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Conserved domains on  [gi|767958596|ref|XP_011517447|]
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collagen alpha-1(XXVII) chain isoform X13 [Homo sapiens]

Protein Classification

collagen-like domain-containing protein; cuticular collagen family protein( domain architecture ID 1904221)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure; cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLFI super family cl02436
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 850-1048 3.29e-56

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


The actual alignment was detected with superfamily member pfam01410:

Pssm-ID: 470578  Cd Length: 233  Bit Score: 194.48  E-value: 3.29e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   850 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 927
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFE-TGETCIYPTKASip 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   928 --------------------KVEF---------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 977
Cdd:pfam01410   83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALLL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958596   978 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1048
Cdd:pfam01410  161 QGSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 558-787 2.58e-30

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: 125.40  E-value: 2.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  558 EGVQGLRGKpGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlpg 637
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  638 rdgqagqqgeqgDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtegrTGLPGNQGEPGSKGQP 717
Cdd:NF038329  184 ------------AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  718 GDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSRGDWG 787
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 372-638 3.87e-27

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 115.77  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  372 GQRGEPGLegdSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGY 451
Cdd:NF038329  117 GEKGEPGP---AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  452 QGQLGEmgvpgdpgppgtPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGhkgivgplgppgpkgeKGEQGEDGkaegpp 531
Cdd:NF038329  194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDG------ 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  532 gppgdrgPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGL 611
Cdd:NF038329  240 -------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312

                         250       260
                  ....*....|....*....|....*..
gi 767958596  612 QGLPGPRGVVGRQGLEGIAGPDGLPGR 638
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 33-270 1.28e-17

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: 86.88  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   33 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 112
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  113 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 192
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958596  193 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMGTPGEPGPQGPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRG 270
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 335-388 2.19e-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: 2.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767958596   335 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 388
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 850-1048 3.29e-56

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 194.48  E-value: 3.29e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   850 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 927
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFE-TGETCIYPTKASip 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   928 --------------------KVEF---------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 977
Cdd:pfam01410   83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALLL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958596   978 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1048
Cdd:pfam01410  161 QGSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 849-1049 1.85e-52

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 183.82  E-value: 1.85e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596    849 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 927
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596    928 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 977
Cdd:smart00038   81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958596    978 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1049
Cdd:smart00038  159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 558-787 2.58e-30

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: 125.40  E-value: 2.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  558 EGVQGLRGKpGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlpg 637
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  638 rdgqagqqgeqgDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtegrTGLPGNQGEPGSKGQP 717
Cdd:NF038329  184 ------------AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  718 GDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSRGDWG 787
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 544-787 4.49e-30

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: 124.63  E-value: 4.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  544 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGR 623
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  624 QGLEGIAGPDGlpgrdgqagqqgeqgddgdpgPMGPAGKRGNPGVAGLPGAQGPPGfkgesglPGQLGPPGKRGTEGRTG 703
Cdd:NF038329  197 RGETGPAGEQG---------------------PAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  704 LPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSR 783
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328


                  ....
gi 767958596  784 GDWG 787
Cdd:NF038329  329 GKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-752 5.56e-30

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: 124.63  E-value: 5.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  517 EKGEQGEDGKAegppGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGK 596
Cdd:NF038329  118 EKGEPGPAGPA----GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  597 QGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQG 676
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958596  677 PPGFKGESGLPgqlGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGP 752
Cdd:NF038329  273 PDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 372-638 3.87e-27

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 115.77  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  372 GQRGEPGLegdSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGY 451
Cdd:NF038329  117 GEKGEPGP---AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  452 QGQLGEmgvpgdpgppgtPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGhkgivgplgppgpkgeKGEQGEDGkaegpp 531
Cdd:NF038329  194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDG------ 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  532 gppgdrgPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGL 611
Cdd:NF038329  240 -------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312

                         250       260
                  ....*....|....*....|....*..
gi 767958596  612 QGLPGPRGVVGRQGLEGIAGPDGLPGR 638
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 336-594 6.70e-25

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.22  E-value: 6.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  336 GPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGE 415
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  416 dgppgppgvtgvRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGVPGDPGppgtpgpkgsRGSLGPTGAPGRMGAQGEPG 495
Cdd:NF038329  197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----------QGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  496 LAGYDGHKGIVGPLGPPGPKGEKGEQGEDGKAegppgppGDRGPvgdRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGH 575
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA-------GKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324

                         250
                  ....*....|....*....
gi 767958596  576 PGPRGWPGPKGSKGAEGPK 594
Cdd:NF038329  325 DGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 311-605 7.28e-21

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.90  E-value: 7.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  311 PgtkglpgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDG 390
Cdd:NF038329  128 A------------------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  391 LKGDRGDPGPDGEHGEKGQEGlmgedgppgppgvtgVRGPEGKSGKQGEKGRTGAKGAKGYQGQlgemgvpgdpgppgtp 470
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAG---------------EQGPAGPAGPDGEAGPAGEDGPAGPAGD---------------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  471 gpkGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGivgplgppgPKGEKGEQGEDGKAegppgppgdrgpvgdrGDRGEPG 550
Cdd:NF038329  233 ---GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------DRGEAGPDGPDGKD----------------GERGPVG 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596  551 DPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGR 605
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-579 1.62e-19

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: 92.66  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  249 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 328
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  329 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 406
Cdd:NF038329  176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  407 KGQEGLMGEDgppgppgvtgvrgpeGKSGKQGEKGRTGAKGakgyqgqlgemgvpgdpgppgtpgpkgSRGSLGPTGAPG 486
Cdd:NF038329  250 QGPDGPAGKD---------------GPRGDRGEAGPDGPDG---------------------------KDGERGPVGPAG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  487 RMGAQGEPGLAGYDghkgivgplgppgpkgekGEQGEDGKAegppgppgdrgpvgdrgdrGEPGDPGYPGQEGVQGLRGK 566
Cdd:NF038329  288 KDGQNGKDGLPGKD------------------GKDGQNGKD-------------------GLPGKDGKDGQPGKDGLPGK 330

                         330
                  ....*....|...
gi 767958596  567 PGQQGQPGHPGPR 579
Cdd:NF038329  331 DGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 33-270 1.28e-17

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: 86.88  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   33 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 112
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  113 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 192
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958596  193 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMGTPGEPGPQGPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRG 270
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 163-438 1.44e-17

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: 86.50  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  163 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 242
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  243 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGsrgfpgipgpsgppgtkglpgepgp 322
Cdd:NF038329  176 -----AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG------------------------- 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  323 qgpQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 402
Cdd:NF038329  226 ---PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767958596  403 EHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQG 438
Cdd:NF038329  303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 237-456 4.64e-17

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: 84.96  E-value: 4.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  237 GPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPSGPPGTKGL 316
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  317 PgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPlGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRG 396
Cdd:NF038329  206 Q------------------GPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  397 DPGPDGEHGEKGQEGLMGEDgppGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLG 456
Cdd:NF038329  267 EAGPDGPDGKDGERGPVGPA---GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 652-794 1.11e-16

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: 83.80  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  652 GDPGPMGPAGKRGnpgvaglpgAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGL 731
Cdd:NF038329  120 GEPGPAGPAGPAG---------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958596  732 FGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLP--GPKGDKGSRGDWGLQGPRGP 794
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-405 2.44e-15

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: 79.56  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  105 GPPGDNGPEGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGF 184
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  185 MGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGSMGhpgmpggmgtpgepgpqgppgsrgppgmRGAKGRRGPRGPDGPAG 264
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  265 EQGSRGlkgppgpqgrpgrpgqqgvagERGHLGSRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAV 344
Cdd:NF038329  249 PQGPDG---------------------PAGKDGPRGDRGEAGPD------------------------------GPDGKD 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958596  345 GEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHG 405
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 11-178 5.56e-12

