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Conserved domains on  [gi|157821459|ref|NP_001101178|]
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olfactomedin-like protein 3 precursor [Rattus norvegicus]

Protein Classification

olfactomedin domain-containing protein( domain architecture ID 10490292)

olfactomedin domain-containing protein adopts a five-bladed beta-propeller structure, similar to gliomedin that interacts with neuronal cell adhesion molecules such as neurofascin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
151-407 2.38e-105

Olfactomedin-like domain;


:

Pssm-ID: 460482  Cd Length: 246  Bit Score: 311.39  E-value: 2.38e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  151 ISQVRSMKILKRFGGSAGLWTKDPLGPAEKIYVLD-GTQNDTAFVFPRLRDFTLtmaARKASRIRVPFPWVGTGQLVYGG 229
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDrGTSGNTLREYASLDDFKN---GSPSKKYKLPYPWQGTGHVVYNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  230 FLYYARrppggaggggelENTLQLIKFHLANRTVVDSSVFPAERL--IPPYGLTVDTYIDLAADEEGLWAVYATREDDRH 307
Cdd:pfam02191  78 SLYYNK------------YNSRNIVKYDLTTRTVAARRVLPGAGYnnRFPYSWGGHTDIDLAVDENGLWVIYATEENEGN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  308 LCLAKLDPQTLDTEQQWDTPCPRENAEAAFVICGTLYVVYNtRPASRARIQCSFDasgTLT-PERAALSYFPRRYGAHAS 386
Cdd:pfam02191 146 IVVSKLDPETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRS-VNTRREEIFYAFD---TYTgKEEAVSIPFPNRYGKISM 221
                         250       260
                  ....*....|....*....|.
gi 157821459  387 LRYNPRERQLYAWDDGYQIVY 407
Cdd:pfam02191 222 LDYNPRDKKLYAWDDGYQVTY 242
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
43-112 1.14e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821459   43 ERRLAALEERLAQCQDQSSRHAAELRDFKNKmlplLEVAEKERETLRTEADSISG-RVDRLEREVDYLETQ 112
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEAR----LDALREELDELEAQIRGNGGdRLEQLEREIERLERE 353
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
151-407 2.38e-105

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 311.39  E-value: 2.38e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  151 ISQVRSMKILKRFGGSAGLWTKDPLGPAEKIYVLD-GTQNDTAFVFPRLRDFTLtmaARKASRIRVPFPWVGTGQLVYGG 229
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDrGTSGNTLREYASLDDFKN---GSPSKKYKLPYPWQGTGHVVYNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  230 FLYYARrppggaggggelENTLQLIKFHLANRTVVDSSVFPAERL--IPPYGLTVDTYIDLAADEEGLWAVYATREDDRH 307
Cdd:pfam02191  78 SLYYNK------------YNSRNIVKYDLTTRTVAARRVLPGAGYnnRFPYSWGGHTDIDLAVDENGLWVIYATEENEGN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  308 LCLAKLDPQTLDTEQQWDTPCPRENAEAAFVICGTLYVVYNtRPASRARIQCSFDasgTLT-PERAALSYFPRRYGAHAS 386
Cdd:pfam02191 146 IVVSKLDPETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRS-VNTRREEIFYAFD---TYTgKEEAVSIPFPNRYGKISM 221
                         250       260
                  ....*....|....*....|.
gi 157821459  387 LRYNPRERQLYAWDDGYQIVY 407
Cdd:pfam02191 222 LDYNPRDKKLYAWDDGYQVTY 242
OLF smart00284
Olfactomedin-like domains;
165-407 3.90e-47

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 162.31  E-value: 3.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459   165 GSAGLWTKDPLGPA---EKIYVLD--GTQNDTAFVFPRLRDFtltMAARKASRIRVPFPWVGTGQLVYGGFLYYARrppg 239
Cdd:smart00284  18 GKSGAWMKDPLWNTtkkSLYWYMPlnTRVLRSVREYSSMSDF---QMGKNPTDHPLPHAGQGTGVVVYNGSLYFNK---- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459   240 gaggggelENTLQLIKFHLANRTVVdssvfpAERLIP--------PYGLTVDTYIDLAADEEGLWAVYATREDDRHLCLA 311
Cdd:smart00284  91 --------FNSHDICRFDLTTETYQ------KEPLLNgagynnrfPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVIS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459   312 KLDPQTLDTEQQWDTPCPRENAEAAFVICGTLYVVyNTRPASRARIQCSFDasgTLTPERAALSY-FPRRYGAHASLRYN 390
Cdd:smart00284 157 KLNPATLTIENTWITTYNKRSASNAFMICGILYVT-RSLGSKGEKVFYAYD---TNTGKEGHLDIpFENMYEYISMLDYN 232
                          250
                   ....*....|....*..
gi 157821459   391 PRERQLYAWDDGYQIVY 407
Cdd:smart00284 233 PNDRKLYAWNNGHLVHY 249
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
43-112 1.14e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821459   43 ERRLAALEERLAQCQDQSSRHAAELRDFKNKmlplLEVAEKERETLRTEADSISG-RVDRLEREVDYLETQ 112
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEAR----LDALREELDELEAQIRGNGGdRLEQLEREIERLERE 353
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
40-110 1.64e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 1.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821459   40 EYMERRLAALEERLAQCQDQSSRHAAELRDFKNKMLPLlevaEKERETLRTEADSISGRVDRLEREVDYLE 110
Cdd:pfam20492   2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAEEL----EEERRQAEEEAERLEQKRQEAEEEKERLE 68
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
151-407 2.38e-105

