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Conserved domains on  [gi|205360958|ref|NP_077300|]
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protein disulfide isomerase CRELD2 isoform b precursor [Homo sapiens]

Protein Classification

furin-like repeat-containing protein( domain architecture ID 10644877)

furin-like repeat (FU)-containing protein contains a cysteine-rich region; similar to Homo sapiens protein disulfide isomerase CRELD2 that might play a role in the unfolded protein response, as well as regulate transport of alpha4-beta2 neuronal acetylcholine receptor

CATH:  2.10.220.10
SCOP:  4004103

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FU smart00261
Furin-like repeats;
194-230 4.81e-04

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 37.49  E-value: 4.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 205360958   194 SICTACDESCKTCSGLTNRDCGECEVGWVLDEGACVD 230
Cdd:smart00261   2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVS 38
FU smart00261
Furin-like repeats;
255-295 8.03e-04

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 36.72  E-value: 8.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 205360958   255 TCEECDSSCVGCTGEGPGNCKECISGYAREHGQCadVDECS 295
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKC--VSECP 41
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 288-328 1.09e-03

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


The actual alignment was detected with superfamily member cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 205360958 288 CADVDECSLAEKTCvrkNENCYNTPGSYVCVCPDGFEETED 328
Cdd:cd01475  184 CVVPDLCATLSHVC---QQVCISTPGSYLCACTEGYALLED 221
 
Name Accession Description Interval E-value
FU smart00261
Furin-like repeats;
194-230 4.81e-04

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 37.49  E-value: 4.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 205360958   194 SICTACDESCKTCSGLTNRDCGECEVGWVLDEGACVD 230
Cdd:smart00261   2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVS 38
FU smart00261
Furin-like repeats;
255-295 8.03e-04

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 36.72  E-value: 8.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 205360958   255 TCEECDSSCVGCTGEGPGNCKECISGYAREHGQCadVDECS 295
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKC--VSECP 41
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 288-328 1.09e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 205360958 288 CADVDECSLAEKTCvrkNENCYNTPGSYVCVCPDGFEETED 328
Cdd:cd01475  184 CVVPDLCATLSHVC---QQVCISTPGSYLCACTEGYALLED 221
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 258-295 3.80e-03

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 35.19  E-value: 3.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 205360958 258 ECDSSCVGCTGEGPGNCKECISGYAREHGQCadVDECS 295
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTC--VSECP 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
290-325 4.09e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.53  E-value: 4.09e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 205360958   290 DVDECslAEKTCVRKNENCYNTPGSYVCVCPDGFEE 325
Cdd:smart00179   1 DIDEC--ASGNPCQNGGTCVNTVGSYRCECPPGYTD 34
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 198-230 8.28e-03

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 34.03  E-value: 8.28e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 205360958 198 ACDESCKTCSGLTNRDCGECEVGWVLDEGACVD 230
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVS 33
 
Name Accession Description Interval E-value
FU smart00261
Furin-like repeats;
194-230 4.81e-04

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 37.49  E-value: 4.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 205360958   194 SICTACDESCKTCSGLTNRDCGECEVGWVLDEGACVD 230
Cdd:smart00261   2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVS 38
FU smart00261
Furin-like repeats;
255-295 8.03e-04

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 36.72  E-value: 8.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 205360958   255 TCEECDSSCVGCTGEGPGNCKECISGYAREHGQCadVDECS 295
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKC--VSECP 41
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 288-328 1.09e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 205360958 288 CADVDECSLAEKTCvrkNENCYNTPGSYVCVCPDGFEETED 328
Cdd:cd01475  184 CVVPDLCATLSHVC---QQVCISTPGSYLCACTEGYALLED 221
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 258-295 3.80e-03

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 35.19  E-value: 3.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 205360958 258 ECDSSCVGCTGEGPGNCKECISGYAREHGQCadVDECS 295
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTC--VSECP 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
290-325 4.09e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.53  E-value: 4.09e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 205360958   290 DVDECslAEKTCVRKNENCYNTPGSYVCVCPDGFEE 325
Cdd:smart00179   1 DIDEC--ASGNPCQNGGTCVNTVGSYRCECPPGYTD 34
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 198-230 8.28e-03

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 34.03  E-value: 8.28e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 205360958 198 ACDESCKTCSGLTNRDCGECEVGWVLDEGACVD 230
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVS 33
 
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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