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Conserved domains on  [gi|514388117|ref|NP_001265500|]
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ciliary neurotrophic factor receptor subunit alpha precursor [Bos taurus]

Protein Classification

Ig and FN3 domain-containing protein( domain architecture ID 10307510)

Ig and FN3 domain-containing protein similar to Homo sapiens contactins, which are comprised of six immunoglobulin (Ig)-like domains followed by four fibronectin type III (Fn3) domains anchored to the membrane by glycosylphosphatidylinositol, and to Robo (roundabout) receptors which typically contain five Ig-like domains and three FN3 domains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 204-300 3.09e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117 204 PDPPENVVARPVpsNPRRLEVTWQTPstwPDPESFPLKFFLRYRPLILDQWQHVE--LSDGTAHTITDAYAGKEYIIQVA 281
Cdd:cd00063    1 PSPPTNLRVTDV--TSTSVTLSWTPP---EDDGGPITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTEYEFRVR 75

                         90
                 ....*....|....*....
gi 514388117 282 AKDNeiGTWSDWSVAAHAT 300
Cdd:cd00063   76 AVNG--GGESPPSESVTVT 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 39-89 7.08e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd04979:

Pssm-ID: 472250  Cd Length: 88  Bit Score: 38.21  E-value: 7.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514388117  39 GSDVTLPCGTASWDAAVTWRVNGTDL----APDLLNGSQ--LVLRSLELGHGGLYAC 89
Cdd:cd04979   11 GDTVILSCSVKSNNAPVTWIHNGKKVpryrSPRLVLKTErgLLIRSAQEADAGVYEC 67
 
Name Accession Description Interval E-value
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 204-300 3.09e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117 204 PDPPENVVARPVpsNPRRLEVTWQTPstwPDPESFPLKFFLRYRPLILDQWQHVE--LSDGTAHTITDAYAGKEYIIQVA 281
Cdd:cd00063    1 PSPPTNLRVTDV--TSTSVTLSWTPP---EDDGGPITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTEYEFRVR 75

                         90
                 ....*....|....*....
gi 514388117 282 AKDNeiGTWSDWSVAAHAT 300
Cdd:cd00063   76 AVNG--GGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
205-291 1.55e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117  205 DPPENVVARPVpsNPRRLEVTWQTPSTWPDPesfPLKFFLRYRPLI-LDQWQHVELSDGTA-HTITDAYAGKEYIIQVAA 282
Cdd:pfam00041   1 SAPSNLTVTDV--TSTSLTVSWTPPPDGNGP---ITGYEVEYRPKNsGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQA 75

                          90
                  ....*....|
gi 514388117  283 -KDNEIGTWS 291
Cdd:pfam00041  76 vNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 204-288 6.11e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.14  E-value: 6.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117   204 PDPPENVVARPVpsNPRRLEVTWQTPSTwPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAK 283
Cdd:smart00060   1 PSPPSNLRVTDV--TSTSVTLSWEPPPD-DGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 514388117   284 dNEIG 288
Cdd:smart00060  78 -NGAG 81
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
176-306 1.97e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.45  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117 176 KYKVSISVSNALGHNATAITFDEFTI-VKPDPPENVVArpVPSNPRRLEVTWqTPSTWPDPESFPLkfflrYR-PLILDQ 253
Cdd:COG3401  204 TYYYRVAATDTGGESAPSNEVSVTTPtTPPSAPTGLTA--TADTPGSVTLSW-DPVTESDATGYRV-----YRsNSGDGP 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 514388117 254 WQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEiGTWSDWSVAAHATPWTEEP 306
Cdd:COG3401  276 FTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAA-GNESAPSNVVSVTTDLTPP 327
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 39-89 7.08e-04

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 38.21  E-value: 7.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514388117  39 GSDVTLPCGTASWDAAVTWRVNGTDL----APDLLNGSQ--LVLRSLELGHGGLYAC 89
Cdd:cd04979   11 GDTVILSCSVKSNNAPVTWIHNGKKVpryrSPRLVLKTErgLLIRSAQEADAGVYEC 67
 
Name Accession Description Interval E-value
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 204-300 3.09e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117 204 PDPPENVVARPVpsNPRRLEVTWQTPstwPDPESFPLKFFLRYRPLILDQWQHVE--LSDGTAHTITDAYAGKEYIIQVA 281
Cdd:cd00063    1 PSPPTNLRVTDV--TSTSVTLSWTPP---EDDGGPITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTEYEFRVR 75

                         90
                 ....*....|....*....
gi 514388117 282 AKDNeiGTWSDWSVAAHAT 300
Cdd:cd00063   76 AVNG--GGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
205-291 1.55e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117  205 DPPENVVARPVpsNPRRLEVTWQTPSTWPDPesfPLKFFLRYRPLI-LDQWQHVELSDGTA-HTITDAYAGKEYIIQVAA 282
Cdd:pfam00041   1 SAPSNLTVTDV--TSTSLTVSWTPPPDGNGP---ITGYEVEYRPKNsGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQA 75

                          90
                  ....*....|
gi 514388117  283 -KDNEIGTWS 291
Cdd:pfam00041  76 vNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 204-288 6.11e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.14  E-value: 6.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117   204 PDPPENVVARPVpsNPRRLEVTWQTPSTwPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAK 283
Cdd:smart00060   1 PSPPSNLRVTDV--TSTSVTLSWEPPPD-DGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                   ....*
gi 514388117   284 dNEIG 288
Cdd:smart00060  78 -NGAG 81
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
176-306 1.97e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.45  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117 176 KYKVSISVSNALGHNATAITFDEFTI-VKPDPPENVVArpVPSNPRRLEVTWqTPSTWPDPESFPLkfflrYR-PLILDQ 253
Cdd:COG3401  204 TYYYRVAATDTGGESAPSNEVSVTTPtTPPSAPTGLTA--TADTPGSVTLSW-DPVTESDATGYRV-----YRsNSGDGP 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 514388117 254 WQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEiGTWSDWSVAAHATPWTEEP 306
Cdd:COG3401  276 FTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAA-GNESAPSNVVSVTTDLTPP 327
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
201-303 2.90e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 42.68  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388117 201 IVKPDPPENVVArpVPSNPRRLEVTWQTPStwpdpeSFPLKFFLRYR-PLILDQWQHV-ELSDGTAHTITDAYAGKEYII 278
Cdd:COG3401  324 LTPPAAPSGLTA--TAVGSSSITLSWTASS------DADVTGYNVYRsTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYY 395

                         90       100
                 ....*....|....*....|....*
gi 514388117 279 QVAAKDnEIGTWSDWSVAAHATPWT 303
Cdd:COG3401  396 KVTAVD-AAGNESAPSEEVSATTAS 419
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 39-89 7.08e-04

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 38.21  E-value: 7.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514388117  39 GSDVTLPCGTASWDAAVTWRVNGTDL----APDLLNGSQ--LVLRSLELGHGGLYAC 89
Cdd:cd04979   11 GDTVILSCSVKSNNAPVTWIHNGKKVpryrSPRLVLKTErgLLIRSAQEADAGVYEC 67
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 30-89 2.83e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 36.86  E-value: 2.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514388117  30 TPHVQYERLGSDVTLPCGTASW-DAAVTWRVNGTDLAPDL-------LNGSQLVLRSLELGHGGLYAC 89
Cdd:cd05736    6 YPEFQAKEPGVEASLRCHAEGIpLPRVQWLKNGMDINPKLskqltliANGSELHISNVRYEDTGAYTC 73
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
 38-90 7.26e-03

Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are composed of the immunoglobulin (Ig)-like domain of Sema4B and similar proteins. Sema4B is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4B has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4B has been shown to preferentially regulate the development of the postsynaptic specialization at the glutamatergic synapses. This cytoplasmic domain includes a PDZ-binding motif upon which the synaptic localization of Sem4B is dependent. Sema4B is a ligand of CLCP1. CLCP1 was identified in an expression profiling analysis, which compared a highly metastic lung cancer subline with its low metastic parental line. Sema4B was shown to promote CLCP1 endocytosis and their interaction is a potential target for therapeutic intervention of metastasis.


Pssm-ID: 409456  Cd Length: 86  Bit Score: 35.49  E-value: 7.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514388117  38 LGSDVTLPCGTASWDAAVTWRVNGTDLAPD----LLNGSQLVLRSLELGHGGLYACF 90
Cdd:cd05872   10 AGADVVLPCQLRSNLASPVWLFNGTPLNAQfsylRLGTDGLLILVTSPEHSGTYRCY 66
 
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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