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Conserved domains on  [gi|125987809|sp|P02462|]
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RecName: Full=Collagen alpha-1(IV) chain; Contains: RecName: Full=Arresten; Flags: Precursor [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1445-1554 4.96e-67

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 144854  Cd Length: 110  Bit Score: 223.33  E-value: 4.96e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1445 GFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLS 1524
Cdd:pfam01413    1 GFLIAVHSQTTQIPQCPAGWSSLWTGYSFLMHTGNAEGHGQDLGSPGSCLERFRTMPFIECNGNGVCNYASRNDYSFWLS 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 125987809  1525 TPEPMPMSMAPITGENIRPFISRCAVCEAP 1554
Cdd:pfam01413   81 TIEPMPMPMTPKAGREIRPYISRCQVCEAP 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1555-1668 1.66e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 128421  Cd Length: 114  Bit Score: 210.71  E-value: 1.66e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   1555 AMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NAYSFWL 1633
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 125987809   1634 ATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRR 1668
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
975-1033 9.97e-07

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 48.25  E-value: 9.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 125987809   975 GVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGP 1033
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1103-1162 2.05e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 47.10  E-value: 2.05e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1103 GSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSA 1162
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
839-896 1.31e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 44.79  E-value: 1.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   839 PGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPV 896
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
876-935 4.06e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   876 GSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKP 935
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1064-1123 4.67e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.67e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1064 GEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLP 1123
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
275-325 7.18e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 39.78  E-value: 7.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 125987809   275 GEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEA 325
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
510-585 2.07e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 38.24  E-value: 2.07e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809   510 GVPGPQGTPGLIGQPGAKGEPGEfyfdlrlkgdkgdpgfPGQPGMTGRAGSPGRDGHPGLPGPKGSPGSVGLKGER 585
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGP----------------PGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
645-683 5.75e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


:

Pssm-ID: 189968  Cd Length: 60  Bit Score: 36.70  E-value: 5.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 125987809   645 PGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGA 683
Cdd:pfam01391   15 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1445-1554 4.96e-67

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 144854  Cd Length: 110  Bit Score: 223.33  E-value: 4.96e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1445 GFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLS 1524
Cdd:pfam01413    1 GFLIAVHSQTTQIPQCPAGWSSLWTGYSFLMHTGNAEGHGQDLGSPGSCLERFRTMPFIECNGNGVCNYASRNDYSFWLS 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 125987809  1525 TPEPMPMSMAPITGENIRPFISRCAVCEAP 1554
Cdd:pfam01413   81 TIEPMPMPMTPKAGREIRPYISRCQVCEAP 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1555-1668 1.66e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 210.71  E-value: 1.66e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   1555 AMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NAYSFWL 1633
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 125987809   1634 ATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRR 1668
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1555-1668 1.01e-58

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 144854  Cd Length: 110  Bit Score: 199.45  E-value: 1.01e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1555 AMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NAYSFWL 1633
Cdd:pfam01413    1 GFLIAVHSQTTQIPQCPAGWSSLWTGYSFLMHT-GNAEGHGQDLGSPGSCLERFRTMPFIECNGNGVCNYASrNDYSFWL 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 125987809  1634 ATIERsemfkKPTPSTLKAG-ELRTHVSRCQVCMRR 1668
Cdd:pfam01413   80 STIEP-----MPMPMTPKAGrEIRPYISRCQVCEAP 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1445-1554 1.30e-54

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 187.98  E-value: 1.30e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   1445 GFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLS 1524
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 125987809   1525 TPEP-----MPMSMAPITGEnIRPFISRCAVCEAP 1554
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAGD-LRPYISRCQVCEKP 114
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
975-1033 9.97e-07

