NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1900307711|ref|XP_036002453|]
View 

collagen alpha-1(XXV) chain isoform X12 [Fundulus heteroclitus]

Protein Classification

collagen-like domain-containing protein( domain architecture ID 1903237)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

PubMed:  21421911|15837519

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 215-508 3.54e-27

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: 115.00  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 215 GETGLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGIPGRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSsaagiK 294
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE-----K 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 295 GEPGEPGRSGQKGEpglpglpglpgiKGEPGFLGPQGEPGLPGLPGTKGEKGDHGPAGKGERGEIGPAGPKGSQGESGMP 374
Cdd:NF038329  192 GPQGPRGETGPAGE------------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 375 GPKGSKGDTGDKGDLGSVGPRGPPGQKGDRGAteiidyngnieealqrittitvtgppgppgpmgppgfKGDRGLPGLPG 454
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ-------------------------------------NGKDGLPGKDG 302

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1900307711 455 FDGERgykgskgdmGMPGASGEKGSTGLPGLPGVNGAKGDKGDPGLPGPQGPSI 508
Cdd:NF038329  303 KDGQN---------GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEV 347
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 534-670 1.33e-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: 76.48  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 534 GEPGLHGLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGT 613
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1900307711 614 PGLDGLPGLKGDKGDDgergekgEKGKKGKKGPKGEKGEQGAPGLDAPC-PLGPDGLP 670
Cdd:NF038329  206 QGPAGPAGPDGEAGPA-------GEDGPAGPAGDGQQGPDGDPGPTGEDgPQGPDGPA 256
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 215-508 3.54e-27

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: 115.00  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 215 GETGLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGIPGRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSsaagiK 294
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE-----K 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 295 GEPGEPGRSGQKGEpglpglpglpgiKGEPGFLGPQGEPGLPGLPGTKGEKGDHGPAGKGERGEIGPAGPKGSQGESGMP 374
Cdd:NF038329  192 GPQGPRGETGPAGE------------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 375 GPKGSKGDTGDKGDLGSVGPRGPPGQKGDRGAteiidyngnieealqrittitvtgppgppgpmgppgfKGDRGLPGLPG 454
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ-------------------------------------NGKDGLPGKDG 302

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1900307711 455 FDGERgykgskgdmGMPGASGEKGSTGLPGLPGVNGAKGDKGDPGLPGPQGPSI 508
Cdd:NF038329  303 KDGQN---------GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 345-614 2.26e-26

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: 112.69  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 345 KGDHGPAGKGERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPRGPPGQKGDRGATeiidyngnieealqrit 424
Cdd:NF038329  108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA----------------- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 425 titvtgppgppgpmgppgfkGDRGLPGLPGFDGERGYKGSKGDMGMPGASGEKGSTGLPGLPGVNGAKGDKGDPGLPGPQ 504
Cdd:NF038329  171 --------------------GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 505 GPSITGPPGPPGPHGPPGPMGPHGFPGPKGEPGLHGLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLA 584
Cdd:NF038329  231 GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310

                         250       260       270
                  ....*....|....*....|....*....|
gi 1900307711 585 GPKGDIGEKGAPGEPGPRGPYGLPGAAGTP 614
Cdd:NF038329  311 GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 170-397 2.66e-25

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: 109.22  E-value: 2.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 170 GDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHPGETGLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGI 249
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 250 PGRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSAAGIKGEPGEPGRSGQKGEPGLPGLPGLPGIKGEPGFLGP 329
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900307711 330 QGEPGLPGLPGTKGEKGDHGPAGK-GERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPRGP 397
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 143-377 2.66e-21

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: 97.28  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 143 QGDQGPRGLPGLPTLAALHSNQiltvkGDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHPGETGLMGL 222
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPP-----GPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 223 EGPQGPKGSLGPPGIPGIDGRKGDVGIP--GRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSA-AGIKGEPGE 299
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGkDGERGPVGP 285

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1900307711 300 PGRSGQKGEpglpglpglpgiKGEPGFLGPQGEPGLPGLPGTKGEKGDHGPAGKgergeigpAGPKGSQGESGMPGPK 377
Cdd:NF038329  286 AGKDGQNGK------------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL--------PGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 534-670 1.33e-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: 76.48  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 534 GEPGLHGLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGT 613
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1900307711 614 PGLDGLPGLKGDKGDDgergekgEKGKKGKKGPKGEKGEQGAPGLDAPC-PLGPDGLP 670
Cdd:NF038329  206 QGPAGPAGPDGEAGPA-------GEDGPAGPAGDGQQGPDGDPGPTGEDgPQGPDGPA 256
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 539-672 1.24e-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: 70.32  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 539 HGLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTPGLDG 618
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1900307711 619 LPGLKGDKGDDGERGEKGEKGKKGKKGPKGEKgeqGAPGLDAPCPLGPDGLPMP 672
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGED---GPAGPAGDGQQGPDGDPGP 243
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-300 6.32e-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: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 135 GPQGEKGDQGDQGPRGLPGLPTLAAlhsnqiltvKGDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHP 214
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDG---------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 215 GETGLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGIPGRDgipGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSaagik 294
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD---GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD----- 334


