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Conserved domains on  [gi|17567743|ref|NP_509276|]
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Nematode cuticle collagen N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 18387949)

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Gene Ontology:  GO:0042302|GO:0005581
PubMed:  1916105|21421911

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-300 6.40e-17

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: 80.72  E-value: 6.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  126 PQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPAPNYDWCFDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQ 205
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  206 GPPGNAGAPGANGNPGNAGTPGIPGKtievpAPAGPAGAPGPAGPPGTAGTPGSQGQPGKDGSPGDAGDNGTAGSPGHPG 285
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGP-----AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                        170
                 ....*....|....*
gi 17567743  286 GEGPVGPDGARGPSG 300
Cdd:NF038329 279 ERGPVGPAGKDGQNG 293
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 21-73 1.81e-16

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 72.11  E-value: 1.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17567743     21 KFAFYGVATSTIATLFSVISVPILYSVMQHMQSSMQSEVDFCRLRSGNIWREL 73
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-300 6.40e-17

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: 80.72  E-value: 6.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  126 PQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPAPNYDWCFDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQ 205
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  206 GPPGNAGAPGANGNPGNAGTPGIPGKtievpAPAGPAGAPGPAGPPGTAGTPGSQGQPGKDGSPGDAGDNGTAGSPGHPG 285
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGP-----AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                        170
                 ....*....|....*
gi 17567743  286 GEGPVGPDGARGPSG 300
Cdd:NF038329 279 ERGPVGPAGKDGQNG 293
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 21-73 1.81e-16

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 72.11  E-value: 1.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17567743     21 KFAFYGVATSTIATLFSVISVPILYSVMQHMQSSMQSEVDFCRLRSGNIWREL 73
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 24-73 1.41e-14

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 66.71  E-value: 1.41e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17567743    24 FYGVATSTIATLFSVISVPILYSVMQHMQSSMQSEVDFCRLRSGNIWREL 73
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-300 5.41e-14

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: 71.86  E-value: 5.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  126 PQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPAPNYDWCfDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQ 205
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  206 GPPGNAGAPGANGNPGNAGTPGIPGKtievpapagpagapgpagppgtAGTPGSQGQPGKDGSPgdaGDNGTAGSPGHPG 285
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGK----------------------DGQNGKDGLPGKDGKD---GQNGKDGLPGKDG 317

                        170
                 ....*....|....*
gi 17567743  286 GEGPVGPDGARGPSG 300
Cdd:NF038329 318 KDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 99-295 1.12e-10

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: 61.84  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743   99 GPLESAVESAPANVGGGGGGCCGCGVSPQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPapnydwcfdcppgppgpa 178
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------------ 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  179 gsagvkGPSGNPGAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPGIPGKtievpapagpagapgpagppgtagtPG 258
Cdd:NF038329 269 ------GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK-------------------------DG 317

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17567743  259 SQGQPGKDGSPGDAGDNGTAGSPGHPGGEGPVGPDGA 295
Cdd:NF038329 318 KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 188-300 4.98e-09

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: 56.84  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  188 GNPGAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPGIPGKTievpapagpagapgpaGPPGTAGTPGSQGQPGKDG 267
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK----------------GPAGPQGEAGPQGPAGKDG 180

                         90       100       110
                 ....*....|....*....|....*....|...
gi 17567743  268 SPGDAGDNGTAGSPGHPGGEGPVGPDGARGPSG 300
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 185-231 2.22e-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: 41.33  E-value: 2.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 17567743   185 GPSGNPGAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPGIPGK 231
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
126-312 2.78e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743 126 PQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPAPNYDWCFDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQ 205
Cdd:COG5164  11 PSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGT 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743 206 GPPGNAGAPGANGNPGNAGTPGIPGKT--IEVPAPAGPAGAPGPAGPPGTAGTPGSQGQPGKDGSPGDAGDNGTAGSPGH 283
Cdd:COG5164  91 RPAGNTGGTTPAGDGGATGPPDDGGATgpPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGP 170

                       170       180
                ....*....|....*....|....*....
gi 17567743 284 PGGEGPVGPDGARGPSGGCEHCPPPRTAP 312
Cdd:COG5164 171 GGSTTPPDDGGSTTPPNKGETGTDIPTGG 199
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-300 6.40e-17

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: 80.72  E-value: 6.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  126 PQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPAPNYDWCFDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQ 205
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  206 GPPGNAGAPGANGNPGNAGTPGIPGKtievpAPAGPAGAPGPAGPPGTAGTPGSQGQPGKDGSPGDAGDNGTAGSPGHPG 285
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGP-----AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                        170
                 ....*....|....*
gi 17567743  286 GEGPVGPDGARGPSG 300
Cdd:NF038329 279 ERGPVGPAGKDGQNG 293
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 21-73 1.81e-16

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 72.11  E-value: 1.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17567743     21 KFAFYGVATSTIATLFSVISVPILYSVMQHMQSSMQSEVDFCRLRSGNIWREL 73
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 24-73 1.41e-14

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 66.71  E-value: 1.41e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17567743    24 FYGVATSTIATLFSVISVPILYSVMQHMQSSMQSEVDFCRLRSGNIWREL 73
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-300 5.41e-14

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: 71.86  E-value: 5.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  126 PQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPAPNYDWCfDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQ 205
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  206 GPPGNAGAPGANGNPGNAGTPGIPGKtievpapagpagapgpagppgtAGTPGSQGQPGKDGSPgdaGDNGTAGSPGHPG 285
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGK----------------------DGQNGKDGLPGKDGKD---GQNGKDGLPGKDG 317

                        170
                 ....*....|....*
gi 17567743  286 GEGPVGPDGARGPSG 300
Cdd:NF038329 318 KDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 99-295 1.12e-10

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: 61.84  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743   99 GPLESAVESAPANVGGGGGGCCGCGVSPQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPapnydwcfdcppgppgpa 178
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------------ 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  179 gsagvkGPSGNPGAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPGIPGKtievpapagpagapgpagppgtagtPG 258
Cdd:NF038329 269 ------GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK-------------------------DG 317

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17567743  259 SQGQPGKDGSPGDAGDNGTAGSPGHPGGEGPVGPDGA 295
Cdd:NF038329 318 KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 188-300 4.98e-09

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: 56.84  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743  188 GNPGAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPGIPGKTievpapagpagapgpaGPPGTAGTPGSQGQPGKDG 267
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK----------------GPAGPQGEAGPQGPAGKDG 180

                         90       100       110
                 ....*....|....*....|....*....|...
gi 17567743  268 SPGDAGDNGTAGSPGHPGGEGPVGPDGARGPSG 300
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 185-231 2.22e-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: 41.33  E-value: 2.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 17567743   185 GPSGNPGAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPGIPGK 231
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
126-312 2.78e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743 126 PQGPPGVPGRDGDNGADGEAGAPGKDGPDGPAATPAPNYDWCFDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQ 205
Cdd:COG5164  11 PSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGT 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743 206 GPPGNAGAPGANGNPGNAGTPGIPGKT--IEVPAPAGPAGAPGPAGPPGTAGTPGSQGQPGKDGSPGDAGDNGTAGSPGH 283
Cdd:COG5164  91 RPAGNTGGTTPAGDGGATGPPDDGGATgpPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGP 170

                       170       180
                ....*....|....*....|....*....
gi 17567743 284 PGGEGPVGPDGARGPSGGCEHCPPPRTAP 312
Cdd:COG5164 171 GGSTTPPDDGGSTTPPNKGETGTDIPTGG 199
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 184-227 2.11e-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 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: 35.93  E-value: 2.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 17567743   184 KGPSGNPGAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPG 227
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 191-231 5.78e-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 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: 34.39  E-value: 5.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17567743   191 GAPGTDGPAGNKGGQGPPGNAGAPGANGNPGNAGTPGIPGK 231
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
140-309 8.85e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 37.70  E-value: 8.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743 140 GADGEAGAPGKDGPDGPAATPAPNYDWCFDCPPGPPGPAGSAGVKGPSGNPGAPGTDGPAGNKGGQGPPGNAGAPGANGN 219
Cdd:COG5164   7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567743 220 PGNAGTPGIPGKTIEVPAPAGPAGAPGPAGPPGTAGTPGSQGQPGKDGSPGDAGDNGTA--GSPGHPGGEGPVGPDGARG 297
Cdd:COG5164  87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPgpGSTGPGGSTTPPGDGGSTT 166

                       170
                ....*....|..
gi 17567743 298 PSGGCEHCPPPR 309
Cdd:COG5164 167 PPGPGGSTTPPD 178
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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