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 48.25  E-value: 9.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 125987809   975 GVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGP 1033
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1103-1162 2.05e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 47.10  E-value: 2.05e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1103 GSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSA 1162
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
839-896 1.31e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 44.79  E-value: 1.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   839 PGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPV 896
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
876-935 4.06e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   876 GSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKP 935
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1064-1123 4.67e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.67e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1064 GEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLP 1123
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
275-325 7.18e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 39.78  E-value: 7.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 125987809   275 GEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEA 325
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
510-585 2.07e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 38.24  E-value: 2.07e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809   510 GVPGPQGTPGLIGQPGAKGEPGEfyfdlrlkgdkgdpgfPGQPGMTGRAGSPGRDGHPGLPGPKGSPGSVGLKGER 585
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGP----------------PGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
645-683 5.75e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 36.70  E-value: 5.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 125987809   645 PGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGA 683
Cdd:pfam01391   15 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
958-1153 7.20e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  958 QIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGP--QG 1035
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAsdGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809 1036 SPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGDQGIAGfpGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPG 1115
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPA--PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 125987809 1116 EKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEP 1153
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
861-1177 1.63e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 255446 [Multi-domain]  Cd Length: 768  Bit Score: 48.46  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   861 GLPGQQGAP-GIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGdhgfpgsSGPRGDPGLKGDKGDVGLPGKPGSMD 939
Cdd:pfam09606   83 GTRGPQMGPmGPGPGRPMGQQMGGPGTASNLLQSLNVRGQMPMGAAG-------MGPHQMSRVGTMQPGGQAGGMMQQSS 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   940 KVDMGSMKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGpKGDPGISGTPGAPGLPGPKGSVGGMGLP 1019
Cdd:pfam09606  156 GQPQSQQPNQMGPQQGQAQGQAGGMNQGQQGPVGQQQPPQMGQPGMPGGGG-QGQMQQQGQPGGQQQQNPQMQQQLQNQQ 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1020 GTP-GEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPG-LRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSP- 1096
Cdd:pfam09606  235 QQQmDQQQGPADAQAQMGQQQQGQGGMQPQQMQGGQMQVPMQQqPPQQQPQQSQLGMLPNQMQQMPGGGQGGPGQPMGPp 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1097 ---------GLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIP-----GVKGEAGLPGTPG-PTGPAGQKGEPGSDGIPGS 1161
Cdd:pfam09606  315 pqrpgavpqGGQAVQQGVMSAGQQQLKQMKLRNMRGQQQTQQqqqqqGGNHPAAHQQQMNqQVGQGGQMVALGYLNIQGN 394
                          330
                   ....*....|....*.
gi 125987809  1162 AGEKGEPGLpGRGFPG 1177
Cdd:pfam09606  395 QGGLGANPM-QQGQPG 409
PHA03247 PHA03247
large tegument protein UL36; Provisional
851-1155 1.62e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  851 PGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGS-------PGPVGAPGLPGEKGDHGFPGSSGPRGDPGlk 923
Cdd:PHA03247 2580 PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpppPSPSPAANEPDPHPPPTVPPPERPRDDPA-- 2657
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  924 gdKGDVGLPGKPGSMDKVDMGSMKGQKGDQgeKGQIGPIGEKGSRGDPGTPG-VPGKDGQAGQPGQPGPKG-DPGISGTP 1001
Cdd:PHA03247 2658 --PGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSLADPPPPPpTPEPAPHALVSATPLPPGpAAARQASP 2733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809 1002 GAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAkgekgqAGPPGIGIPGLRGEKGDQGIAGFPGSPGEK 1081
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------GPPRRLTRPAVASLSESRESLPSPWDPADP 2807
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809 1082 GEKGSIGIPGMP--GSPGLKGSPGSVGYPGSPGLPGEKGDKGLPgldgipgvkgeagLPGTPGPTGPAGQKGEPGS 1155
Cdd:PHA03247 2808 PAAVLAPAAALPpaASPAGPLPPPTSAQPTAPPPPPGPPPPSLP-------------LGGSVAPGGDVRRRPPSRS 2870
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1445-1554 4.96e-67

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 144854  Cd Length: 110  Bit Score: 223.33  E-value: 4.96e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1445 GFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLS 1524
Cdd:pfam01413    1 GFLIAVHSQTTQIPQCPAGWSSLWTGYSFLMHTGNAEGHGQDLGSPGSCLERFRTMPFIECNGNGVCNYASRNDYSFWLS 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 125987809  1525 TPEPMPMSMAPITGENIRPFISRCAVCEAP 1554
Cdd:pfam01413   81 TIEPMPMPMTPKAGREIRPYISRCQVCEAP 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1555-1668 1.66e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 210.71  E-value: 1.66e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   1555 AMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NAYSFWL 1633
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 125987809   1634 ATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRR 1668
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1555-1668 1.01e-58

