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Conserved domains on  [gi|148839305|ref|NP_056110|]
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structural maintenance of chromosomes flexible hinge domain-containing protein 1 [Homo sapiens]

Protein Classification

kinesin family protein; M56 family metallopeptidase( domain architecture ID 13015024)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to carboxy-terminal kinesins that contains a C-terminal domain responsible for the motor activity (it hydrolyzes ATP and binds microtubules)| M56 family metallopeptidase is an integral membrane metallopeptidase, containing a zinc-binding HEXXH motif; it allows bacteria to respond to presence of beta-lactam antibiotics by expression of beta-lactamases and penicillin-binding proteins; includes transmembrane proteins BlaR1 and MecR1; may also contain type IVB secretion system protein DotG/IcmE at the C-terminal end

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HATPase_SMCHD1-like cd16937
Histidine kinase-like ATPase domain of structural maintenance of chromosomes flexible hinge ...
 128-246 8.21e-84

Histidine kinase-like ATPase domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein; This family includes histidine kinase-like ATPase (HATPase) domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein, which is involved in gene silencing and in DNA damage. It has critical roles in X-chromosome inactivation and is also an important regulator of autosomal gene clusters. Upon DNA damage, SMCHD1 promotes non-homologous end joining and inhibits homologous recombination repair. SMCHD1 is implicated in the pathogenesis of facioscapulohumeral muscular dystrophy.


:

Pssm-ID: 340414 [Multi-domain]  Cd Length: 119  Bit Score: 269.94  E-value: 8.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  128 GMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTR 207
Cdd:cd16937     1 GMYEYYASEGQNPLPFALAELIDNSLSATRRNTDIRRIQIKLLFDEAQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 148839305  208 QGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFV 246
Cdd:cd16937    81 QGDFESDHSGYVRPDPVPRSLNSDISYFGVGGKQAVFFV 119
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 1720-1846 1.51e-17

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


:

Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 80.35  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305   1720 GDVLGKIAHLAQIeDDRAAMVISWHLASDMDCVVTLTTDAARRIYDETQ----GRQQVLPLDSIYKKTLPDWKRSLPHFR 1795
Cdd:smart00968    1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKknrlGRATFLPLDKIKPRSPAGSKLREALLP 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 148839305   1796 NGklyfkpiGDPVFARDLLTFPDnveHCETVFGMLLGDTIILDNLDAANHY 1846
Cdd:smart00968   80 EP-------GFVGPAIDLVEYDP---ELRPALEYLLGNTLVVDDLETARRL 120
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1621-1958 7.86e-10

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: 64.31  E-value: 7.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1621 QQMAALTKEKDQLSQSIVMYKSLFEASQQLLNEMKCQVEEARLKEAQLRNELKIHNidipttQQVPHIEALLKRKLSEQE 1700
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ------ARLDSLERLQENLEGFSE 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1701 ELKkkprrscTLPNYTKGSGDVLGKIAHLAQI-EDDRAAMVISwhLASDMDCVVTLTTDAARRIYD----ETQGRQQVLP 1775
Cdd:TIGR02168  507 GVK-------ALLKNQSGLSGILGVLSELISVdEGYEAAIEAA--LGGRLQAVVVENLNAAKKAIAflkqNELGRVTFLP 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1776 LDSIYKKTLPDWKRSLPHFRNGKLyfkpigdpVFARDLLTFPDNVEhceTVFGMLLGDTIILDNLDAANHYRKevvKITH 1855
Cdd:TIGR02168  578 LDSIKGTEIQGNDREILKNIEGFL--------GVAKDLVKFDPKLR---KALSYLLGGVLVVDDLDNALELAK---KLRP 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1856 CPTLLTRDGDRIR--------SNGKFGGLQNKAPPMDKLRgmvfgapvpKQCLILGEQIDLLQQyrsAVCKLDSVNKDLN 1927
Cdd:TIGR02168  644 GYRIVTLDGDLVRpggvitggSAKTNSSILERRREIEELE---------EKIEELEEKIAELEK---ALAELRKELEELE 711

