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Conserved domains on  [gi|755506573|ref|XP_011248359|]
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collagen alpha-1(XXVII) chain isoform X6 [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 ...
 959-1224 8.70e-32

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: 130.03  E-value: 8.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  959 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSR 1038
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------------------------ERGEK 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1039 GLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPGs 1118
Cdd:NF038329  162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------PAGEDGPAG- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1119 qgpqgpVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDG 1198
Cdd:NF038329  229 ------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                         250       260
                  ....*....|....*....|....*.
gi 755506573 1199 EHGEKGQEGLKGEDGSPGPPGITGVP 1224
Cdd:NF038329  303 KDGQNGKDGLPGKDGKDGQPGKDGLP 328
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 728-974 3.53e-29

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: 122.32  E-value: 3.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  728 FPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLI 807
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  808 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGvpgvSGDPGFQGDKGSHGLPGLPGGRGKPGPLGKAGDKGslgf 887
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG---- 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  888 pgppgPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEgpmgppGVPGLEGQPGRKGFPGRPGLDGSKGEPG 967
Cdd:NF038329  267 -----EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN------GKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ....*..
gi 755506573  968 DPGRPGP 974
Cdd:NF038329  336 QPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 601-822 1.14e-22

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: 102.68  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  601 GPTPFPMLMGPPGSKGDcglPGPPGLPGLPGSPGARGPRGPPGPYGNPGPPGPPGAKGQKGDPGLSPGQAHDGAKGNMGL 680
Cdd:NF038329  123 GPAGPAGPAGEQGPRGD---RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  681 PGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPG--PEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGE 758
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755506573  759 RGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPK 822
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 43-221 2.39e-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: 69.69  E-value: 2.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573     43 DVDVLQRLGLSwTKAGGGRSPTppGVIPFPSGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFAIRSRK 122
Cdd:smart00210    1 GQDLLQVFDLP-SLSFAIRQVV--GPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573    123 HKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDSMLDPQ 195
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQPPIDTD 156

                           170       180
                    ....*....|....*....|....*.
gi 755506573    196 GSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  157 GIEVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 269-567 1.74e-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: 52.61  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   269 GLGNLTRTPATLGArPVSRALAVTLAPAMPTKPLRTvhpdvsehSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP- 347
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPt 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   348 --AAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTV 419
Cdd:pfam05109  518 pnATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV 595

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   420 rpvqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSKSktTSWASKPVLARSSVPKTLQQTVLSQSPVSY-LGSQTLA 498
Cdd:pfam05109  596 ---------------------GETSPQANTTNHTLGGTSS--TPVVTSPPKNATSAVTTGQHNITSSSTSSMsLRPSSIS 652

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755506573   499 PALPPLGVGNPRTMPPTRDSAlTPAGSKKFTGRETSKKTRQKSSPRKPEPlSPGKSARDASP--RDLTTKP 567
Cdd:pfam05109  653 ETLSPSTSDNSTSHMPLLTSA-HPTGGENITQVTPASTSTHHVSTSSPAP-RPGTTSQASGPgnSSTSTKP 721
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1224 8.70e-32

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: 130.03  E-value: 8.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  959 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSR 1038
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------------------------ERGEK 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1039 GLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPGs 1118
Cdd:NF038329  162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------PAGEDGPAG- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1119 qgpqgpVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDG 1198
Cdd:NF038329  229 ------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                         250       260
                  ....*....|....*....|....*.
gi 755506573 1199 EHGEKGQEGLKGEDGSPGPPGITGVP 1224
Cdd:NF038329  303 KDGQNGKDGLPGKDGKDGQPGKDGLP 328
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 728-974 3.53e-29

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: 122.32  E-value: 3.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  728 FPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLI 807
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  808 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGvpgvSGDPGFQGDKGSHGLPGLPGGRGKPGPLGKAGDKGslgf 887
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG---- 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  888 pgppgPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEgpmgppGVPGLEGQPGRKGFPGRPGLDGSKGEPG 967
Cdd:NF038329  267 -----EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN------GKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ....*..
gi 755506573  968 DPGRPGP 974
Cdd:NF038329  336 QPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 909-1217 2.03e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.85  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  909 EGMKGKPGARGLPGPPGQLGPEGDegpmgppgvpglegqPGRKGFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVG 988
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGD---------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  989 EPGIVGEKGdrgvmgppgAPgpkgsmghpgtpggignpgepgpwgppgsrGLPGMRGAKGHRGPRGPDGPAGEQGSKGLK 1068
Cdd:NF038329  181 EAGAKGPAG---------EK------------------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1069 GRVGPRGRPGQpGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPgsqgpqgpvgppgemGPKGPPGAVGEPGLPGD 1148
Cdd:NF038329  222 GEDGPAGPAGD-GQQGPDGDPGPTGEDG------------PQGPDGPA---------------GKDGPRGDRGEAGPDGP 273

