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Conserved domains on  [gi|1039765076|ref|XP_017175213|]
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collagen alpha-1(XXIV) chain isoform X2 [Mus musculus]

Protein Classification

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 ...
 934-1164 3.38e-42

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: 161.23  E-value: 3.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP 1013
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1014 RGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGgpagSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPG 1093
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039765076 1094 EDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPK 1164
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1016 8.75e-31

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: 127.33  E-value: 8.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  724 GSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdigipGQNGP 803
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------------GPAGK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  804 EGPKGHLGNRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGlKGEVGDQGDIGKTGETGPVGLPGEVG 883
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  884 ITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgPLGLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAK 963
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERG---------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039765076  964 GEKGNQGKRGLPGLPGKAgSPGERGVQGKPGFQ-------GLPGSSGDVGPAGE-PGPRGL 1016
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKP-APKTPEVPQKPDTAphtpktpQIPGQSKDVTPAPQnPSNRGL 382
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-761 1.17e-23

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: 105.76  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  517 GPpgpmgipgpsgkRGPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGL 596
Cdd:NF038329   126 GP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  597 PGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPG--SKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGD 674
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  675 FGDRGPAGLDGSPGLVGGTGPPGFPGVTGSvgpagptgppgapgpmglSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKG 754
Cdd:NF038329   274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGK------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                   ....*..
gi 1039765076  755 NIGSPGP 761
Cdd:NF038329   336 QPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1144-1266 2.62e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 67.24  E-value: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1144 GPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEdstvlgppg 1223
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP--------- 187

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1039765076 1224 ppgePGPMGEQGETGEHGEEGYKGHMGVPGLRGATGQQGPPAP 1266
Cdd:NF038329   188 ----AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 41-230 7.06e-06

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 48.12  E-value: 7.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076    41 GIDILQQLGLGGrdvrYTSSVTAVPSSSWSTPlpqgvhltdfGVILTDNAYIESPLVNILPISLRQPLTVLIGLQSFKVN 120
Cdd:smart00210    1 GQDLLQVFDLPS----LSFAIRQVVGPEPGSP----------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKS 66

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076   121 NAFLFSIRN-NNRLQFGVQL--LPKKLIVH---VGGKQ-TVTF-NYSAHDERWHSFAITVDHHVISMFVECGK--RHFSG 190
Cdd:smart00210   67 RGVLFAIYDaQNVRQFGLEVdgRANTLLLRyqgVDGKQhTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEidSRPLD 146

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1039765076   191 EttSDVQTFDPHSVFTLGSINNSSAHFEGTVCQLEIMPST 230
Cdd:smart00210  147 R--PGQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 934-1164 3.38e-42

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: 161.23  E-value: 3.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP 1013
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1014 RGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGgpagSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPG 1093
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039765076 1094 EDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPK 1164
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1213 9.43e-41

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: 156.99  E-value: 9.43e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  959 GHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRglpgiaglpgemGVEGPPGTEGDS 1038
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDGEA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGaPGGSGLPGEDGDKGEMGLPGTAGPVGRPgqmgl 1118
Cdd:NF038329   183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPA----- 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1119 pgpegivgtpgqrGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPG 1198
Cdd:NF038329   257 -------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*
gi 1039765076 1199 PSGLPGPKGEKGYPG 1213
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 855-1121 1.26e-39

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: 153.52  E-value: 1.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  855 EGLKGEVGDqgdiGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplglpglvgARG 934
Cdd:NF038329   108 EGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------ERG 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  935 APGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPaGEPGPR 1014
Cdd:NF038329   160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPD 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1015 GLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKgdgGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGE 1094
Cdd:NF038329   239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD---GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315

                          250       260
                   ....*....|....*....|....*..
gi 1039765076 1095 DGDKGEMGLPGTAGPVGRPGQMGLPGP 1121
Cdd:NF038329   316 DGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 844-1098 2.21e-39

