLSKHKTPAQPQlkaancceeVKELKAQVANlssLLSELNKKQERDWVSVVMQVMELESNSKRMESRLTDAESKYSEM 105
Cdd:COG3206   279 LAELSARYTPNHPD---------VIALRAQIAA---LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346

                          90       100
                  ....*....|....*....|....*.
gi 2217263034 106 NN-QIDIMQLQAAQTVTQtsadAIYD 130
Cdd:COG3206   347 PElEAELRRLEREVEVAR----ELYE 368
 
Name Accession Description Interval E-value
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 129-224 4.64e-50

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 [Multi-domain]  Cd Length: 212  Bit Score: 162.83  E-value: 4.64e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034  129 YDCSSLYQKNYRISGVYKLPPDDFlgSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEH 208
Cdd:smart00186   3 RDCSDVLQNGGKTSGLYTIYPDGS--SRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80

                           90
                   ....*....|....*..
gi 2217263034  209 IHRLSRQ-PTRLRVEME 224
Cdd:smart00186  81 IHLLTSQgKYELRIDLE 97
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 129-224 8.77e-49

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 [Multi-domain]  Cd Length: 215  Bit Score: 159.71  E-value: 8.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034 129 YDCSSLYQKNYRISGVYKLPPDDFlgSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEH 208
Cdd:cd00087     4 RDCSEVLQRGGRTSGVYTIQPPGS--NEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEK 81

                          90
                  ....*....|....*..
gi 2217263034 209 IHRLSRQ-PTRLRVEME 224
Cdd:cd00087    82 IHLLTSQgPYELRIDLE 98
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
130-224 1.30e-36

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 128.79  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034 130 DCSSLYQKNYRISGVYKLPPDDFLGSpeLEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSI-RGDFWLGNEH 208
Cdd:pfam00147   4 DCSDVYNKGAKTSGLYTIRPDGATKP--FEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90
                  ....*....|....*..
gi 2217263034 209 IHRLSRQ-PTRLRVEME 224
Cdd:pfam00147  82 IHLLTKQgPYVLRIDLE 98
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 131-174 4.41e-10

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 53.72  E-value: 4.41e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217263034 131 CSSLYQKNYRI-SGVYKLPPDDFLGSPELEVFCDMETSGGGWTII 174
Cdd:NF040941    2 CWEILQAGPSApSGVYWIDPDGMGGLAPFQVYCDMTTDGGGWTLV 46
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 37-109 3.92e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 3.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217263034  37 QPQLKAANccEEVKELKAQVANLSSLLSELNKKQERDWVSVVMQvmELESNSKRM---ESRLTDAESKYSEMNNQI 109
Cdd:TIGR04523 273 QKELEQNN--KKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS--ELKNQEKKLeeiQNQISQNNKIISQLNEQI 344
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
26-130 1.03e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263034  26 LQKLSKHKTPAQPQlkaancceeVKELKAQVANlssLLSELNKKQERDWVSVVMQVMELESNSKRMESRLTDAESKYSEM 105
Cdd:COG3206   279 LAELSARYTPNHPD---------VIALRAQIAA---LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346

                          90       100
                  ....*....|....*....|....*.
gi 2217263034 106 NN-QIDIMQLQAAQTVTQtsadAIYD 130
Cdd:COG3206   347 PElEAELRRLEREVEVAR----ELYE 368
 
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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