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755506573 1149 SGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGP 1217
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-859 1.24e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.54  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  640 GPPGPYGNPGPpgppgakgqKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGA 719
Cdd:NF038329  126 GPAGPAGEQGP---------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  720 KGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGS--DGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGL 797
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755506573  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 ...
 808-1093 2.51e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 104.60  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  808 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKGshglpglpggrgKPGPLGKAGDKgslgf 887
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG------------EAGPQGPAGKD----- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  888 pgppgpegfpgdiGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRKGfPGRPGLDGSKGEPG 967
Cdd:NF038329  180 -------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTG 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  968 DPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSRGLPGMRGAK 1047
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------------------------ERGPVGPAGKDGQN 292

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 755506573 1048 GHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSG 1093
Cdd:NF038329  293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 601-822 1.14e-22

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: 102.68  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  601 GPTPFPMLMGPPGSKGDcglPGPPGLPGLPGSPGARGPRGPPGPYGNPGPPGPPGAKGQKGDPGLSPGQAHDGAKGNMGL 680
Cdd:NF038329  123 GPAGPAGPAGEQGPRGD---RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  681 PGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPG--PEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGE 758
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755506573  759 RGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPK 822
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 43-221 2.39e-13

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 69.69  E-value: 2.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573     43 DVDVLQRLGLSwTKAGGGRSPTppGVIPFPSGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFAIRSRK 122
Cdd:smart00210    1 GQDLLQVFDLP-SLSFAIRQVV--GPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573    123 HKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDSMLDPQ 195
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQPPIDTD 156

                           170       180
                    ....*....|....*....|....*.
gi 755506573    196 GSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  157 GIEVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 269-567 1.74e-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: 52.61  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   269 GLGNLTRTPATLGArPVSRALAVTLAPAMPTKPLRTvhpdvsehSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP- 347
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPt 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   348 --AAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTV 419
Cdd:pfam05109  518 pnATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV 595

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   420 rpvqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSKSktTSWASKPVLARSSVPKTLQQTVLSQSPVSY-LGSQTLA 498
Cdd:pfam05109  596 ---------------------GETSPQANTTNHTLGGTSS--TPVVTSPPKNATSAVTTGQHNITSSSTSSMsLRPSSIS 652

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755506573   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 ...
 745-801 1.60e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755506573   745 GLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPP 801
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1042-1096 2.13e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755506573  1042 GMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKG 1096
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 682-737 3.12e-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: 3.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755506573   682 GLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGP 737
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
699-932 7.12e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  699 PGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSrgyiglpglfglPGSDGERGLPGVPGKRGEMGRPGFPG 778
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------AQNQGSTTPAGNTGGTRPAGNQGATG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  779 DFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDK 858
Cdd:COG5164    74 PAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPG 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755506573  859 GSHGLPGLPGGRGKPGPLGKAGDKGSlgfpGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGD 932
Cdd:COG5164   154 GSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDD 223
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
872-1087 1.80e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.79  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  872 KPGPLGKAGDKGSLGFPGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRK 951
Cdd:COG5164     8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  952 GFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVG-----EPGIVGEKGDRGVMGPPGAPGPKGSMGHPGTPGGIGNP 1026
Cdd:COG5164    88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755506573 1027 GEPGPWGPPGSRGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAG 1087
Cdd:COG5164   168 PGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 318-577 3.72e-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: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  318 PLSPAKQSARKTPSPSSSASLANSTRVYRPAAAQP-RQITTTSPTKRSPTKP---SVSPLS-------VTPMKSPHATQK 386
Cdd:PLN03209  312 PLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPvTPEAPSPPIEEEPPQPkavVPRPLSpytayedLKPPTSPIPTPP 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  387 TGVPSFTKPVPPTQKPAPFTSYLAPSKASS---PTVRPVQKTFMTPRPPVPSPQPLRPTTGLSKK---FTNPTVAKSKSK 460
Cdd:PLN03209  392 SSSPASSKSVDAVAKPAEPDVVPSPGSASNvpeVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTaptGVSPSVSSTSSV 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  461 TTSWASKPVLARSSvpKTLQQTVLSQSPVSYLGSQTLAPALPPLGVGNPRTMPPTRDSALTPAGSkkfTGRETSKKTRQK 540
Cdd:PLN03209  472 PAVPDTAPATAATD--AAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGN---SAPPTALADEQH 546

