NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442619454|ref|NP_001138064|]
View 

uncharacterized protein Dmel_CG42342, isoform O [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 504-725 3.09e-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: 106.53  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 504 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDDgmSD 583
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 584 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQ 663
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619454 664 GETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 725
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 264-537 3.78e-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: 72.25  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGmdvfqtvkdlqeagvnvsastviklkgepgepgppgppgeagqpgA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG---------------------------------------------P 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:NF038329 152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 424 RGEPGPIGPAGPPGEKGPRGKRGKrifgpggtkidedyddppvtllrgppgppgiAGKDGRDGRDGSKGEPGEPGEPgsl 503
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGP-------------------------------AGKDGPRGDRGEAGPDGPDGKD--- 277

                        250       260       270
                 ....*....|....*....|....*....|....
gi 442619454 504 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 537
Cdd:NF038329 278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
DUF2046 super family cl25730
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.35e-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: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619454  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 ...
 504-725 3.09e-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: 106.53  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 504 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDDgmSD 583
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 584 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQ 663
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619454 664 GETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 725
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-734 3.00e-22

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: 100.36  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 508 LDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRR--RQDDGMSDAP 585
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAgaKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 586 HMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDpGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQGE 665
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442619454 666 TGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDapcplGADGLP 734
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD-----GKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 264-537 3.78e-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: 72.25  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGmdvfqtvkdlqeagvnvsastviklkgepgepgppgppgeagqpgA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG---------------------------------------------P 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:NF038329 152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 424 RGEPGPIGPAGPPGEKGPRGKRGKrifgpggtkidedyddppvtllrgppgppgiAGKDGRDGRDGSKGEPGEPGEPgsl 503
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGP-------------------------------AGKDGPRGDRGEAGPDGPDGKD--- 277

                        250       260       270
                 ....*....|....*....|....*....|....
gi 442619454 504 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 537
Cdd:NF038329 278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 646-702 8.47e-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: 46.33  E-value: 8.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619454  646 GESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPP 702
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 343-390 3.02e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 3.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442619454  343 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRG 390
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-391 3.86e-05

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: 46.82  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKDLQEAGvnvsastviklkgepge 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG----------------- 236

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619454 329 pgPPGPPGEAGQPGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGL 391
Cdd:NF038329 237 --PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.35e-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: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619454  210 L 210
Cdd:pfam09755 248 Q 248
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
480-727 4.94e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.01  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 480 GKDGRDGRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGdigppglmgppgLPGPPGYPGV 559
Cdd:COG5164   43 GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTT------------PAGDGGATGP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 560 KGDKGDRGDSYRKMRRRQDDGMSDAPHMPTieylygpPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLP 639
Cdd:COG5164  111 PDDGGATGPPDDGGSTTPPSGGSTTPPGDG-------GSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGST 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 640 GPmGMRGESGPSGPSGKAGIPGAQGETGHKGergdpGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGV 719
Cdd:COG5164  184 TP-PNKGETGTDIPTGGTPRQGPDGPVKKDD-----KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAEL 257


                 ....*...
gi 442619454 720 PGLDAPCP 727
Cdd:COG5164  258 TALEAENR 265
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 639-717 5.46e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.27  E-value: 5.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442619454 639 PGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 717
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 504-725 3.09e-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: 106.53  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 504 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRRRQDDgmSD 583
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 584 APHMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQ 663
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619454 664 GETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 725
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-734 3.00e-22

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: 100.36  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 508 LDGLPGEPGIEGPPGLPGYQGPPGEKGDRGDIGPPGLMGPPGLPGPPGYPGVKGDKGDRGDSYRKMRR--RQDDGMSDAP 585
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAgaKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 586 HMPTIEYLYGPPGPPGPMGPPGHTGSQGERGLDGRKGDpGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQGE 665
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442619454 666 TGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDapcplGADGLP 734
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD-----GKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 264-537 3.78e-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: 72.25  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGmdvfqtvkdlqeagvnvsastviklkgepgepgppgppgeagqpgA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG---------------------------------------------P 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:NF038329 152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 424 RGEPGPIGPAGPPGEKGPRGKRGKrifgpggtkidedyddppvtllrgppgppgiAGKDGRDGRDGSKGEPGEPGEPgsl 503
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGP-------------------------------AGKDGPRGDRGEAGPDGPDGKD--- 277

                        250       260       270
                 ....*....|....*....|....*....|....
gi 442619454 504 GPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRG 537
Cdd:NF038329 278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 646-702 8.47e-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: 46.33  E-value: 8.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619454  646 GESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPP 702
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 634-690 1.11e-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: 1.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619454  634 GPMGLPGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPR 690
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 640-696 1.18e-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: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619454  640 GPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSR 696
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 661-716 1.06e-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: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442619454  661 GAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGE 716
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 667-721 1.26e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 1.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619454  667 GHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPG 721
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 343-390 3.02e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 3.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442619454  343 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRG 390
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-391 3.86e-05

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: 46.82  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 249 GPPGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKDLQEAGvnvsastviklkgepge 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG----------------- 236

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619454 329 pgPPGPPGEAGQPGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGL 391
Cdd:NF038329 237 --PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 670-726 4.21e-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: 4.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619454  670 GERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAPC 726
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 625-679 4.65e-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: 4.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619454  625 GEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPG 679
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 343-389 4.88e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 4.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 442619454  343 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDR 389
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 652-706 9.16e-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: 40.55  E-value: 9.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619454  652 GPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRG 706
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 658-712 1.59e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619454  658 GIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRG 712
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 609-657 1.05e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442619454  609 TGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKA 657
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 2.35e-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: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619454  210 L 210
Cdd:pfam09755 248 Q 248
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
480-727 4.94e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.01  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 480 GKDGRDGRDGSKGEPGEPGEPGSLGPRGLDGLPGEPGIEGPPGLPGYQGPPGEKGDRGdigppglmgppgLPGPPGYPGV 559
Cdd:COG5164   43 GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTT------------PAGDGGATGP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 560 KGDKGDRGDSYRKMRRRQDDGMSDAPHMPTieylygpPGPPGPMGPPGHTGSQGERGLDGRKGDPGEKGHKGDQGPMGLP 639
Cdd:COG5164  111 PDDGGATGPPDDGGSTTPPSGGSTTPPGDG-------GSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGST 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 640 GPmGMRGESGPSGPSGKAGIPGAQGETGHKGergdpGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGV 719
Cdd:COG5164  184 TP-PNKGETGTDIPTGGTPRQGPDGPVKKDD-----KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAEL 257


                 ....*...
gi 442619454 720 PGLDAPCP 727
Cdd:COG5164  258 TALEAENR 265
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 639-717 5.46e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.27  E-value: 5.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442619454 639 PGPMGMRGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 717
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
609-736 6.56e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 39.63  E-value: 6.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 609 TGSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPMGMRGESGPSGPSGKAGiPGAQGETGHKGERGD-PGLPGTDGIPGQE 687
Cdd:COG5164   78 QGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGStPPGPGSTGPGGST 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442619454 688 GPRGEQGSRGDAGPPGKRGRKGDRG-----DKGEQGVPGLDAPCPLGADGLPLP 736
Cdd:COG5164  157 TPPGDGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVK 210
PHA03169 PHA03169
hypothetical protein; Provisional
 610-718 8.65e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 8.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619454 610 GSQGERGLDGRKGDPGEKGHKGDQGPMGLPGPmgmrGESGPSGPSGKAGIPGAQGETGHKGERGDPGLPGTDGIPGQEGP 689
Cdd:PHA03169 115 ASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSP 190

                         90       100
                 ....*....|....*....|....*....
gi 442619454 690 RGEQGSRGDAGPPGKRGRKGDRGDKGEQG 718
Cdd:PHA03169 191 GPPQSETPTSSPPPQSPPDEPGEPQSPTP 219
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH