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Conserved domains on  [gi|767983973|ref|XP_011519803|]
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gliomedin isoform X2 [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;
184-424 7.21e-107

Olfactomedin-like domain;


:

Pssm-ID: 460482  Cd Length: 246  Bit Score: 316.01  E-value: 7.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  184 ITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTF-IHLPYYFHGCGHVVYNNSLY 262
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDRGTSGNTLREYASLDDFKNGSPSKkYKLPYPWQGTGHVVYNGSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  263 YHKGGSNTLVRFEFGQET-SQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQ 341
Cdd:pfam02191  81 YNKYNSRNIVKYDLTTRTvAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  342 HVNTTYPKSKAGNAFIARGILYVTD---TKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLM 418
Cdd:pfam02191 161 TWNTSYPKRSAGNAFMVCGVLYAVRsvnTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGYQV 240


                  ....*.
gi 767983973  419 LYPVQF 424
Cdd:pfam02191 241 TYPVTF 246
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 37-92 7.28e-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: 68.67  E-value: 7.28e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767983973   37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQ 92
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-171 3.87e-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: 73.79  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGElglQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQG 116
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---AGPQGPAGKDGEAGAKGP-------AGEKGPQG 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767983973 117 PPGPPGPPGPpgppgppgsRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEK 171
Cdd:NF038329 196 PRGETGPAGE---------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
184-424 7.21e-107

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 316.01  E-value: 7.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  184 ITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTF-IHLPYYFHGCGHVVYNNSLY 262
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDRGTSGNTLREYASLDDFKNGSPSKkYKLPYPWQGTGHVVYNGSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  263 YHKGGSNTLVRFEFGQET-SQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQ 341
Cdd:pfam02191  81 YNKYNSRNIVKYDLTTRTvAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  342 HVNTTYPKSKAGNAFIARGILYVTD---TKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLM 418
Cdd:pfam02191 161 TWNTSYPKRSAGNAFMVCGVLYAVRsvnTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGYQV 240


                  ....*.
gi 767983973  419 LYPVQF 424
Cdd:pfam02191 241 TYPVTF 246
OLF smart00284
Olfactomedin-like domains;
184-424 1.06e-42

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 150.75  E-value: 1.06e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973   184 ITSIGNPVQV-LKVTETFGTWIRESANKS--DDRIWVTEHFSGIM--VKEFKDQPSLLNGSYTFIH-LPYYFHGCGHVVY 257
Cdd:smart00284   3 LAGISKPVTLqTSWKGKSGAWMKDPLWNTtkKSLYWYMPLNTRVLrsVREYSSMSDFQMGKNPTDHpLPHAGQGTGVVVY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973   258 NNSLYYHKGGSNTLVRFEFGQETSQTLK-LENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERT 336
Cdd:smart00284  83 NGSLYFNKFNSHDICRFDLTTETYQKEPlLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNPAT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973   337 FSVVQHVNTTYPKSKAGNAFIARGILYVTDT---KDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWE 413
Cdd:smart00284 163 LTIENTWITTYNKRSASNAFMICGILYVTRSlgsKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYAWN 242

                          250
                   ....*....|.
gi 767983973   414 DGHLMLYPVQF 424
Cdd:smart00284 243 NGHLVHYDIAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 37-92 7.28e-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: 68.67  E-value: 7.28e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767983973   37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQ 92
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-171 3.87e-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: 73.79  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGElglQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQG 116
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---AGPQGPAGKDGEAGAKGP-------AGEKGPQG 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767983973 117 PPGPPGPPGPpgppgppgsRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEK 171
Cdd:NF038329 196 PRGETGPAGE---------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-114 1.83e-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: 65.70  E-value: 1.83e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGdvsndvlLAGAKGD 114
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG-------KDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-121 2.19e-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: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDVSNDVllAGAKGDQG 116
Cdd:NF038329 162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--DGQQGPDG 239


                 ....*
gi 767983973 117 PPGPP 121
Cdd:NF038329 240 DPGPT 244
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-150 2.10e-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: 62.23  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPG--QKGEKGDKGDVSNDVLlAGAKGD 114
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGP-QGPDGP 255

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767983973 115 QGPPGPPGPPGPPGPPGPPGSRRAKGPRQPSMFNGQ 150
Cdd:NF038329 256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 36-100 9.72e-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: 60.30  E-value: 9.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983973  36 NGLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKG 100
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 55-118 1.35e-06

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: 50.29  E-value: 1.35e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983973  55 GKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQGPP 118
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-------AGPQGEAGPQ 173
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
37-101 8.98e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 38.47  E-value: 8.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767983973  37 GLDGQPGPQG---PKGEKGANGKRGKMGIPGAAGNPGERGEKGDHG---ELGLQGNEGPPGQKGEKGDKGD 101
Cdd:COG5164   52 GSTTPAGNTGgtrPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGgttPAGDGGATGPPDDGGATGPPDD 122
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
184-424 7.21e-107

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 316.01  E-value: 7.21e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  184 ITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTF-IHLPYYFHGCGHVVYNNSLY 262
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTDRGTSGNTLREYASLDDFKNGSPSKkYKLPYPWQGTGHVVYNGSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  263 YHKGGSNTLVRFEFGQET-SQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQ 341
Cdd:pfam02191  81 YNKYNSRNIVKYDLTTRTvAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  342 HVNTTYPKSKAGNAFIARGILYVTD---TKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLM 418
Cdd:pfam02191 161 TWNTSYPKRSAGNAFMVCGVLYAVRsvnTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGYQV 240


                  ....*.
gi 767983973  419 LYPVQF 424
Cdd:pfam02191 241 TYPVTF 246
OLF smart00284
Olfactomedin-like domains;
184-424 1.06e-42

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 150.75  E-value: 1.06e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973   184 ITSIGNPVQV-LKVTETFGTWIRESANKS--DDRIWVTEHFSGIM--VKEFKDQPSLLNGSYTFIH-LPYYFHGCGHVVY 257
Cdd:smart00284   3 LAGISKPVTLqTSWKGKSGAWMKDPLWNTtkKSLYWYMPLNTRVLrsVREYSSMSDFQMGKNPTDHpLPHAGQGTGVVVY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973   258 NNSLYYHKGGSNTLVRFEFGQETSQTLK-LENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERT 336
Cdd:smart00284  83 NGSLYFNKFNSHDICRFDLTTETYQKEPlLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNPAT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973   337 FSVVQHVNTTYPKSKAGNAFIARGILYVTDT---KDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWE 413
Cdd:smart00284 163 LTIENTWITTYNKRSASNAFMICGILYVTRSlgsKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYAWN 242

                          250
                   ....*....|.
gi 767983973   414 DGHLMLYPVQF 424
Cdd:smart00284 243 NGHLVHYDIAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 37-92 7.28e-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: 68.67  E-value: 7.28e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767983973   37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQ 92
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-171 3.87e-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: 73.79  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGElglQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQG 116
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---AGPQGPAGKDGEAGAKGP-------AGEKGPQG 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767983973 117 PPGPPGPPGPpgppgppgsRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEK 171
Cdd:NF038329 196 PRGETGPAGE---------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-114 1.83e-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: 65.70  E-value: 1.83e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGdvsndvlLAGAKGD 114
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG-------KDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-121 2.19e-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: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDVSNDVllAGAKGDQG 116
Cdd:NF038329 162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--DGQQGPDG 239


                 ....*
gi 767983973 117 PPGPP 121
Cdd:NF038329 240 DPGPT 244
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 37-150 2.10e-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: 62.23  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983973  37 GLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPG--QKGEKGDKGDVSNDVLlAGAKGD 114
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGP-QGPDGP 255

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767983973 115 QGPPGPPGPPGPPGPPGPPGSRRAKGPRQPSMFNGQ 150
Cdd:NF038329 256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 36-100 9.72e-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: 60.30  E-value: 9.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983973  36 NGLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKG 100
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 43-95 1.58e-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: 53.65  E-value: 1.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767983973   43 GPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGdhgelglqgnegPPGQKGE 95
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG------------PPGPPGP 41
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 55-118 1.35e-06

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: 50.29  E-value: 1.35e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983973  55 GKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDvsndvllAGAKGDQGPP 118
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-------AGPQGEAGPQ 173
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
37-101 8.98e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 38.47  E-value: 8.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767983973  37 GLDGQPGPQG---PKGEKGANGKRGKMGIPGAAGNPGERGEKGDHG---ELGLQGNEGPPGQKGEKGDKGD 101
Cdd:COG5164   52 GSTTPAGNTGgtrPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGgttPAGDGGATGPPDDGGATGPPDD 122
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 61-112 9.49e-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: 34.39  E-value: 9.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767983973   61 GIPGAAGNPGERGEKGdhgelglqgnegPPGQKGEKGDKGDvsndvllAGAK 112
Cdd:pfam01391   1 GPPGPPGPPGPPGPPG------------PPGPPGPPGPPGP-------PGEP 33
 
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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