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 755506573  541 SSPRKPEPLSPGKSARDASPrdlttkPSRPsTPALVL 577
Cdd:PLN03209  547 HAQPKPRPLSPYTMYEDLKP------PTSP-TPSPVL 576
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 124-205 4.67e-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: 42.02  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  124 KLQLGLQFLPGRTIIHLGPRqsvafdldVHDGRWHHLALELRGRTVTMVTACGQHrVPVPLPsRRDSMLDPQGSFLLGKV 203
Cdd:cd00110    57 RLVLRYDLGSGSLVLSSKTP--------LNDGQWHSVSVERNGRSVTLSVDGERV-VESGSP-GGSALLNLDGPLYLGGL 126


                  ..
gi 755506573  204 NP 205
Cdd:cd00110   127 PE 128
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 124-206 1.76e-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: 39.71  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   124 KLQLGLQFLPGRTIIHLGPRQsvafdldVHDGRWHHLALELRGRTVTMVTaCGQHRVPVPLPSRRDsMLDPQGSFLLGKV 203
Cdd:pfam02210   29 RLVLRYDLGSGPESLLSSGKN-------LNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPPGESL-LLNLNGPLYLGGL 99


                   ...
gi 755506573   204 NPR 206
Cdd:pfam02210  100 PPL 102
PHA03169 PHA03169
hypothetical protein; Provisional
 1044-1221 8.05e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1044 RGAKGHRGPRGPDGPAGEQGSkglkgrvGPRGRPGQPGQQGAAGERGHSGAKGFLGIPGPSGPPGAKGLPGEPGSQGPQG 1123
Cdd:PHA03169   81 HGEKEERGQGGPSGSGSESVG-------SPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1124 PVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEK 1203
Cdd:PHA03169  154 SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEH 233

                         170
                  ....*....|....*...
gi 755506573 1204 GQEGLKGEDGSPGPPGIT 1221
Cdd:PHA03169  234 EDEPTEPEREGPPFPGHR 251
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1224 8.70e-32

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: 130.03  E-value: 8.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  959 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSR 1038
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------------------------ERGEK 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1039 GLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPGs 1118
Cdd:NF038329  162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------PAGEDGPAG- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1119 qgpqgpVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDG 1198
Cdd:NF038329  229 ------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                         250       260
                  ....*....|....*....|....*.
gi 755506573 1199 EHGEKGQEGLKGEDGSPGPPGITGVP 1224
Cdd:NF038329  303 KDGQNGKDGLPGKDGKDGQPGKDGLP 328
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 728-974 3.53e-29

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: 122.32  E-value: 3.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  728 FPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLI 807
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  808 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGvpgvSGDPGFQGDKGSHGLPGLPGGRGKPGPLGKAGDKGslgf 887
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG---- 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  888 pgppgPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEgpmgppGVPGLEGQPGRKGFPGRPGLDGSKGEPG 967
Cdd:NF038329  267 -----EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN------GKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ....*..
gi 755506573  968 DPGRPGP 974
Cdd:NF038329  336 QPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 909-1217 2.03e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.85  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  909 EGMKGKPGARGLPGPPGQLGPEGDegpmgppgvpglegqPGRKGFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVG 988
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGD---------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  989 EPGIVGEKGdrgvmgppgAPgpkgsmghpgtpggignpgepgpwgppgsrGLPGMRGAKGHRGPRGPDGPAGEQGSKGLK 1068
Cdd:NF038329  181 EAGAKGPAG---------EK------------------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1069 GRVGPRGRPGQpGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPgsqgpqgpvgppgemGPKGPPGAVGEPGLPGD 1148
Cdd:NF038329  222 GEDGPAGPAGD-GQQGPDGDPGPTGEDG------------PQGPDGPA---------------GKDGPRGDRGEAGPDGP 273