                  ....*.
gi 1900307711 295 GEPGEP 300
Cdd:NF038329  335 GQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 567-621 8.55e-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: 8.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900307711 567 GKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTPGLDGLPG 621
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 253-391 2.23e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 253 DGIPGAKGEKGEQGEKGDMGEDGPKGDTG----EKGDAGSSAAGIKGEPGEPGRSGQKGEPGLPGLPGLPGIKGEPGFLG 328
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASGlspeNTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900307711 329 PQGEPGL-PGLPGTKGEKGDHGPAGKGERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGS 391
Cdd:PHA03169  169 PSHEDSPeEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 218-273 8.35e-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: 37.86  E-value: 8.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900307711 218 GLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGIPGRDGIPGAKGEKGEQGEKGDMGE 273
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
170-381 1.54e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 170 GDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHPGETGLMGLEGPQGPKGSLGPPGIPGIDGRKG--DV 247
Cdd:COG5164    52 GSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppSG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 248 GIPGRDGI-------PGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSAAGIKGEPGEPGRSGQKGEPglpglpglpgi 320
Cdd:COG5164   132 GSTTPPGDggstppgPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGT----------- 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900307711 321 kGEPGFLGPQGEPGLPGLPGTKGEKGDHGPAgKGERGEIGPAGPKGSQGESGMPGPKGSKG 381
Cdd:COG5164   201 -PRQGPDGPVKKDDKNGKGNPPDDRGGKTGP-KDQRPKTNPIERRGPERPEAAALPAELTA 259
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 215-508 3.54e-27

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: 115.00  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 215 GETGLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGIPGRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSsaagiK 294
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE-----K 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 295 GEPGEPGRSGQKGEpglpglpglpgiKGEPGFLGPQGEPGLPGLPGTKGEKGDHGPAGKGERGEIGPAGPKGSQGESGMP 374
Cdd:NF038329  192 GPQGPRGETGPAGE------------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 375 GPKGSKGDTGDKGDLGSVGPRGPPGQKGDRGAteiidyngnieealqrittitvtgppgppgpmgppgfKGDRGLPGLPG 454
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ-------------------------------------NGKDGLPGKDG 302

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1900307711 455 FDGERgykgskgdmGMPGASGEKGSTGLPGLPGVNGAKGDKGDPGLPGPQGPSI 508
Cdd:NF038329  303 KDGQN---------GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 345-614 2.26e-26

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: 112.69  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 345 KGDHGPAGKGERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPRGPPGQKGDRGATeiidyngnieealqrit 424
Cdd:NF038329  108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA----------------- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 425 titvtgppgppgpmgppgfkGDRGLPGLPGFDGERGYKGSKGDMGMPGASGEKGSTGLPGLPGVNGAKGDKGDPGLPGPQ 504
Cdd:NF038329  171 --------------------GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 505 GPSITGPPGPPGPHGPPGPMGPHGFPGPKGEPGLHGLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLA 584
Cdd:NF038329  231 GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310

                         250       260       270
                  ....*....|....*....|....*....|
gi 1900307711 585 GPKGDIGEKGAPGEPGPRGPYGLPGAAGTP 614
Cdd:NF038329  311 GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 170-397 2.66e-25

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: 109.22  E-value: 2.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 170 GDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHPGETGLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGI 249
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 250 PGRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSAAGIKGEPGEPGRSGQKGEPGLPGLPGLPGIKGEPGFLGP 329
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900307711 330 QGEPGLPGLPGTKGEKGDHGPAGK-GERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPRGP 397
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 143-377 2.66e-21

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: 97.28  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 143 QGDQGPRGLPGLPTLAALHSNQiltvkGDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHPGETGLMGL 222
Cdd:NF038329  131 AGEQGPRGDRGETGPAGPAGPP-----GPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 223 EGPQGPKGSLGPPGIPGIDGRKGDVGIP--GRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSA-AGIKGEPGE 299
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGkDGERGPVGP 285

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1900307711 300 PGRSGQKGEpglpglpglpgiKGEPGFLGPQGEPGLPGLPGTKGEKGDHGPAGKgergeigpAGPKGSQGESGMPGPK 377
Cdd:NF038329  286 AGKDGQNGK------------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL--------PGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 534-670 1.33e-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: 76.48  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 534 GEPGLHGLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGT 613
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1900307711 614 PGLDGLPGLKGDKGDDgergekgEKGKKGKKGPKGEKGEQGAPGLDAPC-PLGPDGLP 670
Cdd:NF038329  206 QGPAGPAGPDGEAGPA-------GEDGPAGPAGDGQQGPDGDPGPTGEDgPQGPDGPA 256
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 539-672 1.24e-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: 70.32  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 539 HGLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTPGLDG 618
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1900307711 619 LPGLKGDKGDDGERGEKGEKGKKGKKGPKGEKgeqGAPGLDAPCPLGPDGLPMP 672
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGED---GPAGPAGDGQQGPDGDPGP 243
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-300 6.32e-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: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 135 GPQGEKGDQGDQGPRGLPGLPTLAAlhsnqiltvKGDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHP 214
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDG---------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 215 GETGLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGIPGRDgipGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSaagik 294
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD---GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD----- 334