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 69.16  E-value: 5.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   11 PGDLGVLGPIGYPGPKGMKGLMGSVGEPGLKGD--KGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGs 88
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG- 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   89 igfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGdegpmgppgapgLEGQPGRKGFPGRPGLDGVKG 168
Cdd:NF038329  279 --------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------LPGKDGKDGQPGKDGLPGKDG 332

                         170
                  ....*....|
gi 767958596  169 EPGDPGRPGP 178
Cdd:NF038329  333 KDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 689-819 8.44e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 62.23  E-value: 8.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  689 QLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGIL 768
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767958596  769 GPSGLPGPKGDKGSRGDWGLQGPRGPPGPRGRPGPPGPPGGPIQLQQDDLG 819
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 652-706 6.73e-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: 6.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   652 GDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPG 706
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
613-787 3.16e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  613 GLPGPRGVVGRQGLEGIAGPDGLPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 692
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  693 PGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLF--GPKGPPGDIGfkgiQGPRGpPGLMGKEGIVGPLGILGP 770
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG----STPPG-PGSTGPGGSTTPPGDGGS 164

                         170
                  ....*....|....*..
gi 767958596  771 SGLPGPKGDKGSRGDWG 787
Cdd:COG5164   165 TTPPGPGGSTTPPDDGG 181
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
381-637 1.03e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  381 GDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGV 460
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  461 PGDPGPPGTPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGiVGPLGPPgpkgekGEQGEDGKAEGPPGPPGDRGPV 540
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPP------GDGGSTPPGPGSTGPGGSTTPP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  541 GDRGDRGEPGDPGYPGQEGVQGlRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGvqGLQGLPGPRGV 620
Cdd:COG5164   160 GDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236

                         250
                  ....*....|....*..
gi 767958596  621 VGRQGLEGIAGPDGLPG 637
Cdd:COG5164   237 TNPIERRGPERPEAAAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 24-79 1.52e-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: 1.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958596    24 GPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 79
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 335-388 2.19e-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: 2.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767958596   335 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 388
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 850-1048 3.29e-56

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 194.48  E-value: 3.29e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   850 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 927
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFE-TGETCIYPTKASip 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   928 --------------------KVEF---------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 977
Cdd:pfam01410   83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALLL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958596   978 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1048
Cdd:pfam01410  161 QGSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 849-1049 1.85e-52

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 183.82  E-value: 1.85e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596    849 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 927
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596    928 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 977
Cdd:smart00038   81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958596    978 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1049
Cdd:smart00038  159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 558-787 2.58e-30

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: 125.40  E-value: 2.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  558 EGVQGLRGKpGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlpg 637
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  638 rdgqagqqgeqgDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtegrTGLPGNQGEPGSKGQP 717
Cdd:NF038329  184 ------------AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  718 GDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSRGDWG 787
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 544-787 4.49e-30

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: 124.63  E-value: 4.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  544 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGR 623
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  624 QGLEGIAGPDGlpgrdgqagqqgeqgddgdpgPMGPAGKRGNPGVAGLPGAQGPPGfkgesglPGQLGPPGKRGTEGRTG 703
Cdd:NF038329  197 RGETGPAGEQG---------------------PAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  704 LPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSR 783
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328


                  ....
gi 767958596  784 GDWG 787
Cdd:NF038329  329 GKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-752 5.56e-30

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: 124.63  E-value: 5.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  517 EKGEQGEDGKAegppGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGK 596
Cdd:NF038329  118 EKGEPGPAGPA----GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  597 QGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQG 676
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958596  677 PPGFKGESGLPgqlGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGP 752
Cdd:NF038329  273 PDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 372-638 3.87e-27

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 115.77  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  372 GQRGEPGLegdSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGY 451
Cdd:NF038329  117 GEKGEPGP---AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  452 QGQLGEmgvpgdpgppgtPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGhkgivgplgppgpkgeKGEQGEDGkaegpp 531
Cdd:NF038329  194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDG------ 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  532 gppgdrgPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGL 611
Cdd:NF038329  240 -------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312

