NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2294897769|gb|UWD62036|]
View 

MAG: Prophage endopeptidase tail [Bacteriophage sp.]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Prophage_tail super family cl23994
Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting ...
 134-381 1.42e-14

Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting as endopeptidases.


The actual alignment was detected with superfamily member pfam06605:

Pssm-ID: 451647  Cd Length: 253  Bit Score: 74.67  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 134 EIGINEISDKtRSITFDSQNGTkLEQLHSLMNQFDAEFIFRTelNRdgtlkkfVIDIYQQpdeshhgIGKVRGDVILYYQ 213
Cdd:pfam06605  38 EIGTVDSFPS-RTVENFGNNNA-LELLQQILEDFGGELRFDS--NR-------HVDIYKL-------VGKDTGATFRYGY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 214 NgLKGVQVASDKTQLFNAGYFFGQEGTNLESVEfeeknelgqvefyskKGNPVVYAPLSLEKYpsTLSNGDtDRWTRKDF 293
Cdd:pfam06605 100 N-LKDIEIETDTTSLATRIYGYGKDDLTIETIN---------------DGKEYLEDSPAVDKY--GISRKA-DPITDDRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 294 EteykDVNALKGYALRTIKQYAYPLLTYTVDIQ--SSFIENYKDINLGDTVKIINNNFrgGLALEARVSEMVISFDMPLN 371
Cdd:pfam06605 161 T----DPDSLKEYAKEQLQEYSKPDVSLTVTAAdlSKLTGEIEDFELGDYVRVIDEEL--GLDVKVRIVGITRYPFEPWN 234

                         250
                  ....*....|
gi 2294897769 372 NSVVFTNFRK 381
Cdd:pfam06605 235 TELTLGNKRR 244
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 492-544 6.77e-14

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: 66.75  E-value: 6.77e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2294897769 492 GRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVKGADGK 544
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-628 6.75e-13

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: 71.86  E-value: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 492 GRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPK---------GDQGIPGVKGADGKTQYTHIAYADTVSGSGFS 562
Cdd:NF038329  135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQgpagkdgeaGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2294897769 563 QTDTDKAFIGMYQDFNTTDSRNPQDYRWSK-WKGSDGRDGIPGKAGADGRTPYVHFAYADSGDGRTG 628
Cdd:NF038329  215 DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTgEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
 
Name Accession Description Interval E-value
Prophage_tail pfam06605
Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting ...
 134-381 1.42e-14

Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting as endopeptidases.


Pssm-ID: 429028  Cd Length: 253  Bit Score: 74.67  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 134 EIGINEISDKtRSITFDSQNGTkLEQLHSLMNQFDAEFIFRTelNRdgtlkkfVIDIYQQpdeshhgIGKVRGDVILYYQ 213
Cdd:pfam06605  38 EIGTVDSFPS-RTVENFGNNNA-LELLQQILEDFGGELRFDS--NR-------HVDIYKL-------VGKDTGATFRYGY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 214 NgLKGVQVASDKTQLFNAGYFFGQEGTNLESVEfeeknelgqvefyskKGNPVVYAPLSLEKYpsTLSNGDtDRWTRKDF 293
Cdd:pfam06605 100 N-LKDIEIETDTTSLATRIYGYGKDDLTIETIN---------------DGKEYLEDSPAVDKY--GISRKA-DPITDDRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 294 EteykDVNALKGYALRTIKQYAYPLLTYTVDIQ--SSFIENYKDINLGDTVKIINNNFrgGLALEARVSEMVISFDMPLN 371
Cdd:pfam06605 161 T----DPDSLKEYAKEQLQEYSKPDVSLTVTAAdlSKLTGEIEDFELGDYVRVIDEEL--GLDVKVRIVGITRYPFEPWN 234

                         250
                  ....*....|
gi 2294897769 372 NSVVFTNFRK 381
Cdd:pfam06605 235 TELTLGNKRR 244
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 492-544 6.77e-14

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: 66.75  E-value: 6.77e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2294897769 492 GRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVKGADGK 544
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-628 6.75e-13

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: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 492 GRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPK---------GDQGIPGVKGADGKTQYTHIAYADTVSGSGFS 562
Cdd:NF038329  135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQgpagkdgeaGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2294897769 563 QTDTDKAFIGMYQDFNTTDSRNPQDYRWSK-WKGSDGRDGIPGKAGADGRTPYVHFAYADSGDGRTG 628
Cdd:NF038329  215 DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTgEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 489-628 1.72e-12

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: 70.70  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 489 VSDGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVKGADGKtqythiayADTVSGSGFSQTDTDK 568
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE--------AGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 569 AFIGMYQDFNTTDSRNPQdyrwskwkGSDGRDGIPGKAGADGRTPYVHFAYADsGDGRTG 628
Cdd:NF038329  186 GPAGEKGPQGPRGETGPA--------GEQGPAGPAGPDGEAGPAGEDGPAGPA-GDGQQG 236
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-637 6.94e-12

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: 68.78  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 491 DGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVK---------------GADGKTQYTHIAYADT 555
Cdd:NF038329  149 AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRgetgpageqgpagpaGPDGEAGPAGEDGPAG 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 556 VSGSGFSQTDTDKAFIGMYQD-----FNTTDSRNPQDYRWSKW--KGSDGRDGIPGKAGADGRTPYVHFAYADSGDGRTG 628
Cdd:NF038329  229 PAGDGQQGPDGDPGPTGEDGPqgpdgPAGKDGPRGDRGEAGPDgpDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG 308


                  ....*....
gi 2294897769 629 fsltQDGTK 637
Cdd:NF038329  309 ----KDGLP 313
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-628 2.73e-11

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: 66.85  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 491 DGRNGVKGDKGDpGSQGPQGVQGERGLTGPAGPQGL---QGPKGDQGIPGVKGADGKtqythiayadtvsgsgfsqtDTD 567
Cdd:NF038329  221 AGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPagkDGPRGDRGEAGPDGPDGK--------------------DGE 279

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2294897769 568 KAFIGMyqdfNTTDSRNPQDYRWSK--WKGSDGRDGIPGKAGADGRTPYVHFAYADSGDGRTG 628
Cdd:NF038329  280 RGPVGP----AGKDGQNGKDGLPGKdgKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-615 2.25e-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: 64.16  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 491 DGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPqglQGPKGDQGIPGVKGADGKtqythiayadtvsgsgfsqtdtdkaf 570
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK---DGQNGKDGLPGKDGKDGQ-------------------------- 306

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2294897769 571 igmyqdfNTTDSRNPQDYRwskwKGSDGRDGIPGKAGADG-------RTPYV 615
Cdd:NF038329  307 -------NGKDGLPGKDGK----DGQPGKDGLPGKDGKDGqpgkpapKTPEV 347
put_anti_recept TIGR01665
phage minor structural protein, N-terminal region; This model represents the conserved ...
 136-376 5.18e-03

phage minor structural protein, N-terminal region; This model represents the conserved N-terminal region, typically from about residue 25 to about residue 350, of a family of uncharacterized phage proteins 500 to 1700 residues in length. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273743 [Multi-domain]  Cd Length: 317  Bit Score: 40.08  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 136 GINEISD-KTRSITFDsqnGTKLEQLHSLmNQFDAEFIFRTELNrDGTLKKFVIDIYQQpdeshhgIGKVRGDVILYYQN 214
Cdd:TIGR01665 104 KLGECSDiKTISITFY---QTSRNALQAI-AKLYKLSIFYQWGG-DNTITGKIVNLYKK-------IGSETGKEFEYGKN 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 215 gLKGVQVASDKTQLFNAGYFFGQEGTNLESVEFEEKNelgqvefyskKGNPVVYAPlslekypSTLSNGDTDRWTRKDFE 294
Cdd:TIGR01665 172 -LVGLNRKEDTKNIVTRLIPFGKGEGGEKGLTIESSN----------VGDEYIVDK-------DRQYKPNVDTTWVDGRY 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 295 TEYKDVNALKGYALRTIKQyAYPLLTYTVDIQS-SFIENYK---DINLGDTVKIINNNFRggLALEARVSEMVISFDMPL 370
Cdd:TIGR01665 234 TDETTLRAYAKQKLMTLKK-DMPKVSYEVTVADlENLSEYKslePIGIGDTVRLKHTDFN--IKVYARVIKVEYSPVTPK 310


                  ....*.
gi 2294897769 371 NNSVVF 376
Cdd:TIGR01665 311 QNSIEF 316
 
Name Accession Description Interval E-value
Prophage_tail pfam06605
Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting ...
 134-381 1.42e-14

Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting as endopeptidases.


Pssm-ID: 429028  Cd Length: 253  Bit Score: 74.67  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 134 EIGINEISDKtRSITFDSQNGTkLEQLHSLMNQFDAEFIFRTelNRdgtlkkfVIDIYQQpdeshhgIGKVRGDVILYYQ 213
Cdd:pfam06605  38 EIGTVDSFPS-RTVENFGNNNA-LELLQQILEDFGGELRFDS--NR-------HVDIYKL-------VGKDTGATFRYGY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 214 NgLKGVQVASDKTQLFNAGYFFGQEGTNLESVEfeeknelgqvefyskKGNPVVYAPLSLEKYpsTLSNGDtDRWTRKDF 293
Cdd:pfam06605 100 N-LKDIEIETDTTSLATRIYGYGKDDLTIETIN---------------DGKEYLEDSPAVDKY--GISRKA-DPITDDRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 294 EteykDVNALKGYALRTIKQYAYPLLTYTVDIQ--SSFIENYKDINLGDTVKIINNNFrgGLALEARVSEMVISFDMPLN 371
Cdd:pfam06605 161 T----DPDSLKEYAKEQLQEYSKPDVSLTVTAAdlSKLTGEIEDFELGDYVRVIDEEL--GLDVKVRIVGITRYPFEPWN 234

                         250
                  ....*....|
gi 2294897769 372 NSVVFTNFRK 381
Cdd:pfam06605 235 TELTLGNKRR 244
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 492-544 6.77e-14

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: 66.75  E-value: 6.77e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2294897769 492 GRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVKGADGK 544
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 492-543 6.91e-14

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: 66.75  E-value: 6.91e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2294897769 492 GRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVKGADG 543
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-628 6.75e-13

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: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 492 GRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPK---------GDQGIPGVKGADGKTQYTHIAYADTVSGSGFS 562
Cdd:NF038329  135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQgpagkdgeaGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2294897769 563 QTDTDKAFIGMYQDFNTTDSRNPQDYRWSK-WKGSDGRDGIPGKAGADGRTPYVHFAYADSGDGRTG 628
Cdd:NF038329  215 DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTgEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 489-628 1.72e-12

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: 70.70  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 489 VSDGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVKGADGKtqythiayADTVSGSGFSQTDTDK 568
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE--------AGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 569 AFIGMYQDFNTTDSRNPQdyrwskwkGSDGRDGIPGKAGADGRTPYVHFAYADsGDGRTG 628
Cdd:NF038329  186 GPAGEKGPQGPRGETGPA--------GEQGPAGPAGPDGEAGPAGEDGPAGPA-GDGQQG 236
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-637 6.94e-12

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: 68.78  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 491 DGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVK---------------GADGKTQYTHIAYADT 555
Cdd:NF038329  149 AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRgetgpageqgpagpaGPDGEAGPAGEDGPAG 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 556 VSGSGFSQTDTDKAFIGMYQD-----FNTTDSRNPQDYRWSKW--KGSDGRDGIPGKAGADGRTPYVHFAYADSGDGRTG 628
Cdd:NF038329  229 PAGDGQQGPDGDPGPTGEDGPqgpdgPAGKDGPRGDRGEAGPDgpDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG 308


                  ....*....
gi 2294897769 629 fsltQDGTK 637
Cdd:NF038329  309 ----KDGLP 313
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-628 2.73e-11

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: 66.85  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 491 DGRNGVKGDKGDpGSQGPQGVQGERGLTGPAGPQGL---QGPKGDQGIPGVKGADGKtqythiayadtvsgsgfsqtDTD 567
Cdd:NF038329  221 AGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPagkDGPRGDRGEAGPDGPDGK--------------------DGE 279

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2294897769 568 KAFIGMyqdfNTTDSRNPQDYRWSK--WKGSDGRDGIPGKAGADGRTPYVHFAYADSGDGRTG 628
Cdd:NF038329  280 RGPVGP----AGKDGQNGKDGLPGKdgKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-615 2.25e-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: 64.16  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 491 DGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPqglQGPKGDQGIPGVKGADGKtqythiayadtvsgsgfsqtdtdkaf 570
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK---DGQNGKDGLPGKDGKDGQ-------------------------- 306

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2294897769 571 igmyqdfNTTDSRNPQDYRwskwKGSDGRDGIPGKAGADG-------RTPYV 615
Cdd:NF038329  307 -------NGKDGLPGKDGK----DGQPGKDGLPGKDGKDGqpgkpapKTPEV 347
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 504-544 7.65e-10

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: 55.58  E-value: 7.65e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2294897769 504 GSQGPQGVQGERGLTGPAGPQGLQGPKGDQGIPGVKGADGK 544
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 491-534 2.70e-09

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 53.65  E-value: 2.70e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2294897769 491 DGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQGLQGPKGDQG 534
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 490-525 6.60e-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: 6.60e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2294897769 490 SDGRNGVKGDKGDPGSQGPQGVQGERGLTGPAGPQG 525
Cdd:pfam01391  20 PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
put_anti_recept TIGR01665
phage minor structural protein, N-terminal region; This model represents the conserved ...
 136-376 5.18e-03

phage minor structural protein, N-terminal region; This model represents the conserved N-terminal region, typically from about residue 25 to about residue 350, of a family of uncharacterized phage proteins 500 to 1700 residues in length. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273743 [Multi-domain]  Cd Length: 317  Bit Score: 40.08  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 136 GINEISD-KTRSITFDsqnGTKLEQLHSLmNQFDAEFIFRTELNrDGTLKKFVIDIYQQpdeshhgIGKVRGDVILYYQN 214
Cdd:TIGR01665 104 KLGECSDiKTISITFY---QTSRNALQAI-AKLYKLSIFYQWGG-DNTITGKIVNLYKK-------IGSETGKEFEYGKN 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 215 gLKGVQVASDKTQLFNAGYFFGQEGTNLESVEFEEKNelgqvefyskKGNPVVYAPlslekypSTLSNGDTDRWTRKDFE 294
Cdd:TIGR01665 172 -LVGLNRKEDTKNIVTRLIPFGKGEGGEKGLTIESSN----------VGDEYIVDK-------DRQYKPNVDTTWVDGRY 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294897769 295 TEYKDVNALKGYALRTIKQyAYPLLTYTVDIQS-SFIENYK---DINLGDTVKIINNNFRggLALEARVSEMVISFDMPL 370
Cdd:TIGR01665 234 TDETTLRAYAKQKLMTLKK-DMPKVSYEVTVADlENLSEYKslePIGIGDTVRLKHTDFN--IKVYARVIKVEYSPVTPK 310


                  ....*.
gi 2294897769 371 NNSVVF 376
Cdd:TIGR01665 311 QNSIEF 316
 
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