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755506573 1149 SGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGP 1217
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-859 1.24e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.54  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  640 GPPGPYGNPGPpgppgakgqKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGA 719
Cdd:NF038329  126 GPAGPAGEQGP---------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  720 KGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGS--DGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGL 797
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755506573  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 ...
 808-1093 2.51e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 104.60  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  808 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKGshglpglpggrgKPGPLGKAGDKgslgf 887
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG------------EAGPQGPAGKD----- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  888 pgppgpegfpgdiGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRKGfPGRPGLDGSKGEPG 967
Cdd:NF038329  180 -------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTG 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  968 DPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSRGLPGMRGAK 1047
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------------------------ERGPVGPAGKDGQN 292

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 755506573 1048 GHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSG 1093
Cdd:NF038329  293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 601-822 1.14e-22

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: 102.68  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  601 GPTPFPMLMGPPGSKGDcglPGPPGLPGLPGSPGARGPRGPPGPYGNPGPPGPPGAKGQKGDPGLSPGQAHDGAKGNMGL 680
Cdd:NF038329  123 GPAGPAGPAGEQGPRGD---RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  681 PGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPG--PEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGE 758
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755506573  759 RGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPK 822
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 43-221 2.39e-13

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 69.69  E-value: 2.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573     43 DVDVLQRLGLSwTKAGGGRSPTppGVIPFPSGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFAIRSRK 122
Cdd:smart00210    1 GQDLLQVFDLP-SLSFAIRQVV--GPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573    123 HKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDSMLDPQ 195
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQPPIDTD 156

                           170       180
                    ....*....|....*....|....*.
gi 755506573    196 GSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  157 GIEVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 269-567 1.74e-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: 52.61  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   269 GLGNLTRTPATLGArPVSRALAVTLAPAMPTKPLRTvhpdvsehSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP- 347
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPt 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   348 --AAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTV 419
Cdd:pfam05109  518 pnATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV 595

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   420 rpvqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSKSktTSWASKPVLARSSVPKTLQQTVLSQSPVSY-LGSQTLA 498
Cdd:pfam05109  596 ---------------------GETSPQANTTNHTLGGTSS--TPVVTSPPKNATSAVTTGQHNITSSSTSSMsLRPSSIS 652

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755506573   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 ...
 745-801 1.60e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755506573   745 GLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPP 801
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1042-1096 2.13e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755506573  1042 GMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKG 1096
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 682-737 3.12e-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: 3.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755506573   682 GLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGP 737
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
699-932 7.12e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  699 PGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSrgyiglpglfglPGSDGERGLPGVPGKRGEMGRPGFPG 778
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------AQNQGSTTPAGNTGGTRPAGNQGATG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  779 DFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDK 858
Cdd:COG5164    74 PAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPG 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755506573  859 GSHGLPGLPGGRGKPGPLGKAGDKGSlgfpGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGD 932
Cdd:COG5164   154 GSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDD 223
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 712-768 7.41e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 7.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755506573   712 GPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 768
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 676-732 9.95e-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: 41.33  E-value: 9.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755506573   676 GNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPV 732
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
872-1087 1.80e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.79  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  872 KPGPLGKAGDKGSLGFPGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRK 951
Cdd:COG5164     8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  952 GFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVG-----EPGIVGEKGDRGVMGPPGAPGPKGSMGHPGTPGGIGNP 1026
Cdd:COG5164    88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755506573 1027 GEPGPWGPPGSRGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAG 1087
Cdd:COG5164   168 PGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 694-748 2.18e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755506573   694 GHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPG 748
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 308-579 2.21e-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: 45.34  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   308 DVSEHSSSQTPLSPAKQSARKTPSPSSSASLANstrvyrpAAAQPRQITTTSPTKRSPTKP---SVSPLSVTPMKSPHAT 384
Cdd:pfam17823  108 DGAASRALAAAASSSPSSAAQSLPAAIAALPSE-------AFSAPRAAACRANASAAPRAAiaaASAPHAASPAPRTAAS 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   385 QKTGVPSFT-KPVPPTQKPAPFTSYLAP----SKASSPTVRPVQKTFMTP-RPPVPSPQPLRPTTGLSKKFTNPTVAKSK 458
Cdd:pfam17823  181 STTAASSTTaASSAPTTAASSAPATLTPargiSTAATATGHPAAGTALAAvGNSSPAAGTVTAAVGTVTPAALATLAAAA 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   459 SKTTSWA-----SKPVLARSSVPKTLQQTVLSQSPVSYLGSQTLAPAL-----PPLGVGNPRTMPPTRDSALTPAGSKKF 528
Cdd:pfam17823  261 GTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIqvstdQPVHNTAGEPTPSPSNTTLEPNTPKSV 340

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755506573   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 ...
 685-741 3.37e-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: 3.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755506573   685 GNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSR 741
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 318-577 3.72e-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: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  318 PLSPAKQSARKTPSPSSSASLANSTRVYRPAAAQP-RQITTTSPTKRSPTKP---SVSPLS-------VTPMKSPHATQK 386
Cdd:PLN03209  312 PLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPvTPEAPSPPIEEEPPQPkavVPRPLSpytayedLKPPTSPIPTPP 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  387 TGVPSFTKPVPPTQKPAPFTSYLAPSKASS---PTVRPVQKTFMTPRPPVPSPQPLRPTTGLSKK---FTNPTVAKSKSK 460
Cdd:PLN03209  392 SSSPASSKSVDAVAKPAEPDVVPSPGSASNvpeVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTaptGVSPSVSSTSSV 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  461 TTSWASKPVLARSSvpKTLQQTVLSQSPVSYLGSQTLAPALPPLGVGNPRTMPPTRDSALTPAGSkkfTGRETSKKTRQK 540
Cdd:PLN03209  472 PAVPDTAPATAATD--AAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGN---SAPPTALADEQH 546

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 755506573  541 SSPRKPEPLSPGKSARDASPrdlttkPSRPsTPALVL 577
Cdd:PLN03209  547 HAQPKPRPLSPYTMYEDLKP------PTSP-TPSPVL 576
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 124-205 4.67e-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: 42.02  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  124 KLQLGLQFLPGRTIIHLGPRqsvafdldVHDGRWHHLALELRGRTVTMVTACGQHrVPVPLPsRRDSMLDPQGSFLLGKV 203
Cdd:cd00110    57 RLVLRYDLGSGSLVLSSKTP--------LNDGQWHSVSVERNGRSVTLSVDGERV-VESGSP-GGSALLNLDGPLYLGGL 126


                  ..
gi 755506573  204 NP 205
Cdd:cd00110   127 PE 128
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 688-742 6.26e-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: 6.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755506573   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 7.93e-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: 7.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 755506573   754 GSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPG 802
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1156-1218 8.57e-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: 8.57e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755506573  1156 GPLGPPGEQGLIGQRGEPGlegdhgPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPP 1218
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPG------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1141-1196 1.23e-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: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755506573  1141 GEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGP 1196
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 751-802 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: 38.24  E-value: 1.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 755506573   751 GLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPG 802
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 124-206 1.76e-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: 39.71  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   124 KLQLGLQFLPGRTIIHLGPRQsvafdldVHDGRWHHLALELRGRTVTMVTaCGQHRVPVPLPSRRDsMLDPQGSFLLGKV 203
Cdd:pfam02210   29 RLVLRYDLGSGPESLLSSGKN-------LNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPPGESL-LLNLNGPLYLGGL 99


                   ...
gi 755506573   204 NPR 206
Cdd:pfam02210  100 PPL 102
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
966-1222 1.79e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  966 PGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGVMGPPGAPGPKGSMGHPGTPGGignpgePGPWGPPGSRGLPGMRG 1045
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGG------TRPAGNQGATGPAQNQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1046 AKGHRGPRGPDGPAGEQGSKGlkgRVGPRGRPGQPGQQGAAGERGHSGAKGFLGIPGPSGPPGAKGLPGEPGSQGPQGPV 1125
Cdd:COG5164    80 GTTPAQNQGGTRPAGNTGGTT---PAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGST 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1126 GPPGEMGPKGPPGAVGEPGLPGD--SGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDR-GDPGPDGEHGE 1202
Cdd:COG5164   157 TPPGDGGSTTPPGPGGSTTPPDDggSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRgGKTGPKDQRPK 236

