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Conserved domains on  [gi|1692857622|gb|TPP52587|]
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Core histone H2A/H2B/H3/H4 family protein [Leishmania donovani]

Protein Classification

histone H3 family protein( domain architecture ID 11269512)

histone H3 family protein similar to histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes

Gene Ontology:  GO:0003677|GO:0046982|GO:0034080|GO:0005654
PubMed:  8121801
SCOP:  4000793

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
H3 smart00428
Histone H3;
373-475 1.43e-57

Histone H3;


:

Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 185.73  E-value: 1.43e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622  373 GVKKSHRRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEG--LRFQSSAIMALQEATEAYVVSLMADTNLA 450
Cdd:smart00428   1 GGKTKHRRYRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGvdLRFQSSAIMALQEAAEAYLVGLFEDTNLL 80

                           90       100
                   ....*....|....*....|....*
gi 1692857622  451 CIHAKRVTIQPKDIQLALRLRGERH 475
Cdd:smart00428  81 AIHAKRVTIMPKDIQLARRIRGERL 105
 
Name Accession Description Interval E-value
H3 smart00428
Histone H3;
373-475 1.43e-57

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 185.73  E-value: 1.43e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622  373 GVKKSHRRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEG--LRFQSSAIMALQEATEAYVVSLMADTNLA 450
Cdd:smart00428   1 GGKTKHRRYRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGvdLRFQSSAIMALQEAAEAYLVGLFEDTNLL 80

                           90       100
                   ....*....|....*....|....*
gi 1692857622  451 CIHAKRVTIQPKDIQLALRLRGERH 475
Cdd:smart00428  81 AIHAKRVTIMPKDIQLARRIRGERL 105
PTZ00018 PTZ00018
histone H3; Provisional
 355-474 2.82e-53

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 175.48  E-value: 2.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 355 PTRTITSKKSKKAPSAASGVKKSHRrWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEGLRFQSSAIMALQE 434
Cdd:PTZ00018   17 PRKQLASKAARKSAPVTGGIKKPHR-YRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVLALQE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1692857622 435 ATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRLRGER 474
Cdd:PTZ00018   96 AAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGER 135
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 379-472 2.97e-51

histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called the histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467036  Cd Length: 95  Bit Score: 168.87  E-value: 2.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 379 RRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQK-EGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRV 457
Cdd:cd22911     1 RRYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKtKDLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80

                          90
                  ....*....|....*
gi 1692857622 458 TIQPKDIQLALRLRG 472
Cdd:cd22911    81 TLMPKDMQLARRIRG 95
Histone pfam00125
Core histone H2A/H2B/H3/H4;
354-471 1.17e-50

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 168.38  E-value: 1.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 354 RPTRTITSKKSKKAPSAASGVKKSHRRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEGLRFQSSAIMALQ 433
Cdd:pfam00125   9 NPRRGGTAPEKKISQKSSSSSKKKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQ 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1692857622 434 EATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRLR 471
Cdd:pfam00125  89 EAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
405-470 4.89e-04

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 38.27  E-value: 4.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1692857622 405 APFQRLVREVSsaqkeGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRL 470
Cdd:COG2036     5 APVDRIIKKAG-----AERVSEDAVEALAEILEEYAEEIAKEAVELAKHAGRKTVKAEDIELAAKL 65
 
Name Accession Description Interval E-value
H3 smart00428
Histone H3;
373-475 1.43e-57

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 185.73  E-value: 1.43e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622  373 GVKKSHRRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEG--LRFQSSAIMALQEATEAYVVSLMADTNLA 450
Cdd:smart00428   1 GGKTKHRRYRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGvdLRFQSSAIMALQEAAEAYLVGLFEDTNLL 80

                           90       100
                   ....*....|....*....|....*
gi 1692857622  451 CIHAKRVTIQPKDIQLALRLRGERH 475
Cdd:smart00428  81 AIHAKRVTIMPKDIQLARRIRGERL 105
PTZ00018 PTZ00018
histone H3; Provisional
 355-474 2.82e-53

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 175.48  E-value: 2.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 355 PTRTITSKKSKKAPSAASGVKKSHRrWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEGLRFQSSAIMALQE 434
Cdd:PTZ00018   17 PRKQLASKAARKSAPVTGGIKKPHR-YRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVLALQE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1692857622 435 ATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRLRGER 474
Cdd:PTZ00018   96 AAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGER 135
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 379-472 2.97e-51

histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called the histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467036  Cd Length: 95  Bit Score: 168.87  E-value: 2.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 379 RRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQK-EGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRV 457
Cdd:cd22911     1 RRYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKtKDLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80

                          90
                  ....*....|....*
gi 1692857622 458 TIQPKDIQLALRLRG 472
Cdd:cd22911    81 TLMPKDMQLARRIRG 95
Histone pfam00125
Core histone H2A/H2B/H3/H4;
354-471 1.17e-50

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 168.38  E-value: 1.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 354 RPTRTITSKKSKKAPSAASGVKKSHRRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEGLRFQSSAIMALQ 433
Cdd:pfam00125   9 NPRRGGTAPEKKISQKSSSSSKKKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTDLRISADAVVALQ 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1692857622 434 EATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRLR 471
Cdd:pfam00125  89 EAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
PLN00121 PLN00121
histone H3; Provisional
 355-474 3.12e-49

histone H3; Provisional


Pssm-ID: 177733 [Multi-domain]  Cd Length: 136  Bit Score: 164.84  E-value: 3.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 355 PTRTITSKKSKKAPSAASGVKKSHRrWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSAQKEGLRFQSSAIMALQE 434
Cdd:PLN00121   17 PRKQLATKAARKSAPATGGVKKPHR-YRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVLALQE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1692857622 435 ATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRLRGER 474
Cdd:PLN00121   96 AAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGER 135
PLN00161 PLN00161
histone H3; Provisional
 350-472 3.05e-37

histone H3; Provisional


Pssm-ID: 215082 [Multi-domain]  Cd Length: 135  Bit Score: 133.20  E-value: 3.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 350 ARELRPTRTITSKKSKKAPSAASGVK--KSHRRWRPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVSSA-QKEGLRFQS 426
Cdd:PLN00161    2 ARRLQGKRFRKGKKPQKEASGVTRQEldKKPHRYRPGTVALREIRKYQKSTELLIRKLPFARLVREISNEmLREPFRWTA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1692857622 427 SAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRLRG 472
Cdd:PLN00161   82 EALLALQEATEDFLVHLFEDCNLCAIHAKRVTIMPKDMQLARRIRG 127
PLN00160 PLN00160
histone H3; Provisional
 382-473 1.12e-31

histone H3; Provisional


Pssm-ID: 165727  Cd Length: 97  Bit Score: 117.07  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1692857622 382 RPGTCAIREIRKFQKSTSLLIQCAPFQRLVREVS-SAQKEGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQ 460
Cdd:PLN00160    2 RPGEKALKEIKMYQKSTDLLIRRLPFARLVREIQmEMSREAYRWQGSAILALQEAAEAHLVGLFEDSNLCAIHGKRVTIM 81

                          90
                  ....*....|...
gi 1692857622 461 PKDIQLALRLRGE 473
Cdd:PLN00160   82 PKDMQLARRIRGQ 94
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 423-469 5.49e-05

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 41.05  E-value: 5.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1692857622 423 RFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALR 469
Cdd:cd00076    17 SVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 405-469 3.76e-04

histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription regulators and similar proteins; The family includes many archaeal histone-fold proteins and histone-like transcription regulators, which may bind and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. They can increase the resistance of DNA to thermal denaturation.


Pssm-ID: 467034  Cd Length: 64  Bit Score: 38.68  E-value: 3.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1692857622 405 APFQRLVREVSsaqkeGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALR 469
Cdd:cd22909     5 APVKRIIKKAG-----AERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAVK 64
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
405-470 4.89e-04

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 38.27  E-value: 4.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1692857622 405 APFQRLVREVSsaqkeGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALRL 470
Cdd:COG2036     5 APVDRIIKKAG-----AERVSEDAVEALAEILEEYAEEIAKEAVELAKHAGRKTVKAEDIELAAKL 65
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 405-468 1.78e-03

Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes archaebacterial histones and histone like transcription factors from eukaryotes.


Pssm-ID: 395650  Cd Length: 65  Bit Score: 36.82  E-value: 1.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1692857622 405 APFQRLVREVSSAQkeglRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLAL 468
Cdd:pfam00808   6 ARVKRIMKSDPDAG----RISQDAKELIAECVEEFIEFVASEAAEICNKAGRKTINPEHIKQAV 65
HFD_POLE3_DPB4 cd22928
histone-fold domain found in DNA polymerase epsilon subunit 3 (POLE3) and similar proteins; ...
 408-469 1.87e-03

histone-fold domain found in DNA polymerase epsilon subunit 3 (POLE3) and similar proteins; POLE3, also called arsenic-transactivated protein (AsTP), chromatin accessibility complex 17 kDa protein (CHRAC-17), DNA polymerase II subunit 3, or DNA polymerase epsilon subunit p17, may participate in DNA repair and in chromosomal DNA replication. It is an accessory component of the DNA polymerase epsilon complex, which consists of four subunits: the catalytic subunit POLE and the accessory subunits POLE2, POLE3 and POLE4. It forms a complex with CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1. In fungi, POLE3 has been named as DNA polymerase epsilon subunit D (DPB4, also known as DNA polymerase II subunit D). DPB4 acts as an accessory component of the DNA polymerase epsilon (DNA polymerase II) that consists of POL2, DPB2, DPB3 and DPB4, and participates in chromosomal DNA replication. It also functions as a component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA.


Pssm-ID: 467053  Cd Length: 87  Bit Score: 37.49  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1692857622 408 QRLVREvssAQKEGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALR 469
Cdd:cd22928    11 TRIIKE---ALPEGVQVSKDARLALSRAATVFILYLTAAANEIAKSNKRKTISADDVLKALE 69
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 409-469 4.83e-03

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 36.38  E-value: 4.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1692857622 409 RLVREVSSaQKEGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALR 469
Cdd:cd22920     6 SLVKKLFK-HFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMK 65
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
 409-469 4.95e-03

histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also called MHF1, apoptosis-inducing TAF9-like domain-containing protein 1 (APITD1), FANCM-associated histone fold protein 1, FANCM-interacting histone fold protein 1, or Fanconi anemia-associated polypeptide of 16 kDa (FAAP16), is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-S, together with CENP-X, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-S acts as a crucial cofactor for FANCM, in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-S also forms a discrete complex with FANCM and CENP-X, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-X (CENP-T-W-S-X heterotetramer), CENP-S is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, CENP-S binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-X. It does not bind DNA on its own.


Pssm-ID: 467044  Cd Length: 77  Bit Score: 36.00  E-value: 4.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1692857622 409 RLVREVssAQKEGLRFQSSAIMALQEATEAYVVSLMADTNLACIHAKRVTIQPKDIQLALR 469
Cdd:cd22919    11 KICEEE--AEEKGVTVSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKLLAR 69
 
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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