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: 152.75  E-value: 2.21e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  844 GRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKgvmgypgppgapgpmgp 923
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD----------------- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  924 lglpglvGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSpGERGVQGKPGFQGLPGSSG 1003
Cdd:NF038329   180 -------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1004 DVGPAGEPGPRGLPGIAGLPGEMGVEGPpgtEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLK 1083
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAGPDGPDGKDGE---RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                          250
                   ....*....|....*
gi 1039765076 1084 GAPGGSGLPGEDGDK 1098
Cdd:NF038329   329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1016 8.75e-31

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: 127.33  E-value: 8.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  724 GSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdigipGQNGP 803
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------------GPAGK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  804 EGPKGHLGNRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGlKGEVGDQGDIGKTGETGPVGLPGEVG 883
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  884 ITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgPLGLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAK 963
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERG---------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039765076  964 GEKGNQGKRGLPGLPGKAgSPGERGVQGKPGFQ-------GLPGSSGDVGPAGE-PGPRGL 1016
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKP-APKTPEVPQKPDTAphtpktpQIPGQSKDVTPAPQnPSNRGL 382
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1039-1263 4.89e-28

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: 118.85  E-value: 4.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGlpgEDGDKGEMGLPGTAGPVGRPGQMGL 1118
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---EAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1119 PGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSvGENGPKGARGTRGAVGPlglMGPEGEPGIPGYRGHQGQPG 1198
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGP---QGPDGPAGKDGPRGDRGEAG 269

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1199 PSGLPGPKGEKGYPGEDstvlgppgppGEPGPMGEQGETGEHGEEGYKGHMGVPGLRGATGQQGP 1263
Cdd:NF038329   270 PDGPDGKDGERGPVGPA----------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-951 4.24e-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: 109.99  E-value: 4.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  640 GSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDRGPAGLDGSPglvggtgppgfpgvtgsvgpagptgppGAPgp 719
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------------------------GPQ-- 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  720 mglsGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdiGIPG 799
Cdd:NF038329   168 ----GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD------------------------GEAG 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  800 QNGPEGPKGHLGnRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLP 879
Cdd:NF038329   220 PAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039765076  880 GEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplgLPGLVGARGAPGSPGPKGQRGPRGPD 951
Cdd:NF038329   299 GKDGKDGQNGKDGLPGKDGKDGQPGKDG------------------LPGKDGKDGQPGKPAPKTPEVPQKPD 352
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-761 1.17e-23

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: 105.76  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  517 GPpgpmgipgpsgkRGPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGL 596
Cdd:NF038329   126 GP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  597 PGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPG--SKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGD 674
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  675 FGDRGPAGLDGSPGLVGGTGPPGFPGVTGSvgpagptgppgapgpmglSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKG 754
Cdd:NF038329   274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGK------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                   ....*..
gi 1039765076  755 NIGSPGP 761
Cdd:NF038329   336 QPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1144-1266 2.62e-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: 67.24  E-value: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1144 GPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEdstvlgppg 1223
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP--------- 187

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1039765076 1224 ppgePGPMGEQGETGEHGEEGYKGHMGVPGLRGATGQQGPPAP 1266
Cdd:NF038329   188 ----AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1060-1115 2.29e-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: 45.95  E-value: 2.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076 1060 GEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQ 1115
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 41-230 7.06e-06

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 48.12  E-value: 7.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076    41 GIDILQQLGLGGrdvrYTSSVTAVPSSSWSTPlpqgvhltdfGVILTDNAYIESPLVNILPISLRQPLTVLIGLQSFKVN 120
Cdd:smart00210    1 GQDLLQVFDLPS----LSFAIRQVVGPEPGSP----------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKS 66

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076   121 NAFLFSIRN-NNRLQFGVQL--LPKKLIVH---VGGKQ-TVTF-NYSAHDERWHSFAITVDHHVISMFVECGK--RHFSG 190
Cdd:smart00210   67 RGVLFAIYDaQNVRQFGLEVdgRANTLLLRyqgVDGKQhTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEidSRPLD 146

