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Conserved domains on  [gi|442619464|ref|NP_001262641|]
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uncharacterized protein Dmel_CG42342, isoform T [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 ...
 509-739 8.71e-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: 105.37  E-value: 8.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 509 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDdgmsd 588
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET----- 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 589 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGPP 668
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER 280

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442619464 669 GLDGmkgaqgETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 739
Cdd:NF038329 281 GPVG------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 350-542 9.49e-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: 71.09  E-value: 9.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 350 GERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLtttiKGDEFPTGIIEGPPGPAG--PPGPPGEPG 427
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP----QGEAGPQGPAGKDGEAGAkgPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 428 ARGEPGPIGPAGPPGEKGPRGKRGKR----IFGPGGTKIDEDYDDPPVTLLRGPPGPPGIAGKDGRDGRDGSKGEPGEPG 503
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAgedgPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 442619464 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 1.68e-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: 44.90  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSVTTLHGGTLGYAeivavk 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442619464 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 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619464  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 ...
 509-739 8.71e-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: 105.37  E-value: 8.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 509 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDdgmsd 588
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET----- 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 589 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGPP 668
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER 280

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442619464 669 GLDGmkgaqgETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 739
Cdd:NF038329 281 GPVG------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 615-750 4.02e-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: 97.28  E-value: 4.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 615 GSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIP---GPPGLDGMKGAQGETGHKGERGDPGL 691
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAgakGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 692 PGTDGIPGQEGPRGEQGSRGDaGPPGKRGRKGDRGDKGEQGVPGLDAP-CPLGADGLPLP 750
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKdGPRGDRGEAGP 270
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 350-542 9.49e-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: 71.09  E-value: 9.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 350 GERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLtttiKGDEFPTGIIEGPPGPAG--PPGPPGEPG 427
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP----QGEAGPQGPAGKDGEAGAkgPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 428 ARGEPGPIGPAGPPGEKGPRGKRGKR----IFGPGGTKIDEDYDDPPVTLLRGPPGPPGIAGKDGRDGRDGSKGEPGEPG 503
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAgedgPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 442619464 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 2.54e-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: 60.30  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKrsvttlhggtlgyaeivavkge 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK---------------------- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 331 pgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRglTTTIKGDEFPTGii 410
Cdd:NF038329 186 ----------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG--QQGPDGDPGPTG-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 411 egppgpagppgppgepgargepgpigpagppgEKGPRGKRGKRifGPGGTKIDEDYDDPPvtllrGPPGPPGIAGKDGRD 490
Cdd:NF038329 246 --------------------------------EDGPQGPDGPA--GKDGPRGDRGEAGPD-----GPDGKDGERGPVGPA 286

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442619464 491 GRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 542
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 639-693 6.98e-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: 6.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619464  639 GPMGLPGPMGMRGESGPSGPSGKAGIPGPPGLDGMKGAQGETGHKGERGDPGLPG 693
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-395 2.72e-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: 2.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442619464  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 1.68e-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: 44.90  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSVTTLHGGTLGYAeivavk 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442619464 329 gepgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGL 396
Cdd:NF038329 248 ------------------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
PHA03169 PHA03169
hypothetical protein; Provisional
 614-778 1.14e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 614 TGSQGERGLDGRKGDPGEKGHKGDqgpmGLPGPMGMRGESGPSGPSGKAGIPGPPGLDGMKGAQGETGHKGERGDPGLPG 693
Cdd:PHA03169 123 TSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 694 TDGIPGQEGPRGEqgsrgdaGPPGKRGRKGDRGDKGEQGVPGLDAPCPLGADGLPLPG--------CGWRPPKEP----- 760
Cdd:PHA03169 199 TSSPPPQSPPDEP-------GEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGhrshsytvVGWKPSTRPggvpk 271

                        170       180
                 ....*....|....*....|..
gi 442619464 761 ----IISTPVHKDYLPDVTQPE 778
Cdd:PHA03169 272 lclrCTSHPSHRSRLPEGQQSE 293
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619464  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 ...
 509-739 8.71e-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: 105.37  E-value: 8.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 509 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDdgmsd 588
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET----- 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 589 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGPP 668
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER 280