                  ....*.
gi 1900307711 295 GEPGEP 300
Cdd:NF038329  335 GQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 567-621 8.55e-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: 8.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900307711 567 GKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTPGLDGLPG 621
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 576-627 1.32e-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: 42.87  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1900307711 576 GPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTPGLDGLPGLKGDKG 627
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 573-627 1.33e-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: 42.87  E-value: 1.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900307711 573 GTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTPGLDGLPGLKGDKG 627
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 558-614 1.60e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and 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: 42.87  E-value: 1.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1900307711 558 GLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTP 614
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 540-596 1.91e-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: 1.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1900307711 540 GLKGMRGEPGHKGDRGPLGLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAP 596
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 570-624 1.97e-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: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900307711 570 GIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAAGTPGLDGLPGLKG 624
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 253-391 2.23e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 253 DGIPGAKGEKGEQGEKGDMGEDGPKGDTG----EKGDAGSSAAGIKGEPGEPGRSGQKGEPGLPGLPGLPGIKGEPGFLG 328
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASGlspeNTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900307711 329 PQGEPGL-PGLPGTKGEKGDHGPAGKGERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGS 391
Cdd:PHA03169  169 PSHEDSPeEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 555-611 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: 40.17  E-value: 1.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1900307711 555 GPLGLPGASGLDGKPGIRGTDGPPGPAGLAGPKGDIGEKGAPGEPGPRGPYGLPGAA 611
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 261-408 6.61e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 261 EKGEQGEKGDMGEDGPKGDTGEKGDAGSSAAGIKGEPGEPGRSGQKGEPGLPGLPGLpgiKGEPGFLGPQGEPGLPGLPG 340
Cdd:PHA03169   77 EESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPAS---HSPPPSPPSHPGPHEPAPPE 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900307711 341 TKGEKGDHGP-AGKGERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPR--GPPGQKGDRGATE 408
Cdd:PHA03169  154 SHNPSPNQQPsSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDepGEPQSPTPQQAPS 224
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 218-273 8.35e-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: 37.86  E-value: 8.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900307711 218 GLMGLEGPQGPKGSLGPPGIPGIDGRKGDVGIPGRDGIPGAKGEKGEQGEKGDMGE 273
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
170-381 1.54e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 170 GDQGQAGPPGPPGPPGPPGPRGPPGDTGKDGPRGLPGLPGDPGHPGETGLMGLEGPQGPKGSLGPPGIPGIDGRKG--DV 247
Cdd:COG5164    52 GSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppSG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900307711 248 GIPGRDGI-------PGAKGEKGEQGEKGDMGEDGPKGDTGEKGDAGSSAAGIKGEPGEPGRSGQKGEPglpglpglpgi 320
Cdd:COG5164   132 GSTTPPGDggstppgPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGT----------- 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900307711 321 kGEPGFLGPQGEPGLPGLPGTKGEKGDHGPAgKGERGEIGPAGPKGSQGESGMPGPKGSKG 381
Cdd:COG5164   201 -PRQGPDGPVKKDDKNGKGNPPDDRGGKTGP-KDQRPKTNPIERRGPERPEAAALPAELTA 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 354-406 1.65e-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: 37.09  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1900307711 354 GERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPRGPPGQKGDRGA 406
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 227-282 3.92e-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: 3.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900307711 227 GPKGSLGPPGIPGIDGRKGDVGIPGRDGIPGAKGEKGEQGEKGDMGEDGPKGDTGE 282
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 350-404 5.21e-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: 35.55  E-value: 5.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900307711 350 PAGKGERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPRGPPGQKGDR 404
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 448-503 5.32e-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: 35.55  E-value: 5.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1900307711 448 GLPGLPGFDGERGYKGSKGDMGMPGASGEKGSTGLPGLPGVNGAKGDKGDPGLPGP 503
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 197-245 7.89e-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: 35.16  E-value: 7.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1900307711 197 GKDGPRGLPGLPGDPGHPGETGLMGLEGPQGPKGSLGPPGIPGIDGRKG 245
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 354-406 8.05e-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: 35.16  E-value: 8.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1900307711 354 GERGEIGPAGPKGSQGESGMPGPKGSKGDTGDKGDLGSVGPRGPPGQKGDRGA 406
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
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