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Conserved domains on  [gi|442619460|ref|NP_001262640|]
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uncharacterized protein Dmel_CG42342, isoform R [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 ...
 264-522 8.55e-23

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: 101.52  E-value: 8.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGmdvfqtvkdlqeagvnvsastviklkgepgepgppgppgeagQPGA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG------------------------------------------PPGP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 424 RGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPG------------LPGTDGIPGQEGPRGEQG 491
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGpagkdgqngkdgLPGKDGKDGQNGKDGLPG 314

                        250       260       270
                 ....*....|....*....|....*....|.
gi 442619460 492 SRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 522
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
DUF2046 super family cl25730
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 5.51e-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: 39.04  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619460  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 ...
 264-522 8.55e-23

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: 101.52  E-value: 8.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGmdvfqtvkdlqeagvnvsastviklkgepgepgppgppgeagQPGA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG------------------------------------------PPGP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 424 RGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPG------------LPGTDGIPGQEGPRGEQG 491
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGpagkdgqngkdgLPGKDGKDGQNGKDGLPG 314

                        250       260       270
                 ....*....|....*....|....*....|.
gi 442619460 492 SRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 522
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 330-548 6.76e-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: 95.74  E-value: 6.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 330 GPPGPPGEAGQPGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTiKGDEFPTGiiEGPP 409
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE-KGPQGPRG--ETGP 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 410 GPAGPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGE 489
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619460 490 QGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP----CPLGADGLPLPGCGWRPPKEPIISTP 548
Cdd:NF038329 283 VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKdgkdGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-531 2.50e-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: 93.82  E-value: 2.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGhpgmdvfqtvkdlqeagvnvsastviklkgepgepg 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------------------------------ 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 331 ppgppgeagqpgAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGltttikgdefptgiiegpPG 410
Cdd:NF038329 172 ------------PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------------PA 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 411 PAGPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQ 490
Cdd:NF038329 222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442619460 491 GSRGDAGPPGKRGRKGDRGDKGEQGVPGLDapcplGADGLP 531
Cdd:NF038329 302 GKDGQNGKDGLPGKDGKDGQPGKDGLPGKD-----GKDGQP 337
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 458-513 4.31e-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: 4.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442619460  458 GAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGE 513
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 359-514 6.15e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 46.05  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 359 QGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGARGEPGPIGPAGPPGE 438
Cdd:PRK12678  59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619460 439 KGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 514
Cdd:PRK12678 139 RGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
344-524 6.80e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 424 RGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGhkGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRG 503
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDG--PVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                        170       180
                 ....*....|....*....|.
gi 442619460 504 RKGDRGDKGEQGVPGLDAPCP 524
Cdd:COG5164  245 PERPEAAALPAELTALEAENR 265
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 5.51e-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: 39.04  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619460  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 ...
 264-522 8.55e-23

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: 101.52  E-value: 8.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGmdvfqtvkdlqeagvnvsastviklkgepgepgppgppgeagQPGA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG------------------------------------------PPGP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 424 RGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPG------------LPGTDGIPGQEGPRGEQG 491
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGpagkdgqngkdgLPGKDGKDGQNGKDGLPG 314

                        250       260       270
                 ....*....|....*....|....*....|.
gi 442619460 492 SRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP 522
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 330-548 6.76e-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: 95.74  E-value: 6.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 330 GPPGPPGEAGQPGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTiKGDEFPTGiiEGPP 409
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE-KGPQGPRG--ETGP 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 410 GPAGPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGE 489
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619460 490 QGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAP----CPLGADGLPLPGCGWRPPKEPIISTP 548
Cdd:NF038329 283 VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKdgkdGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-531 2.50e-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: 93.82  E-value: 2.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGhpgmdvfqtvkdlqeagvnvsastviklkgepgepg 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------------------------------ 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 331 ppgppgeagqpgAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGltttikgdefptgiiegpPG 410
Cdd:NF038329 172 ------------PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------------PA 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 411 PAGPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQ 490
Cdd:NF038329 222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442619460 491 GSRGDAGPPGKRGRKGDRGDKGEQGVPGLDapcplGADGLP 531
Cdd:NF038329 302 GKDGQNGKDGLPGKDGKDGQPGKDGLPGKD-----GKDGQP 337
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 458-513 4.31e-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: 4.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442619460  458 GAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGE 513
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 464-518 5.35e-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: 5.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619460  464 GHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPG 518
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 343-390 1.34e-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: 1.34e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442619460  343 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRG 390
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 467-523 1.93e-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: 45.18  E-value: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619460  467 GERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAPC 523
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 343-389 2.28e-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: 2.28e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 442619460  343 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDR 389
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 438-489 5.58e-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: 5.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442619460  438 EKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGE 489
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 439-487 4.94e-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: 4.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442619460  439 KGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPR 487
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 359-514 6.15e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 46.05  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 359 QGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGARGEPGPIGPAGPPGE 438
Cdd:PRK12678  59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619460 439 KGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 514
Cdd:PRK12678 139 RGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
344-524 6.80e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 344 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 423
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 424 RGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGhkGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRG 503
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDG--PVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                        170       180
                 ....*....|....*....|.
gi 442619460 504 RKGDRGDKGEQGVPGLDAPCP 524
Cdd:COG5164  245 PERPEAAALPAELTALEAENR 265
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 341-377 1.50e-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: 37.09  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 442619460  341 PGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAP 377
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 369-518 1.74e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.43  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 369 GPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKR 448
Cdd:PRK12678  60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 449 GPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPG 518
Cdd:PRK12678 140 GAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRR 209
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 343-514 2.91e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 343 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGltttikgdefptgiiegPPGPAGPPGPPGEPG 422
Cdd:PRK12678 114 AAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAA-----------------ERTEEEERDERRRRG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460 423 ARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKR 502
Cdd:PRK12678 177 DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                        170
                 ....*....|..
gi 442619460 503 GRKGDRGDKGEQ 514
Cdd:PRK12678 257 GRGGRRGRRFRD 268
PTZ00146 PTZ00146
fibrillarin; Provisional
 464-516 3.26e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 39.72  E-value: 3.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442619460 464 GHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGV 516
Cdd:PTZ00146   5 GFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGKV 57
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 5.51e-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: 39.04  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619460  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619460  210 L 210
Cdd:pfam09755 248 Q 248
 
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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