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Conserved domains on  [gi|1034558063|ref|XP_016856615|]
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BMP/retinoic acid-inducible neural-specific protein 3 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BRINP pfam19052
BMP/retinoic acid-inducible neural-specific protein; This entry represents the BMP/retinoic ...
319-766 0e+00

BMP/retinoic acid-inducible neural-specific protein; This entry represents the BMP/retinoic acid-inducible neural-specific protein (BRINP) family, including BRINP1/2/3. They are predominantly and widely expressed in both the central nervous system (CNS) and peripheral nervous system (PNS). They inhibit neuronal cell proliferation by negative regulation of the cell cycle G1/S transition.


:

Pssm-ID: 465961  Cd Length: 448  Bit Score: 935.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 319 ESDEFKLFMKRLPMNYFLNTSTIMHLWTMDSNFQRRYEQLENSMKQLFLKAQKIVHKLFSLSKRCHKQPLISLPRQRTST 398
Cdd:pfam19052   1 ESEEFQAFVKRLPTDRFLNSSTISHLWAMDAGLQRRYEQLETSLKLLLKKAQRIVRKLFNLSKRCQKQPRIRLPRERPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 399 YWLTRIQSFLYCNENGLLGSFSEETHSCTCPNDQVVCTAFLPCTVGDASACLTCAPDNRTRCGTCNTGYMLSQGLCKPEV 478
Cdd:pfam19052  81 YWLNYIQSLLYCSENNQPGTFSEETHSCTCPYEHPSCQGPIPCSVGEGPACASCASENRTRCGSCNPGYVLSQGLCRPEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 479 AESTDHYIGFETDLQDLEMKYLLQKTDRRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSSLVHMILGLSLQIC 558
Cdd:pfam19052 161 PDSTENYLGLETDLQDLELKYLLQKRDSRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSNLVHMLLGLSLQIC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 559 LTKNSTLEPVLAVYVNPFGGSHSESWFMPVNENSFPDWERTKLDLPLQCYNWTLTLGNKWKTFFETVHIYLRSRIKSNGP 638
Cdd:pfam19052 241 LTKNSTLEPVLSVYVNPFGGSHSESWFMPINENGFPDWERTKLDLPLQCQNWTLTLGNRWKTFFETVHFYLRSRIKTLEP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 639 NGNESIYYEPLEFIDPSRNLGYMKINNIQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNKLSPPGQ 718
Cdd:pfam19052 321 NSNETVYYEPLELADPSRNLGYMKINSLQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNRLSPPGK 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1034558063 719 RRLDLFSCLLRHRLKLSTSEVVRIQSALQAFNAKLPNTMDYDTTKLCS 766
Cdd:pfam19052 401 QRLDLFSCLLRHRLKLSTNEVVRIQSSLQAFSAKLPNSVEYETTKLCS 448
MACPF smart00457
membrane-attack complex / perforin;
79-263 3.99e-39

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 143.34  E-value: 3.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063   79 REFGRWKVNNLAVERRNflgSPLPLAPEFFRNIRLLGRRPTLQQItENLIKKYGTHFLLSATLGGEESLTIFVDKRKLSK 158
Cdd:smart00457   1 FLVARDTVRNRLYSVKL---DELPLALEFLKALRDLPDTYNRGAY-ARFIDDYGTHYITSATLGGEYSLLLVLDKESLER 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063  159 RAEGSDSTT-------NSSSVTLETLHQLAASYFIDRDST-LRRLHHIQIASTAIKVTETRTGPLGCSNYDNLDSVSSVL 230
Cdd:smart00457  77 KGLTSEDISkclagssNSFAGSVSAEHCLQSSSYIKYLSTsLRRESHTQVLGGHVTVLCDLLRGPSSNSLDFSDWAESVP 156
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034558063  231 VQSPENKIQLQGLQVLLPDY-----LQERFVQAALSYI 263
Cdd:smart00457 157 NEPVLIDVSLAPIYELLPPNpelsqKREALRQALRSYL 194
 
Name Accession Description Interval E-value
BRINP pfam19052
BMP/retinoic acid-inducible neural-specific protein; This entry represents the BMP/retinoic ...
319-766 0e+00

BMP/retinoic acid-inducible neural-specific protein; This entry represents the BMP/retinoic acid-inducible neural-specific protein (BRINP) family, including BRINP1/2/3. They are predominantly and widely expressed in both the central nervous system (CNS) and peripheral nervous system (PNS). They inhibit neuronal cell proliferation by negative regulation of the cell cycle G1/S transition.


