NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442619458|ref|NP_001163631|]
View 

uncharacterized protein Dmel_CG42342, isoform Q [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 ...
 264-527 7.47e-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: 7.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSvttlhGGTLGYAEIVAVKGEPGEPGPPGPPGEA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-----AGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 344 GQPGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGtKGDKGDRGDRGlTTTIKGDEFPTGiiegppgpagppgpp 423
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPG-PTGEDGPQGPDG--------------- 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 424 gepgargepgpigPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGP 503
Cdd:NF038329 255 -------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        250       260
                 ....*....|....*....|....
gi 442619458 504 PGKRGRKGDRGDKGEQGVPGLDAP 527
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKPAPKTP 345
DUF2046 super family cl25730
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 4.05e-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: 39.43  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619458  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 ...
 264-527 7.47e-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: 7.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSvttlhGGTLGYAEIVAVKGEPGEPGPPGPPGEA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-----AGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 344 GQPGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGtKGDKGDRGDRGlTTTIKGDEFPTGiiegppgpagppgpp 423
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPG-PTGEDGPQGPDG--------------- 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 424 gepgargepgpigPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGP 503
Cdd:NF038329 255 -------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        250       260
                 ....*....|....*....|....
gi 442619458 504 PGKRGRKGDRGDKGEQGVPGLDAP 527
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-536 5.44e-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: 93.05  E-value: 5.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKrsvttlhggtlgyaeivavkge 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK---------------------- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 331 pgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRglTTTIKGDEFPTGii 410
Cdd:NF038329 186 ----------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG--QQGPDGDPGPTG-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 411 egppgpagppgppgepgargepgpigpagPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEG 490
Cdd:NF038329 246 -----------------------------EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 442619458 491 PRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDapcplGADGLP 536
Cdd:NF038329 297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD-----GKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-534 5.79e-12

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: 68.01  E-value: 5.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 418 GPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGS 497
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442619458 498 RGDAGPPGKRGRKGDRGDKGEQGVPGLDAPCPLGADG 534
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 463-518 5.39e-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: 5.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442619458  463 GAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGE 518
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 364-519 6.61e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 46.05  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 364 QGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGARGEPGPIGPAGPPGE 443
Cdd:PRK12678  59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619458 444 KGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 519
Cdd:PRK12678 139 RGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
349-529 8.46e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 8.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 349 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 428
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 429 RGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGdpGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRG 508
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDD--KNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                        170       180
                 ....*....|....*....|.
gi 442619458 509 RKGDRGDKGEQGVPGLDAPCP 529
Cdd:COG5164  245 PERPEAAALPAELTALEAENR 265
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 4.05e-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: 39.43  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619458  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 ...
 264-527 7.47e-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: 7.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 264 GEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKRSvttlhGGTLGYAEIVAVKGEPGEPGPPGPPGEA 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-----AGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 344 GQPGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGtKGDKGDRGDRGlTTTIKGDEFPTGiiegppgpagppgpp 423
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPG-PTGEDGPQGPDG--------------- 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 424 gepgargepgpigPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGP 503
Cdd:NF038329 255 -------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        250       260
                 ....*....|....*....|....
gi 442619458 504 PGKRGRKGDRGDKGEQGVPGLDAP 527
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-536 5.44e-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: 93.05  E-value: 5.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 251 PGKRGKRGKKGDSGEKGDPGLNGISGEKGAAGKPGDKGQKGDVGHPGMDVFQTVKGLKrsvttlhggtlgyaeivavkge 330
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK---------------------- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 331 pgepgppgppgeagqpGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRglTTTIKGDEFPTGii 410
Cdd:NF038329 186 ----------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG--QQGPDGDPGPTG-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 411 egppgpagppgppgepgargepgpigpagPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEG 490
Cdd:NF038329 246 -----------------------------EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 442619458 491 PRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDapcplGADGLP 536
Cdd:NF038329 297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD-----GKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-534 5.79e-12

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: 68.01  E-value: 5.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 418 GPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGS 497
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442619458 498 RGDAGPPGKRGRKGDRGDKGEQGVPGLDAPCPLGADG 534
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 463-518 5.39e-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: 5.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442619458  463 GAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGE 518
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 469-523 6.69e-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: 6.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442619458  469 GHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPG 523
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-395 1.67e-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: 1.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442619458  348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRG 395
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 472-528 2.40e-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: 2.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442619458  472 GERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPGLDAPC 528
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 348-394 2.83e-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: 2.83e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 442619458  348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDR 394
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 443-494 6.58e-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: 43.64  E-value: 6.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442619458  443 EKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGE 494
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 444-492 5.89e-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: 40.94  E-value: 5.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442619458  444 KGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPR 492
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 364-519 6.61e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 46.05  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 364 QGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGARGEPGPIGPAGPPGE 443
Cdd:PRK12678  59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619458 444 KGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQ 519
Cdd:PRK12678 139 RGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
349-529 8.46e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 8.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 349 PGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGA 428
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 429 RGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGdpGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRG 508
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDD--KNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                        170       180
                 ....*....|....*....|.
gi 442619458 509 RKGDRGDKGEQGVPGLDAPCP 529
Cdd:COG5164  245 PERPEAAALPAELTALEAENR 265
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 346-382 1.79e-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: 36.70  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 442619458  346 PGAPGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAP 382
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 374-523 1.88e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 374 GPPGVAGAPGTKGDKGDRGDRGLTTTIKGDEFPTGIIEGPPGPAGPPGPPGEPGARGEPGPIGPAGPPGEKGPRGKRGKR 453
Cdd:PRK12678  60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 454 GPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGVPG 523
Cdd:PRK12678 140 GAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRR 209
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 348-519 3.38e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.27  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 348 APGERGPPGEIGAQGPQGEAGQPGVAGPPGVAGAPGTKGDKGDRGDRGltttikgdefptgiiegPPGPAGPPGPPGEPG 427
Cdd:PRK12678 114 AAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAA-----------------ERTEEEERDERRRRG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458 428 ARGEPGPIGPAGPPGEKGPRGKRGKRGPPGLDGMKGAQGETGHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKR 507
Cdd:PRK12678 177 DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                        170
                 ....*....|..
gi 442619458 508 GRKGDRGDKGEQ 519
Cdd:PRK12678 257 GRGGRRGRRFRD 268
PTZ00146 PTZ00146
fibrillarin; Provisional
 469-521 3.54e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 39.72  E-value: 3.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442619458 469 GHKGERGDPGLPGTDGIPGQEGPRGEQGSRGDAGPPGKRGRKGDRGDKGEQGV 521
Cdd:PTZ00146   5 GFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGKV 57
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 133-210 4.05e-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: 39.43  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619458  133 RLEQRMQRLqqldarivELELRLEQQQLlhwpaeqTQVLASHPSDRDSSNSNNGSQHLELHVRR---ELHRLRRDVSHLQ 209
Cdd:pfam09755 183 RLWKRMDKL--------EAEKRLLQEKL-------DQPVSAPPSPRDSTSEGDTAQNLTAHIQYlrkEVERLRRQLATAQ 247


                  .
gi 442619458  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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH