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Conserved domains on  [gi|1622831426|ref|XP_028687652|]
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collagen alpha-1(XXIV) chain isoform X3 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COLFI super family cl02436
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1501-1701 7.04e-50

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


The actual alignment was detected with superfamily member pfam01410:

Pssm-ID: 470578  Cd Length: 233  Bit Score: 177.15  E-value: 7.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1501 HSEEIFKTLNYLSNLLHSIKNPLGTRDNPARICKDLLNCEQKVSDGKYWIDPNLGCPSDAIEVFCNFSAGgQTCL----- 1575
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETG-ETCIyptka 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1576 ------------PPV-------SGTKLEFGVGK-------VQMNFLHLLSSEATHIITIHCLNTPRWTSTQTSGPGLPIG 1629
Cdd:pfam01410   80 siprknwwtkesKHVwfgefmnGGSQFSYGVDGvgpsvaaVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426 1630 FKGWNGQIFKV--NTLLEPKVLSDDCKIQDGSWHKATFLFHTQEPNQLPVIEVQKLPHLKTERKYYIESSSVCF 1701
Cdd:pfam01410  160 LQGSNDEEIRAegNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
909-1125 1.36e-42

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 162.77  E-value: 1.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  909 GHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGL 988
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  989 PGEPGLRGLQGDVGPPGEMGIEGPPGIEGESGL-----QGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGL 1063
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831426 1064 KGASGGRGLPGEDGEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIG 1125
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
706-992 3.67e-36

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 143.89  E-value: 3.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  706 NKGLPGIKGDkgeqgsaGELGEPGYPGDKGAVGLPGPQGMRGKPGPSGQTGDPglqgpsgppgpegfpgdiGIPGQNGPE 785
Cdd:NF038329   107 DEGLQQLKGD-------GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPP------------------GPQGERGEK 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  786 GPKGllgnrgppgppgLKGTQGEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGEVGT 865
Cdd:NF038329   162 GPAG------------PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  866 TGSiGEKGERGSPGPLGPQGEKGvmgypgppgvpgpigPLGLPGHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKG 945
Cdd:NF038329   230 AGD-GQQGPDGDPGPTGEDGPQG---------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1622831426  946 EKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEP 992
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1179-1414 6.81e-34

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 136.96  E-value: 6.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1179 GLSGLPGPKGEKGypgedstvlgppgPRGEPGPVGEQGERGEPGAEGYKGHVGVPGLRGATGQQGPPGEPGDQGEQGLKG 1258
Cdd:NF038329   117 GEKGEPGPAGPAG-------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1259 ERGCEGHKGKKGAPGPSGKAGIPGLQGLPGPKGIQGYHGADGILGNPGKvGPPGKQGLPGIRGSPGRTGLAGAPGPPGVK 1338
Cdd:NF038329   184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1339 GSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAG 1414
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
512-756 9.39e-33

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: 133.49  E-value: 9.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  512 RGPRGIPGPHGNPGLPGLPGPKGPKGDpgfspgqavPGEKGDQGLSGLMGPPGMQGDKGLKGHPGLPGLRGEQGIPGFAG 591
Cdd:NF038329   128 AGPAGEQGPRGDRGETGPAGPAGPPGP---------QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  592 NIGSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEagqlgpegergipGIRGKKGFKGRQGFPGDFGDRGPAGLDGSPGlv 671
Cdd:NF038329   199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG-- 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  672 ggtgppgfpgLRGSVGPVGPIGPAGIPGPVGLSGNKGLPGIKGDKGEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGP 751
Cdd:NF038329   264 ----------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333

                   ....*
gi 1622831426  752 SGQTG 756
Cdd:NF038329   334 DGQPG 338
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
41-227 2.59e-11

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: 64.30  E-value: 2.59e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426    41 GIDILHQLGLGGKdvrhSSSATAVPASSTPLPqgvhliesGVILKNDAYIETPFMKILPVNLGRPFTILTGLQSHRVNNA 120
Cdd:smart00210    1 GQDLLQVFDLPSL----SFAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRG 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426   121 FLFSIRNK-NRLQLGVQL--LPKKLVVHIRGK----QAVVF-NYSVHDEQWHLFAITIRNQSVSMFVECGKKYFNTETIS 192
Cdd:smart00210   69 VLFAIYDAqNVRQFGLEVdgRANTLLLRYQGVdgkqHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148
                           170       180       190
                    ....*....|....*....|....*....|....*
gi 1622831426   193 EVQTFDSNSVFTLGSMNNNSVHFEGIVCQLDIIPS 227
Cdd:smart00210  149 GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1140-1195 2.85e-05

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


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1140 GKTGPKGARGTRGAVGHLGLMGPDGEPGIPGYRGHQGQPGLSGLPGPKGEKGYPGE 1195
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1501-1701 7.04e-50

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


Pssm-ID: 460199  Cd Length: 233  Bit Score: 177.15  E-value: 7.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1501 HSEEIFKTLNYLSNLLHSIKNPLGTRDNPARICKDLLNCEQKVSDGKYWIDPNLGCPSDAIEVFCNFSAGgQTCL----- 1575
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETG-ETCIyptka 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1576 ------------PPV-------SGTKLEFGVGK-------VQMNFLHLLSSEATHIITIHCLNTPRWTSTQTSGPGLPIG 1629
Cdd:pfam01410   80 siprknwwtkesKHVwfgefmnGGSQFSYGVDGvgpsvaaVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426 1630 FKGWNGQIFKV--NTLLEPKVLSDDCKIQDGSWHKATFLFHTQEPNQLPVIEVQKLPHLKTERKYYIESSSVCF 1701
Cdd:pfam01410  160 LQGSNDEEIRAegNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1503-1702 3.15e-47

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


Pssm-ID: 197483  Cd Length: 232  Bit Score: 169.57  E-value: 3.15e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  1503 EEIFKTLNYLSNLLHSIKNPLGTRDNPARICKDLLNCEQKVSDGKYWIDPNLGCPSDAIEVFCNFsAGGQTCLPP----- 1577
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNF-ETGETCVSPspssi 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  1578 -------------------VSGTKLEFG------VGKVQMNFLHLLSSEATHIITIHCLNTPRWTSTQTSGPGLPIGFKG 1632
Cdd:smart00038   81 prktwysgkskhvwfgetmNGGFKFSYGdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRLRG 160
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831426  1633 WNGQIFK--VNTLLEPKVLSDDCKIQDGSWHKATFLFHTQEPNQLPVIEVQKLPHLKTERKYYIESSSVCFL 1702
Cdd:smart00038  161 SNDVELSaeGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
909-1125 1.36e-42

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 162.77  E-value: 1.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  909 GHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGL 988
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  989 PGEPGLRGLQGDVGPPGEMGIEGPPGIEGESGL-----QGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGL 1063
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831426 1064 KGASGGRGLPGEDGEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIG 1125
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
836-1102 3.23e-42

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 161.61  E-value: 3.23e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  836 EGLKGEVGDqGNIGKIGETGPVGLPGEVGTTGSIGEKGERGSPGPLGPQGEkgvmgypgppgvpgpigplglpghvgaRG 915
Cdd:NF038329   108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------------------------RG 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  916 PPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPhgligkTGNPGERGVQGKPGLQGLPGSTGDRGLPGEPGlR 995
Cdd:NF038329   160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-D 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  996 GLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGE---EGLQGKDGLKGASGGRGL 1072
Cdd:NF038329   233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQngkDGLPGKDGKDGQNGKDGL 312
                          250       260       270
                   ....*....|....*....|....*....|
gi 1622831426 1073 PGEDGEKGDMGLPGIIGPLGRSGQMGLPGP 1102
Cdd:NF038329   313 PGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
912-1145 3.29e-42

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 161.61  E-value: 3.29e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  912 GARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPhgligkTGNPGERGVQGKPGLQGLPGSTGDRGLPGE 991
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  992 PGLRGLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPaGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRG 1071
Cdd:NF038329   191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426 1072 LPGEDGEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPK 1145
Cdd:NF038329   270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
932-1170 1.24e-40

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 156.99  E-value: 1.24e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  932 DGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKpglqglPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEG 1011
Cdd:NF038329   107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP------AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1012 PPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGlKGASGGRGLPGEDGEKGDMGLPGIIGPL 1091
Cdd:NF038329   181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKD 259
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622831426 1092 GRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAVGHLGLMGPDGEPGIPG 1170
Cdd:NF038329   260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
825-1079 4.32e-40

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: 155.45  E-value: 4.32e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  825 GQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGEVGTTGSIGEKGERGSPGPLGPQGEKgvmgypgppgvpgpigp 904
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD----------------- 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  905 lglpGHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKtgnpGERGVQGKPGLQGLPGSTG 984
Cdd:NF038329   180 ----GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQG 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  985 DRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLrgePGAPGEEGLQGKDGLK 1064
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLP 328
                          250
                   ....*....|....*
gi 1622831426 1065 GASGGRGLPGEDGEK 1079
Cdd:NF038329   329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
780-1033 4.79e-37

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: 146.20  E-value: 4.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  780 GQNGPEGPKGllgnrgppgPPGLKGTQGEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGL 859
Cdd:NF038329   117 GEKGEPGPAG---------PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  860 PGEVGTTGSIGEKGERGSPGPLGPQGEKGvmgypgppgvpgpigplgLPGHVGARGPPGSQGpKGQRGPRGPDGLLGEQG 939
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------EAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  940 IQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGES 1019
Cdd:NF038329   249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
                          250
                   ....*....|....
gi 1622831426 1020 GLQGEPGAKGDVGP 1033
Cdd:NF038329   329 GKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
996-1248 2.80e-36

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 143.89  E-value: 2.80e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  996 GLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGE 1075
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1076 DGEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQrGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAVG 1155
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1156 HLGLMGPDGEPgipgyrGHQGQPGLSGLPGPKGEKGYPGEDstvlgppgprgepgpvgeqgerGEPGAEGYKGHVGVPGL 1235
Cdd:NF038329   276 KDGERGPVGPA------GKDGQNGKDGLPGKDGKDGQNGKD----------------------GLPGKDGKDGQPGKDGL 327
                          250
                   ....*....|...
gi 1622831426 1236 RGATGQQGPPGEP 1248
Cdd:NF038329   328 PGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
706-992 3.67e-36

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 143.89  E-value: 3.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  706 NKGLPGIKGDkgeqgsaGELGEPGYPGDKGAVGLPGPQGMRGKPGPSGQTGDPglqgpsgppgpegfpgdiGIPGQNGPE 785
Cdd:NF038329   107 DEGLQQLKGD-------GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPP------------------GPQGERGEK 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  786 GPKGllgnrgppgppgLKGTQGEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGEVGT 865
Cdd:NF038329   162 GPAG------------PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  866 TGSiGEKGERGSPGPLGPQGEKGvmgypgppgvpgpigPLGLPGHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKG 945
Cdd:NF038329   230 AGD-GQQGPDGDPGPTGEDGPQG---------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1622831426  946 EKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEP 992
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1179-1414 6.81e-34

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 136.96  E-value: 6.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1179 GLSGLPGPKGEKGypgedstvlgppgPRGEPGPVGEQGERGEPGAEGYKGHVGVPGLRGATGQQGPPGEPGDQGEQGLKG 1258
Cdd:NF038329   117 GEKGEPGPAGPAG-------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1259 ERGCEGHKGKKGAPGPSGKAGIPGLQGLPGPKGIQGYHGADGILGNPGKvGPPGKQGLPGIRGSPGRTGLAGAPGPPGVK 1338
Cdd:NF038329   184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1339 GSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAG 1414
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1212-1445 1.49e-33

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: 135.80  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1212 VGEQGERGEPGAEGYkghvgvpglRGATGQQGPPGEPGDQGEQGLKGErgcEGHKGKKGAPGPSGKAGIPGLQGLPGPKG 1291
Cdd:NF038329   125 AGPAGPAGEQGPRGD---------RGETGPAGPAGPPGPQGERGEKGP---AGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1292 IQGYHgadgilGNPGKVGPPGKQGLPGIRGSPGRTGLAGAPGPPGvKGSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHR 1371
Cdd:NF038329   193 PQGPR------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426 1372 GAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGPIGQRGNTGPLGREGIIGPTGR 1445
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
512-756 9.39e-33

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: 133.49  E-value: 9.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  512 RGPRGIPGPHGNPGLPGLPGPKGPKGDpgfspgqavPGEKGDQGLSGLMGPPGMQGDKGLKGHPGLPGLRGEQGIPGFAG 591
Cdd:NF038329   128 AGPAGEQGPRGDRGETGPAGPAGPPGP---------QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  592 NIGSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEagqlgpegergipGIRGKKGFKGRQGFPGDFGDRGPAGLDGSPGlv 671
Cdd:NF038329   199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG-- 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  672 ggtgppgfpgLRGSVGPVGPIGPAGIPGPVGLSGNKGLPGIKGDKGEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGP 751
Cdd:NF038329   264 ----------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333

                   ....*
gi 1622831426  752 SGQTG 756
Cdd:NF038329   334 DGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
594-850 1.18e-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: 133.11  E-value: 1.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  594 GSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEAGQLGPEGERGIPGIRGKKGFKGRQGFPGDFGDRGPAGLDGSPGlvgg 673
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG---- 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  674 tgppgFPGLRGSVGPVGPIGPAGIPGPVGLSGNKGLPGIKGD--KGEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGP 751
Cdd:NF038329   193 -----PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  752 SGQTGDPglqgpsgppgpegfpgdiGIPGQNGPEGPKGLLGNRgppgppglkGTQGEEGPIGPFGELGPRGKPGQKGYAG 831
Cdd:NF038329   268 AGPDGPD------------------GKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
                          250
                   ....*....|....*....
gi 1622831426  832 EPGPEGLKGEVGDQGNIGK 850
Cdd:NF038329   321 QPGKDGLPGKDGKDGQPGK 339
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
918-1177 1.55e-12

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 71.98  E-value: 1.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  918 GSQGPkGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGlpgstgdrglpgepglrgl 997
Cdd:COG5164      2 GLYGP-GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTG------------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  998 qgDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKG-ASGGRGLPGED 1076
Cdd:COG5164     62 --GTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTpPSGGSTTPPGD 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1077 G-----EKGDMGLPGIIGPLGRSGQMGLPGPEGIV--------GIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTG 1143
Cdd:COG5164    140 GgstppGPGSTGPGGSTTPPGDGGSTTPPGPGGSTtppddggsTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGN 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1622831426 1144 PKGARG-------TRGAVGHLGLMGPDGEPGIPGYRGHQGQ 1177
Cdd:COG5164    220 PPDDRGgktgpkdQRPKTNPIERRGPERPEAAALPAELTAL 260
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
41-227 2.59e-11

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 64.30  E-value: 2.59e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426    41 GIDILHQLGLGGKdvrhSSSATAVPASSTPLPqgvhliesGVILKNDAYIETPFMKILPVNLGRPFTILTGLQSHRVNNA 120
Cdd:smart00210    1 GQDLLQVFDLPSL----SFAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRG 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426   121 FLFSIRNK-NRLQLGVQL--LPKKLVVHIRGK----QAVVF-NYSVHDEQWHLFAITIRNQSVSMFVECGKKYFNTETIS 192
Cdd:smart00210   69 VLFAIYDAqNVRQFGLEVdgRANTLLLRYQGVdgkqHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148
                           170       180       190
                    ....*....|....*....|....*....|....*
gi 1622831426   193 EVQTFDSNSVFTLGSMNNNSVHFEGIVCQLDIIPS 227
Cdd:smart00210  149 GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1305-1438 8.05e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.04  E-value: 8.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1305 PGKVGPPGKQGLPGIRGSPGRTGLA---GAPGPPGVKGSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCG 1381
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAqnqGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1382 EPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGPIgQRGNTGPLGREG 1438
Cdd:COG5164     86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGG 141
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1372-1446 2.00e-08

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: 58.76  E-value: 2.00e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1372 GAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGPIGQRGNTGPLGREGIIGPTGRT 1446
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
717-984 2.34e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 58.50  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  717 GEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGPSGQTGDPGLQgpsgppgpegfpgdigipGQNGPEGPKGLLGNRGP 796
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQ------------------GSTTPAGNTGGTRPAGN 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  797 PGPPGLKGTQGEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVglpgEVGTTGSIGEKGERG 876
Cdd:COG5164     69 QGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP----SGGSTTPPGDGGSTP 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  877 S-PGPLGPQGEKGVMGYPGPPGVPGPIGPLGLPGHVGARGPP-----GSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQ 950
Cdd:COG5164    145 PgPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkgetGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDR 224
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622831426  951 -GKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTG 984
Cdd:COG5164    225 gGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1306-1362 1.86e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 1.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1306 GKVGPPGKQGLPGIRGSPGRTGLAGAPGPPGVKGSSGLPGSPGIQGPKGEQGLPGQP 1362
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1002-1056 4.37e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1002 GPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEG 1056
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
573-628 4.25e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 4.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  573 GHPGLPGLRGEQGIPGFAGNIGSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEAGQ 628
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
687-742 4.60e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 4.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  687 GPVGPIGPAGIPGPVGLSGNKGLPGIKGDKGEQGSAGELGEPGYPGDKGAVGLPGP 742
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1140-1195 2.85e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1140 GKTGPKGARGTRGAVGHLGLMGPDGEPGIPGYRGHQGQPGLSGLPGPKGEKGYPGE 1195
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
910-1104 6.69e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 6.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  910 HVGARGPPGSQGPKGQR------------GPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQ 977
Cdd:PHA03169    26 HGGTREQAGRRRGTAARaakpappapttsGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTP 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  978 GLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGEsglqGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGL 1057
Cdd:PHA03169   106 SPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPP 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622831426 1058 QGKDGLKGASGGRGLPGEDGEKGDMGlPGIIGPLGRSGQMGLPGPEG 1104
Cdd:PHA03169   182 TSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNT 227
PHA03169 PHA03169
hypothetical protein; Provisional
1172-1334 1.17e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1172 RGHQGQPGLSGLPGPKGEKGYPGEDSTVLGPPGPRGEPGPVGEQGERGEPGAEGYKGHvgvpglrGATGQQGPPGEPGDQ 1251
Cdd:PHA03169    86 ERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSH-------PGPHEPAPPESHNPS 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1252 GEQGLKGERGCEGHKGKKGAPGPSGKAGIPGLQGLPGPKGIQGYHGADGIlGNPGKVGPPGKQGLPGIRGSPGRTGLAGA 1331
Cdd:PHA03169   159 PNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQAVEHEDEP 237

                   ...
gi 1622831426 1332 PGP 1334
Cdd:PHA03169   238 TEP 240
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1501-1701 7.04e-50

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


Pssm-ID: 460199  Cd Length: 233  Bit Score: 177.15  E-value: 7.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1501 HSEEIFKTLNYLSNLLHSIKNPLGTRDNPARICKDLLNCEQKVSDGKYWIDPNLGCPSDAIEVFCNFSAGgQTCL----- 1575
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETG-ETCIyptka 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1576 ------------PPV-------SGTKLEFGVGK-------VQMNFLHLLSSEATHIITIHCLNTPRWTSTQTSGPGLPIG 1629
Cdd:pfam01410   80 siprknwwtkesKHVwfgefmnGGSQFSYGVDGvgpsvaaVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426 1630 FKGWNGQIFKV--NTLLEPKVLSDDCKIQDGSWHKATFLFHTQEPNQLPVIEVQKLPHLKTERKYYIESSSVCF 1701
Cdd:pfam01410  160 LQGSNDEEIRAegNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1503-1702 3.15e-47

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


Pssm-ID: 197483  Cd Length: 232  Bit Score: 169.57  E-value: 3.15e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  1503 EEIFKTLNYLSNLLHSIKNPLGTRDNPARICKDLLNCEQKVSDGKYWIDPNLGCPSDAIEVFCNFsAGGQTCLPP----- 1577
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNF-ETGETCVSPspssi 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  1578 -------------------VSGTKLEFG------VGKVQMNFLHLLSSEATHIITIHCLNTPRWTSTQTSGPGLPIGFKG 1632
Cdd:smart00038   81 prktwysgkskhvwfgetmNGGFKFSYGdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRLRG 160
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831426  1633 WNGQIFK--VNTLLEPKVLSDDCKIQDGSWHKATFLFHTQEPNQLPVIEVQKLPHLKTERKYYIESSSVCFL 1702
Cdd:smart00038  161 SNDVELSaeGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
909-1125 1.36e-42

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 162.77  E-value: 1.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  909 GHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGL 988
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  989 PGEPGLRGLQGDVGPPGEMGIEGPPGIEGESGL-----QGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGL 1063
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831426 1064 KGASGGRGLPGEDGEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIG 1125
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
836-1102 3.23e-42

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 161.61  E-value: 3.23e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  836 EGLKGEVGDqGNIGKIGETGPVGLPGEVGTTGSIGEKGERGSPGPLGPQGEkgvmgypgppgvpgpigplglpghvgaRG 915
Cdd:NF038329   108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------------------------RG 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  916 PPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPhgligkTGNPGERGVQGKPGLQGLPGSTGDRGLPGEPGlR 995
Cdd:NF038329   160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-D 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  996 GLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGE---EGLQGKDGLKGASGGRGL 1072
Cdd:NF038329   233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQngkDGLPGKDGKDGQNGKDGL 312
                          250       260       270
                   ....*....|....*....|....*....|
gi 1622831426 1073 PGEDGEKGDMGLPGIIGPLGRSGQMGLPGP 1102
Cdd:NF038329   313 PGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
912-1145 3.29e-42

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 161.61  E-value: 3.29e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  912 GARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPhgligkTGNPGERGVQGKPGLQGLPGSTGDRGLPGE 991
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  992 PGLRGLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPaGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRG 1071
Cdd:NF038329   191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426 1072 LPGEDGEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPK 1145
Cdd:NF038329   270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
932-1170 1.24e-40

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 156.99  E-value: 1.24e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  932 DGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKpglqglPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEG 1011
Cdd:NF038329   107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP------AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1012 PPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGlKGASGGRGLPGEDGEKGDMGLPGIIGPL 1091
Cdd:NF038329   181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKD 259
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622831426 1092 GRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAVGHLGLMGPDGEPGIPG 1170
Cdd:NF038329   260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
825-1079 4.32e-40

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: 155.45  E-value: 4.32e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  825 GQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGEVGTTGSIGEKGERGSPGPLGPQGEKgvmgypgppgvpgpigp 904
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD----------------- 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  905 lglpGHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKtgnpGERGVQGKPGLQGLPGSTG 984
Cdd:NF038329   180 ----GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQG 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  985 DRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLrgePGAPGEEGLQGKDGLK 1064
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLP 328
                          250
                   ....*....|....*
gi 1622831426 1065 GASGGRGLPGEDGEK 1079
Cdd:NF038329   329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
780-1033 4.79e-37

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: 146.20  E-value: 4.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  780 GQNGPEGPKGllgnrgppgPPGLKGTQGEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGL 859
Cdd:NF038329   117 GEKGEPGPAG---------PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  860 PGEVGTTGSIGEKGERGSPGPLGPQGEKGvmgypgppgvpgpigplgLPGHVGARGPPGSQGpKGQRGPRGPDGLLGEQG 939
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------EAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  940 IQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGES 1019
Cdd:NF038329   249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
                          250
                   ....*....|....
gi 1622831426 1020 GLQGEPGAKGDVGP 1033
Cdd:NF038329   329 GKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
996-1248 2.80e-36

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 143.89  E-value: 2.80e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  996 GLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGE 1075
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1076 DGEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQrGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAVG 1155
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1156 HLGLMGPDGEPgipgyrGHQGQPGLSGLPGPKGEKGYPGEDstvlgppgprgepgpvgeqgerGEPGAEGYKGHVGVPGL 1235
Cdd:NF038329   276 KDGERGPVGPA------GKDGQNGKDGLPGKDGKDGQNGKD----------------------GLPGKDGKDGQPGKDGL 327
                          250
                   ....*....|...
gi 1622831426 1236 RGATGQQGPPGEP 1248
Cdd:NF038329   328 PGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
706-992 3.67e-36

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 143.89  E-value: 3.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  706 NKGLPGIKGDkgeqgsaGELGEPGYPGDKGAVGLPGPQGMRGKPGPSGQTGDPglqgpsgppgpegfpgdiGIPGQNGPE 785
Cdd:NF038329   107 DEGLQQLKGD-------GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPP------------------GPQGERGEK 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  786 GPKGllgnrgppgppgLKGTQGEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGEVGT 865
Cdd:NF038329   162 GPAG------------PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  866 TGSiGEKGERGSPGPLGPQGEKGvmgypgppgvpgpigPLGLPGHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKG 945
Cdd:NF038329   230 AGD-GQQGPDGDPGPTGEDGPQG---------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1622831426  946 EKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEP 992
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1179-1414 6.81e-34

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 136.96  E-value: 6.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1179 GLSGLPGPKGEKGypgedstvlgppgPRGEPGPVGEQGERGEPGAEGYKGHVGVPGLRGATGQQGPPGEPGDQGEQGLKG 1258
Cdd:NF038329   117 GEKGEPGPAGPAG-------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1259 ERGCEGHKGKKGAPGPSGKAGIPGLQGLPGPKGIQGYHGADGILGNPGKvGPPGKQGLPGIRGSPGRTGLAGAPGPPGVK 1338
Cdd:NF038329   184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1339 GSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAG 1414
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1212-1445 1.49e-33

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: 135.80  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1212 VGEQGERGEPGAEGYkghvgvpglRGATGQQGPPGEPGDQGEQGLKGErgcEGHKGKKGAPGPSGKAGIPGLQGLPGPKG 1291
Cdd:NF038329   125 AGPAGPAGEQGPRGD---------RGETGPAGPAGPPGPQGERGEKGP---AGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1292 IQGYHgadgilGNPGKVGPPGKQGLPGIRGSPGRTGLAGAPGPPGvKGSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHR 1371
Cdd:NF038329   193 PQGPR------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426 1372 GAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGPIGQRGNTGPLGREGIIGPTGR 1445
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
512-756 9.39e-33

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: 133.49  E-value: 9.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  512 RGPRGIPGPHGNPGLPGLPGPKGPKGDpgfspgqavPGEKGDQGLSGLMGPPGMQGDKGLKGHPGLPGLRGEQGIPGFAG 591
Cdd:NF038329   128 AGPAGEQGPRGDRGETGPAGPAGPPGP---------QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  592 NIGSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEagqlgpegergipGIRGKKGFKGRQGFPGDFGDRGPAGLDGSPGlv 671
Cdd:NF038329   199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG-- 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  672 ggtgppgfpgLRGSVGPVGPIGPAGIPGPVGLSGNKGLPGIKGDKGEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGP 751
Cdd:NF038329   264 ----------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333

                   ....*
gi 1622831426  752 SGQTG 756
Cdd:NF038329   334 DGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
594-850 1.18e-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: 133.11  E-value: 1.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  594 GSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEAGQLGPEGERGIPGIRGKKGFKGRQGFPGDFGDRGPAGLDGSPGlvgg 673
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG---- 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  674 tgppgFPGLRGSVGPVGPIGPAGIPGPVGLSGNKGLPGIKGD--KGEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGP 751
Cdd:NF038329   193 -----PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  752 SGQTGDPglqgpsgppgpegfpgdiGIPGQNGPEGPKGLLGNRgppgppglkGTQGEEGPIGPFGELGPRGKPGQKGYAG 831
Cdd:NF038329   268 AGPDGPD------------------GKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
                          250
                   ....*....|....*....
gi 1622831426  832 EPGPEGLKGEVGDQGNIGK 850
Cdd:NF038329   321 QPGKDGLPGKDGKDGQPGK 339
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
918-1177 1.55e-12

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 71.98  E-value: 1.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  918 GSQGPkGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGlpgstgdrglpgepglrgl 997
Cdd:COG5164      2 GLYGP-GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTG------------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  998 qgDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKG-ASGGRGLPGED 1076
Cdd:COG5164     62 --GTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTpPSGGSTTPPGD 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1077 G-----EKGDMGLPGIIGPLGRSGQMGLPGPEGIV--------GIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTG 1143
Cdd:COG5164    140 GgstppGPGSTGPGGSTTPPGDGGSTTPPGPGGSTtppddggsTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGN 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1622831426 1144 PKGARG-------TRGAVGHLGLMGPDGEPGIPGYRGHQGQ 1177
Cdd:COG5164    220 PPDDRGgktgpkdQRPKTNPIERRGPERPEAAALPAELTAL 260
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
41-227 2.59e-11

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 64.30  E-value: 2.59e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426    41 GIDILHQLGLGGKdvrhSSSATAVPASSTPLPqgvhliesGVILKNDAYIETPFMKILPVNLGRPFTILTGLQSHRVNNA 120
Cdd:smart00210    1 GQDLLQVFDLPSL----SFAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRG 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426   121 FLFSIRNK-NRLQLGVQL--LPKKLVVHIRGK----QAVVF-NYSVHDEQWHLFAITIRNQSVSMFVECGKKYFNTETIS 192
Cdd:smart00210   69 VLFAIYDAqNVRQFGLEVdgRANTLLLRYQGVdgkqHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148
                           170       180       190
                    ....*....|....*....|....*....|....*
gi 1622831426   193 EVQTFDSNSVFTLGSMNNNSVHFEGIVCQLDIIPS 227
Cdd:smart00210  149 GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1305-1438 8.05e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.04  E-value: 8.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1305 PGKVGPPGKQGLPGIRGSPGRTGLA---GAPGPPGVKGSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCG 1381
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAqnqGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1382 EPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGPIgQRGNTGPLGREG 1438
Cdd:COG5164     86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGG 141
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1372-1446 2.00e-08

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: 58.76  E-value: 2.00e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1372 GAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGPIGQRGNTGPLGREGIIGPTGRT 1446
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
717-984 2.34e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 58.50  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  717 GEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGPSGQTGDPGLQgpsgppgpegfpgdigipGQNGPEGPKGLLGNRGP 796
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQ------------------GSTTPAGNTGGTRPAGN 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  797 PGPPGLKGTQGEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVglpgEVGTTGSIGEKGERG 876
Cdd:COG5164     69 QGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP----SGGSTTPPGDGGSTP 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  877 S-PGPLGPQGEKGVMGYPGPPGVPGPIGPLGLPGHVGARGPP-----GSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQ 950
Cdd:COG5164    145 PgPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkgetGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDR 224
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622831426  951 -GKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTG 984
Cdd:COG5164    225 gGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1306-1362 1.86e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 1.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1306 GKVGPPGKQGLPGIRGSPGRTGLAGAPGPPGVKGSSGLPGSPGIQGPKGEQGLPGQP 1362
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
638-889 1.95e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.81  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  638 PGIRGKKGFKGRQGFPGDFGDRGPAGLDGSpglvggTGPPGFPGLRGSVGPVGPIGPAGIPGPVGLSGNKGLPGIKGDKG 717
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGS------TRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  718 EQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGPSGQTGDPGLQGPSGPPGPEGFPGDigIPGQNGPEGPkgllGNRGPP 797
Cdd:COG5164     80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPP--GDGGSTPPGP----GSTGPG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  798 GPPGLKGTQGEEGPIGPFGELGP-----RGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGevGTTGSIGEK 872
Cdd:COG5164    154 GSTTPPGDGGSTTPPGPGGSTTPpddggSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPD--DRGGKTGPK 231
                          250
                   ....*....|....*..
gi 1622831426  873 GERGSPGPLGPQGEKGV 889
Cdd:COG5164    232 DQRPKTNPIERRGPERP 248
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1002-1056 4.37e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1002 GPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEG 1056
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1303-1355 4.96e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.96e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622831426 1303 GNPGKVGPPGKQGLPGIRGSPGRTGLAGAPGPPGVKGSSGLPGSPGIQGPKGE 1355
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1309-1363 5.01e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 5.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1309 GPPGKQGLPGIRGSPGRTGLAGAPGPPGVKGSSGLPGSPGIQGPKGEQGLPGQPG 1363
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1327-1383 1.06e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 1.06e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1327 GLAGAPGPPGVKGSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCGEP 1383
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1228-1282 2.90e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 2.90e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1228 GHVGVPGLRGATGQQGPPGEPGDQGEQGLKGERGCEGHKGKKGAPGPSGKAGIPG 1282
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1342-1396 3.29e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 3.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1342 GLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCGEPGLKGQPGEYGVQG 1396
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
999-1054 3.85e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 3.85e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  999 GDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGE 1054
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
1040-1405 3.88e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 51.87  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1040 PGEPGLRGEPGapgeEGLQGKDGLKGASGGRGLPGEdgEKGDMGLPGIIGPLGRSGQMGLPGPEGIVGIPGQRGRLGKkG 1119
Cdd:pfam03157  170 PQQSGQRQQPG----QGQQLRQGQQGQQSGQGQPGY--YPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQ-G 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1120 DKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAVGHLGLMGPDGEPGIPGYRGHQgqPGLSGLPGPKGEKGYPGEDSTv 1199
Cdd:pfam03157  243 QQGQQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYY--PTSQQQAGQLQQEQQLGQEQQ- 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1200 lGPPGPRGEPGPVGEQGERGEPGAEGYKGHVGVPGLRGATGQQGPPGEPGDQGEQGLKGERGCEGHKGKKGAPGPSGKAG 1279
Cdd:pfam03157  320 -DQQPGQGRQGQQPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQG 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1280 -IPGLQGLPGpKGIQGYHGAD---GILGNPGKVGPPGKQGLPGIRGSPGRTGLAGAPGPPGVKGSSGLPGSPGiQGPKGE 1355
Cdd:pfam03157  399 qQPGQGQQPG-QGQPGYYPTSpqqSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPG-QPEQGQ 476
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1356 QGLPGQPGIQGTRGHRGAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPG 1405
Cdd:pfam03157  477 QPGQGQPGYYPTSPQQSGQGQQLGQWQQQGQGQPGYYPTSPLQPGQGQPG 526
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
573-628 4.25e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 4.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  573 GHPGLPGLRGEQGIPGFAGNIGSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEAGQ 628
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
687-742 4.60e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 4.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  687 GPVGPIGPAGIPGPVGLSGNKGLPGIKGDKGEQGSAGELGEPGYPGDKGAVGLPGP 742
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1315-1369 4.83e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 4.83e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1315 GLPGIRGSPGRTGLAGAPGPPGVKGSSGLPGSPGIQGPKGEQGLPGQPGIQGTRG 1369
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
561-617 5.48e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 5.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426  561 GPPGMQGDKGLKGHPGLPGLRGEQGIPGFAGNIGSPGYPGRQGLAGPEGHPGPKGAR 617
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1038-1092 9.23e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 9.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1038 GEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGEDGEKGDMGLPGIIGPLG 1092
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1023-1078 1.10e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 1.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1023 GEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGEDGE 1078
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
951-1006 1.30e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  951 GKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEPGLRGLQGDVGPPGE 1006
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1020-1075 1.41e-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: 44.02  E-value: 1.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1020 GLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGE 1075
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
960-1014 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: 43.64  E-value: 2.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426  960 GKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPG 1014
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
915-969 2.15e-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: 2.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426  915 GPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERG 969
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1231-1291 2.23e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 2.23e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622831426 1231 GVPGLRGATGQQGPPGEPGDQGEQGLKgergceGHKGKKGAPGPSGKAGIPGLQGLPGPKG 1291
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPP------GPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1294-1348 2.49e-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: 2.49e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1294 GYHGADGILGNPGKVGPPGKQGLPGIRGSPGRTGLAGAPGPPGVKGSSGLPGSPG 1348
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
978-1034 2.80e-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: 2.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426  978 GLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPA 1034
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1140-1195 2.85e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1140 GKTGPKGARGTRGAVGHLGLMGPDGEPGIPGYRGHQGQPGLSGLPGPKGEKGYPGE 1195
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
969-1025 3.03e-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: 3.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426  969 GVQGKPGLQGLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGESGLQGEP 1025
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
921-975 3.09e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 3.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426  921 GPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPG 975
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1336-1391 3.34e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 3.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1336 GVKGSSGLPGSPGIQGPKGEQGLPGQPGIQGTRGHRGAQGDQGPCGEPGLKGQPGE 1391
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1032-1086 3.68e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 3.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1032 GPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGEDGEKGDMGLPG 1086
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1005-1060 3.91e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 3.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1005 GEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGK 1060
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
963-1018 5.10e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 5.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  963 GNPGERGVQGKPGLQGLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGE 1018
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1029-1085 5.25e-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: 5.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1029 GDVGPAGSVGEPGEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGEDGEKGDMGLP 1085
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1240-1294 5.79e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.79e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1240 GQQGPPGEPGDQGEQGLKGERGCEGHKGKKGAPGPSGKAGIPGLQGLPGPKGIQG 1294
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
588-643 6.45e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  588 GFAGNIGSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEAGQLGPEGERGIPGIRGK 643
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
910-1104 6.69e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 6.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  910 HVGARGPPGSQGPKGQR------------GPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQ 977
Cdd:PHA03169    26 HGGTREQAGRRRGTAARaakpappapttsGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTP 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  978 GLPGSTGDRGLPGEPGLRGLQGDVGPPGEMGIEGPPGIEGEsglqGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGL 1057
Cdd:PHA03169   106 SPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPP 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622831426 1058 QGKDGLKGASGGRGLPGEDGEKGDMGlPGIIGPLGRSGQMGLPGPEG 1104
Cdd:PHA03169   182 TSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNT 227
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
911-1186 6.76e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 47.70  E-value: 6.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  911 VGARGPPGSQ-GPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLP 989
Cdd:pfam09606  104 PGPGGPMGQQmGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQG 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  990 GEPGLRGLQGD---VGPPGEMGIEGPPG-IEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPgaPGEEGLQGKDGLKG 1065
Cdd:pfam09606  184 QAGGMNGGQQGpmgGQMPPQMGVPGMPGpADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQ--PQQQGQQSQLGMGI 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1066 ASGGRgLPGEDGEKGDMGLPGiiGPLGRSGQMglPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKT-GP 1144
Cdd:pfam09606  262 NQMQQ-MPQGVGGGAGQGGPG--QPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSvGQ 336
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1622831426 1145 KGARGTRGAVGHLGLMGPDGEPGIPGYRGHQGQPGLSGLPGP 1186
Cdd:pfam09606  337 GGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSP 378
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
570-626 7.33e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 7.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426  570 GLKGHPGLPGLRGEQGIPGFAGNIGSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEA 626
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1041-1096 7.85e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 7.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1041 GEPGLRGEPGAPGEEGLQGKDGLKGASGGRGLPGEDGEKGDMGLPGIIGPLGRSGQ 1096
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
548-600 8.33e-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: 8.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622831426  548 PGEKGDQGLSGLMGPPGMQGDKGLKGHPGLPGLRGEQGIPGFAGNIGSPGYPG 600
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1369-1424 9.10e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 9.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426 1369 GHRGAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGP 1424
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
603-659 1.01e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 1.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426  603 GLAGPEGHPGPKGARGFIGSPGEAGQLGPEGERGIPGIRGKKGFKGRQGFPGDFGDR 659
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1246-1300 1.11e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1246 GEPGDQGEQGLKGERGCEGHKGKKGAPGPSGKAGIPGLQGLPGPKGIQGYHGADG 1300
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1119-1173 1.35e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.35e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1119 GDKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAVGHLGLMGPDGEPGIPGYRG 1173
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
519-579 1.85e-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: 40.94  E-value: 1.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622831426  519 GPHGNPGLPGLPGPKGPKGDPGFspgqavPGEKGDQGLSGLMGPPGMQGDKGLKGHPGLPG 579
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGP------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1267-1323 2.00e-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: 40.94  E-value: 2.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1267 GKKGAPGPSGKAGIPGLQGLPGPKGIQGYHGADGILGNPGKVGPPGKQGLPGIRGSP 1323
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
511-564 2.25e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.25e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622831426  511 KRGPRGIPGPHGNPGLPGLPGPKGPKGDPGFSPGQAVPGEKGDQGLSGLMGPPG 564
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
594-648 2.87e-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: 2.87e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426  594 GSPGYPGRQGLAGPEGHPGPKGARGFIGSPGEAGQLGPEGERGIPGIRGKKGFKG 648
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
807-863 3.75e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426  807 GEEGPIGPFGELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGEV 863
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1137-1193 4.14e-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: 4.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1137 GKIGKTGPKGARGTRGAVGHLGLMGPDGEPGIPGYRGHQGQPGLSGLPGPKGEKGYP 1193
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1372-1428 4.61e-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: 4.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1372 GAQGDQGPCGEPGLKGQPGEYGVQGLTGFQGFPGPKGPEGDAGIVGISGPKGPIGQR 1428
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
920-1081 4.95e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.58  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  920 QGPKGQRGPRGPDGllgeQGIQGAKGEKGDQGKRGPHGLIGKTGNPGERGVQGKPGLQGLPGSTGDRGLPGEPG---LRG 996
Cdd:PHA03169    81 HGEKEERGQGGPSG----SGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAppeSHN 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  997 LQGDVGPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGlRGEPGAPGEEGLQGKDGLKGASGGRGLPGED 1076
Cdd:PHA03169   157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPP-QSPPDEPGEPQSPTPQQAPSPNTQQAVEHED 235

                   ....*
gi 1622831426 1077 GEKGD 1081
Cdd:PHA03169   236 EPTEP 240
PHA03169 PHA03169
hypothetical protein; Provisional
915-1061 6.76e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.19  E-value: 6.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426  915 GPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGkrGPHGLIGKTGNPGERGvQGKPGLQGLPGStgDRGLPGEPGL 994
Cdd:PHA03169    90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGS--SPESPASHSPPPSPPS-HPGPHEPAPPES--HNPSPNQQPS 164
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426  995 RGLQGDV--------GPPGEMGIEGPPGIEGESGLQGEPGAKgdvgPAGSVGEPGEPGLRGEPGAPGEEGLQGKD 1061
Cdd:PHA03169   165 SFLQPSHedspeepePPTSEPEPDSPGPPQSETPTSSPPPQS----PPDEPGEPQSPTPQQAPSPNTQQAVEHED 235
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1116-1170 1.11e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1116 GKKGDKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAVGHLGLMGPDGEPGIPG 1170
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
1172-1334 1.17e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1172 RGHQGQPGLSGLPGPKGEKGYPGEDSTVLGPPGPRGEPGPVGEQGERGEPGAEGYKGHvgvpglrGATGQQGPPGEPGDQ 1251
Cdd:PHA03169    86 ERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSH-------PGPHEPAPPESHNPS 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1252 GEQGLKGERGCEGHKGKKGAPGPSGKAGIPGLQGLPGPKGIQGYHGADGIlGNPGKVGPPGKQGLPGIRGSPGRTGLAGA 1331
Cdd:PHA03169   159 PNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQAVEHEDEP 237

                   ...
gi 1622831426 1332 PGP 1334
Cdd:PHA03169   238 TEP 240
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
600-654 1.17e-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: 38.63  E-value: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426  600 GRQGLAGPEGHPGPKGARGFIGSPGEAGQLGPEGERGIPGIRGKKGFKGRQGFPG 654
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
906-955 1.39e-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: 1.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622831426  906 GLPGHVGARGPPGSQGPKGQRGPRGPDGLLGEQGIQGAKGEKGDQGKRGP 955
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
609-663 1.56e-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: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426  609 GHPGPKGARGFIGSPGEAGQLGPEGERGIPGIRGKKGFKGRQGFPGDFGDRGPAG 663
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
708-754 1.85e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.85e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622831426  708 GLPGIKGDKGEQGSAGELGEPGYPGDKGAVGLPGPQGMRGKPGPSGQ 754
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1098-1154 1.96e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.96e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831426 1098 GLPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPKGARGTRGAV 1154
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
621-669 2.61e-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: 2.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1622831426  621 GSPGEAGQLGPEGERGIPGIRGKKGFKGRQGFPGDFGDRGPAGLDGSPG 669
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
LamG smart00282
Laminin G domain;
119-219 3.17e-03

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 39.63  E-value: 3.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426   119 NAFLFSIRNKNRLQ-LGVQLLPKKLVVHIRG----KQAVVFNYSVHDEQWHLFAITIRNQSVSMFVECGKKyFNTETISE 193
Cdd:smart00282   12 NGLLLYAGSKGGGDyLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNR-VSGESPGG 90
                            90       100
                    ....*....|....*....|....*.
gi 1622831426   194 VQTFDSNSVFTLGSMNNNSVHFEGIV 219
Cdd:smart00282   91 LTILNLDGPLYLGGLPEDLKLPPLPV 116
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
630-701 4.80e-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: 4.80e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831426  630 GPEGERGIPGIRGKKGFKGRQGFPGDFGDRGPAGLDGSPGLvggtgppgfpglrgsVGPVGPIGPAGIPGPV 701
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP---------------PGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
816-871 6.26e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 6.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831426  816 GELGPRGKPGQKGYAGEPGPEGLKGEVGDQGNIGKIGETGPVGLPGEVGTTGSIGE 871
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
864-937 6.32e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 6.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831426  864 GTTGSIGEKGERGSPGPLGPQGEKGvmgypgppgvpgpigplgLPGHVGARGPPGSQGPKGQRGPRGPDGLLGE 937
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG------------------PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1095-1149 6.32e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 6.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622831426 1095 GQMGLPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRGSPGKIGKTGPKGARG 1149
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
1002-1174 8.87e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1002 GPPGEMGIEGPPGIEGESGLQGEPGAKGDVGPAGSVGEPGEPGLRGEPGAPGEEGlqgkDGLKGASGGRGLPGEDGEKGD 1081
Cdd:PHA03169    82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSP----PPSPPSHPGPHEPAPPESHNP 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831426 1082 MGLPGIIGPLGRSGQMGLPGPEGIVGIPGQRGRLGKKGDKGQIGPTGEVGSRgSPGKIGKTGPKGARGTRGAVGHLGLMG 1161
Cdd:PHA03169   158 SPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSPNTQQAVEHEDE 236
                          170
                   ....*....|....*..
gi 1622831426 1162 PDGE----PGIPGYRGH 1174
Cdd:PHA03169   237 PTEPeregPPFPGHRSH 253
 
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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