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 311.39  E-value: 2.38e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  151 ISQVRSMKILKRFGGSAGLWTKDPLGPAEKIYVLD-GTQNDTAFVFPRLRDFTLtmaARKASRIRVPFPWVGTGQLVYGG 229
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDrGTSGNTLREYASLDDFKN---GSPSKKYKLPYPWQGTGHVVYNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  230 FLYYARrppggaggggelENTLQLIKFHLANRTVVDSSVFPAERL--IPPYGLTVDTYIDLAADEEGLWAVYATREDDRH 307
Cdd:pfam02191  78 SLYYNK------------YNSRNIVKYDLTTRTVAARRVLPGAGYnnRFPYSWGGHTDIDLAVDENGLWVIYATEENEGN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459  308 LCLAKLDPQTLDTEQQWDTPCPRENAEAAFVICGTLYVVYNtRPASRARIQCSFDasgTLT-PERAALSYFPRRYGAHAS 386
Cdd:pfam02191 146 IVVSKLDPETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRS-VNTRREEIFYAFD---TYTgKEEAVSIPFPNRYGKISM 221
                         250       260
                  ....*....|....*....|.
gi 157821459  387 LRYNPRERQLYAWDDGYQIVY 407
Cdd:pfam02191 222 LDYNPRDKKLYAWDDGYQVTY 242
OLF smart00284
Olfactomedin-like domains;
165-407 3.90e-47

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 162.31  E-value: 3.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459   165 GSAGLWTKDPLGPA---EKIYVLD--GTQNDTAFVFPRLRDFtltMAARKASRIRVPFPWVGTGQLVYGGFLYYARrppg 239
Cdd:smart00284  18 GKSGAWMKDPLWNTtkkSLYWYMPlnTRVLRSVREYSSMSDF---QMGKNPTDHPLPHAGQGTGVVVYNGSLYFNK---- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459   240 gaggggelENTLQLIKFHLANRTVVdssvfpAERLIP--------PYGLTVDTYIDLAADEEGLWAVYATREDDRHLCLA 311
Cdd:smart00284  91 --------FNSHDICRFDLTTETYQ------KEPLLNgagynnrfPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVIS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821459   312 KLDPQTLDTEQQWDTPCPRENAEAAFVICGTLYVVyNTRPASRARIQCSFDasgTLTPERAALSY-FPRRYGAHASLRYN 390
Cdd:smart00284 157 KLNPATLTIENTWITTYNKRSASNAFMICGILYVT-RSLGSKGEKVFYAYD---TNTGKEGHLDIpFENMYEYISMLDYN 232
                          250
                   ....*....|....*..
gi 157821459   391 PRERQLYAWDDGYQIVY 407
Cdd:smart00284 233 PNDRKLYAWNNGHLVHY 249
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
43-112 1.14e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821459   43 ERRLAALEERLAQCQDQSSRHAAELRDFKNKmlplLEVAEKERETLRTEADSISG-RVDRLEREVDYLETQ 112
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEAR----LDALREELDELEAQIRGNGGdRLEQLEREIERLERE 353
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
40-110 1.64e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 1.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821459   40 EYMERRLAALEERLAQCQDQSSRHAAELRDFKNKMLPLlevaEKERETLRTEADSISGRVDRLEREVDYLE 110
Cdd:pfam20492   2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAEEL----EEERRQAEEEAERLEQKRQEAEEEKERLE 68
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
43-105 2.92e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 38.37  E-value: 2.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157821459   43 ERRLAALEERLAQCQDQSSRHAAELRDfKNKmlpLLEVAEKERETLRTEADSISGRVDRLERE 105
Cdd:pfam08614  98 ERRLAALEAERAQLEEKLKDREEELRE-KRK---LNQDLQDELVALQLQLNMAEEKLRKLEKE 156
 
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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