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1039765076   191 EttSDVQTFDPHSVFTLGSINNSSAHFEGTVCQLEIMPST 230
Cdd:smart00210  147 R--PGQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
PHA03169 PHA03169
hypothetical protein; Provisional
 980-1132 1.06e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.58  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  980 KAGSPGERGvQGKPGFQGLPGSSGDVGPAGEPGPRGLPGiaGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPA--GSAG 1057
Cdd:PHA03169    80 RHGEKEERG-QGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAppESHN 156

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1058 ATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPvGRPGQMGLPGPEGIVGTPGQRG 1132
Cdd:PHA03169   157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQA 230
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
532-770 2.71e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.49  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  532 GPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLkghpglPGLRGEHGLPGLAGN 611
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRP------AGNQGATGPAQNQGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  612 IGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERG--TPGVRGKKGPKGRQG-FPGDFGDRGPAGLDGSPG 688
Cdd:COG5164     81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  689 LVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMGlSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPgiRGKS 768
Cdd:COG5164    161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGT-DIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ--RPKT 237


                   ..
gi 1039765076  769 GP 770
Cdd:COG5164    238 NP 239
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1153-1208 2.85e-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: 2.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076 1153 GPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGE 1208
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 580-634 2.38e-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: 2.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  580 GPPGLQGAKGLKGHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKG 634
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 722-771 4.98e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 4.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039765076  722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPS 771
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 979-1210 6.69e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.83  E-value: 6.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  979 GKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDS-GLQGEPGAKGDGGPAGSAG 1057
Cdd:cd21118    122 QGSGGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGPLNYGTNSqGAVAQPGYGTVRGNNQNSG 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1058 ATGEPgPRGEPGAPGEEGLQGKDGLKGAPG--GSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLG 1135
Cdd:cd21118    202 CTNPP-PSGSHESFSNSGGSSSSGSSGSQGshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGS 280

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1136 KKGDKGQVGPTGEAGSRGppGSVGENGPKGArgtrgavgplglmGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKG 1210
Cdd:cd21118    281 SSGGSNGWGGSSSSGGSG--GSGGGNKPECN-------------NPGNDVRMAGGGGSQGSKESSGSHGSNGGNG 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
642-908 1.75e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  642 PGEVGQLGPEGERGTPGVRGKKGPkgrqgfPGDFGDRGPAGLDGSPGLVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMG 721
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKP------AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSGQPGDPGPQGPSGPpgpegfpgdigiPGQN 801
Cdd:COG5164     80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGST------------PPGP 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  802 GPEGPKGHLGNRGPPGPPGLKGTQGEEGPIGPfgelGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGe 881
Cdd:COG5164    148 GSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPD- 222

                          250       260
                   ....*....|....*....|....*..
gi 1039765076  882 vGITGSIGEKGERGSPGPLGPQGEKGV 908
Cdd:COG5164    223 -DRGGKTGPKDQRPKTNPIERRGPERP 248
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 934-1164 3.38e-42

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: 161.23  E-value: 3.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP 1013
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1014 RGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGgpagSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPG 1093
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039765076 1094 EDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPK 1164
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1213 9.43e-41

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: 156.99  E-value: 9.43e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  959 GHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRglpgiaglpgemGVEGPPGTEGDS 1038
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDGEA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGaPGGSGLPGEDGDKGEMGLPGTAGPVGRPgqmgl 1118
Cdd:NF038329   183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPA----- 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1119 pgpegivgtpgqrGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPG 1198
Cdd:NF038329   257 -------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*
gi 1039765076 1199 PSGLPGPKGEKGYPG 1213
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 855-1121 1.26e-39

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: 153.52  E-value: 1.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  855 EGLKGEVGDqgdiGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplglpglvgARG 934
Cdd:NF038329   108 EGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------ERG 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  935 APGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPaGEPGPR 1014
Cdd:NF038329   160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPD 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1015 GLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKgdgGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGE 1094
Cdd:NF038329   239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD---GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315

                          250       260
                   ....*....|....*....|....*..
gi 1039765076 1095 DGDKGEMGLPGTAGPVGRPGQMGLPGP 1121
Cdd:NF038329   316 DGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 844-1098 2.21e-39

