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Conserved domains on  [gi|1475409001|ref|NP_001352621|]
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cerebral cavernous malformations 2 protein-like isoform 1 [Homo sapiens]

Protein Classification

cerebral cavernous malformations 2 family protein( domain architecture ID 10881498)

cerebral cavernous malformations 2 (CCM2) family protein is a PTB (phosphotyrosine-binding) domain-containing protein, similar to Homo sapiens CCM2, also called malcavernin, which is a component of the CCM signaling pathway that is a crucial regulator of heart and vessel formation and integrity

Gene Ontology:  GO:0005515
PubMed:  15567406|8987385|10610414

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_CCM2 cd13166
Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22 ...
 41-345 1.28e-101

Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signalling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain and a C-terminal Karet domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269987  Cd Length: 193  Bit Score: 305.19  E-value: 1.28e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001  41 SMPLYPPDYLIDPQILLCDYLEKEVKFLGHLTWVTSSLNPSSRDELLQLLDTARQLKELPLKTTAEQDSILSLSARCLLL 120
Cdd:cd13166     1 SVPLYPPDYRVDPDVLLNDYIEKEVKYLGQLTSVPGSLDPSSRTELLQLLDTARRLGQLPLQLTPEQDAILSLSAYNVKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 121 TWRDNEELILRIPTHEIAAASYLQDDALHLLVLKTGLGVDPVPAGVDASPGGagrdpgppggapekrrvgtaerrhtics 200
Cdd:cd13166    81 LWRDGEDLILRVPTHDIAAVSYVRDDSLHLVVLKTASEPGISPSQSLSAESS---------------------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 201 ldwrmgwgggaaearaggggggslerqragarasgswerrqtfsgswerrhggggggggagkpggswerrqagsggggsw 280
Cdd:cd13166       --------------------------------------------------------------------------------

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1475409001 281 errhPGPNPLDPQDPSPDAYCNLVILAVANRDAAEESCALICQVFQIIYGDQSIECVDRAGYHYT 345
Cdd:cd13166   133 ----PTSGSLSESGPVPVEYCNLVVLACENKAAAEELCSLLCQVFQIVYTESTIDFLDRAIFDGA 193
CCM2_C pfam16545
Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical ...
 403-496 1.44e-51

Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical region of a family of vertebral proteins, mutations in which cause cerebral cavernous malformations (CCMs). These malformations are congenital vascular anomalies of the central nervous system that can result in haemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. This domain is structurally homologous to the N-terminal domain of harmonin, so it is named the CCM2 harmonin-homology domain or CCM2_HHD. This protein is often called Malcavernin.


:

Pssm-ID: 435415  Cd Length: 95  Bit Score: 171.47  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 403 SGSDHSSLGLEQLQDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLYGDRRKFLLLGMRPFIPDQDIGYFE 482
Cdd:pfam16545   1 SDSSNSSSAAELLQDYMVTLRSKLSPDEIQQFALLLREYRLGKSILEFCSELLQLYGDERKFLLLGMRPFIPEKDIGYFE 80

                          90
                  ....*....|....*
gi 1475409001 483 GFLEGVGIREG-GIL 496
Cdd:pfam16545  81 SFLESIGIREGnGIL 95
 
Name Accession Description Interval E-value
PTB_CCM2 cd13166
Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22 ...
 41-345 1.28e-101

Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signalling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain and a C-terminal Karet domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269987  Cd Length: 193  Bit Score: 305.19  E-value: 1.28e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001  41 SMPLYPPDYLIDPQILLCDYLEKEVKFLGHLTWVTSSLNPSSRDELLQLLDTARQLKELPLKTTAEQDSILSLSARCLLL 120
Cdd:cd13166     1 SVPLYPPDYRVDPDVLLNDYIEKEVKYLGQLTSVPGSLDPSSRTELLQLLDTARRLGQLPLQLTPEQDAILSLSAYNVKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 121 TWRDNEELILRIPTHEIAAASYLQDDALHLLVLKTGLGVDPVPAGVDASPGGagrdpgppggapekrrvgtaerrhtics 200
Cdd:cd13166    81 LWRDGEDLILRVPTHDIAAVSYVRDDSLHLVVLKTASEPGISPSQSLSAESS---------------------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 201 ldwrmgwgggaaearaggggggslerqragarasgswerrqtfsgswerrhggggggggagkpggswerrqagsggggsw 280
Cdd:cd13166       --------------------------------------------------------------------------------

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1475409001 281 errhPGPNPLDPQDPSPDAYCNLVILAVANRDAAEESCALICQVFQIIYGDQSIECVDRAGYHYT 345
Cdd:cd13166   133 ----PTSGSLSESGPVPVEYCNLVVLACENKAAAEELCSLLCQVFQIVYTESTIDFLDRAIFDGA 193
CCM2_C pfam16545
Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical ...
 403-496 1.44e-51

Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical region of a family of vertebral proteins, mutations in which cause cerebral cavernous malformations (CCMs). These malformations are congenital vascular anomalies of the central nervous system that can result in haemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. This domain is structurally homologous to the N-terminal domain of harmonin, so it is named the CCM2 harmonin-homology domain or CCM2_HHD. This protein is often called Malcavernin.


Pssm-ID: 435415  Cd Length: 95  Bit Score: 171.47  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 403 SGSDHSSLGLEQLQDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLYGDRRKFLLLGMRPFIPDQDIGYFE 482
Cdd:pfam16545   1 SDSSNSSSAAELLQDYMVTLRSKLSPDEIQQFALLLREYRLGKSILEFCSELLQLYGDERKFLLLGMRPFIPEKDIGYFE 80

                          90
                  ....*....|....*
gi 1475409001 483 GFLEGVGIREG-GIL 496
Cdd:pfam16545  81 SFLESIGIREGnGIL 95
HHD_CCM2 cd13516
harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called ...
 398-493 1.71e-46

harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain. The C-terminal domain of malcavernin, which is represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin. It has also been referred to as the Karet domain.


Pssm-ID: 259825  Cd Length: 97  Bit Score: 158.19  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 398 HGSHCSGSDHS-SLGLEQLQDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLYGDRRKFLLLGMRPFIPDQ 476
Cdd:cd13516     1 HSTSASRSDSSiVSADELLQDYMEVLRSKLTPDELQQFAALLREYRTGSPIEEFCQKLLELYGPERKFLLLGMRPFIPEK 80

                          90
                  ....*....|....*..
gi 1475409001 477 DIGYFEGFLEGVGIREG 493
Cdd:cd13516    81 DLPYFESFLEKIGIADG 97
 
Name Accession Description Interval E-value
PTB_CCM2 cd13166
Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22 ...
 41-345 1.28e-101

Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signalling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain and a C-terminal Karet domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269987  Cd Length: 193  Bit Score: 305.19  E-value: 1.28e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001  41 SMPLYPPDYLIDPQILLCDYLEKEVKFLGHLTWVTSSLNPSSRDELLQLLDTARQLKELPLKTTAEQDSILSLSARCLLL 120
Cdd:cd13166     1 SVPLYPPDYRVDPDVLLNDYIEKEVKYLGQLTSVPGSLDPSSRTELLQLLDTARRLGQLPLQLTPEQDAILSLSAYNVKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 121 TWRDNEELILRIPTHEIAAASYLQDDALHLLVLKTGLGVDPVPAGVDASPGGagrdpgppggapekrrvgtaerrhtics 200
Cdd:cd13166    81 LWRDGEDLILRVPTHDIAAVSYVRDDSLHLVVLKTASEPGISPSQSLSAESS---------------------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 201 ldwrmgwgggaaearaggggggslerqragarasgswerrqtfsgswerrhggggggggagkpggswerrqagsggggsw 280
Cdd:cd13166       --------------------------------------------------------------------------------

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1475409001 281 errhPGPNPLDPQDPSPDAYCNLVILAVANRDAAEESCALICQVFQIIYGDQSIECVDRAGYHYT 345
Cdd:cd13166   133 ----PTSGSLSESGPVPVEYCNLVVLACENKAAAEELCSLLCQVFQIVYTESTIDFLDRAIFDGA 193
CCM2_C pfam16545
Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical ...
 403-496 1.44e-51

Cerebral cavernous malformation protein, harmonin-homology; CCM2_HHD is a folded-helical region of a family of vertebral proteins, mutations in which cause cerebral cavernous malformations (CCMs). These malformations are congenital vascular anomalies of the central nervous system that can result in haemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. This domain is structurally homologous to the N-terminal domain of harmonin, so it is named the CCM2 harmonin-homology domain or CCM2_HHD. This protein is often called Malcavernin.


Pssm-ID: 435415  Cd Length: 95  Bit Score: 171.47  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 403 SGSDHSSLGLEQLQDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLYGDRRKFLLLGMRPFIPDQDIGYFE 482
Cdd:pfam16545   1 SDSSNSSSAAELLQDYMVTLRSKLSPDEIQQFALLLREYRLGKSILEFCSELLQLYGDERKFLLLGMRPFIPEKDIGYFE 80

                          90
                  ....*....|....*
gi 1475409001 483 GFLEGVGIREG-GIL 496
Cdd:pfam16545  81 SFLESIGIREGnGIL 95
HHD_CCM2 cd13516
harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called ...
 398-493 1.71e-46

harmonin-homology domain (harmonin_N_like domain) of malcavernin (CCM2); CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain. The C-terminal domain of malcavernin, which is represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin. It has also been referred to as the Karet domain.


Pssm-ID: 259825  Cd Length: 97  Bit Score: 158.19  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409001 398 HGSHCSGSDHS-SLGLEQLQDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLYGDRRKFLLLGMRPFIPDQ 476
Cdd:cd13516     1 HSTSASRSDSSiVSADELLQDYMEVLRSKLTPDELQQFAALLREYRTGSPIEEFCQKLLELYGPERKFLLLGMRPFIPEK 80

                          90
                  ....*....|....*..
gi 1475409001 477 DIGYFEGFLEGVGIREG 493
Cdd:cd13516    81 DLPYFESFLEKIGIADG 97
harmonin_N_like cd07347
N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin ...
 413-482 7.68e-10

N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin homology domain); This domain is found in harmonin, and similar proteins such as delphilin, and whirlin. These are postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold proteins. Harmonin and whirlin are organizers of the Usher protein network of the inner ear and the retina, delphilin is found at the cerebellar parallel fiber-Purkinje cell synapses. This domain is also found in CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM). CCM2 along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours; the C-terminal domain of malcavernin represented here has also been refered to as the Karet domain. Harmonin contains a single copy of this domain at its N-terminus which binds specifically to a short internal peptide fragment of the cadherin 23 cytoplasmic domain (a component of the Usher protein network). Whirlin contains two copies of this domain; the first of these has been assayed for interaction with the cytoplasmic domain of cadherin 23 and no interaction could be detected.


Pssm-ID: 259818  Cd Length: 78  Bit Score: 55.29  E-value: 7.68e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475409001 413 EQLQDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLYG-DRRKFLLLGMRPFIPDQDIGYFE 482
Cdd:cd07347     3 ELARLFSEQADQLLTDQERAYVTQALSEYRKGRSVEALVADLFPVLDtPAKLSLLQGLRSLIPPKDQQRFD 73
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
 416-477 1.06e-05

harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); Mouse Rtel is an essential protein required for the maintenance of both telomeric and genomic stability. RTEL1 appears to maintain genome stability by suppressing homologous recombination (HR). In vitro, purified human and insect RTEL1 have been shown to promote the disassembly of D loop recombination intermediates, in a reaction dependent upon ATP hydrolysis. Human RTEL1 is implicated in the etiology of Dyskeratosis congenital (DC, is an inherited bone marrow failure and cancer predisposition syndrome). Point mutations in its helicase domains, and truncations which result in loss of its C-terminus have been discovered in DC families. RTEL1 is also a candidate gene influencing glioma susceptibility. The C-terminal domain of RTEL1, represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin.


Pssm-ID: 259826 [Multi-domain]  Cd Length: 99  Bit Score: 44.19  E-value: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475409001 416 QDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLY-GDRRKFLLLGMRPFIPDQD 477
Cdd:cd13932    21 SAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFaEPERHPLLRGFRRFVRPHH 83
 
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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