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Conserved domains on  [gi|568926937|ref|XP_006538102|]
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collagen alpha-1(XXVII) chain isoform X9 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 694-974 2.96e-35

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 140.04  E-value: 2.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  694 GHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGR 773
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  774 PGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDtGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPG 853
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  854 FQGDKGshglpglpggrgKPGPLGKAGDKGslgfpgppgpegfpgDIGPPGDNGPEGMKGKPGarglpgppgqlgpegde 933
Cdd:NF038329  276 KDGERG------------PVGPAGKDGQNG---------------KDGLPGKDGKDGQNGKDG----------------- 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568926937  934 gpmgppgvpgLEGQPGRKGFPGRPGLDGSKGEPGDPGRPGP 974
Cdd:NF038329  312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 43-221 1.75e-13

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


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 70.08  E-value: 1.75e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937     43 DVDVLQRLGL-----SWTKAGGGRSPTPpgvipfpsGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFA 117
Cdd:smart00210    1 GQDLLQVFDLpslsfAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFA 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937    118 IRSRKHKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDS 190
Cdd:smart00210   73 IYDAQNVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQP 151

                           170       180       190
                    ....*....|....*....|....*....|.
gi 568926937    191 MLDPQGSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 269-567 2.45e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   269 GLGNLTRTPATLGArPVSRALAVTLAPAMPTKPLRTvhpdvsehSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP- 347
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPt 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   348 --AAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTV 419
Cdd:pfam05109  518 pnATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV 595

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   420 rpvqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSKSktTSWASKPVLARSSVPKTLQQTVLSQSPVSY-LGSQTLA 498
Cdd:pfam05109  596 ---------------------GETSPQANTTNHTLGGTSS--TPVVTSPPKNATSAVTTGQHNITSSSTSSMsLRPSSIS 652

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926937   499 PALPPLGVGNPRTMPPTRDSAlTPAGSKKFTGRETSKKTRQKSSPRKPEPlSPGKSARDASP--RDLTTKP 567
Cdd:pfam05109  653 ETLSPSTSDNSTSHMPLLTSA-HPTGGENITQVTPASTSTHHVSTSSPAP-RPGTTSQASGPgnSSTSTKP 721
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1000 9.09e-03

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: 39.89  E-value: 9.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568926937  959 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRG 1000
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG 156
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 694-974 2.96e-35

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 140.04  E-value: 2.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  694 GHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGR 773
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  774 PGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDtGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPG 853
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  854 FQGDKGshglpglpggrgKPGPLGKAGDKGslgfpgppgpegfpgDIGPPGDNGPEGMKGKPGarglpgppgqlgpegde 933
Cdd:NF038329  276 KDGERG------------PVGPAGKDGQNG---------------KDGLPGKDGKDGQNGKDG----------------- 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568926937  934 gpmgppgvpgLEGQPGRKGFPGRPGLDGSKGEPGDPGRPGP 974
Cdd:NF038329  312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 756-991 1.59e-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: 126.17  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  756 DGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPG 835
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  836 LKGDKGEQGVPGVSGDPGFQGDKGSHGLPGLPGGRGKpGPLGKAGDKGslgfpgppgpegfpgDIGPPGDNGPEGMKGKP 915
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPG---------------PTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926937  916 GARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRKGFPGRPGLDGSKGE---PGDPGRPGPVGEQGLMGFIGLVGEPG 991
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKdglPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-859 2.89e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 119.24  E-value: 2.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  640 GPPGPYGNPGPpgppgakgqKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGA 719
Cdd:NF038329  126 GPAGPAGEQGP---------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  720 KGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGS--DGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGL 797
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926937  798 PGPPGVLGLIGDTGALGPVGYPGPKGMKglmGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKG 859
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKD---GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 660-822 6.51e-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: 6.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  660 KGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGA--------KGYPGRQGFPGP 731
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpdgdPGPTGEDGPQGP 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  732 VGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTG 811
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332

                         170
                  ....*....|.
gi 568926937  812 ALGPVGYPGPK 822
Cdd:NF038329  333 KDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 659-802 2.79e-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: 98.05  E-value: 2.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  659 QKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHP-----GAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVG 733
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926937  734 DPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPG 802
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 808-1000 6.29e-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: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  808 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKGshglpglpggrgKPGPLGKAGDKGSLGF 887
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG------------EAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  888 PGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGdEGPMGPPGVPGLEGQPGRKGFPGRPGLDGSKGEPG 967
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568926937  968 DPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRG 1000
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 43-221 1.75e-13

