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Conserved domains on  [gi|386765916|ref|NP_001247143|]
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uncharacterized protein Dmel_CG42342, isoform L [Drosophila melanogaster]

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 ...
 509-730 1.47e-24

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 509 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDDgmSD 588
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 589 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQ 668
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765916 669 GETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 730
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 350-542 5.90e-13

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: 71.86  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 350 GERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLtttiKGDEFPTGIIEGPPGPAG--PPGPPGEPG 427
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP----QGEAGPQGPAGKDGEAGAkgPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 428 ARGEPGPIGPAGPPGEKGPRGKRGKR----IFGPGGTKIDEDYDDPPVTLLRGPPGPPGIAGKDGRDGRDGSKGEPGEPG 503
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAgedgPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 386765916 504 EPgslGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 542
Cdd:NF038329 276 KD---GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-396 1.30e-04

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: 45.28  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSVTTLHGGTLGYAeivavk 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765916 329 gepgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGL 396
Cdd:NF038329 248 ------------------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
DUF2046 super family cl25730
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.49e-03

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


The actual alignment was detected with superfamily member pfam09755:

Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 40.58  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 386765916  210 L 210
Cdd:pfam09755 248 Q 248
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 509-730 1.47e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 509 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDDgmSD 588
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 589 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQ 668
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765916 669 GETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 730
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 615-739 3.46e-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: 94.20  E-value: 3.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 615 GSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGP 694
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386765916 695 RGEQGSRGDAGPPGKRGRKGD--RGDKGEQGVPGLDAPCplGADGLP 739
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQ--GPDGPA 256
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 350-542 5.90e-13

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: 71.86  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 350 GERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLtttiKGDEFPTGIIEGPPGPAG--PPGPPGEPG 427
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP----QGEAGPQGPAGKDGEAGAkgPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 428 ARGEPGPIGPAGPPGEKGPRGKRGKR----IFGPGGTKIDEDYDDPPVTLLRGPPGPPGIAGKDGRDGRDGSKGEPGEPG 503
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAgedgPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 386765916 504 EPgslGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 542
Cdd:NF038329 276 KD---GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-542 1.46e-09

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: 61.07  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKrsvttlhggtlgyaeivavkge 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK---------------------- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 331 pgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRglTTTIKGDEFPTGii 410
Cdd:NF038329 186 ----------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG--QQGPDGDPGPTG-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 411 egppgpagppgppgepgargepgpigpagppgEKGPRGKRGKRifGPGGTKIDEDYDDPPvtllrGPPGPPGIAGKDGRD 490
Cdd:NF038329 246 --------------------------------EDGPQGPDGPA--GKDGPRGDRGEAGPD-----GPDGKDGERGPVGPA 286

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386765916 491 GRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 542
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 651-707 5.46e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 5.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386765916  651 GESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPP 707
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-395 2.04e-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: 2.04e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 386765916  348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRG 395
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-396 1.30e-04

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: 45.28  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSVTTLHGGTLGYAeivavk 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765916 329 gepgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGL 396
Cdd:NF038329 248 ------------------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.49e-03

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 40.58  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 386765916  210 L 210
Cdd:pfam09755 248 Q 248
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 644-722 5.24e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.27  E-value: 5.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386765916 644 PGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 722
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
485-732 8.50e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 39.63  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 485 GKDGRDGRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGdigppglmgppgLPGPPGYPGV 564
Cdd:COG5164   43 GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTT------------PAGDGGATGP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 565 KGDKGDRGDSYRKMRRRQDDGMSDAPHMPTieylygpPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLP 644
Cdd:COG5164  111 PDDGGATGPPDDGGSTTPPSGGSTTPPGDG-------GSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGST 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 645 GPmGMRGESGPSGPSGKAGIPGAQGETGHKGergdpGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGV 724
Cdd:COG5164  184 TP-PNKGETGTDIPTGGTPRQGPDGPVKKDD-----KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAEL 257


                 ....*...
gi 386765916 725 PGLDAPCP 732
Cdd:COG5164  258 TALEAENR 265
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 509-730 1.47e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 509 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDDgmSD 588
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 589 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQ 668
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765916 669 GETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 730
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 615-739 3.46e-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: 94.20  E-value: 3.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 615 GSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGP 694
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386765916 695 RGEQGSRGDAGPPGKRGRKGD--RGDKGEQGVPGLDAPCplGADGLP 739
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQ--GPDGPA 256
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 350-542 5.90e-13

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: 71.86  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 350 GERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLtttiKGDEFPTGIIEGPPGPAG--PPGPPGEPG 427
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP----QGEAGPQGPAGKDGEAGAkgPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 428 ARGEPGPIGPAGPPGEKGPRGKRGKR----IFGPGGTKIDEDYDDPPVTLLRGPPGPPGIAGKDGRDGRDGSKGEPGEPG 503
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAgedgPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 386765916 504 EPgslGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 542
Cdd:NF038329 276 KD---GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-542 1.46e-09

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: 61.07  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKrsvttlhggtlgyaeivavkge 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK---------------------- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 331 pgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRglTTTIKGDEFPTGii 410
Cdd:NF038329 186 ----------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG--QQGPDGDPGPTG-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 411 egppgpagppgppgepgargepgpigpagppgEKGPRGKRGKRifGPGGTKIDEDYDDPPvtllrGPPGPPGIAGKDGRD 490
Cdd:NF038329 246 --------------------------------EDGPQGPDGPA--GKDGPRGDRGEAGPD-----GPDGKDGERGPVGPA 286

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386765916 491 GRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 542
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 651-707 5.46e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 5.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386765916  651 GESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPP 707
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 639-695 7.18e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 7.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386765916  639 GPMGLPGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPR 695
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 645-701 7.92e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 7.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386765916  645 GPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSR 701
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 666-721 6.93e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 6.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386765916  666 GAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGE 721
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 672-726 8.43e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 8.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386765916  672 GHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPG 726
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-395 2.04e-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: 2.04e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 386765916  348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRG 395
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 675-731 2.93e-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: 2.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386765916  675 GERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAPC 731
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 630-684 3.17e-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: 3.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386765916  630 GEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPG 684
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-394 3.37e-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: 3.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 386765916  348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDR 394
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 657-711 6.25e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 6.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386765916  657 GPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRG 711
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 663-717 1.07e-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: 1.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386765916  663 GIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRG 717
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-396 1.30e-04

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: 45.28  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSVTTLHGGTLGYAeivavk 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765916 329 gepgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGL 396
Cdd:NF038329 248 ------------------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 614-662 7.76e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 7.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 386765916  614 TGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKA 662
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.49e-03

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 40.58  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 386765916  210 L 210
Cdd:pfam09755 248 Q 248
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 644-722 5.24e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.27  E-value: 5.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386765916 644 PGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 722
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
PHA03169 PHA03169
hypothetical protein; Provisional
 615-769 5.66e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 615 GSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPmgmrGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGP 694
Cdd:PHA03169 115 ASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSP 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 695 RGEQGSRGDAGPPGK---------RGRKGDRGDKGE--QGVPGLDAPCPLGADGLPLPG--------CGWRPPKEP---- 751
Cdd:PHA03169 191 GPPQSETPTSSPPPQsppdepgepQSPTPQQAPSPNtqQAVEHEDEPTEPEREGPPFPGhrshsytvVGWKPSTRPggvp 270

                        170       180
                 ....*....|....*....|...
gi 386765916 752 -----IISTPVHKDYLPDVTQPE 769
Cdd:PHA03169 271 klclrCTSHPSHRSRLPEGQQSE 293
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
485-732 8.50e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 39.63  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 485 GKDGRDGRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGdigppglmgppgLPGPPGYPGV 564
Cdd:COG5164   43 GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTT------------PAGDGGATGP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 565 KGDKGDRGDSYRKMRRRQDDGMSDAPHMPTieylygpPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLP 644
Cdd:COG5164  111 PDDGGATGPPDDGGSTTPPSGGSTTPPGDG-------GSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGST 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765916 645 GPmGMRGESGPSGPSGKAGIPGAQGETGHKGergdpGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGV 724
Cdd:COG5164  184 TP-PNKGETGTDIPTGGTPRQGPDGPVKKDD-----KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAEL 257


                 ....*...
gi 386765916 725 PGLDAPCP 732
Cdd:COG5164  258 TALEAENR 265
 
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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