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Conserved domains on  [gi|17541560|ref|NP_502297|]
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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 ...
 110-271 2.75e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.40  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  110 EDGDHGLVGEDGTPGADGNLGVPLSANgcivcPAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPG 189
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAG-----PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  190 RPGNDGRPGAPGAPGTRSVGRPGTAGSPGPQGPPGQNGNDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAAGQPG 269
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293


                 ..
gi 17541560  270 GD 271
Cdd:NF038329 294 KD 295
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-58 3.31e-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. 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: 65.95  E-value: 3.31e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17541560      6 YLVSIAAAASTFAVLASIVSLVYLVNDVNNYYDDVTRNIENFKDDANTVWHQM 58
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 ...
 110-271 2.75e-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: 73.40  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  110 EDGDHGLVGEDGTPGADGNLGVPLSANgcivcPAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPG 189
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAG-----PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  190 RPGNDGRPGAPGAPGTRSVGRPGTAGSPGPQGPPGQNGNDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAAGQPG 269
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293


                 ..
gi 17541560  270 GD 271
Cdd:NF038329 294 KD 295
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-58 3.31e-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. 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: 65.95  E-value: 3.31e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17541560      6 YLVSIAAAASTFAVLASIVSLVYLVNDVNNYYDDVTRNIENFKDDANTVWHQM 58
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 10-58 4.53e-12

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: 60.17  E-value: 4.53e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17541560    10 IAAAASTFAVLASIVSLVYLVNDVNNYYDDVTRNIENFKDDANTVWHQM 58
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 192-269 4.59e-08

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: 49.03  E-value: 4.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541560   192 GNDGRPGAPGAPGTRsvgrpgtagspgpqgppgqngndGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAAGQPG 269
Cdd:pfam01391   1 GPPGPPGPPGPPGPP-----------------------GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 142-271 6.30e-08

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: 53.76  E-value: 6.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  142 PAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPGRPGNDGRPGAPGAPGTRsvGRPGTAGSPGPQG 221
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA--GEKGPQGPRGETG 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17541560  222 PPGQNGNDGQPGNDGAPGQPGQPGPDGHPG--QPGNAGPPGTPGAAGQPGGD 271
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 161-271 1.53e-06

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: 49.52  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  161 DGQPGQDAMGGGQGAPGPQGPAGDNGQPGRPGNDGRPGAPGAPGtrSVGRPGTAGSPGPQGPpgqNGNDGQPGNDGAPGQ 240
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG--EKGPAGPQGEAGPQGP---AGKDGEAGAKGPAGE 190

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17541560  241 PGQPGPDGHPGQPGNAGPPGTPGAAGQPGGD 271
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-282 4.51e-06

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: 47.98  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560   63 PQGGKQRQVYESLFGRTKRQAAQCNCGANSAASNCPAGPPGPPGAPGEDGDHGLVGEDGTPGADGNLGVP--LSANGciv 140
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgkDGPRG--- 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  141 cPAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPGRPGNDGRPGAPGapgtrsvgrpgtagspgpq 220
Cdd:NF038329 264 -DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG------------------- 323

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541560  221 gppgqngNDGQPGNDGAPGQPGQPGPDGH--PGQPGNAgpPGTPGAAGQPGGDAAYCPCPSRSS 282
Cdd:NF038329 324 -------KDGLPGKDGKDGQPGKPAPKTPevPQKPDTA--PHTPKTPQIPGQSKDVTPAPQNPS 378
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 194-334 3.61e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  194 DGRPGAPGAPGTRSVGRPGTAGSPGPQGPPGQNGNDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPP----------GTPG 263
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPkhvavpdasdGGDG 668

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17541560  264 AAGQPGGDAAYCPCPSRSSVVRAQAAVARNRHVAARHRSVSRRKAVAARRSKARRVVAAKHRAVAKRHRAV 334
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 110-271 2.75e-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: 73.40  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  110 EDGDHGLVGEDGTPGADGNLGVPLSANgcivcPAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPG 189
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAG-----PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  190 RPGNDGRPGAPGAPGTRSVGRPGTAGSPGPQGPPGQNGNDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAAGQPG 269
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293


                 ..
gi 17541560  270 GD 271
Cdd:NF038329 294 KD 295
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-58 3.31e-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. 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: 65.95  E-value: 3.31e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17541560      6 YLVSIAAAASTFAVLASIVSLVYLVNDVNNYYDDVTRNIENFKDDANTVWHQM 58
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 10-58 4.53e-12