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 70.08  E-value: 1.75e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937     43 DVDVLQRLGL-----SWTKAGGGRSPTPpgvipfpsGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFA 117
Cdd:smart00210    1 GQDLLQVFDLpslsfAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFA 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937    118 IRSRKHKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDS 190
Cdd:smart00210   73 IYDAQNVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQP 151

                           170       180       190
                    ....*....|....*....|....*....|.
gi 568926937    191 MLDPQGSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVC 182
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 745-801 2.56e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 2.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   745 GLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPP 801
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
699-979 1.63e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  699 PGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGlfglPGSDGERGLPGvpgkrGEMGRPGFPG 778
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTT----PAGNTGGTRPA-----GNQGATGPAQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  779 DFGERGPPGldgNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPglkgDKGEQGVPGVSG----DPGF 854
Cdd:COG5164    77 NQGGTTPAQ---NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP----SGGSTTPPGDGGstppGPGS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  855 QGDKGSHGLPGLPGGRGKPGPLGKAGDKGSlgfpGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEG 934
Cdd:COG5164   150 TGPGGSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568926937  935 PMGppgvpgleGQPGRKGFPGRPGLDGSKGEPGDPGRPGPVGEQG 979
Cdd:COG5164   226 GKT--------GPKDQRPKTNPIERRGPERPEAAALPAELTALEA 262
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 269-567 2.45e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   269 GLGNLTRTPATLGArPVSRALAVTLAPAMPTKPLRTvhpdvsehSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP- 347
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPt 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   348 --AAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTV 419
Cdd:pfam05109  518 pnATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV 595

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   420 rpvqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSKSktTSWASKPVLARSSVPKTLQQTVLSQSPVSY-LGSQTLA 498
Cdd:pfam05109  596 ---------------------GETSPQANTTNHTLGGTSS--TPVVTSPPKNATSAVTTGQHNITSSSTSSMsLRPSSIS 652

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926937   499 PALPPLGVGNPRTMPPTRDSAlTPAGSKKFTGRETSKKTRQKSSPRKPEPlSPGKSARDASP--RDLTTKP 567
Cdd:pfam05109  653 ETLSPSTSDNSTSHMPLLTSA-HPTGGENITQVTPASTSTHHVSTSSPAP-RPGTTSQASGPgnSSTSTKP 721
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 124-205 3.07e-04

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 42.41  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  124 KLQLGLQFLPGRTIIHLGPRqsvafdldVHDGRWHHLALELRGRTVTMVTACGQHrVPVPLPsRRDSMLDPQGSFLLGKV 203
Cdd:cd00110    57 RLVLRYDLGSGSLVLSSKTP--------LNDGQWHSVSVERNGRSVTLSVDGERV-VESGSP-GGSALLNLDGPLYLGGL 126


                  ..
gi 568926937  204 NP 205
Cdd:cd00110   127 PE 128
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 318-577 3.17e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 44.53  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  318 PLSPAKQSARKTPSPSSSASLANSTRVYRPAAAQP-RQITTTSPTKRSPTKP---SVSPLS-------VTPMKSPHATQK 386
Cdd:PLN03209  312 PLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPvTPEAPSPPIEEEPPQPkavVPRPLSpytayedLKPPTSPIPTPP 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  387 TGVPSFTKPVPPTQKPAPFTSYLAPSKASS---PTVRPVQKTFMTPRPPVPSPQPLRPTTGLSKK---FTNPTVAKSKSK 460
Cdd:PLN03209  392 SSSPASSKSVDAVAKPAEPDVVPSPGSASNvpeVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTaptGVSPSVSSTSSV 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  461 TTSWASKPVLARSSvpKTLQQTVLSQSPVSYLGSQTLAPALPPLGVGNPRTMPPTRDSALTPAGSkkfTGRETSKKTRQK 540
Cdd:PLN03209  472 PAVPDTAPATAATD--AAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGN---SAPPTALADEQH 546

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 568926937  541 SSPRKPEPLSPGKSARDASPrdlttkPSRPsTPALVL 577
Cdd:PLN03209  547 HAQPKPRPLSPYTMYEDLKP------PTSP-TPSPVL 576
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 124-206 1.10e-03

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 40.10  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   124 KLQLGLQFLPGRTIIHLGPRQsvafdldVHDGRWHHLALELRGRTVTMVTaCGQHRVPVPLPSRRDsMLDPQGSFLLGKV 203
Cdd:pfam02210   29 RLVLRYDLGSGPESLLSSGKN-------LNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPPGESL-LLNLNGPLYLGGL 99


                   ...
gi 568926937   204 NPR 206
Cdd:pfam02210  100 PPL 102
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1000 9.09e-03

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: 39.89  E-value: 9.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568926937  959 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRG 1000
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG 156
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 694-974 2.96e-35

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 140.04  E-value: 2.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  694 GHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGR 773
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  774 PGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDtGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPG 853
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  854 FQGDKGshglpglpggrgKPGPLGKAGDKGslgfpgppgpegfpgDIGPPGDNGPEGMKGKPGarglpgppgqlgpegde 933
Cdd:NF038329  276 KDGERG------------PVGPAGKDGQNG---------------KDGLPGKDGKDGQNGKDG----------------- 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568926937  934 gpmgppgvpgLEGQPGRKGFPGRPGLDGSKGEPGDPGRPGP 974
Cdd:NF038329  312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 756-991 1.59e-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: 126.17  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  756 DGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPG 835
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  836 LKGDKGEQGVPGVSGDPGFQGDKGSHGLPGLPGGRGKpGPLGKAGDKGslgfpgppgpegfpgDIGPPGDNGPEGMKGKP 915
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPG---------------PTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926937  916 GARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRKGFPGRPGLDGSKGE---PGDPGRPGPVGEQGLMGFIGLVGEPG 991
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKdglPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-859 2.89e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 119.24  E-value: 2.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  640 GPPGPYGNPGPpgppgakgqKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGA 719
Cdd:NF038329  126 GPAGPAGEQGP---------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  720 KGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGS--DGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGL 797
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926937  798 PGPPGVLGLIGDTGALGPVGYPGPKGMKglmGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKG 859
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKD---GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 660-822 6.51e-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: 6.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  660 KGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGA--------KGYPGRQGFPGP 731
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpdgdPGPTGEDGPQGP 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  732 VGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTG 811
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332

                         170
                  ....*....|.
gi 568926937  812 ALGPVGYPGPK 822
Cdd:NF038329  333 KDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 659-802 2.79e-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: 98.05  E-value: 2.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  659 QKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHP-----GAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVG 733
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926937  734 DPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPG 802
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 808-1000 6.29e-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: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  808 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKGshglpglpggrgKPGPLGKAGDKGSLGF 887
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG------------EAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  888 PGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGdEGPMGPPGVPGLEGQPGRKGFPGRPGLDGSKGEPG 967
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568926937  968 DPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRG 1000
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 43-221 1.75e-13

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 70.08  E-value: 1.75e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937     43 DVDVLQRLGL-----SWTKAGGGRSPTPpgvipfpsGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFA 117
Cdd:smart00210    1 GQDLLQVFDLpslsfAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFA 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937    118 IRSRKHKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDS 190
Cdd:smart00210   73 IYDAQNVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQP 151

                           170       180       190
                    ....*....|....*....|....*....|.
gi 568926937    191 MLDPQGSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVC 182
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 745-801 2.56e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 2.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   745 GLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPP 801
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 682-737 5.33e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 5.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568926937   682 GLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGP 737
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 712-768 1.49e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 1.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   712 GPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 768
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
699-979 1.63e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  699 PGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGlfglPGSDGERGLPGvpgkrGEMGRPGFPG 778
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTT----PAGNTGGTRPA-----GNQGATGPAQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  779 DFGERGPPGldgNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPglkgDKGEQGVPGVSG----DPGF 854
Cdd:COG5164    77 NQGGTTPAQ---NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP----SGGSTTPPGDGGstppGPGS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  855 QGDKGSHGLPGLPGGRGKPGPLGKAGDKGSlgfpGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEG 934
Cdd:COG5164   150 TGPGGSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568926937  935 PMGppgvpgleGQPGRKGFPGRPGLDGSKGEPGDPGRPGPVGEQG 979
Cdd:COG5164   226 GKT--------GPKDQRPKTNPIERRGPERPEAAALPAELTALEA 262
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 676-732 1.85e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 1.85e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   676 GNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPV 732
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 269-567 2.45e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   269 GLGNLTRTPATLGArPVSRALAVTLAPAMPTKPLRTvhpdvsehSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP- 347
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPt 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   348 --AAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTV 419
Cdd:pfam05109  518 pnATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV 595