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 144854  Cd Length: 110  Bit Score: 199.45  E-value: 1.01e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1555 AMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NAYSFWL 1633
Cdd:pfam01413    1 GFLIAVHSQTTQIPQCPAGWSSLWTGYSFLMHT-GNAEGHGQDLGSPGSCLERFRTMPFIECNGNGVCNYASrNDYSFWL 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 125987809  1634 ATIERsemfkKPTPSTLKAG-ELRTHVSRCQVCMRR 1668
Cdd:pfam01413   80 STIEP-----MPMPMTPKAGrEIRPYISRCQVCEAP 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1445-1554 1.30e-54

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 187.98  E-value: 1.30e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   1445 GFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLS 1524
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 125987809   1525 TPEP-----MPMSMAPITGEnIRPFISRCAVCEAP 1554
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAGD-LRPYISRCQVCEKP 114
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
975-1033 9.97e-07

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 48.25  E-value: 9.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 125987809   975 GVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGP 1033
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1103-1162 2.05e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 47.10  E-value: 2.05e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1103 GSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSA 1162
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
984-1041 2.61e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 47.10  E-value: 2.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   984 GQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPG 1041
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1088-1147 6.22e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 45.94  E-value: 6.22e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1088 GIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPA 1147
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1109-1168 7.09e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 45.56  E-value: 7.09e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1109 GSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEP 1168
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
996-1055 1.12e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 45.17  E-value: 1.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   996 GISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPP 1055
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
839-896 1.31e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 44.79  E-value: 1.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   839 PGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPV 896
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
951-1009 2.58e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 44.02  E-value: 2.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 125987809   951 GDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGP 1009
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
855-912 3.38e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.63  E-value: 3.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   855 GQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPG 912
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
840-899 3.47e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.63  E-value: 3.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   840 GPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAP 899
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
843-902 3.57e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.63  E-value: 3.57e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   843 GDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLP 902
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1002-1056 3.60e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.63  E-value: 3.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 125987809  1002 GAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPG 1056
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
876-935 4.06e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   876 GSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKP 935
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1100-1157 4.18e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809  1100 GSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDG 1157
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1112-1171 4.38e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.38e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1112 GLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLP 1171
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1064-1123 4.67e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 43.25  E-value: 4.67e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1064 GEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLP 1123
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
960-1019 5.51e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 42.86  E-value: 5.51e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   960 GPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLP 1019
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
957-1014 7.14e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 42.48  E-value: 7.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   957 GQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVG 1014
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
861-920 8.36e-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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 42.48  E-value: 8.36e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   861 GLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDP 920
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1130-1191 1.11e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 42.09  E-value: 1.11e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125987809  1130 GVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLPGRgfPGFPGAKGDKGSKGEV 1191
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGP--PGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1076-1135 1.25e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 42.09  E-value: 1.25e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1076 GSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEA 1135
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
954-1011 1.49e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 41.71  E-value: 1.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   954 GEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKG 1011
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
849-906 1.56e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 41.71  E-value: 1.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   849 GLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKG 906
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
948-1007 1.93e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 41.32  E-value: 1.93e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   948 GQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLP 1007
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1082-1141 2.37e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 40.94  E-value: 2.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1082 GEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTP 1141
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1073-1130 2.84e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 40.94  E-value: 2.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809  1073 GFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPG 1130
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
885-936 3.20e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 40.55  E-value: 3.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 125987809   885 GTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPG 936
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
947-1004 3.26e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 40.55  E-value: 3.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 125987809   947 KGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAP 1004
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
275-325 7.18e-04

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 39.78  E-value: 7.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 125987809   275 GEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEA 325
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
278-323 1.13e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 39.01  E-value: 1.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 125987809   278 GEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKG 323
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
882-937 1.26e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 39.01  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809   882 GVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPGS 937
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGA 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1058-1114 1.77e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 38.62  E-value: 1.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 125987809  1058 GIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLP 1114
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
510-585 2.07e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 38.24  E-value: 2.07e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809   510 GVPGPQGTPGLIGQPGAKGEPGEfyfdlrlkgdkgdpgfPGQPGMTGRAGSPGRDGHPGLPGPKGSPGSVGLKGER 585
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGP----------------PGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
645-683 5.75e-03

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 hydroxyproline. Collagens are post translationally modified by proline hydroxylase to form the hydroxyproline 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.


