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Conserved domains on  [gi|161484654|ref|NP_034061|]
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collagen alpha-1(IV) chain precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1556-1667 8.22e-68

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 460201  Cd Length: 110  Bit Score: 223.24  E-value: 8.22e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  1556 MVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTSAGaEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLAT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 161484654  1636 IErsEMFKKPTPSTLKAG-ELRTHVSRCQVCMR 1667
Cdd:pfam01413   80 VE--EQFRKPMSQTPKAGnELRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1446-1553 6.50e-64

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 460201  Cd Length: 110  Bit Score: 212.07  E-value: 6.50e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  1446 FLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASrNDYSYWLST 1525
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 161484654  1526 PE---PMPMSMAPISGDNIRPFISRCAVCEA 1553
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 948-1163 4.69e-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: 128.48  E-value: 4.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  948 GQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGV 1027
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1028 PGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGH 1107
Cdd:NF038329  203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654 1108 PGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAG 1163
Cdd:NF038329  283 VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 717-992 4.29e-21

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.44  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  717 GFNGLPGNPGPQGQKGEPGI-GLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGvqgpagp 795
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG------- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  796 pgvpgigppgamgppggqgppgSSGPPGIKGEKGFPGfpgldMPGPKGDKGSQGLPGLTGQSGLPGLPGqQGTPGVPGFP 875
Cdd:NF038329  190 ----------------------EKGPQGPRGETGPAG-----EQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  876 GSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPgmpgsmehvdmgsmkGQKGDQGE 955
Cdd:NF038329  242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP---------------GKDGKDGQ 306

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 161484654  956 KGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPK 992
Cdd:NF038329  307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1103-1335 2.52e-20

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: 96.13  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1103 GNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGRgfPGFPGSK 1182
Cdd:NF038329  108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK--DGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1183 GDKGSKGEVGFPGLAGSPGIPGVKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFpgiN 1262
Cdd:NF038329  186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP---R 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161484654 1263 GPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGLPGVPGFQGQKGLPGLQGVKGDQGDQG 1335
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 506-766 1.70e-18

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: 90.35  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  506 DGLEGLPGPQGSPGLIGQPGAKGEPGEiffdmrlkgdKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGER 585
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGE----------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  586 GPPGGVGFPGSRGDIGPpgppgvgpigpVGEKGQAGFPGGPGSPGLPGPKGEAGKvvPLPGPPGAAGLPGSPGFPGPQGD 665
Cdd:NF038329  186 GPAGEKGPQGPRGETGP-----------AGEQGPAGPAGPDGEAGPAGEDGPAGP--AGDGQQGPDGDPGPTGEDGPQGP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  666 RGFPGTPGRPGIPGEkgavgqpgigfPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPgiGLPGLKGQP 745
Cdd:NF038329  253 DGPAGKDGPRGDRGE-----------AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD--GLPGKDGKD 319

                         250       260
                  ....*....|....*....|.
gi 161484654  746 GLPGIPGTPGEKGSIGGPGVP 766
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 273-577 7.12e-18

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: 88.42  E-value: 7.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  273 GYGEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPLGEKGDRGYPGAP 352
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  353 GLRGEPGPKgfpgtpgqpgppgfPTPGQAGAPGFPGERGEKGDQGFPGVSLPGPSGRDgapgppgppgppgqpghtngiv 432
Cdd:NF038329  195 GPRGETGPA--------------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD---------------------- 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  433 ecqpgppgdqgppgtpgqpGLTGEVGQKGQKGesclacdteglrgppgpqgppgEIGFPGQPGAKGDRGLPGRDGLEGLP 512
Cdd:NF038329  239 -------------------GDPGPTGEDGPQG----------------------PDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161484654  513 GPQGSPGLIGQPGAKGEPGEIFFDmrlkGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPG 577
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKD----GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 42-331 1.00e-14

