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Conserved domains on  [gi|1690553870|ref|NP_001357932|]
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EMI domain-containing protein 1 isoform 5 precursor [Mus musculus]

Protein Classification

EMI and Collagen domain-containing protein( domain architecture ID 10540621)

EMI and Collagen domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-99 1.52e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 79.39  E-value: 1.52e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1690553870  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQNCPWPMGCPGNRTVVRPLYKVTYKTVTAREWRCCPGHSG 99
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCSTYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-368 3.99e-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: 3.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553870 319 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 368
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 295-424 1.60e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 50.29  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 295 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 374
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1690553870 375 GLHQLREALKILAERvlileTMIGLYEPDLGSG-AGPDGTGTPSLLRGKRG 424
Cdd:NF038329  221 AGEDGPAGPAGDGQQ-----GPDGDPGPTGEDGpQGPDGPAGKDGPRGDRG 266
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 163-369 3.88e-03

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: 39.50  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 163 PSVPATPEDSALLWGSPAARGSPGDGSLQDRLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKM 242
Cdd:NF038329  124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 243 GPPGPPGPPGPPGPPAPVGPPYGQvslhgdpllsntftemgshwpqgptgppgppgppgpmgPPGLPGPMGAPGSPGHMG 322
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPA--------------------------------------GPAGDGQQGPDGDPGPTG 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1690553870 323 IPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEK 369
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN 292
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-99 1.52e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 79.39  E-value: 1.52e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1690553870  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQNCPWPMGCPGNRTVVRPLYKVTYKTVTAREWRCCPGHSG 99
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCSTYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-368 3.99e-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: 3.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553870 319 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 368
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 295-424 1.60e-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: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 295 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 374
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1690553870 375 GLHQLREALKILAERvlileTMIGLYEPDLGSG-AGPDGTGTPSLLRGKRG 424
Cdd:NF038329  221 AGEDGPAGPAGDGQQ-----GPDGDPGPTGEDGpQGPDGPAGKDGPRGDRG 266
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 163-369 3.88e-03

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: 39.50  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 163 PSVPATPEDSALLWGSPAARGSPGDGSLQDRLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKM 242
Cdd:NF038329  124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 243 GPPGPPGPPGPPGPPAPVGPPYGQvslhgdpllsntftemgshwpqgptgppgppgppgpmgPPGLPGPMGAPGSPGHMG 322
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPA--------------------------------------GPAGDGQQGPDGDPGPTG 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1690553870 323 IPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEK 369
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN 292
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 187-374 3.95e-03

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: 39.50  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 187 DGSLQDRLDSW--GLPGPTGPKGGTDSQSPvriRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPY 264
Cdd:NF038329  107 DEGLQQLKGDGekGEPGPAGPAGPAGEQGP---RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 265 GQvslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGER 342
Cdd:NF038329  184 AK----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPD 253

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1690553870 343 GLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 374
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-99 1.52e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 79.39  E-value: 1.52e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1690553870  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQNCPWPMGCPGNRTVVRPLYKVTYKTVTAREWRCCPGHSG 99
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCSTYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-368 3.99e-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: 3.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553870 319 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 368
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 322-369 2.93e-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: 49.80  E-value: 2.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1690553870 322 GIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEK 369
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 295-424 1.60e-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: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 295 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 374
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1690553870 375 GLHQLREALKILAERvlileTMIGLYEPDLGSG-AGPDGTGTPSLLRGKRG 424
Cdd:NF038329  221 AGEDGPAGPAGDGQQ-----GPDGDPGPTGEDGpQGPDGPAGKDGPRGDRG 266
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 163-369 3.88e-03

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: 39.50  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 163 PSVPATPEDSALLWGSPAARGSPGDGSLQDRLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKM 242
Cdd:NF038329  124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 243 GPPGPPGPPGPPGPPAPVGPPYGQvslhgdpllsntftemgshwpqgptgppgppgppgpmgPPGLPGPMGAPGSPGHMG 322
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPA--------------------------------------GPAGDGQQGPDGDPGPTG 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1690553870 323 IPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEK 369
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN 292
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 187-374 3.95e-03

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: 39.50  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 187 DGSLQDRLDSW--GLPGPTGPKGGTDSQSPvriRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPY 264
Cdd:NF038329  107 DEGLQQLKGDGekGEPGPAGPAGPAGEQGP---RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553870 265 GQvslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGER 342
Cdd:NF038329  184 AK----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPD 253

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1690553870 343 GLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 374
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 343-374 7.77e-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: 34.78  E-value: 7.77e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1690553870 343 GLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 374
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
 
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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