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: 152.75  E-value: 2.21e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  844 GRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKgvmgypgppgapgpmgp 923
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD----------------- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  924 lglpglvGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSpGERGVQGKPGFQGLPGSSG 1003
Cdd:NF038329   180 -------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1004 DVGPAGEPGPRGLPGIAGLPGEMGVEGPpgtEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLK 1083
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAGPDGPDGKDGE---RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                          250
                   ....*....|....*
gi 1039765076 1084 GAPGGSGLPGEDGDK 1098
Cdd:NF038329   329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1016 8.75e-31

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: 127.33  E-value: 8.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  724 GSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdigipGQNGP 803
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------------GPAGK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  804 EGPKGHLGNRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGlKGEVGDQGDIGKTGETGPVGLPGEVG 883
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  884 ITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgPLGLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAK 963
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERG---------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039765076  964 GEKGNQGKRGLPGLPGKAgSPGERGVQGKPGFQ-------GLPGSSGDVGPAGE-PGPRGL 1016
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKP-APKTPEVPQKPDTAphtpktpQIPGQSKDVTPAPQnPSNRGL 382
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1039-1263 4.89e-28

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: 118.85  E-value: 4.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGlpgEDGDKGEMGLPGTAGPVGRPGQMGL 1118
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---EAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1119 PGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSvGENGPKGARGTRGAVGPlglMGPEGEPGIPGYRGHQGQPG 1198
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGP---QGPDGPAGKDGPRGDRGEAG 269

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1199 PSGLPGPKGEKGYPGEDstvlgppgppGEPGPMGEQGETGEHGEEGYKGHMGVPGLRGATGQQGP 1263
Cdd:NF038329   270 PDGPDGKDGERGPVGPA----------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-951 4.24e-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: 109.99  E-value: 4.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  640 GSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDRGPAGLDGSPglvggtgppgfpgvtgsvgpagptgppGAPgp 719
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------------------------GPQ-- 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  720 mglsGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdiGIPG 799
Cdd:NF038329   168 ----GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD------------------------GEAG 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  800 QNGPEGPKGHLGnRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLP 879
Cdd:NF038329   220 PAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039765076  880 GEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplgLPGLVGARGAPGSPGPKGQRGPRGPD 951
Cdd:NF038329   299 GKDGKDGQNGKDGLPGKDGKDGQPGKDG------------------LPGKDGKDGQPGKPAPKTPEVPQKPD 352
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-761 1.17e-23

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: 105.76  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  517 GPpgpmgipgpsgkRGPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGL 596
Cdd:NF038329   126 GP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  597 PGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPG--SKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGD 674
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  675 FGDRGPAGLDGSPGLVGGTGPPGFPGVTGSvgpagptgppgapgpmglSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKG 754
Cdd:NF038329   274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGK------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                   ....*..
gi 1039765076  755 NIGSPGP 761
Cdd:NF038329   336 QPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1144-1266 2.62e-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: 67.24  E-value: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1144 GPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEdstvlgppg 1223
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP--------- 187

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1039765076 1224 ppgePGPMGEQGETGEHGEEGYKGHMGVPGLRGATGQQGPPAP 1266
Cdd:NF038329   188 ----AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1060-1115 2.29e-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: 45.95  E-value: 2.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076 1060 GEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQ 1115
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 970-1025 2.60e-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: 45.56  E-value: 2.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076  970 GKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGE 1025
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 41-230 7.06e-06

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 48.12  E-value: 7.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076    41 GIDILQQLGLGGrdvrYTSSVTAVPSSSWSTPlpqgvhltdfGVILTDNAYIESPLVNILPISLRQPLTVLIGLQSFKVN 120
Cdd:smart00210    1 GQDLLQVFDLPS----LSFAIRQVVGPEPGSP----------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKS 66

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076   121 NAFLFSIRN-NNRLQFGVQL--LPKKLIVH---VGGKQ-TVTF-NYSAHDERWHSFAITVDHHVISMFVECGK--RHFSG 190
Cdd:smart00210   67 RGVLFAIYDaQNVRQFGLEVdgRANTLLLRyqgVDGKQhTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEidSRPLD 146