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: 60.17  E-value: 4.53e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17541560    10 IAAAASTFAVLASIVSLVYLVNDVNNYYDDVTRNIENFKDDANTVWHQM 58
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 192-269 4.59e-08

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: 49.03  E-value: 4.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541560   192 GNDGRPGAPGAPGTRsvgrpgtagspgpqgppgqngndGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAAGQPG 269
Cdd:pfam01391   1 GPPGPPGPPGPPGPP-----------------------GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 195-265 5.70e-08

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: 48.64  E-value: 5.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17541560   195 GRPGAPGAPGTRsvGRPGTAGSpgpqgppgqngnDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAA 265
Cdd:pfam01391   1 GPPGPPGPPGPP--GPPGPPGP------------PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 142-271 6.30e-08

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: 53.76  E-value: 6.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  142 PAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPGRPGNDGRPGAPGAPGTRsvGRPGTAGSPGPQG 221
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA--GEKGPQGPRGETG 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17541560  222 PPGQNGNDGQPGNDGAPGQPGQPGPDGHPG--QPGNAGPPGTPGAAGQPGGD 271
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 161-271 1.53e-06

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: 49.52  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  161 DGQPGQDAMGGGQGAPGPQGPAGDNGQPGRPGNDGRPGAPGAPGtrSVGRPGTAGSPGPQGPpgqNGNDGQPGNDGAPGQ 240
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG--EKGPAGPQGEAGPQGP---AGKDGEAGAKGPAGE 190

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17541560  241 PGQPGPDGHPGQPGNAGPPGTPGAAGQPGGD 271
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-282 4.51e-06

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: 47.98  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560   63 PQGGKQRQVYESLFGRTKRQAAQCNCGANSAASNCPAGPPGPPGAPGEDGDHGLVGEDGTPGADGNLGVP--LSANGciv 140
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgkDGPRG--- 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  141 cPAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPGRPGNDGRPGAPGapgtrsvgrpgtagspgpq 220
Cdd:NF038329 264 -DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG------------------- 323

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541560  221 gppgqngNDGQPGNDGAPGQPGQPGPDGH--PGQPGNAgpPGTPGAAGQPGGDAAYCPCPSRSS 282
Cdd:NF038329 324 -------KDGLPGKDGKDGQPGKPAPKTPevPQKPDTA--PHTPKTPQIPGQSKDVTPAPQNPS 378
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 186-262 5.64e-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: 5.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17541560   186 GQPGRPGNDGRPGAPGAPgtrsvgrpgtagspgpqgppgqngndGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTP 262
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPP--------------------------GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 194-334 3.61e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  194 DGRPGAPGAPGTRSVGRPGTAGSPGPQGPPGQNGNDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPP----------GTPG 263
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPkhvavpdasdGGDG 668

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17541560  264 AAGQPGGDAAYCPCPSRSSVVRAQAAVARNRHVAARHRSVSRRKAVAARRSKARRVVAAKHRAVAKRHRAV 334
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 184-268 4.07e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 38.83  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  184 DNGQPGRPGNDgRPGAPGAPGTRSVGRPGTAGSPgPQGPPGQNGNDGQPGNDGAPGqPGQPGPD-----GHPGQPGNAGP 258
Cdd:PHA03264 271 SGGSPAPPGDD-RPEAKPEPGPVEDGAPGRETGG-EGEGPEPAGRDGAAGGEPKPG-PPRPAPDadrpeGWPSLEAITFP 347

                         90
                 ....*....|
gi 17541560  259 PGTPGAAGQP 268
Cdd:PHA03264 348 PPTPATPAVP 357
uvrC PRK14666
excinuclease ABC subunit C; Provisional
 188-324 8.00e-03

excinuclease ABC subunit C; Provisional


Pssm-ID: 237782 [Multi-domain]  Cd Length: 694  Bit Score: 37.94  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541560  188 PGRPGNDGRPGAPGAPGTRSVGRPGTAGSPGPQGPPGQNGNDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAAGQ 267
Cdd:PRK14666 314 PWLPDTEGREGDDLAPTAVCTDAGLLPDTPLLPDAPEGSSDPVVPVAAATPVDASLPDVRTGTAPTSLANVSHADPAVAQ 393

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17541560  268 PGGDAAYCPCPSRSSvvraqaavarnrhvaarhRSVSRRKAVAARRSKARRVVAAKH 324
Cdd:PRK14666 394 PTQAATLAGAAPKGA------------------THLMLEETLADLRGGPVRIVPPRN 432
 
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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