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Conserved domains on  [gi|116326001|ref|NP_082046|]
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collagen alpha-1(XXIV) chain isoform 1 precursor [Mus musculus]

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 ...
 1550-1732 2.67e-44

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: 160.97  E-value: 2.67e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1550 IKNPLGTRENPARICKDLLSCQYKVSDGKYWIDPNLGCSSDAFEVFCNFSAgGQTCLSP--------VSVTK-------- 1613
Cdd:pfam01410   19 IRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPtkasiprkNWWTKeskhvwfg 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1614 --------LEFGVSK-------VQMNFLHLLSSEATHTITIHCLNTPRWSSTWADGPELPISFKGWNGQIF--EENTLLE 1676
Cdd:pfam01410   98 efmnggsqFSYGVDGvgpsvaaVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALLLQGSNDEEIraEGNSRFT 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1677 PQVLSDDCKIQDGSWHKAKFLFHTQNPNQLPVTEVQNLPHLGTEQKRYIESNSVCF 1732
Cdd:pfam01410  178 YTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 934-1164 4.84e-43

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: 163.92  E-value: 4.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP 1013
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1014 RGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGgpagSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPG 1093
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116326001 1094 EDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPK 1164
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1095-1352 1.49e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 156.60  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1095 DGDKGEmglpgtAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVG 1174
Cdd:NF038329  116 DGEKGE------PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1175 PLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDstvlgppgppgepgpmgeqgetgehgEEGYKGHMGVPGL 1254
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--------------------------GDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1255 RGATGQQGPPGEPGDqggQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQG 1334
Cdd:NF038329  244 TGEDGPQGPDGPAGK---DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320

                         250
                  ....*....|....*...
gi 116326001 1335 LLGVPGSPGRTGVAGSPG 1352
Cdd:NF038329  321 QPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1016 1.35e-31

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  724 GSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdigipGQNGP 803
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------------GPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  804 EGPKGHLGNRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGlKGEVGDQGDIGKTGETGPVGLPGEVG 883
Cdd:NF038329  179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  884 ITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgPLGLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAK 963
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERG---------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116326001  964 GEKGNQGKRGLPGLPGKAgSPGERGVQGKPGFQ-------GLPGSSGDVGPAGE-PGPRGL 1016
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKP-APKTPEVPQKPDTAphtpktpQIPGQSKDVTPAPQnPSNRGL 382
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1256-1456 8.58e-30

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 8.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1256 GATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQGL 1335
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1336 LGVPGSPGRTGVAGSPGPQG--GKGASGPPGSPGAPGPKGEQGLPGQPGVPGQRGHRGTPGDQGLRgapGLKGQPGEHGD 1413
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGeaGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR---GDRGEAGPDGP 273

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 116326001 1414 QGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQRGNTGPLGRE 1456
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-761 3.28e-24

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.07  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  517 GPpgpmgipgpsgkRGPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGL 596
Cdd:NF038329  126 GP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  597 PGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPG--SKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGD 674
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  675 FGDRGPAGLDGSPGLVGGTGPPGFPGVTGSvgpagptgppgapgpmglSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKG 754
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGK------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ....*..
gi 116326001  755 NIGSPGP 761
Cdd:NF038329  336 QPGKPAP 342
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 41-230 9.78e-06

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: 48.12  E-value: 9.78e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001     41 GIDILQQLGLGGrdvrYTSSVTAVPSSSWSTPlpqgvhltdfGVILTDNAYIESPLVNILPISLRQPLTVLIGLQSFKVN 120
Cdd:smart00210    1 GQDLLQVFDLPS----LSFAIRQVVGPEPGSP----------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKS 66

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001    121 NAFLFSIRN-NNRLQFGVQL--LPKKLIVH---VGGKQ-TVTF-NYSAHDERWHSFAITVDHHVISMFVECGK--RHFSG 190
Cdd:smart00210   67 RGVLFAIYDaQNVRQFGLEVdgRANTLLLRyqgVDGKQhTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEidSRPLD 146

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 116326001    191 EttSDVQTFDPHSVFTLGSINNSSAHFEGTVCQLEIMPST 230
Cdd:smart00210  147 R--PGQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1550-1732 2.67e-44

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: 160.97  E-value: 2.67e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1550 IKNPLGTRENPARICKDLLSCQYKVSDGKYWIDPNLGCSSDAFEVFCNFSAgGQTCLSP--------VSVTK-------- 1613
Cdd:pfam01410   19 IRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPtkasiprkNWWTKeskhvwfg 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1614 --------LEFGVSK-------VQMNFLHLLSSEATHTITIHCLNTPRWSSTWADGPELPISFKGWNGQIF--EENTLLE 1676
Cdd:pfam01410   98 efmnggsqFSYGVDGvgpsvaaVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALLLQGSNDEEIraEGNSRFT 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1677 PQVLSDDCKIQDGSWHKAKFLFHTQNPNQLPVTEVQNLPHLGTEQKRYIESNSVCF 1732
Cdd:pfam01410  178 YTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 934-1164 4.84e-43

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: 163.92  E-value: 4.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP 1013
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1014 RGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGgpagSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPG 1093
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116326001 1094 EDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPK 1164
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1550-1733 9.23e-43

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: 156.48  E-value: 9.23e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   1550 IKNPLGTRENPARICKDLLSCQYKVSDGKYWIDPNLGCSSDAFEVFCNFsAGGQTCLSP--------------------- 1608
Cdd:smart00038   18 LKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNF-ETGETCVSPspssiprktwysgkskhvwfg 96

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   1609 ---VSVTKLEFG------VSKVQMNFLHLLSSEATHTITIHCLNTPRWSSTWADGPELPISFKGWNGQ--IFEENTLLEP 1677
Cdd:smart00038   97 etmNGGFKFSYGdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRLRGSNDVelSAEGNSKFTY 176

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001   1678 QVLSDDCKIQDGSWHKAKFLFHTQNPNQLPVTEVQNLPHLGTEQKRYIESNSVCFL 1733
Cdd:smart00038  177 EVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1213 1.22e-41

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: 160.07  E-value: 1.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  959 GHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRglpgiaglpgemGVEGPPGTEGDS 1038
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGaPGGSGLPGEDGDKGEMGLPGTAGPVGRPgqmgl 1118
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPA----- 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1119 pgpegivgtpgqrGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPG 1198
Cdd:NF038329  257 -------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 116326001 1199 PSGLPGPKGEKGYPG 1213
Cdd:NF038329  324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 855-1121 1.39e-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: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  855 EGLKGEVGDqgdiGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplglpglvgARG 934
Cdd:NF038329  108 EGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------ERG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  935 APGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPaGEPGPR 1014
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPD 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1015 GLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKgdgGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGE 1094
Cdd:NF038329  239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD---GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315

                         250       260
                  ....*....|....*....|....*..
gi 116326001 1095 DGDKGEMGLPGTAGPVGRPGQMGLPGP 1121
Cdd:NF038329  316 DGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1095-1352 1.49e-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: 156.60  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1095 DGDKGEmglpgtAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVG 1174
Cdd:NF038329  116 DGEKGE------PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1175 PLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDstvlgppgppgepgpmgeqgetgehgEEGYKGHMGVPGL 1254
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--------------------------GDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1255 RGATGQQGPPGEPGDqggQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQG 1334
Cdd:NF038329  244 TGEDGPQGPDGPAGK---DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320

                         250
                  ....*....|....*...
gi 116326001 1335 LLGVPGSPGRTGVAGSPG 1352
Cdd:NF038329  321 QPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 844-1098 2.84e-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: 155.83  E-value: 2.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  844 GRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKgvmgypgppgapgpmgp 923
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD----------------- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  924 lglpglvGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSpGERGVQGKPGFQGLPGSSG 1003
Cdd:NF038329  180 -------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1004 DVGPAGEPGPRGLPGIAGLPGEMGVEGPpgtEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLK 1083
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGE---RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         250
                  ....*....|....*
gi 116326001 1084 GAPGGSGLPGEDGDK 1098
Cdd:NF038329  329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1016 1.35e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  724 GSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdigipGQNGP 803
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------------GPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  804 EGPKGHLGNRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGlKGEVGDQGDIGKTGETGPVGLPGEVG 883
Cdd:NF038329  179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  884 ITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgPLGLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAK 963
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERG---------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116326001  964 GEKGNQGKRGLPGLPGKAgSPGERGVQGKPGFQ-------GLPGSSGDVGPAGE-PGPRGL 1016
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKP-APKTPEVPQKPDTAphtpktpQIPGQSKDVTPAPQnPSNRGL 382
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1256-1456 8.58e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 8.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1256 GATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQGL 1335
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1336 LGVPGSPGRTGVAGSPGPQG--GKGASGPPGSPGAPGPKGEQGLPGQPGVPGQRGHRGTPGDQGLRgapGLKGQPGEHGD 1413
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGeaGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR---GDRGEAGPDGP 273

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 116326001 1414 QGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQRGNTGPLGRE 1456
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1207-1452 1.83e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.62  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1207 GEKGYPGedstvlgppgPPGEPGPMGEQGETGEHGEegyKGHMGVPGLRGATGQQGPPGEPGDQGGQGPKGERGSEGPQG 1286
Cdd:NF038329  117 GEKGEPG----------PAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1287 KRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQGllgvpgsPGRTGVAGSPGPQGGKGASGPPGSP 1366
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1367 GAPGPKGEQGLPGQPGVPGQRGHRGTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQ 1446
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ....*.
gi 116326001 1447 RGNTGP 1452
Cdd:NF038329  337 PGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-951 7.86e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 112.69  E-value: 7.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  640 GSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDRGPAGLDGSPglvggtgppgfpgvtgsvgpagptgppGAPgp 719
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------------------------GPQ-- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  720 mglsGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdiGIPG 799
Cdd:NF038329  168 ----GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD------------------------GEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  800 QNGPEGPKGHLGnRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLP 879
Cdd:NF038329  220 PAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116326001  880 GEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplgLPGLVGARGAPGSPGPKGQRGPRGPD 951
Cdd:NF038329  299 GKDGKDGQNGKDGLPGKDGKDGQPGKDG------------------LPGKDGKDGQPGKPAPKTPEVPQKPD 352
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1272-1456 2.63e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.15  E-value: 2.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1272 GQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQGLLGVPGSPGRTGVAGSP 1351
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1352 GPQGGKGASGPPGSPGAPGPKGEQGLPGQPGVPGQ--RGHRGTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPE 1429
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180
                  ....*....|....*....|....*..
gi 116326001 1430 GDAGIVGIVGPKGPIGQRGNTGPLGRE 1456
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-761 3.28e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.07  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  517 GPpgpmgipgpsgkRGPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGL 596
Cdd:NF038329  126 GP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  597 PGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPG--SKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGD 674
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  675 FGDRGPAGLDGSPGLVGGTGPPGFPGVTGSvgpagptgppgapgpmglSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKG 754
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGK------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ....*..
gi 116326001  755 NIGSPGP 761
Cdd:NF038329  336 QPGKPAP 342
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 931-1424 2.06e-09

