NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446198786|ref|WP_000276641|]
View 

BppU family phage baseplate upper protein [Staphylococcus aureus]

Protein Classification

phage tail fiber repeat family protein( domain architecture ID 10566379)

phage tail fiber repeat (PTR) family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
BppU_N pfam10651
BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also ...
5-144 3.52e-37

BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also known as ORF48) which is found in phage from a number of different bacteria. The N-terminal domain exhibits a beta-sandwich immunoglobulin fold.


:

Pssm-ID: 431419  Cd Length: 141  Bit Score: 132.06  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198786    5 KDVETRIKNDGVDLGDIGCRFYTEDENTASIRIGINDKQGRIDLkaHGLTPRLHLFMEDGSIFKNEPLIIDDVVKGFLTY 84
Cdd:pfam10651   1 YDITLDTTAQNNKIKQTGIRFRTGDSNTAVLNFKITKNGQPLDL--TGLTAKFELVKPDDGSIVSDELEILDAKKGKFKY 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446198786   85 KIPKKVIKHAGYVRCKLFLEKE-EEKIHVANFSFNIVDSGIESAVAKEIDVKLVDDAITRI 144
Cdd:pfam10651  79 VLPEEVLKHVGKVKAYFSVFKEdDQVISTRNFSFNVEKSLVEDGIVSSDYIEDFEDLIEEV 139
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
176-208 6.10e-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 hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 6.10e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446198786  176 FKGAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391  23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
178-252 1.49e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.82  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198786 178 GAKGDKGEPGQPGAKGDTGKKGEQGTPGKNGTV---VSINPDT-----KMWQIDGKDTDIKAEPElldkiNIANvEGLeN 249
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKtpeVPQKPDTaphtpKTPQIPGQSKDVTPAPQ-----NPSN-RGL-N 383

                 ...
gi 446198786 250 KLQ 252
Cdd:NF038329 384 KPQ 386
PTR super family cl15092
Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas ...
327-356 1.33e-04

Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas vaginalis. These proteins contain multiple HXH repeats. Some proteins in this family are annotated as having phage tail repeats. The function of this family is unknown.


The actual alignment was detected with superfamily member pfam12789:

Pssm-ID: 472754  Cd Length: 60  Bit Score: 39.84  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 446198786  327 YADKNHSHTIKQIEGLENALSKKSDINHSH 356
Cdd:pfam12789   2 YSKKTHTHTIANITNLQETLNRKADKGHTH 31
 
Name Accession Description Interval E-value
BppU_N pfam10651
BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also ...
5-144 3.52e-37

BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also known as ORF48) which is found in phage from a number of different bacteria. The N-terminal domain exhibits a beta-sandwich immunoglobulin fold.


Pssm-ID: 431419  Cd Length: 141  Bit Score: 132.06  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198786    5 KDVETRIKNDGVDLGDIGCRFYTEDENTASIRIGINDKQGRIDLkaHGLTPRLHLFMEDGSIFKNEPLIIDDVVKGFLTY 84
Cdd:pfam10651   1 YDITLDTTAQNNKIKQTGIRFRTGDSNTAVLNFKITKNGQPLDL--TGLTAKFELVKPDDGSIVSDELEILDAKKGKFKY 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446198786   85 KIPKKVIKHAGYVRCKLFLEKE-EEKIHVANFSFNIVDSGIESAVAKEIDVKLVDDAITRI 144
Cdd:pfam10651  79 VLPEEVLKHVGKVKAYFSVFKEdDQVISTRNFSFNVEKSLVEDGIVSSDYIEDFEDLIEEV 139
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
176-208 6.10e-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 hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 6.10e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446198786  176 FKGAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391  23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
178-252 1.49e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.82  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198786 178 GAKGDKGEPGQPGAKGDTGKKGEQGTPGKNGTV---VSINPDT-----KMWQIDGKDTDIKAEPElldkiNIANvEGLeN 249
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKtpeVPQKPDTaphtpKTPQIPGQSKDVTPAPQ-----NPSN-RGL-N 383

                 ...
gi 446198786 250 KLQ 252
Cdd:NF038329 384 KPQ 386
PTR pfam12789
Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas ...
327-356 1.33e-04

Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas vaginalis. These proteins contain multiple HXH repeats. Some proteins in this family are annotated as having phage tail repeats. The function of this family is unknown.