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1039765076   191 EttSDVQTFDPHSVFTLGSINNSSAHFEGTVCQLEIMPST 230
Cdd:smart00210  147 R--PGQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 976-1032 8.52e-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: 8.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076  976 GLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPP 1032
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 934-988 8.77e-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: 8.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERG 988
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1009-1065 9.40e-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: 44.02  E-value: 9.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076 1009 GEPGPRGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPR 1065
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1039-1094 1.01e-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: 44.02  E-value: 1.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076 1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGE 1094
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 980-1132 1.06e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.58  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  980 KAGSPGERGvQGKPGFQGLPGSSGDVGPAGEPGPRGLPGiaGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPA--GSAG 1057
Cdd:PHA03169    80 RHGEKEERG-QGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAppESHN 156

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1058 ATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPvGRPGQMGLPGPEGIVGTPGQRG 1132
Cdd:PHA03169   157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQA 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1021-1075 1.10e-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: 44.02  E-value: 1.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1021 GLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEG 1075
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 979-1033 1.24e-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: 43.64  E-value: 1.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  979 GKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPG 1033
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 960-1114 1.49e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.81  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  960 HGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEmgveGPPGTEGDSG 1039
Cdd:PHA03169    81 HGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHN 156

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1040 LQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGlPGEDGDKGEMGLPGTAGPVGRPG 1114
Cdd:PHA03169   157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQA 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1030-1086 1.96e-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: 43.25  E-value: 1.96e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076 1030 GPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAP 1086
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1042-1096 2.23e-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: 43.25  E-value: 2.23e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1042 GEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDG 1096
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
532-770 2.71e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.49  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  532 GPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLkghpglPGLRGEHGLPGLAGN 611
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRP------AGNQGATGPAQNQGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  612 IGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERG--TPGVRGKKGPKGRQG-FPGDFGDRGPAGLDGSPG 688
Cdd:COG5164     81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  689 LVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMGlSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPgiRGKS 768
Cdd:COG5164    161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGT-DIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ--RPKT 237


                   ..
gi 1039765076  769 GP 770
Cdd:COG5164    238 NP 239
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1153-1208 2.85e-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: 2.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076 1153 GPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGE 1208
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 928-1123 3.97e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 3.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  928 GLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKaGSPGERGVQGKPGFQGLPGSSGDVGP 1007
Cdd:PHA03169    37 RGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVGSPTPSPSGSAEELA 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1008 AG-EPGPRGLPGIAGLPGEMGVEGPPGTEGDsglqGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAP 1086
Cdd:PHA03169   116 SGlSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPG 191

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039765076 1087 GGSGLPGEDGDKGEMGlPGTAGPVGRPGQMGLPGPEG 1123
Cdd:PHA03169   192 PPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNT 227
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 982-1036 4.61e-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: 42.10  E-value: 4.61e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  982 GSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEG 1036
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1048-1104 5.34e-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: 42.10  E-value: 5.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076 1048 GDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLP 1104
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 973-1027 5.78e-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: 42.10  E-value: 5.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  973 GLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMG 1027
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 934-1089 6.27e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.89  E-value: 6.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGfqglpgSSGDVGPAGEPGP 1013
Cdd:PHA03169    90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPA------PPESHNPSPNQQP 163

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076 1014 RGlpgiaGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPrgEPGAPGEEGLQGKDGLKGAPGGS 1089
Cdd:PHA03169   164 SS-----FLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD--EPGEPQSPTPQQAPSPNTQQAVE 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1138-1192 8.16e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 8.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1138 GDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRG 1192
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1156-1210 1.03e-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: 41.33  E-value: 1.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1156 GSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKG 1210
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 1009-1204 1.07e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1009 GEPGPRGLPGIAGlPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGG 1088
Cdd:PHA03169    82 GEKEERGQGGPSG-SGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPN 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1089 SGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDkgqvgptGEAGSRGPPGSVGENGPKGARG 1168
Cdd:PHA03169   161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-------GEPQSPTPQQAPSPNTQQAVEH 233