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   420 rpvqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSKSktTSWASKPVLARSSVPKTLQQTVLSQSPVSY-LGSQTLA 498
Cdd:pfam05109  596 ---------------------GETSPQANTTNHTLGGTSS--TPVVTSPPKNATSAVTTGQHNITSSSTSSMsLRPSSIS 652

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926937   499 PALPPLGVGNPRTMPPTRDSAlTPAGSKKFTGRETSKKTRQKSSPRKPEPlSPGKSARDASP--RDLTTKP 567
Cdd:pfam05109  653 ETLSPSTSDNSTSHMPLLTSA-HPTGGENITQVTPASTSTHHVSTSSPAP-RPGTTSQASGPgnSSTSTKP 721
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 694-748 4.48e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 4.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568926937   694 GHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPG 748
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 685-741 7.39e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 7.39e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   685 GNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSR 741
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 688-742 1.50e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 1.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568926937   688 GPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRG 742
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 754-802 1.95e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.95e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568926937   754 GSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPG 802
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 901-975 2.20e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.20e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926937   901 GPPGDNGPEGMKGKPGARGLPGPPGQLGPegdegpmgppgvpglegqPGRKGFPGRPGLDGSKGEPGDPGRPGPV 975
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 751-802 3.23e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.23e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568926937   751 GLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPG 802
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 763-819 1.34e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   763 GVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYP 819
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 673-724 1.65e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568926937   673 GAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPG 724
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 673-723 1.77e-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: 1.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568926937   673 GAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYP 723
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
647-834 1.79e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  647 NPGPPGPPGAKGQKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQ 726
Cdd:COG5164    35 STRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  727 GFPGPVGDPGPKG--SRGYIGLPGLFG-LPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDG-----NPGEIGLP 798
Cdd:COG5164   115 GATGPPDDGGSTTppSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGsttppNKGETGTD 194

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568926937  799 GPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEP 834
Cdd:COG5164   195 IPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGP 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 775-829 2.75e-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: 39.78  E-value: 2.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568926937   775 GFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMG 829
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 124-205 3.07e-04

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 42.41  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  124 KLQLGLQFLPGRTIIHLGPRqsvafdldVHDGRWHHLALELRGRTVTMVTACGQHrVPVPLPsRRDSMLDPQGSFLLGKV 203
Cdd:cd00110    57 RLVLRYDLGSGSLVLSSKTP--------LNDGQWHSVSVERNGRSVTLSVDGERV-VESGSP-GGSALLNLDGPLYLGGL 126


                  ..
gi 568926937  204 NP 205
Cdd:cd00110   127 PE 128
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 318-577 3.17e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 44.53  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  318 PLSPAKQSARKTPSPSSSASLANSTRVYRPAAAQP-RQITTTSPTKRSPTKP---SVSPLS-------VTPMKSPHATQK 386
Cdd:PLN03209  312 PLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPvTPEAPSPPIEEEPPQPkavVPRPLSpytayedLKPPTSPIPTPP 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  387 TGVPSFTKPVPPTQKPAPFTSYLAPSKASS---PTVRPVQKTFMTPRPPVPSPQPLRPTTGLSKK---FTNPTVAKSKSK 460
Cdd:PLN03209  392 SSSPASSKSVDAVAKPAEPDVVPSPGSASNvpeVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTaptGVSPSVSSTSSV 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  461 TTSWASKPVLARSSvpKTLQQTVLSQSPVSYLGSQTLAPALPPLGVGNPRTMPPTRDSALTPAGSkkfTGRETSKKTRQK 540
Cdd:PLN03209  472 PAVPDTAPATAATD--AAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGN---SAPPTALADEQH 546