Pssm-ID: 465961  Cd Length: 448  Bit Score: 935.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 319 ESDEFKLFMKRLPMNYFLNTSTIMHLWTMDSNFQRRYEQLENSMKQLFLKAQKIVHKLFSLSKRCHKQPLISLPRQRTST 398
Cdd:pfam19052   1 ESEEFQAFVKRLPTDRFLNSSTISHLWAMDAGLQRRYEQLETSLKLLLKKAQRIVRKLFNLSKRCQKQPRIRLPRERPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 399 YWLTRIQSFLYCNENGLLGSFSEETHSCTCPNDQVVCTAFLPCTVGDASACLTCAPDNRTRCGTCNTGYMLSQGLCKPEV 478
Cdd:pfam19052  81 YWLNYIQSLLYCSENNQPGTFSEETHSCTCPYEHPSCQGPIPCSVGEGPACASCASENRTRCGSCNPGYVLSQGLCRPEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 479 AESTDHYIGFETDLQDLEMKYLLQKTDRRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSSLVHMILGLSLQIC 558
Cdd:pfam19052 161 PDSTENYLGLETDLQDLELKYLLQKRDSRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSNLVHMLLGLSLQIC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 559 LTKNSTLEPVLAVYVNPFGGSHSESWFMPVNENSFPDWERTKLDLPLQCYNWTLTLGNKWKTFFETVHIYLRSRIKSNGP 638
Cdd:pfam19052 241 LTKNSTLEPVLSVYVNPFGGSHSESWFMPINENGFPDWERTKLDLPLQCQNWTLTLGNRWKTFFETVHFYLRSRIKTLEP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 639 NGNESIYYEPLEFIDPSRNLGYMKINNIQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNKLSPPGQ 718
Cdd:pfam19052 321 NSNETVYYEPLELADPSRNLGYMKINSLQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNRLSPPGK 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1034558063 719 RRLDLFSCLLRHRLKLSTSEVVRIQSALQAFNAKLPNTMDYDTTKLCS 766
Cdd:pfam19052 401 QRLDLFSCLLRHRLKLSTNEVVRIQSSLQAFSAKLPNSVEYETTKLCS 448
MACPF smart00457
membrane-attack complex / perforin;
79-263 3.99e-39

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 143.34  E-value: 3.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063   79 REFGRWKVNNLAVERRNflgSPLPLAPEFFRNIRLLGRRPTLQQItENLIKKYGTHFLLSATLGGEESLTIFVDKRKLSK 158
Cdd:smart00457   1 FLVARDTVRNRLYSVKL---DELPLALEFLKALRDLPDTYNRGAY-ARFIDDYGTHYITSATLGGEYSLLLVLDKESLER 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063  159 RAEGSDSTT-------NSSSVTLETLHQLAASYFIDRDST-LRRLHHIQIASTAIKVTETRTGPLGCSNYDNLDSVSSVL 230
Cdd:smart00457  77 KGLTSEDISkclagssNSFAGSVSAEHCLQSSSYIKYLSTsLRRESHTQVLGGHVTVLCDLLRGPSSNSLDFSDWAESVP 156
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034558063  231 VQSPENKIQLQGLQVLLPDY-----LQERFVQAALSYI 263
Cdd:smart00457 157 NEPVLIDVSLAPIYELLPPNpelsqKREALRQALRSYL 194
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
52-159 3.98e-06

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 48.56  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063  52 GPFHRSQEYTDFVDRSRQgfsTRYKIYREFGRWKVNNLAVERRNFLgsplPLAPEFFRNIRLLGRRPTLQQITE--NLIK 129
Cdd:pfam01823   1 GSFSASSEFKKMSDKSKQ---KKKSLIISKSTCSLYQFTLKRSNKL----QLSDEFLQALSDLPDNYDYAAKATyiQFFD 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1034558063 130 KYGTHFLLSATLGGEESLTIFVDKRKLSKR 159
Cdd:pfam01823  74 KYGTHYITSVTLGGKIVYVLKLDKSQLEDL 103
 
Name Accession Description Interval E-value
BRINP pfam19052
BMP/retinoic acid-inducible neural-specific protein; This entry represents the BMP/retinoic ...
319-766 0e+00

BMP/retinoic acid-inducible neural-specific protein; This entry represents the BMP/retinoic acid-inducible neural-specific protein (BRINP) family, including BRINP1/2/3. They are predominantly and widely expressed in both the central nervous system (CNS) and peripheral nervous system (PNS). They inhibit neuronal cell proliferation by negative regulation of the cell cycle G1/S transition.