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039765076 1169 TRGAVGPlglmgPEGEPGIPGYRGHQ---GQPGPSGLPG 1204
Cdd:PHA03169   234 EDEPTEP-----EREGPPFPGHRSHSytvVGWKPSTRPG 267
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1003-1215 1.52e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1003 GDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGL 1082
Cdd:PRK07764   580 GDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAV 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1083 KGAP-GGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRgrlgkkgdkgqVGPTGEAGSRGPPGSVGEN 1161
Cdd:PRK07764   660 PDASdGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP-----------PAGQADDPAAQPPQAAQGA 728

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039765076 1162 GPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGED 1215
Cdd:PRK07764   729 SAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 964-1202 1.52e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 46.15  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  964 GEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP---RGLPGIAG------LPGEMGVEGPPGT 1034
Cdd:pfam09606   61 QQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMgqqMGGPGTASnllaslGRPQMPMGGAGFP 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1035 EGDSGLQGepGAKGDGGPAGSAGATGEPGPrGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPG 1114
Cdd:pfam09606  141 SQMSRVGR--MQPGGQAGGMMQPSSGQPGS-GTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGA 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1115 QM-------GLPGPEGIVGTPGQRGRLGKkgdkgQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPgi 1187
Cdd:pfam09606  218 QMgqqaqanGGMNPQQMGGAPNQVAMQQQ-----QPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ-- 290

                          250
                   ....*....|....*
gi 1039765076 1188 PGYRGHQGQPGPSGL 1202
Cdd:pfam09606  291 PGAMPNVMSIGDQNN 305
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1135-1189 2.01e-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: 40.55  E-value: 2.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1135 GKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPG 1189
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1063-1119 2.22e-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: 2.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076 1063 GPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLP 1119
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 580-634 2.38e-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: 2.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  580 GPPGLQGAKGLKGHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKG 634
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
LamG smart00282
Laminin G domain;
121-221 3.95e-04

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 41.94  E-value: 3.95e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076   121 NAFLFSIRNNNRLQF-GVQLLPKKLIVHV----GGKQTVTFNYSAHDERWHSFAITVDHHVISMFVEcGKRHFSGETTSD 195
Cdd:smart00282   12 NGLLLYAGSKGGGDYlALELRDGRLVLRYdlgsGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD-GGNRVSGESPGG 90

                            90       100
                    ....*....|....*....|....*.
gi 1039765076   196 VQTFDPHSVFTLGSINNSSAHFEGTV 221
Cdd:smart00282   91 LTILNLDGPLYLGGLPEDLKLPPLPV 116
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1162-1214 4.01e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 4.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039765076 1162 GPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGE 1214
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
PHA03169 PHA03169
hypothetical protein; Provisional
 1041-1201 4.27e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.19  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1041 QGEPGAKGDGGPAGSaGATGEPGPRGEPGAPGEEGLQGKDGLKGapggsglpGEDGDKGEMGLPGTAGPVGRPGQMGLPG 1120
Cdd:PHA03169    81 HGEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASGLSPENT--------SGSSPESPASHSPPPSPPSHPGPHEPAP 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1121 PEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPgsvgENGPKGARGTRGAVGPLGLMGPEgEPGIPGYRGHQGQPGPS 1200
Cdd:PHA03169   152 PESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPE----PDSPGPPQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSPN 226


                   .
gi 1039765076 1201 G 1201
Cdd:PHA03169   227 T 227
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 722-771 4.98e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 4.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039765076  722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPS 771
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 991-1046 5.03e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076  991 GKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGA 1046
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1028-1217 5.75e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 5.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1028 VEGPPGTEGDSGLQGEPGAKGDGG----PAGSAGATGEPGPRGEPGAPGEEGLQgkdglkGAPGGSGLPGEDGDKGEMGL 1103
Cdd:PRK07764   587 VVGPAPGAAGGEGPPAPASSGPPEeaarPAAPAAPAAPAAPAPAGAAAAPAEAS------AAPAPGVAAPEHHPKHVAVP 660

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1104 PGTAGPVGRPGQMGLPGPEGIVGTP---GQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGEN-GPKGARGTRGAVGPLGLM 1179
Cdd:PRK07764   661 DASDGGDGWPAKAGGAAPAAPPPAPapaAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPpQAAQGASAPSPAADDPVP 740

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039765076 1180 GPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDST 1217
Cdd:PRK07764   741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSP 778
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 979-1210 6.69e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.83  E-value: 6.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  979 GKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDS-GLQGEPGAKGDGGPAGSAG 1057
Cdd:cd21118    122 QGSGGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGPLNYGTNSqGAVAQPGYGTVRGNNQNSG 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1058 ATGEPgPRGEPGAPGEEGLQGKDGLKGAPG--GSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLG 1135
Cdd:cd21118    202 CTNPP-PSGSHESFSNSGGSSSSGSSGSQGshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGS 280

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1136 KKGDKGQVGPTGEAGSRGppGSVGENGPKGArgtrgavgplglmGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKG 1210
Cdd:cd21118    281 SSGGSNGWGGSSSSGGSG--GSGGGNKPECN-------------NPGNDVRMAGGGGSQGSKESSGSHGSNGGNG 340
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 927-1131 7.17e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  927 PGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGakgekgnqgkrglPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVG 1006
Cdd:PRK07764   601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAA-------------PAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1007 PAgepgprglPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGlkGAP 1086
Cdd:PRK07764   668 GW--------PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA--ADD 737

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039765076 1087 GGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQR 1131
Cdd:PRK07764   738 PVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1117-1173 1.11e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076 1117 GLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAV 1173
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 530-594 1.26e-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: 38.24  E-value: 1.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  530 KRGPRGIPGPHGNPGLPGLPGPKGPKGDPglspgqaasGEKGDPGLLGLVGPPGLQGAKGLKGHP 594
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPP---------GEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1114-1168 1.43e-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: 37.86  E-value: 1.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076 1114 GQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARG 1168
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
642-908 1.75e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  642 PGEVGQLGPEGERGTPGVRGKKGPkgrqgfPGDFGDRGPAGLDGSPGLVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMG 721
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKP------AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSGQPGDPGPQGPSGPpgpegfpgdigiPGQN 801
Cdd:COG5164     80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGST------------PPGP 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  802 GPEGPKGHLGNRGPPGPPGLKGTQGEEGPIGPfgelGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGe 881
Cdd:COG5164    148 GSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPD- 222

                          250       260
                   ....*....|....*....|....*..
gi 1039765076  882 vGITGSIGEKGERGSPGPLGPQGEKGV 908
Cdd:COG5164    223 -DRGGKTGPKDQRPKTNPIERRGPERP 248
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 589-645 1.90e-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: 37.47  E-value: 1.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076  589 GLKGHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEV 645
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 607-662 2.34e-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: 37.47  E-value: 2.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076  607 GLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERGTPGVRGK 662
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1108-1163 2.82e-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: 2.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076 1108 GPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGP 1163
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 958-1073 2.88e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.97  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076  958 GGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVG---PAGEPGPRgLPGIAGLPGEMGVEGPPgt 1034
Cdd:PRK14959   374 SGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPAtpaPSAAPSPR-VPWDDAPPAPPRSGIPP-- 450

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1039765076 1035 EGDSGLQGEPGAKgdGGPAGSAGATGEPGPRGEPGAPGE 1073
Cdd:PRK14959   451 RPAPRMPEASPVP--GAPDSVASASDAPPTLGDPSDTAE 487
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 592-647 3.90e-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: 36.70  E-value: 3.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076  592 GHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQ 647
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 925-975 4.66e-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: 36.70  E-value: 4.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039765076  925 GLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLP 975
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 622-678 5.78e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 5.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039765076  622 GLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDR 678
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1084-1143 6.64e-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: 6.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039765076 1084 GAPGGSGLPGEDGDKGEmglPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQV 1143
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGP---PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 604-658 7.55e-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: 7.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039765076  604 GLPGLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERGTPG 658
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 547-602 9.85e-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: 9.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039765076  547 GLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGLPGLRGE 602
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 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.
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