NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|497277003|ref|WP_009591220|]
View 

stalk domain-containing protein [Paenibacillus sp. HGF5]

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
BclA_C pfam18573
BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein ...
 297-423 4.06e-51

BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host.


:

Pssm-ID: 436587 [Multi-domain]  Cd Length: 127  Bit Score: 168.22  E-value: 4.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003  297 YAGNTSGGVIPVLLGGTPVPLPDNPKVAGIMADGSSTLFTVHETGIYYISYTINLTSDLLMGSRITRNGISIMQSDEAPI 376
Cdd:pfam18573   1 YAANTSGSTIAVVLGGTPVPLPNNQNLSGITVNGTNTTFTVNEAGRYYISYQVNTTAALLVGLRLLVNGTPVPGSIITPA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 497277003  377 KSKSHFHAQFIEQLNAGDMLNLQLYGVLGAATLAQGNGASLTIIKLA 423
Cdd:pfam18573  81 LSTSSYSNSVIVTLTAGDTISLQLFGLAGAATLGGGTGASLTIIRLA 127
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 151-301 2.41e-28

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: 115.77  E-value: 2.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 151 GNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQgpqgpqgpsgssgssgsqgptGPAGPSGPKGDPGPTGSPGPKGDKGDQ 230
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------------------GPAGPPGPQGERGEKGPAGPQGEAGPQ 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497277003 231 GPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAGGSSTGTYAYAGNT 301
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPT 244
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 48-144 4.90e-25

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


:

Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 98.06  E-value: 4.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003   48 VKGKVLVPIKHVTEILGLSIRWDASAKMITAVRGDLSAELVLGSDVATVRKdtivTKVKLDQPAKLQDNRVMVPLRFLAE 127
Cdd:pfam07833   1 KNGRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNG----QEITLDVPPVLINGRTYVPLRFVAE 76

                          90
                  ....*....|....*..
gi 497277003  128 VFEAKVQWNQQKQLVSI 144
Cdd:pfam07833  77 ALGAKVDWDEATRTVYI 93
 
Name Accession Description Interval E-value
BclA_C pfam18573
BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein ...
 297-423 4.06e-51

BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host.


Pssm-ID: 436587 [Multi-domain]  Cd Length: 127  Bit Score: 168.22  E-value: 4.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003  297 YAGNTSGGVIPVLLGGTPVPLPDNPKVAGIMADGSSTLFTVHETGIYYISYTINLTSDLLMGSRITRNGISIMQSDEAPI 376
Cdd:pfam18573   1 YAANTSGSTIAVVLGGTPVPLPNNQNLSGITVNGTNTTFTVNEAGRYYISYQVNTTAALLVGLRLLVNGTPVPGSIITPA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 497277003  377 KSKSHFHAQFIEQLNAGDMLNLQLYGVLGAATLAQGNGASLTIIKLA 423
Cdd:pfam18573  81 LSTSSYSNSVIVTLTAGDTISLQLFGLAGAATLGGGTGASLTIIRLA 127
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 151-301 2.41e-28

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: 115.77  E-value: 2.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 151 GNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQgpqgpqgpsgssgssgsqgptGPAGPSGPKGDPGPTGSPGPKGDKGDQ 230
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------------------GPAGPPGPQGERGEKGPAGPQGEAGPQ 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497277003 231 GPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAGGSSTGTYAYAGNT 301
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPT 244
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 48-144 4.90e-25

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 98.06  E-value: 4.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003   48 VKGKVLVPIKHVTEILGLSIRWDASAKMITAVRGDLSAELVLGSDVATVRKdtivTKVKLDQPAKLQDNRVMVPLRFLAE 127
Cdd:pfam07833   1 KNGRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNG----QEITLDVPPVLINGRTYVPLRFVAE 76

                          90
                  ....*....|....*..
gi 497277003  128 VFEAKVQWNQQKQLVSI 144
Cdd:pfam07833  77 ALGAKVDWDEATRTVYI 93
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 204-322 7.13e-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: 97.28  E-value: 7.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 204 GPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGP 283
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 497277003 284 VGPAGGSSTGTYAYAGNTSGGVIPVLLGGTPVPLPDNPK 322
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD 238
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-288 3.67e-16

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: 79.95  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 147 GSGGGNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQGPQGPQGPSGS--------SGSSGSQGPTGPAGPSGPKGDPGPT 218
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgdpgpTGEDGPQGPDGPAGKDGPRGDRGEA 268

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 219 GSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAG 288
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 204-255 2.70e-11

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: 58.27  E-value: 2.70e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 497277003  204 GPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKG 255
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
203-302 2.06e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.19  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 203 TGPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAG 282
Cdd:COG5164   36 TRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGG 115

                         90       100
                 ....*....|....*....|
gi 497277003 283 PVGPAGGSSTGTYAYAGNTS 302
Cdd:COG5164  116 ATGPPDDGGSTTPPSGGSTT 135
PHA03169 PHA03169
hypothetical protein; Provisional
 150-293 6.75e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 51.12  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 150 GGNQEQGQPGPAGP---QGPKGEPGEKGPQGPQGPQGPQGPQGPSGSSGSSGSQGPTGPAGPSGPkGDPGPTGSPGPKGD 226
Cdd:PHA03169  82 GEKEERGQGGPSGSgseSVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPSPN 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497277003 227 KGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAGGSSTG 293
Cdd:PHA03169 161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNT 227
 
Name Accession Description Interval E-value
BclA_C pfam18573
BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein ...
 297-423 4.06e-51

BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host.


Pssm-ID: 436587 [Multi-domain]  Cd Length: 127  Bit Score: 168.22  E-value: 4.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003  297 YAGNTSGGVIPVLLGGTPVPLPDNPKVAGIMADGSSTLFTVHETGIYYISYTINLTSDLLMGSRITRNGISIMQSDEAPI 376
Cdd:pfam18573   1 YAANTSGSTIAVVLGGTPVPLPNNQNLSGITVNGTNTTFTVNEAGRYYISYQVNTTAALLVGLRLLVNGTPVPGSIITPA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 497277003  377 KSKSHFHAQFIEQLNAGDMLNLQLYGVLGAATLAQGNGASLTIIKLA 423
Cdd:pfam18573  81 LSTSSYSNSVIVTLTAGDTISLQLFGLAGAATLGGGTGASLTIIRLA 127
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 151-301 2.41e-28

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: 115.77  E-value: 2.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 151 GNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQgpqgpqgpsgssgssgsqgptGPAGPSGPKGDPGPTGSPGPKGDKGDQ 230
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------------------GPAGPPGPQGERGEKGPAGPQGEAGPQ 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497277003 231 GPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAGGSSTGTYAYAGNT 301
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPT 244
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 48-144 4.90e-25

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 98.06  E-value: 4.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003   48 VKGKVLVPIKHVTEILGLSIRWDASAKMITAVRGDLSAELVLGSDVATVRKdtivTKVKLDQPAKLQDNRVMVPLRFLAE 127
Cdd:pfam07833   1 KNGRTLVPLRAIAEALGAKVDWDGKTKTVTITKGGTTIKLTIGSNTATVNG----QEITLDVPPVLINGRTYVPLRFVAE 76

                          90
                  ....*....|....*..
gi 497277003  128 VFEAKVQWNQQKQLVSI 144
Cdd:pfam07833  77 ALGAKVDWDEATRTVYI 93
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 204-322 7.13e-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: 97.28  E-value: 7.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 204 GPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGP 283
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 497277003 284 VGPAGGSSTGTYAYAGNTSGGVIPVLLGGTPVPLPDNPK 322
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD 238
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-288 3.67e-16

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: 79.95  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 147 GSGGGNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQGPQGPQGPSGS--------SGSSGSQGPTGPAGPSGPKGDPGPT 218
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgdpgpTGEDGPQGPDGPAGKDGPRGDRGEA 268

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 219 GSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAG 288
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 204-255 2.70e-11

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: 58.27  E-value: 2.70e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 497277003  204 GPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKG 255
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 228-284 3.03e-11

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: 58.27  E-value: 3.03e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 497277003  228 GDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPV 284
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 204-260 4.26e-10

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: 55.19  E-value: 4.26e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 497277003  204 GPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPV 260
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 156-240 1.52e-08

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: 50.57  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003  156 GQPGPAGPQGPKGEPGEkgpqgpqgpqgpqgpqgpsgssgssgsqgpTGPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGP 235
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGP------------------------------PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50


                  ....*
gi 497277003  236 QGEKG 240
Cdd:pfam01391  51 PGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
203-302 2.06e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.19  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 203 TGPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAG 282
Cdd:COG5164   36 TRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGG 115

                         90       100
                 ....*....|....*....|
gi 497277003 283 PVGPAGGSSTGTYAYAGNTS 302
Cdd:COG5164  116 ATGPPDDGGSTTPPSGGSTT 135
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
147-288 3.11e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.42  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 147 GSGGGNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQGPQGPQGPSGSSGSSGSQGPTGPAGPSGPKGDPGPTGSPGPKGD 226
Cdd:COG5164   94 GNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGS 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497277003 227 KG--DQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQG-------PQGIQGAQGPQGPAGPAGPVGPAG 288
Cdd:COG5164  174 TTppDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDkngkgnpPDDRGGKTGPKDQRPKTNPIERRG 244
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 240-288 5.21e-08

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: 49.03  E-value: 5.21e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 497277003  240 GDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAG 288
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 203-249 5.37e-08

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: 49.03  E-value: 5.37e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 497277003  203 TGPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQG 249
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 31-77 2.09e-07

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 48.75  E-value: 2.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 497277003   31 TMQVNGITKSLDVAPVMVKGKVLVPIKHVTEILGLSIRWDASAKMIT 77
Cdd:pfam07833  46 TATVNGQEITLDVPPVLINGRTYVPLRFVAEALGAKVDWDEATRTVY 92
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 203-247 2.27e-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: 47.49  E-value: 2.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 497277003  203 TGPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGP 247
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 114-148 3.02e-07

