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Conserved domains on  [gi|1034671501|ref|XP_016870674|]
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FSD1-like protein isoform X8 [Homo sapiens]

Protein Classification

FN3 and SPRY domain-containing protein( domain architecture ID 13228455)

protein containing domains CC_brat-like, FN3, and SPRY

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY super family cl02614
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 315-357 2.08e-17

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


The actual alignment was detected with superfamily member cd12901:

Pssm-ID: 470632  Cd Length: 207  Bit Score: 79.87  E-value: 2.08e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034671501 315 FNLDNSSSHLNLKVEDTCVEWDPTGGKGQEsKIKGKENKGRYG 357
Cdd:cd12901     1 FKLDASSSHQNLKVEDLSVEWDATGGKVLQ-KIKGRENDGRSR 42
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 210-310 1.01e-12

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: 63.28  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501 210 PKAPEIDPVEclvaDNSVTVAWRMPEEDN-KIDHFILEHRKTNFDGlprvkdercWEIIDN--IKGTEYTLSGLKFDSKY 286
Cdd:cd00063     4 PTNLRVTDVT----STSVTLSWTPPEDDGgPITGYVVEYREKGSGD---------WKEVEVtpGSETSYTLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|....
gi 1034671501 287 mNFRVRACNKAVAGEYSDPVTLET 310
Cdd:cd00063    71 -EFRVRAVNGGGESPPSESVTVTT 93
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 49-175 6.06e-09

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


The actual alignment was detected with superfamily member smart00502:

Pssm-ID: 475168  Cd Length: 127  Bit Score: 53.81  E-value: 6.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501   49 QQEALQRIISTLANKNDEIQNFIDTLHHTLKGVQENSSNILSELDEEFDSLYSILDEVKESMINCIKQEQARKSQELQSQ 128
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034671501  129 ISQCNNALENSEELLEFATRSLDIKEPEEFSKAARQIKDRVTMASAF 175
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
 
Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 315-357 2.08e-17

Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis.


Pssm-ID: 293958  Cd Length: 207  Bit Score: 79.87  E-value: 2.08e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034671501 315 FNLDNSSSHLNLKVEDTCVEWDPTGGKGQEsKIKGKENKGRYG 357
Cdd:cd12901     1 FKLDASSSHQNLKVEDLSVEWDATGGKVLQ-KIKGRENDGRSR 42
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 210-310 1.01e-12

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: 63.28  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501 210 PKAPEIDPVEclvaDNSVTVAWRMPEEDN-KIDHFILEHRKTNFDGlprvkdercWEIIDN--IKGTEYTLSGLKFDSKY 286
Cdd:cd00063     4 PTNLRVTDVT----STSVTLSWTPPEDDGgPITGYVVEYREKGSGD---------WKEVEVtpGSETSYTLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|....
gi 1034671501 287 mNFRVRACNKAVAGEYSDPVTLET 310
Cdd:cd00063    71 -EFRVRAVNGGGESPPSESVTVTT 93
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 49-175 6.06e-09

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 53.81  E-value: 6.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501   49 QQEALQRIISTLANKNDEIQNFIDTLHHTLKGVQENSSNILSELDEEFDSLYSILDEVKESMINCIKQEQARKSQELQSQ 128
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034671501  129 ISQCNNALENSEELLEFATRSLDIKEPEEFSKAARQIKDRVTMASAF 175
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 222-297 2.78e-08

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: 50.69  E-value: 2.78e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034671501  222 VADNSVTVAWRMPEEDNkIDHFILEHRKTNfdglpRVKDERCWEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA 297
Cdd:smart00060  12 VTSTSVTLSWEPPPDDG-ITGYIVGYRVEY-----REEGSEWKEVNVTPSSTSYTLTGLKPGTEY-EFRVRAVNGA 80
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
224-310 1.28e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.39  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501 224 DNSVTVAWRmPEEDNKIDHFILEhRKTNFDGlprvkderCWEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA-VAGEY 302
Cdd:COG3401   246 PGSVTLSWD-PVTESDATGYRVY-RSNSGDG--------PFTKVATVTTTSYTDTGLTNGTTY-YYRVTAVDAAgNESAP 314


                  ....*...
gi 1034671501 303 SDPVTLET 310
Cdd:COG3401   315 SNVVSVTT 322
fn3 pfam00041
Fibronectin type III domain;
222-303 3.49e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.71  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501 222 VADNSVTVAWRMPEEDN-KIDHFILEHRKTNfdgLPRVKDERcweiidNIKGTE--YTLSGLKFDSKYmNFRVRACNKAV 298
Cdd:pfam00041  11 VTSTSLTVSWTPPPDGNgPITGYEVEYRPKN---SGEPWNEI------TVPGTTtsVTLTGLKPGTEY-EVRVQAVNGGG 80


                  ....*
gi 1034671501 299 AGEYS 303
Cdd:pfam00041  81 EGPPS 85
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 49-147 8.71e-04

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 38.67  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501  49 QQEALQRIISTLANKNDEIQNFIDTLHHTLKGVQENSSNILSELDEEFDSLYSILDEVKESMINCI------KQ----EQ 118
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELesiynaKQlslnEQ 80

                          90       100
                  ....*....|....*....|....*....
gi 1034671501 119 ARKSQELQSQISQCnnaLENSEELLEFAT 147
Cdd:cd20482    81 QQKLQETIEKIQQG---CEFTERLLKHGS 106
 
Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 315-357 2.08e-17

Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis.


Pssm-ID: 293958  Cd Length: 207  Bit Score: 79.87  E-value: 2.08e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034671501 315 FNLDNSSSHLNLKVEDTCVEWDPTGGKGQEsKIKGKENKGRYG 357
Cdd:cd12901     1 FKLDASSSHQNLKVEDLSVEWDATGGKVLQ-KIKGRENDGRSR 42
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 210-310 1.01e-12

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: 63.28  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501 210 PKAPEIDPVEclvaDNSVTVAWRMPEEDN-KIDHFILEHRKTNFDGlprvkdercWEIIDN--IKGTEYTLSGLKFDSKY 286
Cdd:cd00063     4 PTNLRVTDVT----STSVTLSWTPPEDDGgPITGYVVEYREKGSGD---------WKEVEVtpGSETSYTLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|....
gi 1034671501 287 mNFRVRACNKAVAGEYSDPVTLET 310
Cdd:cd00063    71 -EFRVRAVNGGGESPPSESVTVTT 93
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 49-175 6.06e-09

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 53.81  E-value: 6.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501   49 QQEALQRIISTLANKNDEIQNFIDTLHHTLKGVQENSSNILSELDEEFDSLYSILDEVKESMINCIKQEQARKSQELQSQ 128
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034671501  129 ISQCNNALENSEELLEFATRSLDIKEPEEFSKAARQIKDRVTMASAF 175
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 222-297 2.78e-08

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: 50.69  E-value: 2.78e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034671501  222 VADNSVTVAWRMPEEDNkIDHFILEHRKTNfdglpRVKDERCWEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA 297
Cdd:smart00060  12 VTSTSVTLSWEPPPDDG-ITGYIVGYRVEY-----REEGSEWKEVNVTPSSTSYTLTGLKPGTEY-EFRVRAVNGA 80
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
224-310 1.28e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.39  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501 224 DNSVTVAWRmPEEDNKIDHFILEhRKTNFDGlprvkderCWEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA-VAGEY 302
Cdd:COG3401   246 PGSVTLSWD-PVTESDATGYRVY-RSNSGDG--------PFTKVATVTTTSYTDTGLTNGTTY-YYRVTAVDAAgNESAP 314


                  ....*...
gi 1034671501 303 SDPVTLET 310
Cdd:COG3401   315 SNVVSVTT 322
fn3 pfam00041
Fibronectin type III domain;
222-303 3.49e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.71  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501 222 VADNSVTVAWRMPEEDN-KIDHFILEHRKTNfdgLPRVKDERcweiidNIKGTE--YTLSGLKFDSKYmNFRVRACNKAV 298
Cdd:pfam00041  11 VTSTSLTVSWTPPPDGNgPITGYEVEYRPKN---SGEPWNEI------TVPGTTtsVTLTGLKPGTEY-EVRVQAVNGGG 80


                  ....*
gi 1034671501 299 AGEYS 303
Cdd:pfam00041  81 EGPPS 85
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 49-147 8.71e-04

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 38.67  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671501  49 QQEALQRIISTLANKNDEIQNFIDTLHHTLKGVQENSSNILSELDEEFDSLYSILDEVKESMINCI------KQ----EQ 118
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELesiynaKQlslnEQ 80

                          90       100
                  ....*....|....*....|....*....
gi 1034671501 119 ARKSQELQSQISQCnnaLENSEELLEFAT 147
Cdd:cd20482    81 QQKLQETIEKIQQG---CEFTERLLKHGS 106
 
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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