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Conserved domains on  [gi|18105016|ref|NP_005668.2|]
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acetylcholinesterase collagenic tail peptide isoform I precursor [Homo sapiens]

Protein Classification

Collagen and myxo_disulf_rpt domain-containing protein (domain architecture ID 10476341)

Collagen and myxo_disulf_rpt domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
171-229 1.97e-09

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 54.80  E-value: 1.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18105016   171 GPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGP 229
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
myxo_disulf_rpt super family cl11785
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
373-397 2.13e-05

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


The actual alignment was detected with superfamily member TIGR02232:

Pssm-ID: 200169  Cd Length: 38  Bit Score: 43.13  E-value: 2.13e-05
                          10        20
                  ....*....|....*....|....*
gi 18105016   373 GTCGDGLLQPGEECDDGNSDVGDDC 397
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
 
Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
171-229 1.97e-09

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 54.80  E-value: 1.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18105016   171 GPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGP 229
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
373-397 2.13e-05

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169  Cd Length: 38  Bit Score: 43.13  E-value: 2.13e-05
                          10        20
                  ....*....|....*....|....*
gi 18105016   373 GTCGDGLLQPGEECDDGNSDVGDDC 397
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
375-400 1.13e-04

Domain of unknown function (DUF4215); The function of this family is unknown.


Pssm-ID: 290659  Cd Length: 47  Bit Score: 40.85  E-value: 1.13e-04
                          10        20
                  ....*....|....*....|....*.
gi 18105016   375 CGDGLLQPGEECDDGNSDVGDDCIRC 400
Cdd:pfam13948  21 CGDGIIVNNEQCDDGNNLQFDGCYQC 46
 
Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
171-229 1.97e-09

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 54.80  E-value: 1.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18105016   171 GPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGP 229
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
149-199 2.52e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 45.94  E-value: 2.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18105016   149 PGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGE 199
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
373-397 2.13e-05

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169  Cd Length: 38  Bit Score: 43.13  E-value: 2.13e-05
                          10        20
                  ....*....|....*....|....*
gi 18105016   373 GTCGDGLLQPGEECDDGNSDVGDDC 397
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
195-288 5.67e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 42.09  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18105016   195 GPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGdsgvmgppgkpgpsgqpgrpgppgpppagql 274
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG------------------------------- 49
                          90
                  ....*....|....
gi 18105016   275 imgPKGERGFPGPP 288
Cdd:pfam01391  50 ---PPGAPGAPGPP 60
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
375-400 1.13e-04

Domain of unknown function (DUF4215); The function of this family is unknown.


Pssm-ID: 290659  Cd Length: 47  Bit Score: 40.85  E-value: 1.13e-04
                          10        20
                  ....*....|....*....|....*.
gi 18105016   375 CGDGLLQPGEECDDGNSDVGDDCIRC 400
Cdd:pfam13948  21 CGDGIIVNNEQCDDGNNLQFDGCYQC 46
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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