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 47.98  E-value: 3.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 497277003  114 QDNRVMVPLRFLAEVFEAKVQWNQQKQLVSIAYGS 148
Cdd:pfam07833   1 KNGRTLVPLRAIAEALGAKVDWDGKTKTVTITKGG 35
PHA03169 PHA03169
hypothetical protein; Provisional
 150-293 6.75e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 51.12  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 150 GGNQEQGQPGPAGP---QGPKGEPGEKGPQGPQGPQGPQGPQGPSGSSGSSGSQGPTGPAGPSGPkGDPGPTGSPGPKGD 226
Cdd:PHA03169  82 GEKEERGQGGPSGSgseSVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPSPN 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497277003 227 KGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAGGSSTG 293
Cdd:PHA03169 161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNT 227
PHA03169 PHA03169
hypothetical protein; Provisional
 147-288 1.69e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 147 GSGGGNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQGPQGPQGPSGSSGSSGSQGPTGPAGPSGPKGDPGPTGSPGP--- 223
Cdd:PHA03169  70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPhep 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 224 -----KGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAG 288
Cdd:PHA03169 150 appesHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTP 219
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 203-321 5.10e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.83  E-value: 5.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 203 TGPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAG 282
Cdd:PRK07764 619 AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAP 698

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 497277003 283 PVG--------PAGGSSTGTYAYAGNTSGGVIPVLLGGTPVPLPDNP 321
Cdd:PRK07764 699 AQPapapaatpPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 154-238 1.30e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003  154 EQGQPGPAGPQGPKGEPGEKgpqgpqgpqgpqgpqgpsgssgssgsqgptGPAGPSGPKGDPGPTGSPGPKGDKGDQGPA 233
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPP------------------------------GPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51


                  ....*
gi 497277003  234 GPQGE 238
Cdd:pfam01391  52 GAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 147-291 2.49e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 147 GSGGGNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQGPQGPQGPSGSSGSSGSQGPTGPAGPSGPKGDPGPTGSPGPKGD 226
Cdd:PHA03169 126 SSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQ 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497277003 227 KGDQGPAGPQGEKGDQGdPGPQGIQGDKGDLGPVGPQGPQgiqgaQGPQGPAGPAGPVGPAGGSS 291
Cdd:PHA03169 206 SPPDEPGEPQSPTPQQA-PSPNTQQAVEHEDEPTEPEREG-----PPFPGHRSHSYTVVGWKPST 264
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 147-296 4.05e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 147 GSGGGNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQGPQGPQGPSGSSGSSGSQGPTGPAGPSGPKGDPGPTGSPGPKGD 226
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGA 696

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 227 KGDQGPAGPQGEKGDQGDPGPQGI-----------QGDKGDLGPVGPQGPQGIQGAQGPQGPAGPAGPVGPAGGSSTGTY 295
Cdd:PRK07764 697 APAQPAPAPAATPPAGQADDPAAQppqaaqgasapSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776


                 .
gi 497277003 296 A 296
Cdd:PRK07764 777 S 777
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 211-316 7.91e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 41.53  E-value: 7.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 211 PKGDPGPT--GSPGPKGDKGDQGP--AGPQGEKGDQGDPGPQGIQGDKgdlgpVGPQG-PQGIQGAQGPQGPAGPAG--- 282
Cdd:PHA03264 285 AKPEPGPVedGAPGRETGGEGEGPepAGRDGAAGGEPKPGPPRPAPDA-----DRPEGwPSLEAITFPPPTPATPAVpra 359

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 497277003 283 -PVGPAGGSSTGTYAYAGNTSGGVIPV---LLGGTPVP 316
Cdd:PHA03264 360 rPVIVGTGIAAAAIACVAAAGAVAYFVytrRRGAGPLP 397
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 151-299 8.44e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 151 GNQEQGQPGPAGPQGPKGEPGEKGPQGPQGPQGPQGPQGPSGSSGSSGSQGPTGPAGPSGPKGDPGPTGSPGPKGDKGDQ 230
Cdd:PRK07764 612 AARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPA 691

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003 231 GPAG-PQGEKGDQGDPGPQGIQGDKGdlgpvGPQGPQGIQGAQGPQGPAGPAGPVGPAGGSSTGTYAYAG 299
Cdd:PRK07764 692 APAGaAPAQPAPAPAATPPAGQADDP-----AAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 147-225 1.52e-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: 1.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497277003  147 GSGGGNQEQGQPGPAGPQGPKGEPGEKgpqgpqgpqgpqgpqgpsgssgssgsqgptGPAGPSGPKGDPGPTGSPGPKG 225
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEP------------------------------GPPGPPGPPGPPGPPGAPGAPG 55
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 204-289 4.71e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497277003  204 GPAGPSGPKGDPGPTGSPGPKGDKGDQGPAGPQGEKGDQGDPGPQGIQGDKGDLGPVGPQGP-----QGIQGAQGPQGPA 278
Cdd:PHA03307  828 GGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPkaaaaAPPAGAPAPRPRP 907

                          90
                  ....*....|...
gi 497277003  279 GPAGPVG--PAGG 289
Cdd:PHA03307  908 APRVKLGpmPPGG 920
 
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