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: 62.66  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   931 GARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGF---------QG---- 997
Cdd:pfam03157  218 GQQGQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYyptslqqpgQGqsgy 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   998 LPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGtEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQ 1077
Cdd:pfam03157  298 YPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPG-QGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQ 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1078 GKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGS 1157
Cdd:pfam03157  377 PQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQ 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1158 vGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDSTVLGPPGPPGE-----PGPMG 1232
Cdd:pfam03157  457 -GQQPGQGQQGQQPGQPEQGQQPGQGQPGYYPTSPQQSGQGQQLGQWQQQGQGQPGYYPTSPLQPGQGQPgyyptSPQQP 535

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1233 EQGETGEHGEEGYKGHMGVPGLRGATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSgkPGIPGVPGFPGPKGLQ 1312
Cdd:pfam03157  536 GQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYY--PTSPQQSGQGQQPGQW 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1313 GYPGVDGMSGYPGKPGLPGKQGLLGVPGSPGRTGVAGSPGPQGGKGASGPPGSPGAPGPKGEQGLPGQPGVPGQRGHRGT 1392
Cdd:pfam03157  614 QQPGQGQPGYYPTSSLQLGQGQQGYYPTSPQQPGQGQQPGQWQQSGQGQQGYYPTSPQQSGQAQQPGQGQQPGQWLQPGQ 693

                          490       500       510
                   ....*....|....*....|....*....|..
gi 116326001  1393 pGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPG 1424
Cdd:pfam03157  694 -GQQGYYPTSPQQPGQGQQLGQGQQSGQGQQG 724
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1385-1479 7.76e-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: 56.84  E-value: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1385 GQRGHRGTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQRGNTGPLGregiigptgG 1464
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG---------P 187

                          90
                  ....*....|....*
gi 116326001 1465 TGPRGEKGFRGETGP 1479
Cdd:NF038329  188 AGEKGPQGPRGETGP 202
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1060-1115 6.78e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 6.78e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1060 GEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQ 1115
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
532-770 6.07e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 6.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  532 GPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLkghpglPGLRGEHGLPGLAGN 611
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRP------AGNQGATGPAQNQGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  612 IGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERG--TPGVRGKKGPKGRQG-FPGDFGDRGPAGLDGSPG 688
Cdd:COG5164    81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  689 LVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMGlSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPgiRGKS 768
Cdd:COG5164   161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGT-DIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ--RPKT 237


                  ..
gi 116326001  769 GP 770
Cdd:COG5164   238 NP 239
PHA03169 PHA03169
hypothetical protein; Provisional
 980-1132 6.50e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 50.74  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  980 KAGSPGERGvQGKPGFQGLPGSSGDVGPAGEPGPRGLPGiaGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPA--GSAG 1057
Cdd:PHA03169   80 RHGEKEERG-QGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAppESHN 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116326001 1058 ATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPvGRPGQMGLPGPEGIVGTPGQRG 1132
Cdd:PHA03169  157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQA 230
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 41-230 9.78e-06

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 48.12  E-value: 9.78e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001     41 GIDILQQLGLGGrdvrYTSSVTAVPSSSWSTPlpqgvhltdfGVILTDNAYIESPLVNILPISLRQPLTVLIGLQSFKVN 120
Cdd:smart00210    1 GQDLLQVFDLPS----LSFAIRQVVGPEPGSP----------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKS 66

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001    121 NAFLFSIRN-NNRLQFGVQL--LPKKLIVH---VGGKQ-TVTF-NYSAHDERWHSFAITVDHHVISMFVECGK--RHFSG 190
Cdd:smart00210   67 RGVLFAIYDaQNVRQFGLEVdgRANTLLLRyqgVDGKQhTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEidSRPLD 146

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 116326001    191 EttSDVQTFDPHSVFTLGSINNSSAHFEGTVCQLEIMPST 230
Cdd:smart00210  147 R--PGQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 580-634 8.73e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 8.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   580 GPPGLQGAKGLKGHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKG 634
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 722-771 1.92e-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: 1.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 116326001   722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPS 771
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1391-1447 4.17e-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: 4.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1391 GTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQR 1447
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 979-1210 4.31e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 44.99  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  979 GKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDS-GLQGEPGAKGDGGPAGSAG 1057
Cdd:cd21118   122 QGSGGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGPLNYGTNSqGAVAQPGYGTVRGNNQNSG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1058 ATGEPgPRGEPGAPGEEGLQGKDGLKGAPG--GSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLG 1135
Cdd:cd21118   202 CTNPP-PSGSHESFSNSGGSSSSGSSGSQGshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGS 280

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116326001 1136 KKGDKGQVGPTGEAGSRGppGSVGENGPKGArgtrgavgplglmGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKG 1210
Cdd:cd21118   281 SSGGSNGWGGSSSSGGSG--GSGGGNKPECN-------------NPGNDVRMAGGGGSQGSKESSGSHGSNGGNG 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
642-908 5.01e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  642 PGEVGQLGPEGERGTPGVRGKKGPkgrqgfPGDFGDRGPAGLDGSPGLVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMG 721
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKP------AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSGQPGDPGPQGPSGPpgpegfpgdigiPGQN 801
Cdd:COG5164    80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGST------------PPGP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  802 GPEGPKGHLGNRGPPGPPGLKGTQGEEGPIGPfgelGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGe 881
Cdd:COG5164   148 GSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPD- 222

                         250       260
                  ....*....|....*....|....*..
gi 116326001  882 vGITGSIGEKGERGSPGPLGPQGEKGV 908
Cdd:COG5164   223 -DRGGKTGPKDQRPKTNPIERRGPERP 248
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1550-1732 2.67e-44

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: 160.97  E-value: 2.67e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1550 IKNPLGTRENPARICKDLLSCQYKVSDGKYWIDPNLGCSSDAFEVFCNFSAgGQTCLSP--------VSVTK-------- 1613
Cdd:pfam01410   19 IRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPtkasiprkNWWTKeskhvwfg 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1614 --------LEFGVSK-------VQMNFLHLLSSEATHTITIHCLNTPRWSSTWADGPELPISFKGWNGQIF--EENTLLE 1676
Cdd:pfam01410   98 efmnggsqFSYGVDGvgpsvaaVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALLLQGSNDEEIraEGNSRFT 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1677 PQVLSDDCKIQDGSWHKAKFLFHTQNPNQLPVTEVQNLPHLGTEQKRYIESNSVCF 1732
Cdd:pfam01410  178 YTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 934-1164 4.84e-43

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: 163.92  E-value: 4.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP 1013
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1014 RGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGgpagSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPG 1093
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116326001 1094 EDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPK 1164
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1550-1733 9.23e-43

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: 156.48  E-value: 9.23e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   1550 IKNPLGTRENPARICKDLLSCQYKVSDGKYWIDPNLGCSSDAFEVFCNFsAGGQTCLSP--------------------- 1608
Cdd:smart00038   18 LKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNF-ETGETCVSPspssiprktwysgkskhvwfg 96

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   1609 ---VSVTKLEFG------VSKVQMNFLHLLSSEATHTITIHCLNTPRWSSTWADGPELPISFKGWNGQ--IFEENTLLEP 1677
Cdd:smart00038   97 etmNGGFKFSYGdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRLRGSNDVelSAEGNSKFTY 176

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001   1678 QVLSDDCKIQDGSWHKAKFLFHTQNPNQLPVTEVQNLPHLGTEQKRYIESNSVCFL 1733
Cdd:smart00038  177 EVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 959-1213 1.22e-41

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: 160.07  E-value: 1.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  959 GHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRglpgiaglpgemGVEGPPGTEGDS 1038
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGaPGGSGLPGEDGDKGEMGLPGTAGPVGRPgqmgl 1118
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPA----- 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1119 pgpegivgtpgqrGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPG 1198
Cdd:NF038329  257 -------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 116326001 1199 PSGLPGPKGEKGYPG 1213
Cdd:NF038329  324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 855-1121 1.39e-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: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  855 EGLKGEVGDqgdiGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplglpglvgARG 934
Cdd:NF038329  108 EGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------ERG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  935 APGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPaGEPGPR 1014
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPD 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1015 GLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKgdgGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGE 1094
Cdd:NF038329  239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD---GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315

                         250       260
                  ....*....|....*....|....*..
gi 116326001 1095 DGDKGEMGLPGTAGPVGRPGQMGLPGP 1121
Cdd:NF038329  316 DGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1095-1352 1.49e-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: 156.60  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1095 DGDKGEmglpgtAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVG 1174
Cdd:NF038329  116 DGEKGE------PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1175 PLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDstvlgppgppgepgpmgeqgetgehgEEGYKGHMGVPGL 1254
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--------------------------GDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1255 RGATGQQGPPGEPGDqggQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQG 1334
Cdd:NF038329  244 TGEDGPQGPDGPAGK---DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320

                         250
                  ....*....|....*...
gi 116326001 1335 LLGVPGSPGRTGVAGSPG 1352
Cdd:NF038329  321 QPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 844-1098 2.84e-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: 155.83  E-value: 2.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  844 GRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGEVGITGSIGEKGERGSPGPLGPQGEKgvmgypgppgapgpmgp 923
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD----------------- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  924 lglpglvGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSpGERGVQGKPGFQGLPGSSG 1003
Cdd:NF038329  180 -------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1004 DVGPAGEPGPRGLPGIAGLPGEMGVEGPpgtEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLK 1083
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGE---RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         250
                  ....*....|....*
gi 116326001 1084 GAPGGSGLPGEDGDK 1098
Cdd:NF038329  329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1016 1.35e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  724 GSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdigipGQNGP 803
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------------GPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  804 EGPKGHLGNRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGlKGEVGDQGDIGKTGETGPVGLPGEVG 883
Cdd:NF038329  179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  884 ITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgPLGLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAK 963
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERG---------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116326001  964 GEKGNQGKRGLPGLPGKAgSPGERGVQGKPGFQ-------GLPGSSGDVGPAGE-PGPRGL 1016
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKP-APKTPEVPQKPDTAphtpktpQIPGQSKDVTPAPQnPSNRGL 382
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1256-1456 8.58e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 8.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1256 GATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQGL 1335
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1336 LGVPGSPGRTGVAGSPGPQG--GKGASGPPGSPGAPGPKGEQGLPGQPGVPGQRGHRGTPGDQGLRgapGLKGQPGEHGD 1413
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGeaGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR---GDRGEAGPDGP 273

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 116326001 1414 QGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQRGNTGPLGRE 1456
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1207-1452 1.83e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.62  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1207 GEKGYPGedstvlgppgPPGEPGPMGEQGETGEHGEegyKGHMGVPGLRGATGQQGPPGEPGDQGGQGPKGERGSEGPQG 1286
Cdd:NF038329  117 GEKGEPG----------PAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1287 KRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQGllgvpgsPGRTGVAGSPGPQGGKGASGPPGSP 1366
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1367 GAPGPKGEQGLPGQPGVPGQRGHRGTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQ 1446
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ....*.
gi 116326001 1447 RGNTGP 1452
Cdd:NF038329  337 PGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 640-951 7.86e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 112.69  E-value: 7.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  640 GSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDRGPAGLDGSPglvggtgppgfpgvtgsvgpagptgppGAPgp 719
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------------------------GPQ-- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  720 mglsGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSgqpgdpgpqgpsgppgpegfpgdiGIPG 799
Cdd:NF038329  168 ----GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD------------------------GEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  800 QNGPEGPKGHLGnRGPPGPPGLKGTQGEEGPIGPFGELGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLP 879
Cdd:NF038329  220 PAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116326001  880 GEVGITGSIGEKGERGSPGPLGPQGEKGvmgypgppgapgpmgplgLPGLVGARGAPGSPGPKGQRGPRGPD 951
Cdd:NF038329  299 GKDGKDGQNGKDGLPGKDGKDGQPGKDG------------------LPGKDGKDGQPGKPAPKTPEVPQKPD 352
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1272-1456 2.63e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.15  E-value: 2.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1272 GQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQGLLGVPGSPGRTGVAGSP 1351
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1352 GPQGGKGASGPPGSPGAPGPKGEQGLPGQPGVPGQ--RGHRGTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPE 1429
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180
                  ....*....|....*....|....*..
gi 116326001 1430 GDAGIVGIVGPKGPIGQRGNTGPLGRE 1456
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 517-761 3.28e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.07  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  517 GPpgpmgipgpsgkRGPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGL 596
Cdd:NF038329  126 GP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  597 PGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPG--SKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGD 674
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  675 FGDRGPAGLDGSPGLVGGTGPPGFPGVTGSvgpagptgppgapgpmglSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKG 754
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGK------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ....*..
gi 116326001  755 NIGSPGP 761
Cdd:NF038329  336 QPGKPAP 342
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 931-1424 2.06e-09

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: 62.66  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   931 GARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGF---------QG---- 997
Cdd:pfam03157  218 GQQGQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYyptslqqpgQGqsgy 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   998 LPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGtEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQ 1077
Cdd:pfam03157  298 YPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPG-QGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQ 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1078 GKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGS 1157
Cdd:pfam03157  377 PQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQ 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1158 vGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDSTVLGPPGPPGE-----PGPMG 1232
Cdd:pfam03157  457 -GQQPGQGQQGQQPGQPEQGQQPGQGQPGYYPTSPQQSGQGQQLGQWQQQGQGQPGYYPTSPLQPGQGQPgyyptSPQQP 535

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1233 EQGETGEHGEEGYKGHMGVPGLRGATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSgkPGIPGVPGFPGPKGLQ 1312
Cdd:pfam03157  536 GQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYY--PTSPQQSGQGQQPGQW 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1313 GYPGVDGMSGYPGKPGLPGKQGLLGVPGSPGRTGVAGSPGPQGGKGASGPPGSPGAPGPKGEQGLPGQPGVPGQRGHRGT 1392
Cdd:pfam03157  614 QQPGQGQPGYYPTSSLQLGQGQQGYYPTSPQQPGQGQQPGQWQQSGQGQQGYYPTSPQQSGQAQQPGQGQQPGQWLQPGQ 693

                          490       500       510
                   ....*....|....*....|....*....|..
gi 116326001  1393 pGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPG 1424
Cdd:pfam03157  694 -GQQGYYPTSPQQPGQGQQLGQGQQSGQGQQG 724
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1385-1479 7.76e-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: 56.84  E-value: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1385 GQRGHRGTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQRGNTGPLGregiigptgG 1464
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG---------P 187

                          90
                  ....*....|....*
gi 116326001 1465 TGPRGEKGFRGETGP 1479
Cdd:NF038329  188 AGEKGPQGPRGETGP 202
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1247-1303 1.09e-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: 50.18  E-value: 1.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1247 GHMGVPGLRGATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVP 1303
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1262-1316 1.22e-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: 49.80  E-value: 1.22e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1262 GPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPG 1316
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1250-1304 3.06e-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: 48.64  E-value: 3.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1250 GVPGLRGATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPG 1304
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1060-1115 6.78e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 6.78e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1060 GEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQ 1115
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1256-1310 7.26e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 7.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1256 GATGQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKG 1310
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 970-1025 7.93e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 7.93e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001   970 GKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGE 1025
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1274-1330 1.43e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 1.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1274 GPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLP 1330
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1259-1315 2.62e-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: 2.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1259 GQQGPPGEPGDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYP 1315
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 976-1032 2.70e-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: 2.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001   976 GLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPP 1032
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 934-988 2.87e-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: 2.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERG 988
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1009-1065 3.07e-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: 3.07e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1009 GEPGPRGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPR 1065
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1039-1094 3.16e-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: 3.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1039 GLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGE 1094
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1021-1075 3.70e-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: 3.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1021 GLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEG 1075
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 979-1033 3.92e-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: 3.92e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   979 GKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPG 1033
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 964-1354 3.94e-06

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: 51.93  E-value: 3.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001   964 GEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGP---RGLPGIAG------LPGEMGVEGPPGT 1034
Cdd:pfam09606   61 QQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMgqqMGGPGTASnllaslGRPQMPMGGAGFP 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1035 EGDSGLQGepGAKGDGGPAGSAGATGEPGPrGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPG 1114
Cdd:pfam09606  141 SQMSRVGR--MQPGGQAGGMMQPSSGQPGS-GTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGA 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1115 QM-------GLPGPEGIVGTPGQRGR-------------LGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGAR-GTRGAV 1173
Cdd:pfam09606  218 QMgqqaqanGGMNPQQMGGAPNQVAMqqqqpqqqgqqsqLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQpGAMPNV 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1174 GPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDSTVLGPPGPPGEPGPMGEQGETGEHGEEGYKGHMGVP- 1252
Cdd:pfam09606  298 MSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPs 377

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1253 -----GLRGATGQQG--PPGEPGDQGGQGPkgerGSEGPQGKRGVPGPSgkpgiPGVPGFPGPKglqgypgvdgMSGYPG 1325
Cdd:pfam09606  378 pvpgqQVRQVTPNQFmrQSPQPSVPSPQGP----GSQPPQSHPGGMIPS-----PALIPSPSPQ----------MSQQPA 438

                          410       420
                   ....*....|....*....|....*....
gi 116326001  1326 KPGLPGKQGLLGVPGSPGRTGVAGSPGPQ 1354
Cdd:pfam09606  439 QQRTIGQDSPGGSLNTPGQSAVNSPLNPQ 467
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
532-770 6.07e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 6.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  532 GPRGIPGPHGNPGLPGLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLkghpglPGLRGEHGLPGLAGN 611
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRP------AGNQGATGPAQNQGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  612 IGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERG--TPGVRGKKGPKGRQG-FPGDFGDRGPAGLDGSPG 688
Cdd:COG5164    81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  689 LVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMGlSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPgiRGKS 768
Cdd:COG5164   161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGT-DIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ--RPKT 237


                  ..
gi 116326001  769 GP 770
Cdd:COG5164   238 NP 239
PHA03169 PHA03169
hypothetical protein; Provisional
 980-1132 6.50e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 50.74  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  980 KAGSPGERGvQGKPGFQGLPGSSGDVGPAGEPGPRGLPGiaGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPA--GSAG 1057
Cdd:PHA03169   80 RHGEKEERG-QGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAppESHN 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116326001 1058 ATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPvGRPGQMGLPGPEGIVGTPGQRG 1132
Cdd:PHA03169  157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQA 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1030-1086 6.60e-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: 44.79  E-value: 6.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1030 GPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAP 1086
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1042-1096 7.50e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 7.50e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1042 GEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDG 1096
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 41-230 9.78e-06

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 48.12  E-value: 9.78e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001     41 GIDILQQLGLGGrdvrYTSSVTAVPSSSWSTPlpqgvhltdfGVILTDNAYIESPLVNILPISLRQPLTVLIGLQSFKVN 120
Cdd:smart00210    1 GQDLLQVFDLPS----LSFAIRQVVGPEPGSP----------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKS 66

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001    121 NAFLFSIRN-NNRLQFGVQL--LPKKLIVH---VGGKQ-TVTF-NYSAHDERWHSFAITVDHHVISMFVECGK--RHFSG 190
Cdd:smart00210   67 RGVLFAIYDaQNVRQFGLEVdgRANTLLLRyqgVDGKQhTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEidSRPLD 146

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 116326001    191 EttSDVQTFDPHSVFTLGSINNSSAHFEGTVCQLEIMPST 230
Cdd:smart00210  147 R--PGQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1153-1208 9.87e-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: 9.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1153 GPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGE 1208
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 960-1114 1.03e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  960 HGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEmgveGPPGTEGDSG 1039
Cdd:PHA03169   81 HGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHN 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116326001 1040 LQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGlPGEDGDKGEMGLPGTAGPVGRPG 1114
Cdd:PHA03169  157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQA 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1277-1332 1.34e-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: 44.02  E-value: 1.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1277 GERGSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGK 1332
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 982-1036 1.63e-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: 1.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   982 GSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEG 1036
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1048-1104 1.85e-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: 43.64  E-value: 1.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1048 GDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLP 1104
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 973-1027 1.98e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   973 GLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMG 1027
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 928-1123 2.42e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.81  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  928 GLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKaGSPGERGVQGKPGFQGLPGSSGDVGP 1007
Cdd:PHA03169   37 RGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVGSPTPSPSGSAEELA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1008 AG-EPGPRGLPGIAGLPGEMGVEGPPGTEGDsglqGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAP 1086
Cdd:PHA03169  116 SGlSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPG 191

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 116326001 1087 GGSGLPGEDGDKGEMGlPGTAGPVGRPGQMGLPGPEG 1123
Cdd:PHA03169  192 PPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNT 227
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1138-1192 2.88e-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: 2.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1138 GDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRG 1192
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1156-1212 3.64e-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: 3.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1156 GSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYP 1212
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 934-1089 3.86e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.04  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  934 GAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGfqglpgSSGDVGPAGEPGP 1013
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPA------PPESHNPSPNQQP 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001 1014 RGlpgiaGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPrgEPGAPGEEGLQGKDGLKGAPGGS 1089
Cdd:PHA03169  164 SS-----FLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD--EPGEPQSPTPQQAPSPNTQQAVE 232
PHA03169 PHA03169
hypothetical protein; Provisional
 1009-1204 6.31e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1009 GEPGPRGLPGIAGlPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGLKGAPGG 1088
Cdd:PHA03169   82 GEKEERGQGGPSG-SGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPN 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1089 SGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDkgqvgptGEAGSRGPPGSVGENGPKGARG 1168
Cdd:PHA03169  161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-------GEPQSPTPQQAPSPNTQQAVEH 233

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 116326001 1169 TRGAVGPlglmgPEGEPGIPGYRGHQ---GQPGPSGLPG 1204
Cdd:PHA03169  234 EDEPTEP-----EREGPPFPGHRSHSytvVGWKPSTRPG 267
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1135-1189 7.39e-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: 7.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1135 GKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAVGPLGLMGPEGEPGIPG 1189
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1013-1443 7.77e-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: 7.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1013 PRGLPGIAGLPGEMGVEGPPGTegdsGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEG--LQGKDGLKGAPGGSG 1090
Cdd:pfam09606   63 PQGGQGNGGMGGGQQGMPDPIN----ALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASnlLASLGRPQMPMGGAG 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1091 LPGEDGDKGEMGLPGTAGPvGRPGQMGLPGPegivGTPGQRGRLGKKGDKGQVGPTGEAGS---RGPPGSVGENGPKGAR 1167
Cdd:pfam09606  139 FPSQMSRVGRMQPGGQAGG-MMQPSSGQPGS----GTPNQMGPNGGPGQGQAGGMNGGQQGpmgGQMPPQMGVPGMPGPA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1168 GTRG----AVGPLGLMGPEGEPGIPGYRGHQGQPgpsglPGPKGEkgypgedSTVLGPPGPPGEPGPMGEQGETGEhgee 1243
Cdd:pfam09606  214 DAGAqmgqQAQANGGMNPQQMGGAPNQVAMQQQQ-----PQQQGQ-------QSQLGMGINQMQQMPQGVGGGAGQ---- 277

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1244 gykghmGVPGLRGATGQQGPPGEP--GDQGGQGPKGERGSEGPQGKRGVPGPSGKPGIPGVPGFPGpkGLQGYPGVDGMS 1321
Cdd:pfam09606  278 ------GGPGQPMGPPGQQPGAMPnvMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQG--GQVVALGGLNHL 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1322 GypgkPGLPGKQGLLGVPGS-PGRTGVAGSPGPQGGKGASG--------PPGSPGAPGpkgeqglpgqPGVPGQRGHRGT 1392
Cdd:pfam09606  350 E----TWNPGNFGGLGANPMqRGQPGMMSSPSPVPGQQVRQvtpnqfmrQSPQPSVPS----------PQGPGSQPPQSH 415

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 116326001  1393 PGdqGLRGAPGLKGQPGEHGDQGLAGFQGFP--GPRGPEGDAGIVGIVGPKGP 1443
Cdd:pfam09606  416 PG--GMIPSPALIPSPSPQMSQQPAQQRTIGqdSPGGSLNTPGQSAVNSPLNP 466
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1063-1119 8.07e-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: 8.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1063 GPRGEPGAPGEEGLQGKDGLKGAPGGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLP 1119
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 580-634 8.73e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 8.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   580 GPPGLQGAKGLKGHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKG 634
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1003-1215 1.05e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1003 GDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGL 1082
Cdd:PRK07764  580 GDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAV 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1083 KGAP-GGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRgrlgkkgdkgqVGPTGEAGSRGPPGSVGEN 1161
Cdd:PRK07764  660 PDASdGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP-----------PAGQADDPAAQPPQAAQGA 728

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116326001 1162 GPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGED 1215
Cdd:PRK07764  729 SAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1162-1214 1.49e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 116326001  1162 GPKGARGTRGAVGPLGLMGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGE 1214
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 991-1046 1.90e-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: 1.90e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001   991 GKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDSGLQGEPGA 1046
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 722-771 1.92e-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: 1.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 116326001   722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPS 771
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1028-1217 3.47e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1028 VEGPPGTEGDSGLQGEPGAKGDGG----PAGSAGATGEPGPRGEPGAPGEEGLQgkdglkGAPGGSGLPGEDGDKGEMGL 1103
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEeaarPAAPAAPAAPAAPAPAGAAAAPAEAS------AAPAPGVAAPEHHPKHVAVP 660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1104 PGTAGPVGRPGQMGLPGPEGIVGTP---GQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGEN-GPKGARGTRGAVGPLGLM 1179
Cdd:PRK07764  661 DASDGGDGWPAKAGGAAPAAPPPAPapaAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPpQAAQGASAPSPAADDPVP 740

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 116326001 1180 GPEGEPGIPGYRGHQGQPGPSGLPGPKGEKGYPGEDST 1217
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSP 778
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 530-594 3.67e-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: 3.67e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   530 KRGPRGIPGPHGNPGLPGLPGPKGPKGDPglspgqaasGEKGDPGLLGLVGPPGLQGAKGLKGHP 594
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPP---------GEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1280-1334 3.89e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 3.89e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1280 GSEGPQGKRGVPGPSGKPGIPGVPGFPGPKGLQGYPGVDGMSGYPGKPGLPGKQG 1334
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 927-1131 4.08e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  927 PGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGakgekgnqgkrglPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVG 1006
Cdd:PRK07764  601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAA-------------PAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1007 PAgepgprglPGIAGLPGEMGVEGPPGTEGDSGLQGEPGAKGDGGPAGSAGATGEPGPRGEPGAPGEEGLQGKDGlkGAP 1086
Cdd:PRK07764  668 GW--------PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA--ADD 737

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 116326001 1087 GGSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQR 1131
Cdd:PRK07764  738 PVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1391-1447 4.17e-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: 4.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1391 GTPGDQGLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQR 1447
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1117-1173 4.30e-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: 4.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001  1117 GLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARGTRGAV 1173
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 979-1210 4.31e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 44.99  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  979 GKAGSPGERGVQGKPGFQGLPGSSGDVGPAGEPGPRGLPGIAGLPGEMGVEGPPGTEGDS-GLQGEPGAKGDGGPAGSAG 1057
Cdd:cd21118   122 QGSGGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGPLNYGTNSqGAVAQPGYGTVRGNNQNSG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001 1058 ATGEPgPRGEPGAPGEEGLQGKDGLKGAPG--GSGLPGEDGDKGEMGLPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLG 1135
Cdd:cd21118   202 CTNPP-PSGSHESFSNSGGSSSSGSSGSQGshGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGS 280

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116326001 1136 KKGDKGQVGPTGEAGSRGppGSVGENGPKGArgtrgavgplglmGPEGEPGIPGYRGHQGQPGPSGLPGPKGEKG 1210
Cdd:cd21118   281 SSGGSNGWGGSSSSGGSG--GSGGGNKPECN-------------NPGNDVRMAGGGGSQGSKESSGSHGSNGGNG 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
642-908 5.01e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  642 PGEVGQLGPEGERGTPGVRGKKGPkgrqgfPGDFGDRGPAGLDGSPGLVGGTGPPGFPGVTGSVGPAGPTGPPGAPGPMG 721
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKP------AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  722 LSGSRGPSGIKGDKGEQGVAGEPGEPGYPGDKGNIGSPGPPGIRGKSGPSGQPGDPGPQGPSGPpgpegfpgdigiPGQN 801
Cdd:COG5164    80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGST------------PPGP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  802 GPEGPKGHLGNRGPPGPPGLKGTQGEEGPIGPfgelGSRGKPGRKGYMGEPGPEGLKGEVGDQGDIGKTGETGPVGLPGe 881
Cdd:COG5164   148 GSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDD----GGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPD- 222

                         250       260
                  ....*....|....*....|....*..
gi 116326001  882 vGITGSIGEKGERGSPGPLGPQGEKGV 908
Cdd:COG5164   223 -DRGGKTGPKDQRPKTNPIERRGPERP 248
LamG smart00282
Laminin G domain;
121-221 5.33e-04

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 41.94  E-value: 5.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001    121 NAFLFSIRNNNRLQF-GVQLLPKKLIVHV----GGKQTVTFNYSAHDERWHSFAITVDHHVISMFVEcGKRHFSGETTSD 195
Cdd:smart00282   12 NGLLLYAGSKGGGDYlALELRDGRLVLRYdlgsGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD-GGNRVSGESPGG 90

                            90       100
                    ....*....|....*....|....*.
gi 116326001    196 VQTFDPHSVFTLGSINNSSAHFEGTV 221
Cdd:smart00282   91 LTILNLDGPLYLGGLPEDLKLPPLPV 116
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1114-1168 5.60e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001  1114 GQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGPKGARG 1168
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 589-645 7.45e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001   589 GLKGHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEV 645
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 607-662 9.34e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001   607 GLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERGTPGVRGK 662
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1108-1163 1.14e-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: 1.14e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1108 GPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQVGPTGEAGSRGPPGSVGENGP 1163
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 592-647 1.67e-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: 1.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001   592 GHPGLPGLRGEHGLPGLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQ 647
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 925-975 1.90e-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: 1.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 116326001   925 GLPGLVGARGAPGSPGPKGQRGPRGPDGLAGDQGGHGAKGEKGNQGKRGLP 975
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1397-1452 2.18e-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: 2.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001  1397 GLRGAPGLKGQPGEHGDQGLAGFQGFPGPRGPEGDAGIVGIVGPKGPIGQRGNTGP 1452
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1084-1143 2.36e-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: 2.36e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  1084 GAPGGSGLPGEDGDKGEmglPGTAGPVGRPGQMGLPGPEGIVGTPGQRGRLGKKGDKGQV 1143
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGP---PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 622-678 2.36e-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: 2.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001   622 GLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDR 678
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 958-1073 2.51e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.74  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116326001  958 GGHGAKGEKGNQGKRGLPGLPGKAGSPGERGVQGKPGFQGLPGSSGDVG---PAGEPGPRgLPGIAGLPGEMGVEGPPgt 1034
Cdd:PRK14959  374 SGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPAtpaPSAAPSPR-VPWDDAPPAPPRSGIPP-- 450

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 116326001 1035 EGDSGLQGEPGAKgdGGPAGSAGATGEPGPRGEPGAPGE 1073
Cdd:PRK14959  451 RPAPRMPEASPVP--GAPDSVASASDAPPTLGDPSDTAE 487
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 604-658 3.33e-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: 3.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   604 GLPGLAGNIGSPGYPGRQGLAGPEGNPGSKGVRGFIGSPGEVGQLGPEGERGTPG 658
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 547-602 4.34e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 4.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116326001   547 GLPGPKGPKGDPGLSPGQAASGEKGDPGLLGLVGPPGLQGAKGLKGHPGLPGLRGE 602
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 625-681 4.43e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 4.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001   625 GPEGNPGSKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDRGPA 681
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 628-682 8.74e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 8.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116326001   628 GNPGSKGVRGFIGSPGEVGQLGPEGERGTPGVRGKKGPKGRQGFPGDFGDRGPAG 682
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1372-1432 8.83e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 8.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116326001  1372 KGEQGLPGQPGVPGQRGHRGTPGDQGLRGAPGLKGQPgehgdqglaGFQGFPGPRGPEGDA 1432
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP---------GPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 874-950 9.65e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 9.65e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116326001   874 GPVGLPGEVGITGSIGEKGERGSPGPLGPQGEkgvmgypgppgapgpmgplglPGLVGARGAPGSPGPKGQRGPRGP 950
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------------------PGPPGPPGPPGPPGPPGAPGAPGP 56
 
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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