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Conserved domains on  [gi|1051356712|gb|AOA60066|]
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MCPH1 [Homo sapiens]

Protein Classification

BRCT_microcephalin_rpt1 and Microcephalin domain-containing protein( domain architecture ID 13026447)

BRCT_microcephalin_rpt1 and Microcephalin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 225-607 0e+00

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


:

Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 600.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 225 EYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQR 304
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 305 NIAGKVVTPHQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPR 384
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHSRPKSSSAKRKRTSEDLNSPPKEKLKKKRSSRKSAMPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 385 LQLCRSEGRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCV 464
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 465 GKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTS----APEEALRCCRQAG---KEDACPEGNGFSYTIEDPALPKG 537
Cdd:pfam12258 241 GKKPRSVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSegtpAAEETPGCCRQAGpqkREDAGPEGNSHSHTTDEPALPSG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 538 HDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYS 607
Cdd:pfam12258 321 HHGDLTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSDYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 8-86 1.23e-39

first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat.


:

Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 140.02  E-value: 1.23e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051356712   8 DVVAYVEVWSSNGtENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEECRTAGAHI 86
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
 
Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 225-607 0e+00

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 600.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 225 EYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQR 304
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 305 NIAGKVVTPHQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPR 384
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHSRPKSSSAKRKRTSEDLNSPPKEKLKKKRSSRKSAMPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 385 LQLCRSEGRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCV 464
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 465 GKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTS----APEEALRCCRQAG---KEDACPEGNGFSYTIEDPALPKG 537
Cdd:pfam12258 241 GKKPRSVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSegtpAAEETPGCCRQAGpqkREDAGPEGNSHSHTTDEPALPSG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 538 HDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYS 607
Cdd:pfam12258 321 HHGDLTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSDYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 8-86 1.23e-39

first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat.


Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 140.02  E-value: 1.23e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051356712   8 DVVAYVEVWSSNGtENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEECRTAGAHI 86
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 13-75 1.94e-17

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 76.86  E-value: 1.94e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1051356712  13 VEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLW 75
Cdd:pfam12738   1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT smart00292
breast cancer carboxy-terminal domain;
4-79 6.31e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 47.37  E-value: 6.31e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051356712    4 PILKDVVAYVevwSSNGTENYSKTFTTQLVDMGAKVSKTFN-KQVTHVIFKDGYQST--WDKAQKRGVKLVSVLWVEEC 79
Cdd:smart00292   2 KLFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
 
Name Accession Description Interval E-value
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 225-607 0e+00

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 600.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 225 EYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQR 304
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSSASSGCLSQLTPQKSKSNLSKEEINWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 305 NIAGKVVTPHQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPR 384
Cdd:pfam12258  81 DAVGEVVTPDRKQAEGVSKGMFDEKDSLSPALSATKGHPLGHSRPKSSSAKRKRTSEDLNSPPKEKLKKKRSSRKSAMPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 385 LQLCRSEGRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCV 464
Cdd:pfam12258 161 LQLFKSENSLQLMTRPAVETPDCEESSYDDYFSPDNLKERNSENLPPGSQPLSSPAQLSCRSLSKRERKSILEMSDFSCI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 465 GKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTS----APEEALRCCRQAG---KEDACPEGNGFSYTIEDPALPKG 537
Cdd:pfam12258 241 GKKPRSVDITDLTAKTSSSLQKPTNDEGNTTLSCLTSegtpAAEETPGCCRQAGpqkREDAGPEGNSHSHTTDEPALPSG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051356712 538 HDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYS 607
Cdd:pfam12258 321 HHGDLTPLKGSSEEMRESVDVKSTQKEGATSKTLNSSEGEAQSDYKLNFVGDCNVEKSTEEKENPARGYS 390
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 8-86 1.23e-39

first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat.


Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 140.02  E-value: 1.23e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051356712   8 DVVAYVEVWSSNGtENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEECRTAGAHI 86
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 13-75 1.94e-17

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 76.86  E-value: 1.94e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1051356712  13 VEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLW 75
Cdd:pfam12738   1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 18-79 5.29e-09

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 52.75  E-value: 5.29e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1051356712  18 SNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFK-DGYQSTWDKAQKRGVKLVSVLWVEEC 79
Cdd:cd00027     6 SGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKsPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT smart00292
breast cancer carboxy-terminal domain;
4-79 6.31e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 47.37  E-value: 6.31e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051356712    4 PILKDVVAYVevwSSNGTENYSKTFTTQLVDMGAKVSKTFN-KQVTHVIFKDGYQST--WDKAQKRGVKLVSVLWVEEC 79
Cdd:smart00292   2 KLFKGKTFYI---TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDC 77
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 35-88 1.11e-05

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 44.45  E-value: 1.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1051356712  35 MGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKR-GVKLVSVLWVEECRTAGAHIDE 88
Cdd:cd17729    43 LGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMpGIHVVHPDWLWACAERWERVDE 97
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 4-79 1.41e-05

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 43.44  E-value: 1.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1051356712   4 PILKDVVAYVevwssNGTENYSKTFTTQLV-DMGAKVSKTFNKQVTHVIFKDGyQSTWDKAQKRGVKLVSVLWVEEC 79
Cdd:pfam00533   4 KLFSGKTFVI-----TGLDGLERDELKELIeKLGGKVTDSLSKKTTHVIVEAR-TKKYLKAKELGIPIVTEEWLLDC 74
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 33-80 1.06e-03

sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the sixth BRCT domain.


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 37.96  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1051356712  33 VDMGAKVSKTFNKQVTHVIfkdgYQST-------WDKAQKRGVKLVSVLWVEECR 80
Cdd:cd17727    24 ASLGAEYRWTYDESCTHFI----YQGKandtnreYKSAKEQGKFIVSPHWLYACK 74
BRCT_DNA_ligase_IV_rpt2 cd17717
second BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed ...
 36-78 4.82e-03

second BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the second one.


Pssm-ID: 349349  Cd Length: 88  Bit Score: 36.65  E-value: 4.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1051356712  36 GAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGV-----KLVSVLWVEE 78
Cdd:cd17717    37 GGKVVSELAEGISHVVVDSDHSRVVDFKELRRLlkkkfKIVSESWVTD 84
 
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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