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Conserved domains on  [gi|4757752|ref|NP_004664|]
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angiopoietin-related protein 1 precursor [Homo sapiens]

Protein Classification

PB1 and FReD domain-containing protein( domain architecture ID 10251294)

PB1 and FReD 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 ...
 275-490 6.72e-119

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: 347.69  E-value: 6.72e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752  275 GPFKDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNIDGEYWLGLE 354
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752  355 NIYMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGDSMMWHNGKQFTTLDRDKDMYAGNCAH 434
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4757752  435 FHKGGWWYNACAHSNLNGVWYRGGHyRSKHQDGIFWAEYRGGSYSLRAVQMMIKPI 490
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
PB1 super family cl02720
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 74-138 8.86e-03

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


The actual alignment was detected with superfamily member cd06399:

Pssm-ID: 413452  Cd Length: 92  Bit Score: 35.62  E-value: 8.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757752   74 STIKDMITRMDLEN---LKDVLSRQKREIDVLQLVV---DVDGNIV-----NEVKLLRKESRNMNSRVTQLYMQLL 138
Cdd:cd06399  13 STIRDIAVEEDLSStplLKDLLELTRREFQREDIALnyrDAEGDLIrllsdEDVALMVRQSRGLPSQKRLFPWKLH 88
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 275-490 6.72e-119

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: 347.69  E-value: 6.72e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752  275 GPFKDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNIDGEYWLGLE 354
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752  355 NIYMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGDSMMWHNGKQFTTLDRDKDMYAGNCAH 434
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4757752  435 FHKGGWWYNACAHSNLNGVWYRGGHyRSKHQDGIFWAEYRGGSYSLRAVQMMIKPI 490
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 277-490 1.18e-96

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: 290.72  E-value: 1.18e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752     277 FKDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNIDGEYWLGLENI 356
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752     357 YMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGD-SMMWHNGKQFTTLDRDKDMYAGNCAHF 435
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4757752     436 HKGGWWYNACAHSNLNGVWYRggHYRskHQDGIFWAEYRGGSYSLRAVQMMIKPI 490
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRYYP--NNN--YDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
278-489 5.48e-80

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 248.21  E-value: 5.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752    278 KDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNI-DGEYWLGLENI 356
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752    357 YMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGD-------SMMWHNGKQFTTLDRDKDMYA 429
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDaldtagrSMTYHNGMQFSTWDRDNDSPD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752    430 GNCAHFHKGGWWYNACAHSNLNGVWYRGGHYrsKHQDGIFWAEYRGGSYSLRAVQMMIKP 489
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYYGGTY--SKQNGIIWATWKGRWYSMKKAEMKIRP 220
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 280-321 2.01e-06

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: 44.48  E-value: 2.01e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 4757752   280 CQQAKEAGHS-VSGIYMIKPENSNG--PMQLWCENSLDPGGWTVI 321
Cdd:NF040941   2 CWEILQAGPSaPSGVYWIDPDGMGGlaPFQVYCDMTTDGGGWTLV 46
PB1_P40 cd06399
The PB1 domain is essential part of the p40 adaptor protein which plays an important role in ...
 74-138 8.86e-03

The PB1 domain is essential part of the p40 adaptor protein which plays an important role in activating phagocyte NADPH oxidase during phagocytosis. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes , such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The PB1 domain of p40 represents a type I PB1 domain which interacts with the PB1 domain of oxidase activator p67 which belong to type II PB1 domain. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99721  Cd Length: 92  Bit Score: 35.62  E-value: 8.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757752   74 STIKDMITRMDLEN---LKDVLSRQKREIDVLQLVV---DVDGNIV-----NEVKLLRKESRNMNSRVTQLYMQLL 138
Cdd:cd06399  13 STIRDIAVEEDLSStplLKDLLELTRREFQREDIALnyrDAEGDLIrllsdEDVALMVRQSRGLPSQKRLFPWKLH 88
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 275-490 6.72e-119

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: 347.69  E-value: 6.72e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752  275 GPFKDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNIDGEYWLGLE 354
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752  355 NIYMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGDSMMWHNGKQFTTLDRDKDMYAGNCAH 434
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4757752  435 FHKGGWWYNACAHSNLNGVWYRGGHyRSKHQDGIFWAEYRGGSYSLRAVQMMIKPI 490
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 277-490 1.18e-96

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: 290.72  E-value: 1.18e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752     277 FKDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNIDGEYWLGLENI 356
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752     357 YMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGD-SMMWHNGKQFTTLDRDKDMYAGNCAHF 435
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4757752     436 HKGGWWYNACAHSNLNGVWYRggHYRskHQDGIFWAEYRGGSYSLRAVQMMIKPI 490
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRYYP--NNN--YDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
278-489 5.48e-80

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 248.21  E-value: 5.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752    278 KDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNI-DGEYWLGLENI 356
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752    357 YMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGD-------SMMWHNGKQFTTLDRDKDMYA 429
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDaldtagrSMTYHNGMQFSTWDRDNDSPD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757752    430 GNCAHFHKGGWWYNACAHSNLNGVWYRGGHYrsKHQDGIFWAEYRGGSYSLRAVQMMIKP 489
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYYGGTY--SKQNGIIWATWKGRWYSMKKAEMKIRP 220
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 280-321 2.01e-06

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: 44.48  E-value: 2.01e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 4757752   280 CQQAKEAGHS-VSGIYMIKPENSNG--PMQLWCENSLDPGGWTVI 321
Cdd:NF040941   2 CWEILQAGPSaPSGVYWIDPDGMGGlaPFQVYCDMTTDGGGWTLV 46
PB1_P40 cd06399
The PB1 domain is essential part of the p40 adaptor protein which plays an important role in ...
 74-138 8.86e-03

The PB1 domain is essential part of the p40 adaptor protein which plays an important role in activating phagocyte NADPH oxidase during phagocytosis. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes , such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The PB1 domain of p40 represents a type I PB1 domain which interacts with the PB1 domain of oxidase activator p67 which belong to type II PB1 domain. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99721  Cd Length: 92  Bit Score: 35.62  E-value: 8.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757752   74 STIKDMITRMDLEN---LKDVLSRQKREIDVLQLVV---DVDGNIV-----NEVKLLRKESRNMNSRVTQLYMQLL 138
Cdd:cd06399  13 STIRDIAVEEDLSStplLKDLLELTRREFQREDIALnyrDAEGDLIrllsdEDVALMVRQSRGLPSQKRLFPWKLH 88
 
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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