                         250       260
                  ....*....|....*....|....*..
gi 767958596  612 QGLPGPRGVVGRQGLEGIAGPDGLPGR 638
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 336-594 6.70e-25

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.22  E-value: 6.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  336 GPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGE 415
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  416 dgppgppgvtgvRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGVPGDPGppgtpgpkgsRGSLGPTGAPGRMGAQGEPG 495
Cdd:NF038329  197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----------QGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  496 LAGYDGHKGIVGPLGPPGPKGEKGEQGEDGKAegppgppGDRGPvgdRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGH 575
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA-------GKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324

                         250
                  ....*....|....*....
gi 767958596  576 PGPRGWPGPKGSKGAEGPK 594
Cdd:NF038329  325 DGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 311-605 7.28e-21

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.90  E-value: 7.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  311 PgtkglpgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDG 390
Cdd:NF038329  128 A------------------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  391 LKGDRGDPGPDGEHGEKGQEGlmgedgppgppgvtgVRGPEGKSGKQGEKGRTGAKGAKGYQGQlgemgvpgdpgppgtp 470
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAG---------------EQGPAGPAGPDGEAGPAGEDGPAGPAGD---------------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  471 gpkGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGivgplgppgPKGEKGEQGEDGKAegppgppgdrgpvgdrGDRGEPG 550
Cdd:NF038329  233 ---GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------DRGEAGPDGPDGKD----------------GERGPVG 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596  551 DPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGR 605
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-579 1.62e-19

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: 92.66  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  249 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 328
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  329 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 406
Cdd:NF038329  176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  407 KGQEGLMGEDgppgppgvtgvrgpeGKSGKQGEKGRTGAKGakgyqgqlgemgvpgdpgppgtpgpkgSRGSLGPTGAPG 486
Cdd:NF038329  250 QGPDGPAGKD---------------GPRGDRGEAGPDGPDG---------------------------KDGERGPVGPAG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  487 RMGAQGEPGLAGYDghkgivgplgppgpkgekGEQGEDGKAegppgppgdrgpvgdrgdrGEPGDPGYPGQEGVQGLRGK 566
Cdd:NF038329  288 KDGQNGKDGLPGKD------------------GKDGQNGKD-------------------GLPGKDGKDGQPGKDGLPGK 330

                         330
                  ....*....|...
gi 767958596  567 PGQQGQPGHPGPR 579
Cdd:NF038329  331 DGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 33-270 1.28e-17

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: 86.88  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   33 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 112
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  113 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 192
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958596  193 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMGTPGEPGPQGPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRG 270
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 163-438 1.44e-17

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: 86.50  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  163 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 242
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  243 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGsrgfpgipgpsgppgtkglpgepgp 322
Cdd:NF038329  176 -----AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG------------------------- 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  323 qgpQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 402
Cdd:NF038329  226 ---PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767958596  403 EHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQG 438
Cdd:NF038329  303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 237-456 4.64e-17

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: 84.96  E-value: 4.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  237 GPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPSGPPGTKGL 316
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  317 PgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPlGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRG 396
Cdd:NF038329  206 Q------------------GPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  397 DPGPDGEHGEKGQEGLMGEDgppGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLG 456
Cdd:NF038329  267 EAGPDGPDGKDGERGPVGPA---GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 652-794 1.11e-16

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: 83.80  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  652 GDPGPMGPAGKRGnpgvaglpgAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGL 731
Cdd:NF038329  120 GEPGPAGPAGPAG---------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958596  732 FGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLP--GPKGDKGSRGDWGLQGPRGP 794
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-405 2.44e-15

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: 79.56  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  105 GPPGDNGPEGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGF 184
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  185 MGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGSMGhpgmpggmgtpgepgpqgppgsrgppgmRGAKGRRGPRGPDGPAG 264
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  265 EQGSRGlkgppgpqgrpgrpgqqgvagERGHLGSRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAV 344
Cdd:NF038329  249 PQGPDG---------------------PAGKDGPRGDRGEAGPD------------------------------GPDGKD 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958596  345 GEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHG 405
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 11-178 5.56e-12