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 568926937  541 SSPRKPEPLSPGKSARDASPrdlttkPSRPsTPALVL 577
Cdd:PLN03209  547 HAQPKPRPLSPYTMYEDLKP------PTSP-TPSPVL 576
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 718-774 5.53e-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: 5.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   718 GAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRP 774
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 308-579 6.93e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 6.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   308 DVSEHSSSQTPLSPAKQSARKTPSPSSSASLANstrvyrpAAAQPRQITTTSPTKRSPTKP---SVSPLSVTPMKSPHAT 384
Cdd:pfam17823  108 DGAASRALAAAASSSPSSAAQSLPAAIAALPSE-------AFSAPRAAACRANASAAPRAAiaaASAPHAASPAPRTAAS 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   385 QKTGVPSFT-KPVPPTQKPAPFTSYLAP----SKASSPTVRPVQKTFMTP-RPPVPSPQPLRPTTGLSKKFTNPTVAKSK 458
Cdd:pfam17823  181 STTAASSTTaASSAPTTAASSAPATLTPargiSTAATATGHPAAGTALAAvGNSSPAAGTVTAAVGTVTPAALATLAAAA 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   459 SKTTSWA-----SKPVLARSSVPKTLQQTVLSQSPVSYLGSQTLAPAL-----PPLGVGNPRTMPPTRDSALTPAGSKKF 528
Cdd:pfam17823  261 GTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIqvstdQPVHNTAGEPTPSPSNTTLEPNTPKSV 340

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926937   529 TGRE----TSKKTRQKSSPRKPEPLSPGKSARDASPRDLTTKPS------RPSTPALVLAP 579
Cdd:pfam17823  341 ASTNlavvTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSpllptqGAAGPGILLAP 401
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 796-852 8.19e-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: 8.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568926937   796 GLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDP 852
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 124-206 1.10e-03

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 40.10  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937   124 KLQLGLQFLPGRTIIHLGPRQsvafdldVHDGRWHHLALELRGRTVTMVTaCGQHRVPVPLPSRRDsMLDPQGSFLLGKV 203
Cdd:pfam02210   29 RLVLRYDLGSGPESLLSSGKN-------LNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPPGESL-LLNLNGPLYLGGL 99


                   ...
gi 568926937   204 NPR 206
Cdd:pfam02210  100 PPL 102
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 781-835 1.24e-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: 1.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568926937   781 GERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPG 835
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 784-838 1.65e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 1.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568926937   784 GPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKG 838
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
261-400 1.96e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.07  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  261 LHPEPALLGLGNLTRT--PATLGARPVSRALAVTLAPAMPTKPLRTVHPDVSEHSSSQTPLSPAKQSARKTpspsssaSL 338
Cdd:PRK14971  350 LLVELTLIQLAQLTQKgdDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQP-------AG 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926937  339 ANSTRVYRPAAAQPRQITTTSPTKRSPTkPSVSPLSVTPMKSPHATqktgvPSFTKPVPPTQ 400
Cdd:PRK14971  423 TPPTVSVDPPAAVPVNPPSTAPQAVRPA-QFKEEKKIPVSKVSSLG-----PSTLRPIQEKA 478
PHA03247 PHA03247
large tegument protein UL36; Provisional
 294-573 2.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  294 APAMPTK-PLRTVHPDVSEHSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP--AAAQPRQITTTSPT---KRSPTK 367
Cdd:PHA03247 2610 GPAPPSPlPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPPqrpRRRAAR 2689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  368 PSVSPLS---------VTPMKSPHATQkTGVPSFTKPV-------PPTQKPAPFTSYLAPSKASSPTVRPVQKTFMTPRP 431
Cdd:PHA03247 2690 PTVGSLTsladpppppPTPEPAPHALV-SATPLPPGPAaarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  432 PVPSPQplrPTTGLSKKFTNPTVAKSKSKTTSWASKPVLARSSVPKTLQQTVL--SQSPVSYL----GSQTLAPALPPLG 505
Cdd:PHA03247 2769 PAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALppAASPAGPLppptSAQPTAPPPPPGP 2845

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  506 VGNPRTM-------------PPTRDSALTPAGSKKFTGRETSKKTRQKSS------PRKPEPLSPGKSARDASPRDLTTK 566
Cdd:PHA03247 2846 PPPSLPLggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfalpPDQPERPPQPQAPPPPQPQPQPPP 2925


                  ....*..
gi 568926937  567 PSRPSTP 573
Cdd:PHA03247 2926 PPQPQPP 2932
PHA03247 PHA03247
large tegument protein UL36; Provisional
 245-686 2.95e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  245 PQVGTLFPWDSGPAFALHPEPALLGLgnLTRTPATLGARPVSRAL-AVTLAPAMPTKPLRTVHPdvsehSSSQTPLSPAK 323
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHAL--VSATPLPPGPAAARQASpALPAAPAPPAVPAGPATP-----GGPARPARPPT 2762

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  324 QSARKTPSPSSSASLANSTRVYRPAAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTGVPSFTK--PVPPTQK 401
Cdd:PHA03247 2763 TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSaqPTAPPPP 2842

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  402 PAPFTSYLAPSKASSPTvRPVQKtfmtprppvpspqplRPTTGLskkfTNPTVAKSKSKTTSWASKPVLARSSVPKTLQQ 481
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPG-GDVRR---------------RPPSRS----PAAKPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  482 TVLSQSPVSYLGSQTLAPALPPLgvgNPRTMPPTRDSALTPAGSKKFTGRETSKKTRQKSSPRKPEPLSPGksaRDASPR 561
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPP---PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG---RVAVPR 2976

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  562 DLTTKPsRPSTPALVLAPAYLLSSSPQPTSSSFPFFHL-LGPTPfpmlmgPPGSKGDCGLPGPPGLPGLPGSPGARGPRG 640
Cdd:PHA03247 2977 FRVPQP-APSREAPASSTPPLTGHSLSRVSSWASSLALhEETDP------PPVSLKQTLWPPDDTEDSDADSLFDSDSER 3049

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 568926937  641 PPGPYGNPGPPGPPGAKGQKGDPGLSPGQAHDGAKGNMGLPGLSGN 686
Cdd:PHA03247 3050 SDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPPLSAN 3095
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 262-573 3.28e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  262 HPEPALLGLGNLTRTPATLGARPVSRALAVTLAPAMPTKPlrtVHP-DVSEHSSSQTPLSPAKQSARKTpspsssaslan 340
Cdd:PTZ00449  546 GGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDP---KHPkDPEEPKKPKRPRSAQRPTRPKS----------- 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  341 strvyrPAAAQPRQITTTSPTKRSPTKPSvSPLSVTPMKSPHATQKTGVPSFTKPvPPTQKPaPFtsylapskasSPTVR 420
Cdd:PTZ00449  612 ------PKLPELLDIPKSPKRPESPKSPK-RPPPPQRPSSPERPEGPKIIKSPKP-PKSPKP-PF----------DPKFK 672

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937  421 pvqktfmtprppvpspqplrpttglSKKFTNPTVAKSKSKTTswasKPVLARSSVPKTLQQTVLSQSPVSYLGSQTLAPA 500
Cdd:PTZ00449  673 -------------------------EKFYDDYLDAAAKSKET----KTTVVLDESFESILKETLPETPGTPFTTPRPLPP 723

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568926937  501 LPPLGVGNPRTmPPTRDSALTPAGSKKFTGREtSKKTRQKSSPrkPEPLSPGKSARDASPRDLTTKPSRPSTP 573
Cdd:PTZ00449  724 KLPRDEEFPFE-PIGDPDAEQPDDIEFFTPPE-EERTFFHETP--ADTPLPDILAEEFKEEDIHAETGEPDEA 792
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 946-991 4.08e-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: 4.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568926937   946 GQPGRKGFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPG 991
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
LamG smart00282
Laminin G domain;
124-205 4.70e-03

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 38.47  E-value: 4.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926937    124 KLQLGLQFLPGRTIIHLGPRQsvafdldVHDGRWHHLALELRGRTVTMVTAcGQHRVPVPLPSRRdSMLDPQGSFLLGKV 203
Cdd:smart00282   35 RLVLRYDLGSGPARLTSDPTP-------LNDGQWHRVAVERNGRSVTLSVD-GGNRVSGESPGGL-TILNLDGPLYLGGL 105


                    ..
gi 568926937    204 NP 205
Cdd:smart00282  106 PE 107
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 787-842 5.32e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 5.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568926937   787 GLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGE 842
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1000 9.09e-03

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: 39.89  E-value: 9.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568926937  959 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRG 1000
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG 156
 
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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