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: 78.79  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   42 HGVKGQKGERGLPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPglpgipgqdgppgppg 121
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------------- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  122 ipgcnGTKGERgplgppglpgfsgnpgppglpgmkgdpgeilghvpgtllkGERGFPGIPGMPGSPGLPGLQGPVGPPGF 201
Cdd:NF038329  177 -----GKDGEA----------------------------------------GAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  202 TGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQA-QVKEKGDFAPTGEKGQKGEPGFPGVPgyGEKGEP 280
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDGPDGKDGERGPV--GPAGKD 289

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161484654  281 GKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPP 331
Cdd:NF038329  290 GQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1229-1443 3.56e-07

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: 54.53  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1229 HPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGINGPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMG 1308
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1309 LPGVPGFQGQKGLPGLQGVKGDQGDQGVPGPKGLQGppgppgpydviKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGS 1388
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-----------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654 1389 VGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVD 1443
Cdd:NF038329  262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1556-1667 8.22e-68

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 223.24  E-value: 8.22e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  1556 MVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTSAGaEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLAT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 161484654  1636 IErsEMFKKPTPSTLKAG-ELRTHVSRCQVCMR 1667
Cdd:pfam01413   80 VE--EQFRKPMSQTPKAGnELRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1446-1553 6.50e-64

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 212.07  E-value: 6.50e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  1446 FLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASrNDYSYWLST 1525
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 161484654  1526 PE---PMPMSMAPISGDNIRPFISRCAVCEA 1553
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1555-1668 1.24e-63

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 211.48  E-value: 1.24e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   1555 AMVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NAYSFWL 1633
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 161484654   1634 ATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRR 1668
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1445-1554 2.30e-54

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 185.29  E-value: 2.30e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   1445 GFLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLS 1524
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 161484654   1525 TPEP-----MPMSMAPISGDnIRPFISRCAVCEAP 1554
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAGD-LRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 948-1163 4.69e-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: 128.48  E-value: 4.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  948 GQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGV 1027
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1028 PGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGH 1107
Cdd:NF038329  203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654 1108 PGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAG 1163
Cdd:NF038329  283 VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 903-1146 4.21e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 125.79  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  903 GEKGDHGLPGSSGPRGDPGFKGDKGDVGLPgmpgsmehvdmgsmkGQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQ 982
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------------GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  983 AGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGS--QGVPGSPGEKGAKGEKGQSGLPGIGip 1060
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKD-- 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1061 GRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGT 1140
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ....*.
gi 161484654 1141 PGPTGP 1146
Cdd:NF038329  340 PAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 944-1182 1.29e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 121.17  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  944 GSMKGQKGDqGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPG 1023
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1024 EKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPg 1103
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR- 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1104 niGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGR-GFPGFPGSK 1182
Cdd:NF038329  266 --GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKdGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 717-992 4.29e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.44  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  717 GFNGLPGNPGPQGQKGEPGI-GLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGvqgpagp 795
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG------- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  796 pgvpgigppgamgppggqgppgSSGPPGIKGEKGFPGfpgldMPGPKGDKGSQGLPGLTGQSGLPGLPGqQGTPGVPGFP 875
Cdd:NF038329  190 ----------------------EKGPQGPRGETGPAG-----EQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  876 GSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPgmpgsmehvdmgsmkGQKGDQGE 955
Cdd:NF038329  242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP---------------GKDGKDGQ 306

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 161484654  956 KGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPK 992
Cdd:NF038329  307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 646-902 2.26e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.13  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  646 GPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPG----IGFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGL 721
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGpagpQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  722 PGNPGPQGQKGEPG-IGLPGLKGQPGLPGIPG--TPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGVQGPAGPpgv 798
Cdd:NF038329  200 TGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK--- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  799 pgigppgamgppggqgppgssgppgiKGEKGFPGFPGLDmpgpkGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSK 878
Cdd:NF038329  277 --------------------------DGERGPVGPAGKD-----GQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325

                         250       260
                  ....*....|....*....|....
gi 161484654  879 GEMGVMGTPGQPGSPGPAgTPGLP 902
Cdd:NF038329  326 GLPGKDGKDGQPGKPAPK-TPEVP 348
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1103-1335 2.52e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.13  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1103 GNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGRgfPGFPGSK 1182
Cdd:NF038329  108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK--DGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1183 GDKGSKGEVGFPGLAGSPGIPGVKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFpgiN 1262
Cdd:NF038329  186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP---R 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161484654 1263 GPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGLPGVPGFQGQKGLPGLQGVKGDQGDQG 1335
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 506-766 1.70e-18

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: 90.35  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  506 DGLEGLPGPQGSPGLIGQPGAKGEPGEiffdmrlkgdKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGER 585
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGE----------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  586 GPPGGVGFPGSRGDIGPpgppgvgpigpVGEKGQAGFPGGPGSPGLPGPKGEAGKvvPLPGPPGAAGLPGSPGFPGPQGD 665
Cdd:NF038329  186 GPAGEKGPQGPRGETGP-----------AGEQGPAGPAGPDGEAGPAGEDGPAGP--AGDGQQGPDGDPGPTGEDGPQGP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  666 RGFPGTPGRPGIPGEkgavgqpgigfPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPgiGLPGLKGQP 745
Cdd:NF038329  253 DGPAGKDGPRGDRGE-----------AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD--GLPGKDGKD 319

                         250       260
                  ....*....|....*....|.
gi 161484654  746 GLPGIPGTPGEKGSIGGPGVP 766
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 273-577 7.12e-18

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: 88.42  E-value: 7.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  273 GYGEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPLGEKGDRGYPGAP 352
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  353 GLRGEPGPKgfpgtpgqpgppgfPTPGQAGAPGFPGERGEKGDQGFPGVSLPGPSGRDgapgppgppgppgqpghtngiv 432
Cdd:NF038329  195 GPRGETGPA--------------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD---------------------- 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  433 ecqpgppgdqgppgtpgqpGLTGEVGQKGQKGesclacdteglrgppgpqgppgEIGFPGQPGAKGDRGLPGRDGLEGLP 512
Cdd:NF038329  239 -------------------GDPGPTGEDGPQG----------------------PDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161484654  513 GPQGSPGLIGQPGAKGEPGEIFFDmrlkGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPG 577
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKD----GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 42-331 1.00e-14

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: 78.79  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   42 HGVKGQKGERGLPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPglpgipgqdgppgppg 121
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------------- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  122 ipgcnGTKGERgplgppglpgfsgnpgppglpgmkgdpgeilghvpgtllkGERGFPGIPGMPGSPGLPGLQGPVGPPGF 201
Cdd:NF038329  177 -----GKDGEA----------------------------------------GAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  202 TGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQA-QVKEKGDFAPTGEKGQKGEPGFPGVPgyGEKGEP 280
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDGPDGKDGERGPV--GPAGKD 289

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161484654  281 GKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPP 331
Cdd:NF038329  290 GQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1229-1443 3.56e-07

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: 54.53  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1229 HPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGINGPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMG 1308
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1309 LPGVPGFQGQKGLPGLQGVKGDQGDQGVPGPKGLQGppgppgpydviKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGS 1388
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-----------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654 1389 VGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVD 1443
Cdd:NF038329  262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 958-1153 1.69e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.07  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  958 QIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPG-SQGV 1036
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDaSDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1037 PGSPGEKGAKGEKGQSGLPGIGipGRPGDKGDQGLAGFPGSPGEK-GEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPG 1115
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPA--APAAPAGAAPAQPAPAPAATPpAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 161484654 1116 EKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEP 1153
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1091-1147 1.74e-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: 1.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654  1091 GMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPA 1147
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 275-331 2.16e-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: 46.33  E-value: 2.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   275 GEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPP 331
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 647-1020 4.22e-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: 48.47  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   647 PPGAAGLPGSPGFPGPQGDRGFPGTPGRPgIPGEKGAVGQPGIGFPGLPGPK---GVDGLPGEIGRPGSpGRPGFNGLPG 723
Cdd:pfam09606   81 DPINALQNLAGQGTRPQMMGPMGPGPGGP-MGQQMGGPGTASNLLASLGRPQmpmGGAGFPSQMSRVGR-MQPGGQAGGM 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   724 NPGPQGQKGEPGIGLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGlqgirgdPGPPGVQGPAGPPGVPGIGP 803
Cdd:pfam09606  159 MQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPG-------PADAGAQMGQQAQANGGMNP 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   804 PGAMGPPGGQGPPGSSGPPGIKGEK-GFPGFPGLDMPGPKGDKGSQGLPGLTGQ--SGLPGLPGQQGTPGVPGFPGSKGE 880
Cdd:pfam09606  232 QQMGGAPNQVAMQQQQPQQQGQQSQlGMGINQMQQMPQGVGGGAGQGGPGQPMGppGQQPGAMPNVMSIGDQNNYQQQQT 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   881 MGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPGM-PGSMEHVDMGSMKgqkgDQGEKGQI 959
Cdd:pfam09606  312 RQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMqRGQPGMMSSPSPV----PGQQVRQV 387

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161484654   960 GPTGDKGSRGDPGTPGV--PGKDGQAGHPGQPGP------KGDPGLSGTPGSPGLPGPKGSVGGMGLPG 1020
Cdd:pfam09606  388 TPNQFMRQSPQPSVPSPqgPGSQPPQSHPGGMIPspalipSPSPQMSQQPAQQRTIGQDSPGGSLNTPG 456
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 645-688 3.82e-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: 3.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 161484654   645 PGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPG 688
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 216-353 2.86e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  216 EKGQMGSSFQGPKGDKGEQGVSGPPGVPGqAQVKEKGDFAPTGEKGQKGEPGFPGVPGYGEKGEPGKQGPRGKPGKDGEK 295
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASG-LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFL 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161484654  296 GERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPlGEKGDRGYPGAPG 353
Cdd:PHA03169  168 QPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-GEPQSPTPQQAPS 224
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1556-1667 8.22e-68

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 223.24  E-value: 8.22e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  1556 MVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTSAGaEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLAT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 161484654  1636 IErsEMFKKPTPSTLKAG-ELRTHVSRCQVCMR 1667
Cdd:pfam01413   80 VE--EQFRKPMSQTPKAGnELRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1446-1553 6.50e-64

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 212.07  E-value: 6.50e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  1446 FLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASrNDYSYWLST 1525
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 161484654  1526 PE---PMPMSMAPISGDNIRPFISRCAVCEA 1553
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1555-1668 1.24e-63

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 211.48  E-value: 1.24e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   1555 AMVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NAYSFWL 1633
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 161484654   1634 ATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRR 1668
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1445-1554 2.30e-54

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 185.29  E-value: 2.30e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   1445 GFLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLS 1524
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 161484654   1525 TPEP-----MPMSMAPISGDnIRPFISRCAVCEAP 1554
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAGD-LRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 948-1163 4.69e-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: 128.48  E-value: 4.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  948 GQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGV 1027
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1028 PGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGH 1107
Cdd:NF038329  203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654 1108 PGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAG 1163
Cdd:NF038329  283 VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 903-1146 4.21e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 125.79  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  903 GEKGDHGLPGSSGPRGDPGFKGDKGDVGLPgmpgsmehvdmgsmkGQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQ 982
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------------GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  983 AGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGS--QGVPGSPGEKGAKGEKGQSGLPGIGip 1060
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKD-- 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1061 GRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGT 1140
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ....*.
gi 161484654 1141 PGPTGP 1146
Cdd:NF038329  340 PAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 944-1182 1.29e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 121.17  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  944 GSMKGQKGDqGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPG 1023
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1024 EKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPg 1103
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR- 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1104 niGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGR-GFPGFPGSK 1182
Cdd:NF038329  266 --GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKdGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 717-992 4.29e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.44  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  717 GFNGLPGNPGPQGQKGEPGI-GLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGvqgpagp 795
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG------- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  796 pgvpgigppgamgppggqgppgSSGPPGIKGEKGFPGfpgldMPGPKGDKGSQGLPGLTGQSGLPGLPGqQGTPGVPGFP 875
Cdd:NF038329  190 ----------------------EKGPQGPRGETGPAG-----EQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  876 GSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPgmpgsmehvdmgsmkGQKGDQGE 955
Cdd:NF038329  242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP---------------GKDGKDGQ 306

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 161484654  956 KGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPK 992
Cdd:NF038329  307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 646-902 2.26e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.13  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  646 GPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPG----IGFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGL 721
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGpagpQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  722 PGNPGPQGQKGEPG-IGLPGLKGQPGLPGIPG--TPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGVQGPAGPpgv 798
Cdd:NF038329  200 TGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK--- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  799 pgigppgamgppggqgppgssgppgiKGEKGFPGFPGLDmpgpkGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSK 878
Cdd:NF038329  277 --------------------------DGERGPVGPAGKD-----GQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325

                         250       260
                  ....*....|....*....|....
gi 161484654  879 GEMGVMGTPGQPGSPGPAgTPGLP 902
Cdd:NF038329  326 GLPGKDGKDGQPGKPAPK-TPEVP 348
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1103-1335 2.52e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.13  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1103 GNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGRgfPGFPGSK 1182
Cdd:NF038329  108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK--DGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1183 GDKGSKGEVGFPGLAGSPGIPGVKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFpgiN 1262
Cdd:NF038329  186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP---R 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161484654 1263 GPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGLPGVPGFQGQKGLPGLQGVKGDQGDQG 1335
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 506-766 1.70e-18

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: 90.35  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  506 DGLEGLPGPQGSPGLIGQPGAKGEPGEiffdmrlkgdKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGER 585
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGE----------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  586 GPPGGVGFPGSRGDIGPpgppgvgpigpVGEKGQAGFPGGPGSPGLPGPKGEAGKvvPLPGPPGAAGLPGSPGFPGPQGD 665
Cdd:NF038329  186 GPAGEKGPQGPRGETGP-----------AGEQGPAGPAGPDGEAGPAGEDGPAGP--AGDGQQGPDGDPGPTGEDGPQGP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  666 RGFPGTPGRPGIPGEkgavgqpgigfPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPgiGLPGLKGQP 745
Cdd:NF038329  253 DGPAGKDGPRGDRGE-----------AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD--GLPGKDGKD 319

                         250       260
                  ....*....|....*....|.
gi 161484654  746 GLPGIPGTPGEKGSIGGPGVP 766
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 273-577 7.12e-18

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: 88.42  E-value: 7.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  273 GYGEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPLGEKGDRGYPGAP 352
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  353 GLRGEPGPKgfpgtpgqpgppgfPTPGQAGAPGFPGERGEKGDQGFPGVSLPGPSGRDgapgppgppgppgqpghtngiv 432
Cdd:NF038329  195 GPRGETGPA--------------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD---------------------- 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  433 ecqpgppgdqgppgtpgqpGLTGEVGQKGQKGesclacdteglrgppgpqgppgEIGFPGQPGAKGDRGLPGRDGLEGLP 512
Cdd:NF038329  239 -------------------GDPGPTGEDGPQG----------------------PDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161484654  513 GPQGSPGLIGQPGAKGEPGEIFFDmrlkGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPG 577
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKD----GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 42-331 1.00e-14

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: 78.79  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   42 HGVKGQKGERGLPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPglpgipgqdgppgppg 121
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------------- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  122 ipgcnGTKGERgplgppglpgfsgnpgppglpgmkgdpgeilghvpgtllkGERGFPGIPGMPGSPGLPGLQGPVGPPGF 201
Cdd:NF038329  177 -----GKDGEA----------------------------------------GAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  202 TGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQA-QVKEKGDFAPTGEKGQKGEPGFPGVPgyGEKGEP 280
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDGPDGKDGERGPV--GPAGKD 289

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161484654  281 GKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPP 331
Cdd:NF038329  290 GQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1229-1443 3.56e-07

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: 54.53  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1229 HPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGINGPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMG 1308
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1309 LPGVPGFQGQKGLPGLQGVKGDQGDQGVPGPKGLQGppgppgpydviKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGS 1388
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-----------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654 1389 VGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVD 1443
Cdd:NF038329  262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 958-1153 1.69e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.07  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  958 QIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPG-SQGV 1036
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDaSDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1037 PGSPGEKGAKGEKGQSGLPGIGipGRPGDKGDQGLAGFPGSPGEK-GEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPG 1115
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPA--APAAPAGAAPAQPAPAPAATPpAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 161484654 1116 EKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEP 1153
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1091-1147 1.74e-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: 1.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654  1091 GMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPA 1147
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 275-331 2.16e-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: 46.33  E-value: 2.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   275 GEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPP 331
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1094-1149 4.25e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 4.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654  1094 GSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQ 1149
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1106-1162 5.07e-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: 45.18  E-value: 5.07e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654  1106 GHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSA 1162
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1088-1143 6.05e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 6.05e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654  1088 GTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGP 1143
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1085-1141 1.02e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 1.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654  1085 GSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTP 1141
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1061-1116 1.29e-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: 1.29e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654  1061 GRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGE 1116
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 978-1032 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 161484654   978 GKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPG 1032
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1070-1124 1.55e-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: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654  1070 GLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPG 1124
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 966-1022 1.95e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   966 GSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSP 1022
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 278-332 2.10e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 2.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654   278 GEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPG 332
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 647-1020 4.22e-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: 48.47  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   647 PPGAAGLPGSPGFPGPQGDRGFPGTPGRPgIPGEKGAVGQPGIGFPGLPGPK---GVDGLPGEIGRPGSpGRPGFNGLPG 723
Cdd:pfam09606   81 DPINALQNLAGQGTRPQMMGPMGPGPGGP-MGQQMGGPGTASNLLASLGRPQmpmGGAGFPSQMSRVGR-MQPGGQAGGM 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   724 NPGPQGQKGEPGIGLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGlqgirgdPGPPGVQGPAGPPGVPGIGP 803
Cdd:pfam09606  159 MQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPG-------PADAGAQMGQQAQANGGMNP 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   804 PGAMGPPGGQGPPGSSGPPGIKGEK-GFPGFPGLDMPGPKGDKGSQGLPGLTGQ--SGLPGLPGQQGTPGVPGFPGSKGE 880
Cdd:pfam09606  232 QQMGGAPNQVAMQQQQPQQQGQQSQlGMGINQMQQMPQGVGGGAGQGGPGQPMGppGQQPGAMPNVMSIGDQNNYQQQQT 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   881 MGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPGM-PGSMEHVDMGSMKgqkgDQGEKGQI 959
Cdd:pfam09606  312 RQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMqRGQPGMMSSPSPV----PGQQVRQV 387

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161484654   960 GPTGDKGSRGDPGTPGV--PGKDGQAGHPGQPGP------KGDPGLSGTPGSPGLPGPKGSVGGMGLPG 1020
Cdd:pfam09606  388 TPNQFMRQSPQPSVPSPqgPGSQPPQSHPGGMIPspalipSPSPQMSQQPAQQRTIGQDSPGGSLNTPG 456
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1112-1167 4.85e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 4.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654  1112 GLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGE 1167
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 954-1009 5.85e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654   954 GEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGP 1009
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1058-1114 5.96e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.96e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654  1058 GIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLP 1114
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1079-1135 6.26e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654  1079 GEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEA 1135
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 996-1051 6.91e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654   996 GLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQ 1051
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 840-896 7.26e-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: 7.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   840 GPKGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPA 896
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 984-1040 9.01e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 9.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   984 GHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSP 1040
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1076-1130 9.10e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 9.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654  1076 GSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPG 1130
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 957-1011 1.06e-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: 1.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654   957 GQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKG 1011
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 960-1014 1.23e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654   960 GPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVG 1014
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 858-912 1.26e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654   858 GLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPG 912
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 999-1055 1.31e-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: 1.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   999 GTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLP 1055
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 846-902 1.78e-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: 1.78e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   846 GSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLP 902
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 855-911 1.88e-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: 1.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   855 GQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLP 911
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 879-935 2.53e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   879 GEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPGMP 935
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 981-1042 2.55e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.55e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161484654   981 GQAGHPGQPGPKGDPGLSGTPGSPGLPGPKgsvggmGLPGSPGEKGVPGIPGSQGVPGSPGE 1042
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------GEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 843-899 2.82e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   843 GDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTP 899
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 645-688 3.82e-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: 3.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 161484654   645 PGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPG 688
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 740-788 4.61e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.61e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 161484654   740 GLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPG 788
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1133-1191 5.03e-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: 5.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 161484654  1133 GEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGRgfPGFPGSKGDKGSKGEV 1191
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP--PGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 948-1001 5.34e-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: 39.40  E-value: 5.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 161484654   948 GQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTP 1001
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 867-921 7.10e-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: 7.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654   867 GTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPG 921
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 951-1007 9.45e-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: 9.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   951 GDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLP 1007
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 644-689 1.04e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 161484654   644 LPGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPGI 689
Cdd:pfam01391    8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 743-1168 1.21e-03

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: 43.46  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   743 GQPGLPGIPGTPGEKGSIGGPGVPGEQGLTG----PPGLQGIRGDPGPPGVQGPAGPPGVPGIGPPGAMGPPGGQGPPGS 818
Cdd:pfam09606   61 QQPQGGQGNGGMGGGQQGMPDPINALQNLAGqgtrPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFP 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   819 SGPPGIKGekgfpGFPGLDMPGPKGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAgt 898
Cdd:pfam09606  141 SQMSRVGR-----MQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPA-- 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   899 pglpgeKGDHGLPGSSGPRGDPGfkGDKGDVGLPGMPGSMEHVDMGSMKGQKGDQGEKGQIGPTGDKGSRGDpGTPGVPG 978
Cdd:pfam09606  214 ------DAGAQMGQQAQANGGMN--PQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQ-GGPGQPM 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654   979 KDGQAGhPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIG 1058
Cdd:pfam09606  285 GPPGQQ-PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAN 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  1059 ipgrPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRgSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLP 1138
Cdd:pfam09606  364 ----PMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPS-VPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPA 438

                          410       420       430
                   ....*....|....*....|....*....|..
gi 161484654  1139 G--TPGPTGPAGQKGEPGSDGIPGSAGEKGEQ 1168
Cdd:pfam09606  439 QqrTIGQDSPGGSLNTPGQSAVNSPLNPQEEQ 470
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 885-937 1.31e-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: 1.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161484654   885 GTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPGMPGS 937
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 690-745 1.36e-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: 38.24  E-value: 1.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484654   690 GFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPGIglPGLKGQP 745
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA--PGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 522-585 1.81e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161484654   522 GQPGAKGEPGEiffdmrlKGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGER 585
Cdd:pfam01391    1 GPPGPPGPPGP-------PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 948-1004 1.92e-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: 1.92e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161484654   948 GQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSP 1004
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1121-1172 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 161484654  1121 GLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPG 1172
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 737-787 2.43e-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: 37.86  E-value: 2.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 161484654   737 GLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPP 787
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 216-353 2.86e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  216 EKGQMGSSFQGPKGDKGEQGVSGPPGVPGqAQVKEKGDFAPTGEKGQKGEPGFPGVPGYGEKGEPGKQGPRGKPGKDGEK 295
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASG-LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFL 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161484654  296 GERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPlGEKGDRGYPGAPG 353
Cdd:PHA03169  168 QPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-GEPQSPTPQQAPS 224
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 870-924 6.08e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 6.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 161484654   870 GVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKG 924
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 961-1147 9.44e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654  961 PTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKG-----SVGGMGLPGSPGEKGVPGIPGS-- 1033
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERprddpAPGRVSRPRRARRLGRAAQASSpp 2680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484654 1034 QGvPGSPGEKGAKG-----------EKGQSGLPGIGIPGRPGDKGDQ-GLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGS 1101
Cdd:PHA03247 2681 QR-PRRRAARPTVGsltsladppppPPTPEPAPHALVSATPLPPGPAaARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 161484654 1102 PGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPA 1147
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805
 
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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