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Conserved domains on  [gi|115528995|gb|AAI25033|]
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Col17a1 protein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-812 1.67e-30

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 126.56  E-value: 1.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  508 VEELEKTKVLYHDVQMDKSNRDRLQaeapSLGPGLGKAELDGYSQEAIWLFVRNKLMTEQENGNlRGSPGPKGDMGSQGP 587
Cdd:NF038329   80 LDDTTVNKIYKYLEERDKKLNSYLE----ELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGD-RGETGPAGPAGPPGP 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  588 KGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRglagpmgprgepgpPGSGEKGDRGIAGEQGPQGLPGV 667
Cdd:NF038329  155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR--------------GETGPAGEQGPAGPAGPDGEAGP 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  668 PGPPGLRGhsgspgpQGPPGAVGPQGLRGDVGLPGVKGDKGLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKG 747
Cdd:NF038329  221 AGEDGPAG-------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115528995  748 AMGPAGADGQqgsRGEQGLTGMPGTRgppgpagdpgkpgltGPQGPQGLPGSPGRPGTKGEPGAP 812
Cdd:NF038329  294 KDGLPGKDGK---DGQNGKDGLPGKD---------------GKDGQPGKDGLPGKDGKDGQPGKP 340
COG5099 super family cl34901
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
 32-315 1.71e-04

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5099:

Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 46.28  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   32 PKGSTSNGYAKTGSLGGGSRLEKQ-SLTHGSSGYINSSGSirgNASTSSYRRTHSPASTLPNSPGSTFERKAHMTRHGTY 110
Cdd:COG5099    80 PSGSWSVAISSSTSGSQSLLMELPsSSFNPSTSSRNKSNS---ALSSTQQGNANSSVTLSSSTASSMFNSNKLPLPNPNH 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  111 EGSSSGNSSPEYPRKELASSSTRGR-------------SQTRESEIRVRLQSASPStrWTELDEVKRLLKGSRSASASPT 177
Cdd:COG5099   157 SNSATTNQSGSSFINTPASSSSQPLtnlvvssikrfpyLTSLSPFFNYLIDPSSDS--ATASADTSPSFNPPPNLSPNNL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  178 RNTSNTLPIPKKGTVE---TKTVTASSHSVSGTYDSAILDTNFP-PHM-------WSSTLPAGSSL-GTYQNNITAQST- 244
Cdd:COG5099   235 FSTSDLSPLPDTQSVEnniILNSSSSINELTSIYGSVPSIRNLRgLNSalvsflnVSSSSLAFSALnGKEVSPTGSPSTr 314

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115528995  245 ------SLLNTNAYSTGSVFGVPNNMASCSPTLHPGLSSCSSVFGMQNN--LAPSSSVLSHGTTTASTAYGAKKNVPQP 315
Cdd:COG5099   315 sfarvlPKSSPNNLLTEILTTGVNPPQSLPSLLNPVFLSTSTGFSLTNLsgYLNPNKNLKKNTLSSLSNLGYSSNVPSP 393
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-812 1.67e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 126.56  E-value: 1.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  508 VEELEKTKVLYHDVQMDKSNRDRLQaeapSLGPGLGKAELDGYSQEAIWLFVRNKLMTEQENGNlRGSPGPKGDMGSQGP 587
Cdd:NF038329   80 LDDTTVNKIYKYLEERDKKLNSYLE----ELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGD-RGETGPAGPAGPPGP 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  588 KGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRglagpmgprgepgpPGSGEKGDRGIAGEQGPQGLPGV 667
Cdd:NF038329  155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR--------------GETGPAGEQGPAGPAGPDGEAGP 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  668 PGPPGLRGhsgspgpQGPPGAVGPQGLRGDVGLPGVKGDKGLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKG 747
Cdd:NF038329  221 AGEDGPAG-------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115528995  748 AMGPAGADGQqgsRGEQGLTGMPGTRgppgpagdpgkpgltGPQGPQGLPGSPGRPGTKGEPGAP 812
Cdd:NF038329  294 KDGLPGKDGK---DGQNGKDGLPGKD---------------GKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 697-867 1.47e-19

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: 93.43  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  697 DVGLPGVKGD--KGLMGPPGPKGDQGEKGP---RGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQGSRGEQGLTGMPG 771
Cdd:NF038329  107 DEGLQQLKGDgeKGEPGPAGPAGPAGEQGPrgdRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  772 TRGPPGPAGDPGKPGLTGPQGPQGLPGSPGRPGTKGEPGAPGRVMTSEgsstitvpgppgpPGAMGPPGPPGTPGPAGPA 851
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-------------QGPDGDPGPTGEDGPQGPD 253

                         170
                  ....*....|....*.
gi 115528995  852 GLPGQQGPRGEPGLAG 867
Cdd:NF038329  254 GPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 692-966 1.29e-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: 78.02  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  692 QGLRGDvglpGVKGDKGLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQGSRGEQGLTGMPG 771
Cdd:NF038329  111 QQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  772 TRGPPGPAGDPGKPGLTGPQGPQGLPGSPGRPGTKGEPGAPGRvmtsegsstitvpgppgppgamgppgppgtpgpagpa 851
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP------------------------------------- 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  852 GLPGQQGPRGEPGLAGDSFlssgssisevlsAQGvdlrgppgppgprgppgpsipgppgprgppgegvpgppgppgsflT 931
Cdd:NF038329  230 AGDGQQGPDGDPGPTGEDG------------PQG---------------------------------------------P 252

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 115528995  932 DSETFFTGPPGPPGPPGPKGDQGDPGVPGTPGISG 966
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 708-763 2.46e-13

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: 65.98  E-value: 2.46e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 115528995   708 GLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQGSRGE 763
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
 32-315 1.71e-04

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 46.28  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   32 PKGSTSNGYAKTGSLGGGSRLEKQ-SLTHGSSGYINSSGSirgNASTSSYRRTHSPASTLPNSPGSTFERKAHMTRHGTY 110
Cdd:COG5099    80 PSGSWSVAISSSTSGSQSLLMELPsSSFNPSTSSRNKSNS---ALSSTQQGNANSSVTLSSSTASSMFNSNKLPLPNPNH 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  111 EGSSSGNSSPEYPRKELASSSTRGR-------------SQTRESEIRVRLQSASPStrWTELDEVKRLLKGSRSASASPT 177
Cdd:COG5099   157 SNSATTNQSGSSFINTPASSSSQPLtnlvvssikrfpyLTSLSPFFNYLIDPSSDS--ATASADTSPSFNPPPNLSPNNL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  178 RNTSNTLPIPKKGTVE---TKTVTASSHSVSGTYDSAILDTNFP-PHM-------WSSTLPAGSSL-GTYQNNITAQST- 244
Cdd:COG5099   235 FSTSDLSPLPDTQSVEnniILNSSSSINELTSIYGSVPSIRNLRgLNSalvsflnVSSSSLAFSALnGKEVSPTGSPSTr 314

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115528995  245 ------SLLNTNAYSTGSVFGVPNNMASCSPTLHPGLSSCSSVFGMQNN--LAPSSSVLSHGTTTASTAYGAKKNVPQP 315
Cdd:COG5099   315 sfarvlPKSSPNNLLTEILTTGVNPPQSLPSLLNPVFLSTSTGFSLTNLsgYLNPNKNLKKNTLSSLSNLGYSSNVPSP 393
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 61-330 2.16e-03

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.60  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995    61 SSGYINSSGSIRGNASTSSYRRTHSPAS-TLPNSPGSTFERK--AHMTRHGTYEGSSSGNSSPEyPRKELASSSTRGRSQ 137
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSSTHVPTNlTAPASTGPTVSTAdvTSPTPAGTTSGASPVTPSPS-PRDNGTESKAPDMTS 508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   138 TRESEIRVRLQSASPS---TRWTELDEVKRLLKGS-RSASASPTRNTSNTLP----------IPKKG------TVETKTV 197
Cdd:pfam05109  509 PTSAVTTPTPNATSPTpavTTPTPNATSPTLGKTSpTSAVTTPTPNATSPTPavttptpnatIPTLGktsptsAVTTPTP 588

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   198 TASSHSV------SGTYDSAILDTNFPPHMWSSTLPAGSSLGTYQNNITAQSTSLLNTNAYSTGSVFGVPNNMASCSPTl 271
Cdd:pfam05109  589 NATSPTVgetspqANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHM- 667

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   272 hPGLSSCSSVFGMQNNLAPSSSVLSHGTTTASTAygakknvPQPPTVT-STGVSTSATCT 330
Cdd:pfam05109  668 -PLLTSAHPTGGENITQVTPASTSTHHVSTSSPA-------PRPGTTSqASGPGNSSTST 719
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
686-825 5.98e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  686 PGAVGPQGLRGDVGLPGVKGDKGLMGPPG------PKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQG 759
Cdd:COG5164    39 AGNTGGTRPAQNQGSTTPAGNTGGTRPAGnqgatgPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115528995  760 SRGEQGLTGMPGTRGPPGPAGDPGKPGLTGPQGPQGLPGSPGRPGTKGEPGAPGRVMTSEGSSTIT 825
Cdd:COG5164   119 PPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTT 184
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-812 1.67e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 126.56  E-value: 1.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  508 VEELEKTKVLYHDVQMDKSNRDRLQaeapSLGPGLGKAELDGYSQEAIWLFVRNKLMTEQENGNlRGSPGPKGDMGSQGP 587
Cdd:NF038329   80 LDDTTVNKIYKYLEERDKKLNSYLE----ELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGD-RGETGPAGPAGPPGP 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  588 KGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRglagpmgprgepgpPGSGEKGDRGIAGEQGPQGLPGV 667
Cdd:NF038329  155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR--------------GETGPAGEQGPAGPAGPDGEAGP 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  668 PGPPGLRGhsgspgpQGPPGAVGPQGLRGDVGLPGVKGDKGLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKG 747
Cdd:NF038329  221 AGEDGPAG-------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115528995  748 AMGPAGADGQqgsRGEQGLTGMPGTRgppgpagdpgkpgltGPQGPQGLPGSPGRPGTKGEPGAP 812
Cdd:NF038329  294 KDGLPGKDGK---DGQNGKDGLPGKD---------------GKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 697-867 1.47e-19

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: 93.43  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  697 DVGLPGVKGD--KGLMGPPGPKGDQGEKGP---RGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQGSRGEQGLTGMPG 771
Cdd:NF038329  107 DEGLQQLKGDgeKGEPGPAGPAGPAGEQGPrgdRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  772 TRGPPGPAGDPGKPGLTGPQGPQGLPGSPGRPGTKGEPGAPGRVMTSEgsstitvpgppgpPGAMGPPGPPGTPGPAGPA 851
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-------------QGPDGDPGPTGEDGPQGPD 253

                         170
                  ....*....|....*.
gi 115528995  852 GLPGQQGPRGEPGLAG 867
Cdd:NF038329  254 GPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 692-966 1.29e-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: 78.02  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  692 QGLRGDvglpGVKGDKGLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQGSRGEQGLTGMPG 771
Cdd:NF038329  111 QQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  772 TRGPPGPAGDPGKPGLTGPQGPQGLPGSPGRPGTKGEPGAPGRvmtsegsstitvpgppgppgamgppgppgtpgpagpa 851
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP------------------------------------- 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  852 GLPGQQGPRGEPGLAGDSFlssgssisevlsAQGvdlrgppgppgprgppgpsipgppgprgppgegvpgppgppgsflT 931
Cdd:NF038329  230 AGDGQQGPDGDPGPTGEDG------------PQG---------------------------------------------P 252

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 115528995  932 DSETFFTGPPGPPGPPGPKGDQGDPGVPGTPGISG 966
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 708-763 2.46e-13

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: 65.98  E-value: 2.46e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 115528995   708 GLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQGSRGE 763
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 702-757 1.95e-12

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: 63.28  E-value: 1.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 115528995   702 GVKGDKGLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQ 757
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 573-622 1.88e-11

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: 60.59  E-value: 1.88e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 115528995   573 RGSPGPKGDMGSQGPKGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDPG 622
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 741-812 4.19e-11

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: 59.43  E-value: 4.19e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115528995   741 GEPGAKGAMGPAGADGQQGSRGEQGLTGMPGTRgppgpagdpgkpgltGPQGPQGLPGSPGRPGTKGEPGAP 812
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP---------------GPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 701-752 8.07e-11

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: 58.66  E-value: 8.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 115528995   701 PGVKGDKglmGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPA 752
Cdd:pfam01391    9 PGPPGPP---GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 577-626 1.14e-10

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: 58.27  E-value: 1.14e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 115528995   577 GPKGDMGSQGPKGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDPGMEGP 626
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 572-621 1.86e-09

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: 54.81  E-value: 1.86e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 115528995   572 LRGSPGPKGDMGSQGPKGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDP 621
Cdd:pfam01391    8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 572-626 2.06e-09

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: 54.81  E-value: 2.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 115528995   572 LRGSPGPKGDMGSQGPKGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDPGMEGP 626
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 720-809 4.63e-09

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: 53.65  E-value: 4.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   720 GEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQqgsrgeqgltgmpgtrgppgpagdpgkpgltgpQGPQGLPGS 799
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGP---------------------------------PGPPGPPGP 47

                           90
                   ....*....|
gi 115528995   800 PGRPGTKGEP 809
Cdd:pfam01391   48 PGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 586-633 1.08e-08

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: 52.50  E-value: 1.08e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 115528995   586 GPKGDRGLPGTPGIPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGLA 633
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 692-740 1.31e-08

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: 52.50  E-value: 1.31e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 115528995   692 QGLRGDVGLPGVKGDKGLMGPPGPKGDQGEKGPRGLTGEPGIRGLPGAV 740
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 711-800 5.52e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 5.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   711 GPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQqgsrgeqgltgmpgtrgppgpagdpgkpgltgp 790
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP--------------------------------- 47

                           90
                   ....*....|
gi 115528995   791 QGPQGLPGSP 800
Cdd:pfam01391   48 PGAPGAPGPP 57
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
 32-315 1.71e-04

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 46.28  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   32 PKGSTSNGYAKTGSLGGGSRLEKQ-SLTHGSSGYINSSGSirgNASTSSYRRTHSPASTLPNSPGSTFERKAHMTRHGTY 110
Cdd:COG5099    80 PSGSWSVAISSSTSGSQSLLMELPsSSFNPSTSSRNKSNS---ALSSTQQGNANSSVTLSSSTASSMFNSNKLPLPNPNH 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  111 EGSSSGNSSPEYPRKELASSSTRGR-------------SQTRESEIRVRLQSASPStrWTELDEVKRLLKGSRSASASPT 177
Cdd:COG5099   157 SNSATTNQSGSSFINTPASSSSQPLtnlvvssikrfpyLTSLSPFFNYLIDPSSDS--ATASADTSPSFNPPPNLSPNNL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  178 RNTSNTLPIPKKGTVE---TKTVTASSHSVSGTYDSAILDTNFP-PHM-------WSSTLPAGSSL-GTYQNNITAQST- 244
Cdd:COG5099   235 FSTSDLSPLPDTQSVEnniILNSSSSINELTSIYGSVPSIRNLRgLNSalvsflnVSSSSLAFSALnGKEVSPTGSPSTr 314

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115528995  245 ------SLLNTNAYSTGSVFGVPNNMASCSPTLHPGLSSCSSVFGMQNN--LAPSSSVLSHGTTTASTAYGAKKNVPQP 315
Cdd:COG5099   315 sfarvlPKSSPNNLLTEILTTGVNPPQSLPSLLNPVFLSTSTGFSLTNLsgYLNPNKNLKKNTLSSLSNLGYSSNVPSP 393
Herpes_LP pfam03363
Herpesvirus leader protein;
559-614 1.99e-03

Herpesvirus leader protein;


Pssm-ID: 281372 [Multi-domain]  Cd Length: 174  Bit Score: 40.86  E-value: 1.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 115528995   559 VRNKLMTEQENGNLRGSP-GPKGDMgSQGPKGDRglPGTPGIpgplghpGPEGPKGQ 614
Cdd:pfam03363   46 VRRRVLVQQEEEVVSGSPsGPRGDR-SEGPGPAR--PGPPGI-------GPEGPLGQ 92
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 61-330 2.16e-03

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.60  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995    61 SSGYINSSGSIRGNASTSSYRRTHSPAS-TLPNSPGSTFERK--AHMTRHGTYEGSSSGNSSPEyPRKELASSSTRGRSQ 137
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSSTHVPTNlTAPASTGPTVSTAdvTSPTPAGTTSGASPVTPSPS-PRDNGTESKAPDMTS 508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   138 TRESEIRVRLQSASPS---TRWTELDEVKRLLKGS-RSASASPTRNTSNTLP----------IPKKG------TVETKTV 197
Cdd:pfam05109  509 PTSAVTTPTPNATSPTpavTTPTPNATSPTLGKTSpTSAVTTPTPNATSPTPavttptpnatIPTLGktsptsAVTTPTP 588

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   198 TASSHSV------SGTYDSAILDTNFPPHMWSSTLPAGSSLGTYQNNITAQSTSLLNTNAYSTGSVFGVPNNMASCSPTl 271
Cdd:pfam05109  589 NATSPTVgetspqANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHM- 667

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995   272 hPGLSSCSSVFGMQNNLAPSSSVLSHGTTTASTAygakknvPQPPTVT-STGVSTSATCT 330
Cdd:pfam05109  668 -PLLTSAHPTGGENITQVTPASTSTHHVSTSSPA-------PRPGTTSqASGPGNSSTST 719
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
686-825 5.98e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  686 PGAVGPQGLRGDVGLPGVKGDKGLMGPPG------PKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGADGQQG 759
Cdd:COG5164    39 AGNTGGTRPAQNQGSTTPAGNTGGTRPAGnqgatgPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115528995  760 SRGEQGLTGMPGTRGPPGPAGDPGKPGLTGPQGPQGLPGSPGRPGTKGEPGAPGRVMTSEGSSTIT 825
Cdd:COG5164   119 PPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTT 184
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
574-810 7.29e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  574 GSPGPKGDMGSQGPKGDRG---LPGTPGIPGPLGHPGPEGPKGQKGSIGDPGMEGPIG-QRGLAGPMGPRGEPGPPGSGE 649
Cdd:COG5164    70 GATGPAQNQGGTTPAQNQGgtrPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTpPSGGSTTPPGDGGSTPPGPGS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  650 KGDRGIAGEQGPQGLPGVPGPPGLRGhsgspgpQGPPGAVGPQGLRGDVGLPGVKGDKglmGPPGPKGDQGEKGPRGLTG 729
Cdd:COG5164   150 TGPGGSTTPPGDGGSTTPPGPGGSTT-------PPDDGGSTTPPNKGETGTDIPTGGT---PRQGPDGPVKKDDKNGKGN 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115528995  730 EPGIRGlpGAVGEPGAKGAMGPAGADGQQGSRGEQGLTGMPGTRGPPGPAGDPGKPGlTGPQGPQGLPGSPGRPGTKGEP 809
Cdd:COG5164   220 PPDDRG--GKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAANPEPATK-TIPETTTVKDLATVLGKKGSDL 296


                  .
gi 115528995  810 G 810
Cdd:COG5164   297 V 297
 
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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