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 69.16  E-value: 5.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   11 PGDLGVLGPIGYPGPKGMKGLMGSVGEPGLKGD--KGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGs 88
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG- 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596   89 igfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGdegpmgppgapgLEGQPGRKGFPGRPGLDGVKG 168
Cdd:NF038329  279 --------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------LPGKDGKDGQPGKDGLPGKDG 332

                         170
                  ....*....|
gi 767958596  169 EPGDPGRPGP 178
Cdd:NF038329  333 KDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 689-819 8.44e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 62.23  E-value: 8.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  689 QLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGIL 768
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767958596  769 GPSGLPGPKGDKGSRGDWGLQGPRGPPGPRGRPGPPGPPGGPIQLQQDDLG 819
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 652-706 6.73e-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: 6.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   652 GDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPG 706
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 670-724 1.75e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 1.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   670 GLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMG 724
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
613-787 3.16e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  613 GLPGPRGVVGRQGLEGIAGPDGLPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 692
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  693 PGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLF--GPKGPPGDIGfkgiQGPRGpPGLMGKEGIVGPLGILGP 770
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG----STPPG-PGSTGPGGSTTPPGDGGS 164

                         170
                  ....*....|....*..
gi 767958596  771 SGLPGPKGDKGSRGDWG 787
Cdd:COG5164   165 TTPPGPGGSTTPPDDGG 181
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 664-718 3.69e-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: 3.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   664 GNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPG 718
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 568-622 4.23e-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: 4.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   568 GQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVG 622
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 571-625 4.49e-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: 39.01  E-value: 4.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   571 GQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQG 625
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 562-618 4.76e-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: 39.01  E-value: 4.76e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958596   562 GLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPR 618
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 565-619 6.59e-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: 38.63  E-value: 6.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   565 GKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRG 619
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 691-745 7.20e-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: 38.63  E-value: 7.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   691 GPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKG 745
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 553-607 8.94e-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: 38.24  E-value: 8.94e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   553 GYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRG 607
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
381-637 1.03e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  381 GDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGV 460
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  461 PGDPGPPGTPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGiVGPLGPPgpkgekGEQGEDGKAEGPPGPPGDRGPV 540
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPP------GDGGSTPPGPGSTGPGGSTTPP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958596  541 GDRGDRGEPGDPGYPGQEGVQGlRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGvqGLQGLPGPRGV 620
Cdd:COG5164   160 GDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236

                         250
                  ....*....|....*..
gi 767958596  621 VGRQGLEGIAGPDGLPG 637
Cdd:COG5164   237 TNPIERRGPERPEAAAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-628 1.03e-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: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   574 GHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEG 628
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 682-738 1.04e-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: 1.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958596   682 GESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPP 738
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 667-722 1.25e-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: 1.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958596   667 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGE 722
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 24-79 1.52e-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: 1.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958596    24 GPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 79
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 709-764 1.85e-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: 37.47  E-value: 1.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958596   709 GEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGP 764
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 335-388 2.19e-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: 2.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767958596   335 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 388
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 700-754 2.26e-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: 37.09  E-value: 2.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   700 GRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPG 754
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 543-586 2.97e-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: 2.97e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767958596   543 RGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKG 586
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 544-600 3.41e-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: 3.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958596   544 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKA 600
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 36-88 3.58e-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: 3.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767958596    36 GEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGS 88
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 721-776 3.66e-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: 3.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958596   721 GEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGP 776
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 105-179 5.21e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 5.21e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   105 GPPGDNGPEGMKGKPGARGLPGPRGQLGPegdegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 179
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 583-637 7.51e-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: 7.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767958596   583 GPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGLPG 637
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 30-81 7.81e-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: 7.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767958596    30 GLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLG 81
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
 
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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