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Conserved domains on  [gi|1991455377]
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Chain J, HDA1 complex subunit 3,HDA1 complex subunit 3

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1-272 5.87e-123

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


:

Pssm-ID: 402894  Cd Length: 281  Bit Score: 362.42  E-value: 5.87e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377   1 SGDYWLPTTMSLYQKELTDQIVSLHYSDILRYFETSHYKEDVILESMKTMCL-NGSLVATHPYLLIDHYMPKSLITRDVP 79
Cdd:pfam11496   3 SGDYYLPTPMTSYQKELTEQIVSLHYSDILKYCETSDSKEDISLIKSMTLCLeNLSLVATHPYLLVDHYMPKSLLLKDEP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  80 AHLAENSGKFSVLRDLINLVQEYE----TETAIVCRPGRTMDLLEALLLGNKVHIKRYDGHSIKSKQKAND-------FS 148
Cdd:pfam11496  83 EKLAYTSGKFLVLNDLVNLLIERDrkepINVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLYGENKKVSdsgnkkiHS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 149 CTVHLFSSEGINFTKYPIKSKARFDMLICLDTTVDTSQKDIQYLLQYKRERKGLeryAPIVRLVAINSIDHCRLFFGKKF 228
Cdd:pfam11496 163 TTCHLLSSTGQLTNDDSLLENYKFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNL---APIIRLVVINSIEHVELCFPKPP 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1991455377 229 DknSREYLENVTAAMVILRDRLGTLPPDLRPIYSQKLHYLVEWL 272
Cdd:pfam11496 240 D--SPDYLYKVIAAIVVLRDVVGDLPDDLLPIYEQKLKYLNHWL 281
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
370-504 1.05e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  370 EYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFVKTDNVQDEIEkEERVSVSRDT 449
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE-EALALLRSEL 896
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1991455377  450 EKkyMEQEIKRAVDAIRENEEETHKLNEKQNglesELKLKFEKSEISTKELNEKI 504
Cdd:TIGR02168  897 EE--LSEELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERL 945
 
Name Accession Description Interval E-value
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1-272 5.87e-123

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 362.42  E-value: 5.87e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377   1 SGDYWLPTTMSLYQKELTDQIVSLHYSDILRYFETSHYKEDVILESMKTMCL-NGSLVATHPYLLIDHYMPKSLITRDVP 79
Cdd:pfam11496   3 SGDYYLPTPMTSYQKELTEQIVSLHYSDILKYCETSDSKEDISLIKSMTLCLeNLSLVATHPYLLVDHYMPKSLLLKDEP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  80 AHLAENSGKFSVLRDLINLVQEYE----TETAIVCRPGRTMDLLEALLLGNKVHIKRYDGHSIKSKQKAND-------FS 148
Cdd:pfam11496  83 EKLAYTSGKFLVLNDLVNLLIERDrkepINVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLYGENKKVSdsgnkkiHS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 149 CTVHLFSSEGINFTKYPIKSKARFDMLICLDTTVDTSQKDIQYLLQYKRERKGLeryAPIVRLVAINSIDHCRLFFGKKF 228
Cdd:pfam11496 163 TTCHLLSSTGQLTNDDSLLENYKFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNL---APIIRLVVINSIEHVELCFPKPP 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1991455377 229 DknSREYLENVTAAMVILRDRLGTLPPDLRPIYSQKLHYLVEWL 272
Cdd:pfam11496 240 D--SPDYLYKVIAAIVVLRDVVGDLPDDLLPIYEQKLKYLNHWL 281
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
370-504 1.05e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  370 EYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFVKTDNVQDEIEkEERVSVSRDT 449
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE-EALALLRSEL 896
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1991455377  450 EKkyMEQEIKRAVDAIRENEEETHKLNEKQNglesELKLKFEKSEISTKELNEKI 504
Cdd:TIGR02168  897 EE--LSEELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERL 945
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
395-533 8.26e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 395 KFSQIE-TLEK--DIETLKgSLMAQGET----LSKLKDafvktDNVQDEIEKEERVSVSRDTEKKYMEQEIKR---AVDA 464
Cdd:COG2433   351 KFERVEkKVPPdvDRDEVK-ARVIRGLSieeaLEELIE-----KELPEEEPEAEREKEHEERELTEEEEEIRRleeQVER 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 465 IR-ENEEETHKLNEKQNGLE-SELKLKFEKSEISTK--------ELNEKIGFLKKELKLENDLNEELVGQLS--KTMDNL 532
Cdd:COG2433   425 LEaEVEELEAELEEKDERIErLERELSEARSEERREirkdreisRLDREIERLERELEEERERIEELKRKLErlKELWKL 504

                  .
gi 1991455377 533 E 533
Cdd:COG2433   505 E 505
PTZ00121 PTZ00121
MAEBL; Provisional
363-535 1.50e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  363 EDEKIIKEYETvlRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKgslmaQGETLSKLKDAFVKTdnvQDEIEKEER 442
Cdd:PTZ00121  1657 EENKIKAAEEA--KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----KAEELKKKEAEEKKK---AEELKKAEE 1726
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  443 VSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEkqngleselkLKFEKSEISTKELNEKIGFLKKELKLENDLNEELV 522
Cdd:PTZ00121  1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH----------LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
                          170
                   ....*....|....
gi 1991455377  523 GQLSK-TMDNLENL 535
Cdd:PTZ00121  1797 DKKIKdIFDNFANI 1810
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
86-162 1.63e-03

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 39.00  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  86 SGKFSVLRDLINLVQEyETETAIV-CRPGRTMDLLEALLLGNKVHIKRYDG-HSIKSKQKA-----NDFSCTVHLFS--- 155
Cdd:cd18793    10 SGKLEALLELLEELRE-PGEKVLIfSQFTDTLDILEEALRERGIKYLRLDGsTSSKERQKLvdrfnEDPDIRVFLLStka 88

                  ....*...
gi 1991455377 156 -SEGINFT 162
Cdd:cd18793    89 gGVGLNLT 96
 
Name Accession Description Interval E-value
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1-272 5.87e-123

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 362.42  E-value: 5.87e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377   1 SGDYWLPTTMSLYQKELTDQIVSLHYSDILRYFETSHYKEDVILESMKTMCL-NGSLVATHPYLLIDHYMPKSLITRDVP 79
Cdd:pfam11496   3 SGDYYLPTPMTSYQKELTEQIVSLHYSDILKYCETSDSKEDISLIKSMTLCLeNLSLVATHPYLLVDHYMPKSLLLKDEP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  80 AHLAENSGKFSVLRDLINLVQEYE----TETAIVCRPGRTMDLLEALLLGNKVHIKRYDGHSIKSKQKAND-------FS 148
Cdd:pfam11496  83 EKLAYTSGKFLVLNDLVNLLIERDrkepINVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLYGENKKVSdsgnkkiHS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 149 CTVHLFSSEGINFTKYPIKSKARFDMLICLDTTVDTSQKDIQYLLQYKRERKGLeryAPIVRLVAINSIDHCRLFFGKKF 228
Cdd:pfam11496 163 TTCHLLSSTGQLTNDDSLLENYKFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNL---APIIRLVVINSIEHVELCFPKPP 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1991455377 229 DknSREYLENVTAAMVILRDRLGTLPPDLRPIYSQKLHYLVEWL 272
Cdd:pfam11496 240 D--SPDYLYKVIAAIVVLRDVVGDLPDDLLPIYEQKLKYLNHWL 281
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
370-504 1.05e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  370 EYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFVKTDNVQDEIEkEERVSVSRDT 449
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE-EALALLRSEL 896
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1991455377  450 EKkyMEQEIKRAVDAIRENEEETHKLNEKQNglesELKLKFEKSEISTKELNEKI 504
Cdd:TIGR02168  897 EE--LSEELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERL 945
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
340-532 2.21e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 340 KQELDDYSCLDDLQNDHLKFFSNEDEKIIKEYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGET 419
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 420 LSKLKDafvKTDNVQDEIEKEERVSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNGLESELK------------ 487
Cdd:TIGR04523 477 INKIKQ---NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISdledelnkddfe 553
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1991455377 488 LKFEKSEISTKELNEKIGFLK---KELKLENDLNEELVGQLSKTMDNL 532
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELKqtqKSLKKKQEEKQELIDQKEKEKKDL 601
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
354-535 3.28e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 354 NDHLKFFSNEDEKIIKEYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFVKTDNV 433
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSL 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 434 QDEIEKEERVSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNGLESELK---LKFEKSEISTKELNEKIGFLKKE 510
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqKELEQNNKKIKELEKQLNQLKSE 296
                         170       180       190
                  ....*....|....*....|....*....|
gi 1991455377 511 L-----KLENDLNEELVGQLSKTMDNLENL 535
Cdd:TIGR04523 297 IsdlnnQKEQDWNKELKSELKNQEKKLEEI 326
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
395-533 8.26e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 395 KFSQIE-TLEK--DIETLKgSLMAQGET----LSKLKDafvktDNVQDEIEKEERVSVSRDTEKKYMEQEIKR---AVDA 464
Cdd:COG2433   351 KFERVEkKVPPdvDRDEVK-ARVIRGLSieeaLEELIE-----KELPEEEPEAEREKEHEERELTEEEEEIRRleeQVER 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 465 IR-ENEEETHKLNEKQNGLE-SELKLKFEKSEISTK--------ELNEKIGFLKKELKLENDLNEELVGQLS--KTMDNL 532
Cdd:COG2433   425 LEaEVEELEAELEEKDERIErLERELSEARSEERREirkdreisRLDREIERLERELEEERERIEELKRKLErlKELWKL 504

                  .
gi 1991455377 533 E 533
Cdd:COG2433   505 E 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
383-521 1.08e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 383 NRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFVktdNVQDEIEKEERvsvsrdtEKKYMEQEIKRAV 462
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY---ELLAELARLEQ-------DIARLEERRRELE 315
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1991455377 463 DAIRENEEETHKLNEKQNGLESELKLKFEKSEISTKELNEKIGFLKKELKLENDLNEEL 521
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
PTZ00121 PTZ00121
MAEBL; Provisional
363-535 1.50e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  363 EDEKIIKEYETvlRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKgslmaQGETLSKLKDAFVKTdnvQDEIEKEER 442
Cdd:PTZ00121  1657 EENKIKAAEEA--KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----KAEELKKKEAEEKKK---AEELKKAEE 1726
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  443 VSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEkqngleselkLKFEKSEISTKELNEKIGFLKKELKLENDLNEELV 522
Cdd:PTZ00121  1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH----------LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
                          170
                   ....*....|....
gi 1991455377  523 GQLSK-TMDNLENL 535
Cdd:PTZ00121  1797 DKKIKdIFDNFANI 1810
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
86-162 1.63e-03

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 39.00  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  86 SGKFSVLRDLINLVQEyETETAIV-CRPGRTMDLLEALLLGNKVHIKRYDG-HSIKSKQKA-----NDFSCTVHLFS--- 155
Cdd:cd18793    10 SGKLEALLELLEELRE-PGEKVLIfSQFTDTLDILEEALRERGIKYLRLDGsTSSKERQKLvdrfnEDPDIRVFLLStka 88

                  ....*...
gi 1991455377 156 -SEGINFT 162
Cdd:cd18793    89 gGVGLNLT 96
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
362-534 2.07e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 362 NEDEKIIKEYETVLrtnnENLNRSHELEVENNLKfSQIETLEKDIETLKGSLMAQGETLSKLKDafvktdnvqdEIEKEE 441
Cdd:TIGR04523 284 KELEKQLNQLKSEI----SDLNNQKEQDWNKELK-SELKNQEKKLEEIQNQISQNNKIISQLNE----------QISQLK 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 442 RVSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNGLES---ELKLKFEKSEISTKELNEKIGFLKKELKL---EN 515
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESqinDLESKIQNQEKLNQQKDEQIKKLQQEKELlekEI 428
                         170
                  ....*....|....*....
gi 1991455377 516 DLNEELVGQLSKTMDNLEN 534
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTN 447
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
363-500 4.20e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 363 EDEKIIKEYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFvktdnvqDEIEKEER 442
Cdd:COG2433   386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLEREL-------SEARSEER 458
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1991455377 443 VSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNGLESELKLKFEKSEISTKEL 500
Cdd:COG2433   459 REIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVV 516
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
398-527 4.67e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 398 QIETLEKDIETLKGSLMAQGETLSKLKDAFVKTDN----VQDEIEK-EERVSVSRDT--------EKKYMEQEIKRAVDA 464
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieeVEARIKKyEEQLGNVRNNkeyealqkEIESLKRRISDLEDE 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1991455377 465 IRENEEETHKLNEKQNGLESELKLKFEKSEISTKELNEKIGFLKKELKLENDLNEELVGQLSK 527
Cdd:COG1579   112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
397-533 5.07e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 397 SQIETLEKDIETLKGSLMAQGETLSKLKDAFVKtdnVQDEIEKEERvsvsrdtEKKYMEQEIKRAVDAIRENEE--ETHK 474
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEA---AKTELEDLEK-------EIKRLELEIEEVEARIKKYEEqlGNVR 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1991455377 475 LNEKQNGLESE---LKLKFEKSEISTKELNEKIGFLKKELKLENDLNEELVGQLSKTMDNLE 533
Cdd:COG1579    87 NNKEYEALQKEiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
340-535 5.30e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.03  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  340 KQELDDYSCLDDLQNDHLKFfSNEDEKIIKEYETVLRTNNENLNrshelevennlkfsQIETLEKDIETLKGSLMAQGET 419
Cdd:TIGR01612 1090 KEKLKHYNFDDFGKEENIKY-ADEINKIKDDIKNLDQKIDHHIK--------------ALEEIKKKSENYIDEIKAQIND 1154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  420 LSKLKDAFVKTDNVQdEIEKEERVSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNgleseLKLKFEKSeiSTKE 499
Cdd:TIGR01612 1155 LEDVADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKG-----INLSYGKN--LGKL 1226
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1991455377  500 LNEKIGFLKKElklendlNEELVGQLSKTMDNLENL 535
Cdd:TIGR01612 1227 FLEKIDEEKKK-------SEHMIKAMEAYIEDLDEI 1255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
331-535 7.53e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 7.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  331 EVYMDICVQKQELDDYSCLDDLQ--NDHLKFFsnedEKIIKEYETVLRTNNENLNRSHELEVENNLKFSQietLEKDIET 408
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEelREELEEL----QEELKEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEE 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  409 LKGSLMAQGETLSKLkdafvktdNVQDEIEKEERVSVsrDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNGLESE--- 485
Cdd:TIGR02168  286 LQKELYALANEISRL--------EQQKQILRERLANL--ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEles 355
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1991455377  486 LKLKFEKSEISTKELNEKIGFLKKELKLENDLNEELVGQLSKTMDNLENL 535
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
332-541 8.61e-03

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 38.95  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  332 VYMDICVQKQELDDYSCLDDLQNDHLKFFSNEDEKIIKeyetVLRTNNENLNRSHELEVENnlKFSQIETLEKDIETLKG 411
Cdd:COG5192    505 FYDESLSPEECIEEYKGESAKSSESDLVVQDEPEDFFD----VSKVANESISSNHEKLMES--EFEELKKKWSSLAQLKS 578
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377  412 SLMAQG--------ETLSKLKDAFVKTDNVQDEIEKEERVSVSRDTEKKYMEQEIKRAVDAIRENEEETHKlnekqnglE 483
Cdd:COG5192    579 RFQKDAtldsiegeEELIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARK--------K 650
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1991455377  484 SELKLKFEKSEISTKELNEKIGFLKKELKLENDLneELVGQLSKTMDNLENLTIPRVR 541
Cdd:COG5192    651 EELRGNFELEERGDPEKKDVDWYTEEKRKIEEQL--KINRSEFETMVPESRVVIEGYR 706
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
397-535 9.81e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 9.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1991455377 397 SQIETLEKDIETLKGSL---MAQGETLSKLKDAFVKTDN-VQDEIEkEERVSVSRDTEkkymeqEIKRAVDAIRENEEET 472
Cdd:PRK02224  286 ERLEELEEERDDLLAEAgldDADAEAVEARREELEDRDEeLRDRLE-ECRVAAQAHNE------EAESLREDADDLEERA 358
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1991455377 473 HKLNEKQNGLESELklkfEKSEISTKELNEKIGFLKKELklenDLNEELVGQLSKTMDNLENL 535
Cdd:PRK02224  359 EELREEAAELESEL----EEAREAVEDRREEIEELEEEI----EELRERFGDAPVDLGNAEDF 413
 
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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