Pssm-ID: 189968  Cd Length: 60  Bit Score: 36.70  E-value: 5.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 125987809   645 PGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGA 683
Cdd:pfam01391   15 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
958-1153 7.20e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  958 QIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGP--QG 1035
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAsdGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809 1036 SPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGDQGIAGfpGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPG 1115
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPA--PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 125987809 1116 EKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEP 1153
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
861-1177 1.63e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 255446 [Multi-domain]  Cd Length: 768  Bit Score: 48.46  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   861 GLPGQQGAP-GIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGdhgfpgsSGPRGDPGLKGDKGDVGLPGKPGSMD 939
Cdd:pfam09606   83 GTRGPQMGPmGPGPGRPMGQQMGGPGTASNLLQSLNVRGQMPMGAAG-------MGPHQMSRVGTMQPGGQAGGMMQQSS 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   940 KVDMGSMKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGpKGDPGISGTPGAPGLPGPKGSVGGMGLP 1019
Cdd:pfam09606  156 GQPQSQQPNQMGPQQGQAQGQAGGMNQGQQGPVGQQQPPQMGQPGMPGGGG-QGQMQQQGQPGGQQQQNPQMQQQLQNQQ 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1020 GTP-GEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPG-LRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSP- 1096
Cdd:pfam09606  235 QQQmDQQQGPADAQAQMGQQQQGQGGMQPQQMQGGQMQVPMQQqPPQQQPQQSQLGMLPNQMQQMPGGGQGGPGQPMGPp 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1097 ---------GLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIP-----GVKGEAGLPGTPG-PTGPAGQKGEPGSDGIPGS 1161
Cdd:pfam09606  315 pqrpgavpqGGQAVQQGVMSAGQQQLKQMKLRNMRGQQQTQQqqqqqGGNHPAAHQQQMNqQVGQGGQMVALGYLNIQGN 394
                          330
                   ....*....|....*.
gi 125987809  1162 AGEKGEPGLpGRGFPG 1177
Cdd:pfam09606  395 QGGLGANPM-QQGQPG 409
Sporozoite_P67 pfam05642
Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. ...
912-1115 1.38e-04

Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. A stage specific surface antigen of Theileria parva, p67, is the basis for the development of an anti-sporozoite vaccine for the control of East Coast fever (ECF) in cattle. The antigen has been shown to contain five distinct linear peptide sequences recognized by sporozoite-neutralizing murine monoclonal antibodies.