Pssm-ID: 463707  Cd Length: 60  Bit Score: 39.84  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 446198786  327 YADKNHSHTIKQIEGLENALSKKSDINHSH 356
Cdd:pfam12789   2 YSKKTHTHTIANITNLQETLNRKADKGHTH 31
 
Name Accession Description Interval E-value
BppU_N pfam10651
BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also ...
5-144 3.52e-37

BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also known as ORF48) which is found in phage from a number of different bacteria. The N-terminal domain exhibits a beta-sandwich immunoglobulin fold.


Pssm-ID: 431419  Cd Length: 141  Bit Score: 132.06  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198786    5 KDVETRIKNDGVDLGDIGCRFYTEDENTASIRIGINDKQGRIDLkaHGLTPRLHLFMEDGSIFKNEPLIIDDVVKGFLTY 84
Cdd:pfam10651   1 YDITLDTTAQNNKIKQTGIRFRTGDSNTAVLNFKITKNGQPLDL--TGLTAKFELVKPDDGSIVSDELEILDAKKGKFKY 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446198786   85 KIPKKVIKHAGYVRCKLFLEKE-EEKIHVANFSFNIVDSGIESAVAKEIDVKLVDDAITRI 144
Cdd:pfam10651  79 VLPEEVLKHVGKVKAYFSVFKEdDQVISTRNFSFNVEKSLVEDGIVSSDYIEDFEDLIEEV 139
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
176-208 6.10e-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 hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 6.10e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446198786  176 FKGAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391  23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
178-208 1.81e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 1.81e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 446198786  178 GAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG 40
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
177-207 2.34e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 2.34e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 446198786  177 KGAKGDKGEPGQPGAKGDTGKKGEQGTPGKN 207
Cdd:pfam01391  27 PGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
177-209 4.43e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 4.43e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446198786  177 KGAKGDKGEPGQPGAKGDTGKKGEQGTPGKNGT 209
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
178-208 6.18e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 6.18e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 446198786  178 GAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG 34
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
176-208 1.06e-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 hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 1.06e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446198786  176 FKGAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391  17 PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
178-252 1.49e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.82  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198786 178 GAKGDKGEPGQPGAKGDTGKKGEQGTPGKNGTV---VSINPDT-----KMWQIDGKDTDIKAEPElldkiNIANvEGLeN 249
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKtpeVPQKPDTaphtpKTPQIPGQSKDVTPAPQ-----NPSN-RGL-N 383

                 ...
gi 446198786 250 KLQ 252
Cdd:NF038329 384 KPQ 386
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
178-208 3.84e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 3.84e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 446198786  178 GAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
177-208 5.26e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 5.26e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446198786  177 KGAKGDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG 37
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
178-205 7.42e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 7.42e-05
                          10        20
                  ....*....|....*....|....*...
gi 446198786  178 GAKGDKGEPGQPGAKGDTGKKGEQGTPG 205
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPG 28
PTR pfam12789
Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas ...
327-356 1.33e-04

Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas vaginalis. These proteins contain multiple HXH repeats. Some proteins in this family are annotated as having phage tail repeats. The function of this family is unknown.


Pssm-ID: 463707  Cd Length: 60  Bit Score: 39.84  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 446198786  327 YADKNHSHTIKQIEGLENALSKKSDINHSH 356
Cdd:pfam12789   2 YSKKTHTHTIANITNLQETLNRKADKGHTH 31
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
177-209 1.46e-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 hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 1.46e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446198786  177 KGAKGDKGEPGQPGAKGDTGKKGEQGTPGKNGT 209
Cdd:pfam01391  15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
181-208 2.64e-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 hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 2.64e-04
                          10        20
                  ....*....|....*....|....*...
gi 446198786  181 GDKGEPGQPGAKGDTGKKGEQGTPGKNG 208
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPG 28
PTR pfam12789
Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas ...
320-356 3.62e-04

Phage tail repeat like; This family largely contains proteins from the eukaryote Trichomonas vaginalis. These proteins contain multiple HXH repeats. Some proteins in this family are annotated as having phage tail repeats. The function of this family is unknown.


Pssm-ID: 463707  Cd Length: 60  Bit Score: 38.30  E-value: 3.62e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 446198786  320 KQSLNSlYADKNHSHTIKQIEGLENALSKKSDINHSH 356
Cdd:pfam12789  18 QETLNR-KADKGHTHTIANITNLQETLNRKSDVGHTH 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH