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Conserved domains on  [gi|2217300911|ref|XP_047288389|]
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gliomedin isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
174-414 5.40e-107

Olfactomedin-like domain;


:

Pssm-ID: 460482  Cd Length: 246  Bit Score: 315.63  E-value: 5.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 174 ITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTF-IHLPYYFHGCGHVVYNNSLY 252
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDRGTSGNTLREYASLDDFKNGSPSKkYKLPYPWQGTGHVVYNGSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 253 YHKGGSNTLVRFEFGQET-SQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQ 331
Cdd:pfam02191  81 YNKYNSRNIVKYDLTTRTvAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 332 HVNTTYPKSKAGNAFIARGILYVTD---TKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLM 408
Cdd:pfam02191 161 TWNTSYPKRSAGNAFMVCGVLYAVRsvnTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGYQV 240


                  ....*.
gi 2217300911 409 LYPVQF 414
Cdd:pfam02191 241 TYPVTF 246
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 27-82 9.19e-15

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: 68.29  E-value: 9.19e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQ 82
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-161 6.41e-14

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: 73.02  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGElglQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQG 106
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---AGPQGPAGKDGEAGAKGP-------AGEKGPQG 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217300911 107 PPGPPGPPGPpgppgppgsRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEK 161
Cdd:NF038329  196 PRGETGPAGE---------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
174-414 5.40e-107

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 315.63  E-value: 5.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 174 ITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTF-IHLPYYFHGCGHVVYNNSLY 252
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDRGTSGNTLREYASLDDFKNGSPSKkYKLPYPWQGTGHVVYNGSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 253 YHKGGSNTLVRFEFGQET-SQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQ 331
Cdd:pfam02191  81 YNKYNSRNIVKYDLTTRTvAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 332 HVNTTYPKSKAGNAFIARGILYVTD---TKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLM 408
Cdd:pfam02191 161 TWNTSYPKRSAGNAFMVCGVLYAVRsvnTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGYQV 240


                  ....*.
gi 2217300911 409 LYPVQF 414
Cdd:pfam02191 241 TYPVTF 246
OLF smart00284
Olfactomedin-like domains;
174-414 9.44e-43

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 150.75  E-value: 9.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  174 ITSIGNPVQV-LKVTETFGTWIRESANKS--DDRIWVTEHFSGIM--VKEFKDQPSLLNGSYTFIH-LPYYFHGCGHVVY 247
Cdd:smart00284   3 LAGISKPVTLqTSWKGKSGAWMKDPLWNTtkKSLYWYMPLNTRVLrsVREYSSMSDFQMGKNPTDHpLPHAGQGTGVVVY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  248 NNSLYYHKGGSNTLVRFEFGQETSQTLK-LENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERT 326
Cdd:smart00284  83 NGSLYFNKFNSHDICRFDLTTETYQKEPlLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNPAT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  327 FSVVQHVNTTYPKSKAGNAFIARGILYVTDT---KDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWE 403
Cdd:smart00284 163 LTIENTWITTYNKRSASNAFMICGILYVTRSlgsKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYAWN 242

                          250
                   ....*....|.
gi 2217300911  404 DGHLMLYPVQF 414
Cdd:smart00284 243 NGHLVHYDIAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 27-82 9.19e-15

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: 68.29  E-value: 9.19e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQ 82
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-161 6.41e-14

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: 73.02  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGElglQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQG 106
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---AGPQGPAGKDGEAGAKGP-------AGEKGPQG 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217300911 107 PPGPPGPPGPpgppgppgsRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEK 161
Cdd:NF038329  196 PRGETGPAGE---------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-104 2.31e-11

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: 65.31  E-value: 2.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGdvsndvlLAGAKGD 104
Cdd:NF038329  245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG-------KDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-111 2.88e-11

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: 64.93  E-value: 2.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDVSNDVllAGAKGDQG 106
Cdd:NF038329  162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--DGQQGPDG 239


                  ....*
gi 2217300911 107 PPGPP 111
Cdd:NF038329  240 DPGPT 244
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-140 2.69e-10

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: 61.84  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPG--QKGEKGDKGDVSNDVLlAGAKGD 104
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGP-QGPDGP 255

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217300911 105 QGPPGPPGPPGPPGPPGPPGSRRAKGPRQPSMFNGQ 140
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
174-414 5.40e-107

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 315.63  E-value: 5.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 174 ITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTF-IHLPYYFHGCGHVVYNNSLY 252
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDRGTSGNTLREYASLDDFKNGSPSKkYKLPYPWQGTGHVVYNGSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 253 YHKGGSNTLVRFEFGQET-SQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQ 331
Cdd:pfam02191  81 YNKYNSRNIVKYDLTTRTvAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911 332 HVNTTYPKSKAGNAFIARGILYVTD---TKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLM 408
Cdd:pfam02191 161 TWNTSYPKRSAGNAFMVCGVLYAVRsvnTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGYQV 240


                  ....*.
gi 2217300911 409 LYPVQF 414
Cdd:pfam02191 241 TYPVTF 246
OLF smart00284
Olfactomedin-like domains;
174-414 9.44e-43

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 150.75  E-value: 9.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  174 ITSIGNPVQV-LKVTETFGTWIRESANKS--DDRIWVTEHFSGIM--VKEFKDQPSLLNGSYTFIH-LPYYFHGCGHVVY 247
Cdd:smart00284   3 LAGISKPVTLqTSWKGKSGAWMKDPLWNTtkKSLYWYMPLNTRVLrsVREYSSMSDFQMGKNPTDHpLPHAGQGTGVVVY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  248 NNSLYYHKGGSNTLVRFEFGQETSQTLK-LENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERT 326
Cdd:smart00284  83 NGSLYFNKFNSHDICRFDLTTETYQKEPlLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNPAT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  327 FSVVQHVNTTYPKSKAGNAFIARGILYVTDT---KDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWE 403
Cdd:smart00284 163 LTIENTWITTYNKRSASNAFMICGILYVTRSlgsKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYAWN 242

                          250
                   ....*....|.
gi 2217300911  404 DGHLMLYPVQF 414
Cdd:smart00284 243 NGHLVHYDIAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 27-82 9.19e-15

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: 68.29  E-value: 9.19e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQ 82
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-161 6.41e-14

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: 73.02  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGElglQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQG 106
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---AGPQGPAGKDGEAGAKGP-------AGEKGPQG 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217300911 107 PPGPPGPPGPpgppgppgsRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEK 161
Cdd:NF038329  196 PRGETGPAGE---------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-104 2.31e-11

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: 65.31  E-value: 2.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGdvsndvlLAGAKGD 104
Cdd:NF038329  245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG-------KDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-111 2.88e-11

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: 64.93  E-value: 2.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDVSNDVllAGAKGDQG 106
Cdd:NF038329  162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--DGQQGPDG 239


                  ....*
gi 2217300911 107 PPGPP 111
Cdd:NF038329  240 DPGPT 244
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 26-85 1.16e-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: 56.73  E-value: 1.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  26 NGLDGQPGPQGPKGEKGAngkrgkmgiPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGE 85
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGP---------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-140 2.69e-10

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: 61.84  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300911  27 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPG--QKGEKGDKGDVSNDVLlAGAKGD 104
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGP-QGPDGP 255

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217300911 105 QGPPGPPGPPGPPGPPGPPGSRRAKGPRQPSMFNGQ 140
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 33-85 1.95e-09

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: 53.27  E-value: 1.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217300911  33 GPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGdhgelglqgnegPPGQKGE 85
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG------------PPGPPGP 41
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 25-62 3.71e-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: 3.71e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217300911  25 HNGLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGER 62
Cdd:pfam01391  20 PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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