Pssm-ID: 253298 [Multi-domain]  Cd Length: 727  Bit Score: 45.06  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   912 GSSGPRGDPGLKGDKGDVGLPGKPGS-MDKVDMGSmkgqkgdQGEKGQIGP-IGEKGSRGDPGTpGVPGkdgqAGQPGQP 989
Cdd:pfam05642  136 GKGSKKTQPGVSTSSGSTTSGTDLNTkQSQTGLGA-------SGSHAQQDPaVSQSGVVGVPGL-GVPG----VGVPGGG 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   990 GPKGDPGIsGTPGAPGLPGpkgsvGGMGLPGtpGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPGLRgeKGDQ 1069
Cdd:pfam05642  204 GAGALPGV-GVGRAGVSPG-----VGVGGLG--GVPGVGILASNTSREGQTQDDQERDGDGRVIEPGVGLPGVR--VGDS 273
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 125987809  1070 GIAGFPGSP--GEKGEKGSIGIPGMPGSPGLKGSPG------SVGYP-GSPGLPG 1115
Cdd:pfam05642  274 TSSPSTTRPsgSTTTTTPASSGPSAPGGPGSSSRNAvtrstdSISGPiPSPGAPR 328
PHA03247 PHA03247
large tegument protein UL36; Provisional
851-1155 1.62e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  851 PGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGS-------PGPVGAPGLPGEKGDHGFPGSSGPRGDPGlk 923
Cdd:PHA03247 2580 PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpppPSPSPAANEPDPHPPPTVPPPERPRDDPA-- 2657
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  924 gdKGDVGLPGKPGSMDKVDMGSMKGQKGDQgeKGQIGPIGEKGSRGDPGTPG-VPGKDGQAGQPGQPGPKG-DPGISGTP 1001
Cdd:PHA03247 2658 --PGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSLADPPPPPpTPEPAPHALVSATPLPPGpAAARQASP 2733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809 1002 GAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAkgekgqAGPPGIGIPGLRGEKGDQGIAGFPGSPGEK 1081
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------GPPRRLTRPAVASLSESRESLPSPWDPADP 2807
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809 1082 GEKGSIGIPGMP--GSPGLKGSPGSVGYPGSPGLPGEKGDKGLPgldgipgvkgeagLPGTPGPTGPAGQKGEPGS 1155
Cdd:PHA03247 2808 PAAVLAPAAALPpaASPAGPLPPPTSAQPTAPPPPPGPPPPSLP-------------LGGSVAPGGDVRRRPPSRS 2870
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
843-1048 6.11e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 6.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  843 GDKGAQGLPGiTGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGL 922
Cdd:PRK07764  590 PAPGAAGGEG-PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  923 KGDKGDVGLPGKPGSMDkvdmgsmkGQKGDQGEKGQIGPIGEkgSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPG 1002
Cdd:PRK07764  669 WPAKAGGAAPAAPPPAP--------APAAPAAPAGAAPAQPA--PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 125987809 1003 APGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGE 1048
Cdd:PRK07764  739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784
PHA03169 PHA03169
hypothetical protein; Provisional
1044-1189 8.91e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809 1044 GAKGEKGQAGPPGIGIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLP 1123
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQ 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809 1124 GLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLPGRGFPGFPGAKGDKGSKG 1189
Cdd:PHA03169  162 QPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNT 227
Sporozoite_P67 pfam05642
Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. ...
979-1172 1.09e-03

Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. A stage specific surface antigen of Theileria parva, p67, is the basis for the development of an anti-sporozoite vaccine for the control of East Coast fever (ECF) in cattle. The antigen has been shown to contain five distinct linear peptide sequences recognized by sporozoite-neutralizing murine monoclonal antibodies.


Pssm-ID: 253298 [Multi-domain]  Cd Length: 727  Bit Score: 42.36  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   979 KDGQAGQPGQPGPKGDpgiSGTPGAPGLPGPKGSVGGMGLPGTPGEKG-VPGIPGPQGSPGLpgdkgakgekgqaGPPGI 1057
Cdd:pfam05642  134 KDGKGSKKTQPGVSTS---SGSTTSGTDLNTKQSQTGLGASGSHAQQDpAVSQSGVVGVPGL-------------GVPGV 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1058 GIPGLRGEKGDQGIAgfPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLdGIPGVkGEAGL 1137
Cdd:pfam05642  198 GVPGGGGAGALPGVG--VGRAGVSPGVGVGGLGGVPGVGILASNTSREGQTQDDQERDGDGRVIEPGV-GLPGV-RVGDS 273
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 125987809  1138 PGTPGPTGPAGQKgepgSDGIPGSAGEKGePGLPG 1172
Cdd:pfam05642  274 TSSPSTTRPSGST----TTTTPASSGPSA-PGGPG 303
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
867-1055 2.19e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  867 GAPGIPGFPGSKGEMGVMgTPGQPGSPGPVGAPGLPGekGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPGSMDKVDMGSM 946
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSG-PPEEAARPAAPAAPAAPA--APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  947 KGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTP---GAPGLPGPKGSVGGMGLPGTPG 1023
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPpqaAQGASAPSPAADDPVPLPPEPD 746
                         170       180       190
                  ....*....|....*....|....*....|...
gi 125987809 1024 EKGVPGIPGPQG-SPGLPGDKGAKGEKGQAGPP 1055
Cdd:PRK07764  747 DPPDPAGAPAQPpPPPAPAPAAAPAAAPPPSPP 779
PHA03169 PHA03169
hypothetical protein; Provisional
873-1017 2.48e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  873 GFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGdhgfpGSSGPRGDPGLKGDKGDvglPGKPGSMDKVDMGSMKGQKGD 952
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENT-----SGSSPESPASHSPPPSP---PSHPGPHEPAPPESHNPSPNQ 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125987809  953 QGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISG-TPGAPGLPGPKGSVGGMG 1017
Cdd:PHA03169  162 QPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdEPGEPQSPTPQQAPSPNT 227
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
831-1378 2.96e-03