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442619464 669 GLDGmkgaqgETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 739
Cdd:NF038329 281 GPVG------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 615-750 4.02e-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: 97.28  E-value: 4.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 615 GSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIP---GPPGLDGMKGAQGETGHKGERGDPGL 691
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAgakGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 692 PGTDGIPGQEGPRGEQGSRGDaGPPGKRGRKGDRGDKGEQGVPGLDAP-CPLGADGLPLP 750
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKdGPRGDRGEAGP 270
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 350-542 9.49e-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: 71.09  E-value: 9.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 350 GERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLtttiKGDEFPTGIIEGPPGPAG--PPGPPGEPG 427
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP----QGEAGPQGPAGKDGEAGAkgPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 428 ARGEPGPIGPAGPPGEKGPRGKRGKR----IFGPGGTKIDEDYDDPPVTLLRGPPGPPGIAGKDGRDGRDGSKGEPGEPG 503
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAgedgPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 442619464 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 2.54e-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: 60.30  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKrsvttlhggtlgyaeivavkge 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK---------------------- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 331 pgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRglTTTIKGDEFPTGii 410
Cdd:NF038329 186 ----------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG--QQGPDGDPGPTG-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 411 egppgpagppgppgepgargepgpigpagppgEKGPRGKRGKRifGPGGTKIDEDYDDPPvtllrGPPGPPGIAGKDGRD 490
Cdd:NF038329 246 --------------------------------EDGPQGPDGPA--GKDGPRGDRGEAGPD-----GPDGKDGERGPVGPA 286

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442619464 491 GRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 542
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 639-693 6.98e-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: 6.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619464  639 GPMGLPGPMGMRGESGPSGPSGKAGIPGPPGLDGMKGAQGETGHKGERGDPGLPG 693
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 663-719 1.33e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 1.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619464  663 GIPGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKR 719
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 660-716 1.96e-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: 1.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619464  660 GKAGIPGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPP 716
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 648-704 3.16e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 3.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619464  648 GMRGESGPSGPSGKAGIPGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPR 704
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 675-730 9.41e-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: 9.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442619464  675 GAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGE 730
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 681-735 1.13e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 1.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619464  681 GHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPG 735
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-395 2.72e-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: 2.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442619464  348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRG 395
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 684-740 3.79e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 3.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619464  684 GERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAPC 740
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-394 4.57e-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: 4.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 442619464  348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDR 394
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 630-686 1.01e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619464  630 GEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGPPGLDGMKGAQGETGHKGER 686
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-396 1.68e-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: 44.90  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSVTTLHGGTLGYAeivavk 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442619464 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 9.65e-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: 37.86  E-value: 9.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442619464  614 TGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKA 662
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 614-778 1.14e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 614 TGSQGERGLDGRKGDPGEKGHKGDqgpmGLPGPMGMRGESGPSGPSGKAGIPGPPGLDGMKGAQGETGHKGERGDPGLPG 693
Cdd:PHA03169 123 TSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 694 TDGIPGQEGPRGEqgsrgdaGPPGKRGRKGDRGDKGEQGVPGLDAPCPLGADGLPLPG--------CGWRPPKEP----- 760
Cdd:PHA03169 199 TSSPPPQSPPDEP-------GEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGhrshsytvVGWKPSTRPggvpk 271

                        170       180
                 ....*....|....*....|..
gi 442619464 761 ----IISTPVHKDYLPDVTQPE 778
Cdd:PHA03169 272 lclrCTSHPSHRSRLPEGQQSE 293
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619464  210 L 210
Cdd:pfam09755 248 Q 248
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 650-731 2.75e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.43  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619464 650 RGESGPSGPSGKAGIPGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKG 729
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQG 212


                 ..
gi 442619464 730 EQ 731
Cdd:PRK12678 213 DR 214
 
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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