Pssm-ID: 465961  Cd Length: 448  Bit Score: 935.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 319 ESDEFKLFMKRLPMNYFLNTSTIMHLWTMDSNFQRRYEQLENSMKQLFLKAQKIVHKLFSLSKRCHKQPLISLPRQRTST 398
Cdd:pfam19052   1 ESEEFQAFVKRLPTDRFLNSSTISHLWAMDAGLQRRYEQLETSLKLLLKKAQRIVRKLFNLSKRCQKQPRIRLPRERPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 399 YWLTRIQSFLYCNENGLLGSFSEETHSCTCPNDQVVCTAFLPCTVGDASACLTCAPDNRTRCGTCNTGYMLSQGLCKPEV 478
Cdd:pfam19052  81 YWLNYIQSLLYCSENNQPGTFSEETHSCTCPYEHPSCQGPIPCSVGEGPACASCASENRTRCGSCNPGYVLSQGLCRPEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 479 AESTDHYIGFETDLQDLEMKYLLQKTDRRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSSLVHMILGLSLQIC 558
Cdd:pfam19052 161 PDSTENYLGLETDLQDLELKYLLQKRDSRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSNLVHMLLGLSLQIC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 559 LTKNSTLEPVLAVYVNPFGGSHSESWFMPVNENSFPDWERTKLDLPLQCYNWTLTLGNKWKTFFETVHIYLRSRIKSNGP 638
Cdd:pfam19052 241 LTKNSTLEPVLSVYVNPFGGSHSESWFMPINENGFPDWERTKLDLPLQCQNWTLTLGNRWKTFFETVHFYLRSRIKTLEP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063 639 NGNESIYYEPLEFIDPSRNLGYMKINNIQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNKLSPPGQ 718
Cdd:pfam19052 321 NSNETVYYEPLELADPSRNLGYMKINSLQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNRLSPPGK 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1034558063 719 RRLDLFSCLLRHRLKLSTSEVVRIQSALQAFNAKLPNTMDYDTTKLCS 766
Cdd:pfam19052 401 QRLDLFSCLLRHRLKLSTNEVVRIQSSLQAFSAKLPNSVEYETTKLCS 448
MACPF smart00457
membrane-attack complex / perforin;
79-263 3.99e-39

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 143.34  E-value: 3.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063   79 REFGRWKVNNLAVERRNflgSPLPLAPEFFRNIRLLGRRPTLQQItENLIKKYGTHFLLSATLGGEESLTIFVDKRKLSK 158
Cdd:smart00457   1 FLVARDTVRNRLYSVKL---DELPLALEFLKALRDLPDTYNRGAY-ARFIDDYGTHYITSATLGGEYSLLLVLDKESLER 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063  159 RAEGSDSTT-------NSSSVTLETLHQLAASYFIDRDST-LRRLHHIQIASTAIKVTETRTGPLGCSNYDNLDSVSSVL 230
Cdd:smart00457  77 KGLTSEDISkclagssNSFAGSVSAEHCLQSSSYIKYLSTsLRRESHTQVLGGHVTVLCDLLRGPSSNSLDFSDWAESVP 156
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034558063  231 VQSPENKIQLQGLQVLLPDY-----LQERFVQAALSYI 263
Cdd:smart00457 157 NEPVLIDVSLAPIYELLPPNpelsqKREALRQALRSYL 194
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
52-159 3.98e-06

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 48.56  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558063  52 GPFHRSQEYTDFVDRSRQgfsTRYKIYREFGRWKVNNLAVERRNFLgsplPLAPEFFRNIRLLGRRPTLQQITE--NLIK 129
Cdd:pfam01823   1 GSFSASSEFKKMSDKSKQ---KKKSLIISKSTCSLYQFTLKRSNKL----QLSDEFLQALSDLPDNYDYAAKATyiQFFD 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1034558063 130 KYGTHFLLSATLGGEESLTIFVDKRKLSKR 159
Cdd:pfam01823  74 KYGTHYITSVTLGGKIVYVLKLDKSQLEDL 103
 
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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