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Conserved domains on  [gi|1907067168|ref|XP_036013205|]
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collagen alpha-1(IX) chain isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 2.83e-57

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 191.03  E-value: 2.83e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168   50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168  130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907067168  210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-627 6.38e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 148.90  E-value: 6.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDG---EP 492
Cdd:NF038329  127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpagEQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 493 GPQGIPGAAGDQGQRGPPGETGPEGD-----RGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDV 567
Cdd:NF038329  207 GPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 568 GLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGASGPPWRewfpwsDGNPWSP 627
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK------DGQPGKP 340
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 2.83e-57

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 191.03  E-value: 2.83e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168   50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168  130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907067168  210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-627 6.38e-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: 148.90  E-value: 6.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDG---EP 492
Cdd:NF038329  127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpagEQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 493 GPQGIPGAAGDQGQRGPPGETGPEGD-----RGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDV 567
Cdd:NF038329  207 GPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 568 GLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGASGPPWRewfpwsDGNPWSP 627
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK------DGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-611 2.38e-36

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: 141.58  E-value: 2.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGI 497
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 498 PGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGpkgdtglPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPG 577
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907067168 578 IPGAKGVAGEKGNTGAPGKPGQLGSSGKPGASGP 611
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 427-622 2.44e-35

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: 138.50  E-value: 2.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 427 GMRGHKGAkgeiGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQ 506
Cdd:NF038329  109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 507 RGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPG--TKGEAGKPGPPGDVGLQGLPGVPGIPGAKGV 584
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907067168 585 AGEKGNTGAPGKPGQLGSSGKPGASGPPWREWFPWSDG 622
Cdd:NF038329  265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-580 2.03e-34

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: 136.19  E-value: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 320 GTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppGTTGLPGELGRVGPIGdpgkrgppgppgppgps 399
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER--------------GEKGPAGPQGEAGPQG----------------- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 400 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGiTGIVGD 479
Cdd:NF038329  175 ----------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGP 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 480 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAG 559
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|.
gi 1907067168 560 KPGPPGDVGLQGLPGVPGIPG 580
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-563 7.83e-24

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: 104.60  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 320 GTPGADGLTGPDGSPGSVGPRGQKGEPGvpgsrgfpgrgipgppgppgttglpgelgrvgpigdpgkrgppgppgppgps 399
Cdd:NF038329  174 GPAGKDGEAGAKGPAGEKGPQGPRGETG---------------------------------------------------- 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 400 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGD 479
Cdd:NF038329  202 ----------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 480 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPgspgpkGDTGLPGVDGRDGIPGMPGTKGEAG 559
Cdd:NF038329  265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------GKDGKDGQPGKDGLPGKDGKDGQPG 338


                  ....
gi 1907067168 560 KPGP 563
Cdd:NF038329  339 KPAP 342
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 496-552 1.22e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 51.34  E-value: 1.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 496 GIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
417-613 3.76e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 53.11  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 417 PGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEV--GDQGPPGPQGLR----GITGIVGDKGEKGARGFDG 490
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTppgpGSTGPGGSTTPPGDGGSTT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 491 EPGPQGIPGAAGDQGQRGPP--GETGPEGDRGIQGSRGiPGSPGPKGDtGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVG 568
Cdd:COG5164   167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG-PDGPVKKDD-KNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067168 569 LQGLPGVPGIPGAKGVAGEKGNTGApgkpgqlGSSGKPGASGPPW 613
Cdd:COG5164   245 PERPEAAALPAELTALEAENRAANP-------EPATKTIPETTTV 282
PHA03169 PHA03169
hypothetical protein; Provisional
 433-614 1.86e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 50.74  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 433 GAKGEIGEPGRQGHKGEEGDQGELG---EVGDQGPPGPQGL--RGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQR 507
Cdd:PHA03169   70 ESDTETAEESRHGEKEERGQGGPSGsgsESVGSPTPSPSGSaeELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 508 GPPGETGPEGDRGIQGSRGIPGSPGP---KGDTGLPGVDGRDGIPGMPGTKGEAG-----KPGPPGDVGLQGLPGVPGIP 579
Cdd:PHA03169  150 APPESHNPSPNQQPSSFLQPSHEDSPeepEPPTSEPEPDSPGPPQSETPTSSPPPqsppdEPGEPQSPTPQQAPSPNTQQ 229

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907067168 580 GAKGVAGEKGNTG-APGKPGQLGSSGKPGASGPPWR 614
Cdd:PHA03169  230 AVEHEDEPTEPEReGPPFPGHRSHSYTVVGWKPSTR 265
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 2.83e-57

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 191.03  E-value: 2.83e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168   50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168  130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907067168  210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-627 6.38e-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: 148.90  E-value: 6.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDG---EP 492
Cdd:NF038329  127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpagEQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 493 GPQGIPGAAGDQGQRGPPGETGPEGD-----RGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDV 567
Cdd:NF038329  207 GPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 568 GLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGASGPPWRewfpwsDGNPWSP 627
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK------DGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-611 2.38e-36

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: 141.58  E-value: 2.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGI 497
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 498 PGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGpkgdtglPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPG 577
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907067168 578 IPGAKGVAGEKGNTGAPGKPGQLGSSGKPGASGP 611
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 427-622 2.44e-35

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: 138.50  E-value: 2.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 427 GMRGHKGAkgeiGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQ 506
Cdd:NF038329  109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 507 RGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPG--TKGEAGKPGPPGDVGLQGLPGVPGIPGAKGV 584
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907067168 585 AGEKGNTGAPGKPGQLGSSGKPGASGPPWREWFPWSDG 622
Cdd:NF038329  265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-580 2.03e-34

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: 136.19  E-value: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 320 GTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppGTTGLPGELGRVGPIGdpgkrgppgppgppgps 399
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER--------------GEKGPAGPQGEAGPQG----------------- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 400 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGiTGIVGD 479
Cdd:NF038329  175 ----------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGP 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 480 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAG 559
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|.
gi 1907067168 560 KPGPPGDVGLQGLPGVPGIPG 580
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-563 7.83e-24

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: 104.60  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 320 GTPGADGLTGPDGSPGSVGPRGQKGEPGvpgsrgfpgrgipgppgppgttglpgelgrvgpigdpgkrgppgppgppgps 399
Cdd:NF038329  174 GPAGKDGEAGAKGPAGEKGPQGPRGETG---------------------------------------------------- 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 400 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGD 479
Cdd:NF038329  202 ----------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 480 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPgspgpkGDTGLPGVDGRDGIPGMPGTKGEAG 559
Cdd:NF038329  265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------GKDGKDGQPGKDGLPGKDGKDGQPG 338


                  ....
gi 1907067168 560 KPGP 563
Cdd:NF038329  339 KPAP 342
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 496-552 1.22e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 51.34  E-value: 1.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 496 GIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-512 1.36e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 51.34  E-value: 1.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067168 457 GEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGE 512
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 505-561 2.73e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 2.73e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 505 GQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKP 561
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 556-612 2.76e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 2.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 556 GEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGASGPP 612
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-541 4.46e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.80  E-value: 4.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067168 487 GFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPG 541
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 526-581 4.73e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.80  E-value: 4.73e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067168 526 GIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGA 581
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 541-597 5.22e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.80  E-value: 5.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 541 GVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKP 597
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 481-535 1.68e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 1.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067168 481 GEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKG 535
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 478-533 3.14e-07

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: 47.49  E-value: 3.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067168 478 GDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGP 533
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
417-613 3.76e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 53.11  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 417 PGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEV--GDQGPPGPQGLR----GITGIVGDKGEKGARGFDG 490
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTppgpGSTGPGGSTTPPGDGGSTT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 491 EPGPQGIPGAAGDQGQRGPP--GETGPEGDRGIQGSRGiPGSPGPKGDtGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVG 568
Cdd:COG5164   167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG-PDGPVKKDD-KNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067168 569 LQGLPGVPGIPGAKGVAGEKGNTGApgkpgqlGSSGKPGASGPPW 613
Cdd:COG5164   245 PERPEAAALPAELTALEAENRAANP-------EPATKTIPETTTV 282
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 502-558 6.68e-07

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: 46.33  E-value: 6.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 502 GDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEA 558
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 475-531 9.69e-07

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: 9.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 475 GIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSP 531
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 433-614 1.86e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 50.74  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 433 GAKGEIGEPGRQGHKGEEGDQGELG---EVGDQGPPGPQGL--RGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQR 507
Cdd:PHA03169   70 ESDTETAEESRHGEKEERGQGGPSGsgsESVGSPTPSPSGSaeELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 508 GPPGETGPEGDRGIQGSRGIPGSPGP---KGDTGLPGVDGRDGIPGMPGTKGEAG-----KPGPPGDVGLQGLPGVPGIP 579
Cdd:PHA03169  150 APPESHNPSPNQQPSSFLQPSHEDSPeepEPPTSEPEPDSPGPPQSETPTSSPPPqsppdEPGEPQSPTPQQAPSPNTQQ 229

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907067168 580 GAKGVAGEKGNTG-APGKPGQLGSSGKPGASGPPWR 614
Cdd:PHA03169  230 AVEHEDEPTEPEReGPPFPGHRSHSYTVVGWKPSTR 265
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-472 2.85e-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: 44.79  E-value: 2.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067168 418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRG 472
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 451-507 3.29e-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: 41.71  E-value: 3.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067168 451 GDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQR 507
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 487-604 6.08e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 46.21  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 487 GFDGEPGPQGIPG-AAGDQGQRGPPGETGPEGD---RGIQGSRGIPGSPGPkGDTGLPGVDGrDGIPGMPGTKGEAGKPG 562
Cdd:PRK14959  376 GGASAPSGSAAEGpASGGAATIPTPGTQGPQGTapaAGMTPSSAAPATPAP-SAAPSPRVPW-DDAPPAPPRSGIPPRPA 453

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907067168 563 PpgdvGLQGLPGVPGIPGAKGVAGEKGNT-GAPGKPGQLGSSG 604
Cdd:PRK14959  454 P----RMPEASPVPGAPDSVASASDAPPTlGDPSDTAEHTPSG 492
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 492-611 1.01e-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: 45.38  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 492 PGPQGIPGaagdqGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQG 571
Cdd:pfam09606 104 PGPGGPMG-----QQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNG 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907067168 572 LPGVPGIPGAKGVAgekGNTGAPGKPGQLGSSGKPGASGP 611
Cdd:pfam09606 179 GPGQGQAGGMNGGQ---QGPMGGQMPPQMGVPGMPGPADA 215
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 416-629 1.98e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhkGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQ 495
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPA--APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 496 GIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGV 575
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067168 576 PGIPGAKGVAGekgnTGAPGKPGQLGSSGKPGASGPPWREWFPWSDGNPWSPRH 629
Cdd:PRK07764  748 PPDPAGAPAQP----PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
PHA03169 PHA03169
hypothetical protein; Provisional
 424-597 3.34e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 424 GLPGMRGHKGAKGEIGEPGRQGHKG-------EEGDQGELGEVGDQGPPGPQGLRG--ITGIVGDKGEKGARGFDGEPGP 494
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELasglspeNTSGSSPESPASHSPPPSPPSHPGphEPAPPESHNPSPNQQPSSFLQP 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 495 QGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDtGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPG 574
Cdd:PHA03169  170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-GEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248

                         170       180
                  ....*....|....*....|...
gi 1907067168 575 VPGIPGAKgVAGEKGNTGAPGKP 597
Cdd:PHA03169  249 GHRSHSYT-VVGWKPSTRPGGVP 270
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 505-612 5.77e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.13  E-value: 5.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067168 505 GQRGPPGETGPEGD-RGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGtKGEAGKPGPPGDvGLQGLPGVPGIPgAKG 583
Cdd:PRK14959  376 GGASAPSGSAAEGPaSGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPA-PSAAPSPRVPWD-DAPPAPPRSGIP-PRP 452

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907067168 584 VAGEKGNTGAPGKPGQLGS-SGKPGASGPP 612
Cdd:PRK14959  453 APRMPEASPVPGAPDSVASaSDAPPTLGDP 482
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 416-465 9.22e-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: 37.47  E-value: 9.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907067168 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPP 465
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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