                         250       260
                  ....*....|....*....|
gi 755506573 1203 KGQEGLKGEDGSPGPPGITG 1222
Cdd:COG5164   237 TNPIERRGPERPEAAALPAE 256
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 901-975 2.30e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 2.30e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755506573   901 GPPGDNGPEGMKGKPGARGLPGPPGQLGPegdegpmgppgvpglegqPGRKGFPGRPGLDGSKGEPGDPGRPGPV 975
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
261-400 2.41e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.07  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  261 LHPEPALLGLGNLTRT--PATLGARPVSRALAVTLAPAMPTKPLRTVHPDVSEHSSSQTPLSPAKQSARKTpspsssaSL 338
Cdd:PRK14971  350 LLVELTLIQLAQLTQKgdDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQP-------AG 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755506573  339 ANSTRVYRPAAAQPRQITTTSPTKRSPTkPSVSPLSVTPMKSPHATqktgvPSFTKPVPPTQ 400
Cdd:PRK14971  423 TPPTVSVDPPAAVPVNPPSTAPQAVRPA-QFKEEKKIPVSKVSSLG-----PSTLRPIQEKA 478
PHA03247 PHA03247
large tegument protein UL36; Provisional
 294-573 3.35e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  294 APAMPTK-PLRTVHPDVSEHSSSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP--AAAQPRQITTTSPT---KRSPTK 367
Cdd:PHA03247 2610 GPAPPSPlPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPPqrpRRRAAR 2689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  368 PSVSPLS---------VTPMKSPHATQkTGVPSFTKPV-------PPTQKPAPFTSYLAPSKASSPTVRPVQKTFMTPRP 431
Cdd:PHA03247 2690 PTVGSLTsladpppppPTPEPAPHALV-SATPLPPGPAaarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  432 PVPSPQplrPTTGLSKKFTNPTVAKSKSKTTSWASKPVLARSSVPKTLQQTVL--SQSPVSYL----GSQTLAPALPPLG 505
Cdd:PHA03247 2769 PAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALppAASPAGPLppptSAQPTAPPPPPGP 2845

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  506 VGNPRTM-------------PPTRDSALTPAGSKKFTGRETSKKTRQKSS------PRKPEPLSPGKSARDASPRDLTTK 566
Cdd:PHA03247 2846 PPPSLPLggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfalpPDQPERPPQPQAPPPPQPQPQPPP 2925


                  ....*..
gi 755506573  567 PSRPSTP 573
Cdd:PHA03247 2926 PPQPQPP 2932
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
647-834 3.56e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  647 NPGPPGPPGAKGQKGDPGLSPGQAHDGAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQ 726
Cdd:COG5164    35 STRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  727 GFPGPVGDPGPKG--SRGYIGLPGLFG-LPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDG-----NPGEIGLP 798
Cdd:COG5164   115 GATGPPDDGGSTTppSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGsttppNKGETGTD 194

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 755506573  799 GPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEP 834
Cdd:COG5164   195 IPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGP 230
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 262-573 3.72e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  262 HPEPALLGLGNLTRTPATLGARPVSRALAVTLAPAMPTKPlrtVHP-DVSEHSSSQTPLSPAKQSARKTpspsssaslan 340
Cdd:PTZ00449  546 GGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDP---KHPkDPEEPKKPKRPRSAQRPTRPKS----------- 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  341 strvyrPAAAQPRQITTTSPTKRSPTKPSvSPLSVTPMKSPHATQKTGVPSFTKPvPPTQKPaPFtsylapskasSPTVR 420
Cdd:PTZ00449  612 ------PKLPELLDIPKSPKRPESPKSPK-RPPPPQRPSSPERPEGPKIIKSPKP-PKSPKP-PF----------DPKFK 672

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  421 pvqktfmtprppvpspqplrpttglSKKFTNPTVAKSKSKTTswasKPVLARSSVPKTLQQTVLSQSPVSYLGSQTLAPA 500
Cdd:PTZ00449  673 -------------------------EKFYDDYLDAAAKSKET----KTTVVLDESFESILKETLPETPGTPFTTPRPLPP 723