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 111993 [Multi-domain]  Cd Length: 779  Bit Score: 40.83  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   831 PGFPGLDMPGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGF-PGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHG 909
Cdd:pfam03157   65 PQQPGQGQQPGKGQEPGQGQQGYYPTSLQQPGQGQQIEKGKPGYyPTSPQQPGQLQQPAQGQQIGQGQQGRQPGQGQPGY 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   910 FPGSsgPRGDPGLKGDKGDVGLPGKPGsmdkvdmgsmKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQP 989
Cdd:pfam03157  145 YPTS--PQHQPGQLQQPAQGQQGQQIG----------QGQQGQQPEQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQ 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809   990 GPKGDPGISGTPGAPGLPGPKGSVGGMGLPG-TPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGD 1068
Cdd:pfam03157  213 GYYPGQLQQSGQGQPGHYPTSLQQLGQGQQGhYLASPQQPGQGQQPGQLQQPAQGQQPEQGQQGQQPAQGQQGHQPAQGQ 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1069 QGIAGFPGSPGEKGEKGSIGIPG-MPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPA 1147
Cdd:pfam03157  293 QPGQGQPGHYPASPQQPGQGQPGhYPASSQQPTQSQEPGQGQQGQQVGQGQQAQIPAQGQQPGQGQPGHYPASPLQQGPG 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1148 GQKGEPGSDGIPGSAGEKGEPGLPGRGFPGFPGAKGDKGSKGEVGFPGLAGSPGIPGSKGEQGF----MGPPGPQGQPGL 1223
Cdd:pfam03157  373 QPGHYLTSLQQLGQGQQIGQLQQSAPGQKGQQPGQGQQPGQGQQGQQPGQGEQEQQPGQGQPGYyptsLQQPGQGQQPGQ 452
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  1224 PGSPGHATEGPKGDRGPQGQPGLPGLPGPMGPPGLPGIDGVKGDKGNPGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGS 1303
Cdd:pfam03157  453 WQQPGQGQPGYYPTSLLQPGQGQPGHDPASLQQPGQGQQPGQLQQPAQGQPGQQLAQGQQGQQPAQVQQGQQPAQGQQGQ 532
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125987809  1304 KGDMGPPGVPGFQGPKGLPGLQGIKGDQGDQGVPGAKGLPGPPGPPGPYDIIKGEPGLPGPEGPPGLKGLQGLPG 1378
Cdd:pfam03157  533 QLGQGQQGQQPGQGQHPAQGEQGQQPGQGQQGQQPGQGQQPGQGQPWYYPTSPQESGQGQQPGQWQQPGQWQQPG 607
uvrC PRK14666
excinuclease ABC subunit C; Provisional
1054-1170 3.92e-03

excinuclease ABC subunit C; Provisional


Pssm-ID: 237782 [Multi-domain]  Cd Length: 694  Bit Score: 40.64  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809 1054 PPGIGIPGLRGEKGDQGIAGFPGSPGEkgekgsiGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKG 1133
Cdd:PRK14666  308 PPRIVVPWLPDTEGREGDDLAPTAVCT-------DAGLLPDTPLLPDAPEGSSDPVVPVAAATPVDASLPDVRTGTAPTS 380
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 125987809 1134 EAGLP-GTPGPtgpagqkGEPGSDGIPGSAGEKGEPGL 1170
Cdd:PRK14666  381 LANVShADPAV-------AQPTQAATLAGAAPKGATHL 411
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
976-1168 5.43e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809  976 VPGKDGQAGQPG---QPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKgAKGEKGQA 1052
Cdd:PRK07764  587 VVGPAPGAAGGEgppAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHV-AVPDASDG 665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125987809 1053 GPPGIGIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGL----PGEKGDKGLPGLDGI 1128
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQgasaPSPAADDPVPLPPEP 745
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 125987809 1129 PGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEP 1168
Cdd:PRK07764  746 DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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