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755506573  501 LPPLGVGNPRTmPPTRDSALTPAGSKKFTGREtSKKTRQKSSPrkPEPLSPGKSARDASPRDLTTKPSRPSTP 573
Cdd:PTZ00449  724 KLPRDEEFPFE-PIGDPDAEQPDDIEFFTPPE-EERTFFHETP--ADTPLPDILAEEFKEEDIHAETGEPDEA 792
PHA03247 PHA03247
large tegument protein UL36; Provisional
 245-686 4.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  245 PQVGTLFPWDSGPAFALHPEPALLGLgnLTRTPATLGARPVSRAL-AVTLAPAMPTKPLRTVHPdvsehSSSQTPLSPAK 323
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHAL--VSATPLPPGPAAARQASpALPAAPAPPAVPAGPATP-----GGPARPARPPT 2762

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  324 QSARKTPSPSSSASLANSTRVYRPAAAQPRQITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTGVPSFTK--PVPPTQK 401
Cdd:PHA03247 2763 TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSaqPTAPPPP 2842

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  402 PAPFTSYLAPSKASSPTvRPVQKtfmtprppvpspqplRPTTGLskkfTNPTVAKSKSKTTSWASKPVLARSSVPKTLQQ 481
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPG-GDVRR---------------RPPSRS----PAAKPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  482 TVLSQSPVSYLGSQTLAPALPPLgvgNPRTMPPTRDSALTPAGSKKFTGRETSKKTRQKSSPRKPEPLSPGksaRDASPR 561
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPP---PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG---RVAVPR 2976

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573  562 DLTTKPsRPSTPALVLAPAYLLSSSPQPTSSSFPFFHL-LGPTPfpmlmgPPGSKGDCGLPGPPGLPGLPGSPGARGPRG 640
Cdd:PHA03247 2977 FRVPQP-APSREAPASSTPPLTGHSLSRVSSWASSLALhEETDP------PPVSLKQTLWPPDDTEDSDADSLFDSDSER 3049

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 755506573  641 PPGPYGNPGPPGPPGAKGQKGDPGLSPGQAHDGAKGNMGLPGLSGN 686
Cdd:PHA03247 3050 SDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPPLSAN 3095
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 763-817 4.57e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 4.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755506573   763 GVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVG 817
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 673-724 5.41e-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: 36.32  E-value: 5.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 755506573   673 GAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPG 724
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1038-1086 6.09e-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: 6.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 755506573  1038 RGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAA 1086
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 266-421 6.13e-03

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: 40.71  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   266 ALLGLGNLTRTPATLGAR--PVSRALAVTLAPAMPTkpLRTVHPDVSEHSSSQTPLSPAKQSARKTPSPSSSASLANSTR 343
Cdd:pfam17823  227 ALAAVGNSSPAAGTVTAAvgTVTPAALATLAAAAGT--VASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQ 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573   344 --VYRPAAAQPRQITTTSPTKrSPTKPSVSPLSVTPMKSPHATQKTGVPSFTKPVPPTQKPAPFTSYLAPSKASSPTVRP 421
Cdd:pfam17823  305 gpIIQVSTDQPVHNTAGEPTP-SPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQP 383
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1132-1182 6.15e-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: 6.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755506573  1132 GPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPV 1182
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
LamG smart00282
Laminin G domain;
124-205 7.36e-03

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 38.09  E-value: 7.36e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573    124 KLQLGLQFLPGRTIIHLGPRQsvafdldVHDGRWHHLALELRGRTVTMVTAcGQHRVPVPLPSRRDsMLDPQGSFLLGKV 203
Cdd:smart00282   35 RLVLRYDLGSGPARLTSDPTP-------LNDGQWHRVAVERNGRSVTLSVD-GGNRVSGESPGGLT-ILNLDGPLYLGGL 105


                    ..
gi 755506573    204 NP 205
Cdd:smart00282  106 PE 107
PHA03169 PHA03169
hypothetical protein; Provisional
 1044-1221 8.05e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1044 RGAKGHRGPRGPDGPAGEQGSkglkgrvGPRGRPGQPGQQGAAGERGHSGAKGFLGIPGPSGPPGAKGLPGEPGSQGPQG 1123
Cdd:PHA03169   81 HGEKEERGQGGPSGSGSESVG-------SPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755506573 1124 PVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEK 1203
Cdd:PHA03169  154 SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEH 233

                         170
                  ....*....|....*...
gi 755506573 1204 GQEGLKGEDGSPGPPGIT 1221
Cdd:PHA03169  234 EDEPTEPEREGPPFPGHR 251
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 775-829 8.35e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 8.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755506573   775 GFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMG 829
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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