                          330       340       350
                   ....*....|....*....|....*....|.
gi 148839305  1928 SQLEYLRTpDMRKKKQELDEHEKNLKLIEEK 1958
Cdd:TIGR02168  712 EELEQLRK-ELEELSRQISALRKDLARLEAE 741
 
Name Accession Description Interval E-value
HATPase_SMCHD1-like cd16937
Histidine kinase-like ATPase domain of structural maintenance of chromosomes flexible hinge ...
 128-246 8.21e-84

Histidine kinase-like ATPase domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein; This family includes histidine kinase-like ATPase (HATPase) domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein, which is involved in gene silencing and in DNA damage. It has critical roles in X-chromosome inactivation and is also an important regulator of autosomal gene clusters. Upon DNA damage, SMCHD1 promotes non-homologous end joining and inhibits homologous recombination repair. SMCHD1 is implicated in the pathogenesis of facioscapulohumeral muscular dystrophy.


Pssm-ID: 340414 [Multi-domain]  Cd Length: 119  Bit Score: 269.94  E-value: 8.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  128 GMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTR 207
Cdd:cd16937     1 GMYEYYASEGQNPLPFALAELIDNSLSATRRNTDIRRIQIKLLFDEAQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 148839305  208 QGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFV 246
Cdd:cd16937    81 QGDFESDHSGYVRPDPVPRSLNSDISYFGVGGKQAVFFV 119
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 1720-1846 1.51e-17

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 80.35  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305   1720 GDVLGKIAHLAQIeDDRAAMVISWHLASDMDCVVTLTTDAARRIYDETQ----GRQQVLPLDSIYKKTLPDWKRSLPHFR 1795
Cdd:smart00968    1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKknrlGRATFLPLDKIKPRSPAGSKLREALLP 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 148839305   1796 NGklyfkpiGDPVFARDLLTFPDnveHCETVFGMLLGDTIILDNLDAANHY 1846
Cdd:smart00968   80 EP-------GFVGPAIDLVEYDP---ELRPALEYLLGNTLVVDDLETARRL 120
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 1721-1847 3.61e-14

SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 70.75  E-value: 3.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1721 DVLGKIAHLAQIEDD-RAAmvISWHLASDMDCVVTLTTDAARRIYDE----TQGRQQVLPLDSIykktLPDWKRSLPHFR 1795
Cdd:pfam06470    3 GVLGRLADLIEVDEGyEKA--VEAALGGRLQAVVVDDEDDAKRAIEFlkknKLGRATFLPLDRL----KPRPRRPGADLK 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 148839305  1796 NGklyfkpigdPVFARDLLTFPDNVEHcetVFGMLLGDTIILDNLDAANHYR 1847
Cdd:pfam06470   77 GG---------AGPLLDLVEYDDEYRK---ALRYLLGNTLVVDDLDEALELA 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1621-1958 7.86e-10

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: 64.31  E-value: 7.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1621 QQMAALTKEKDQLSQSIVMYKSLFEASQQLLNEMKCQVEEARLKEAQLRNELKIHNidipttQQVPHIEALLKRKLSEQE 1700
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ------ARLDSLERLQENLEGFSE 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1701 ELKkkprrscTLPNYTKGSGDVLGKIAHLAQI-EDDRAAMVISwhLASDMDCVVTLTTDAARRIYD----ETQGRQQVLP 1775
Cdd:TIGR02168  507 GVK-------ALLKNQSGLSGILGVLSELISVdEGYEAAIEAA--LGGRLQAVVVENLNAAKKAIAflkqNELGRVTFLP 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1776 LDSIYKKTLPDWKRSLPHFRNGKLyfkpigdpVFARDLLTFPDNVEhceTVFGMLLGDTIILDNLDAANHYRKevvKITH 1855
Cdd:TIGR02168  578 LDSIKGTEIQGNDREILKNIEGFL--------GVAKDLVKFDPKLR---KALSYLLGGVLVVDDLDNALELAK---KLRP 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1856 CPTLLTRDGDRIR--------SNGKFGGLQNKAPPMDKLRgmvfgapvpKQCLILGEQIDLLQQyrsAVCKLDSVNKDLN 1927
Cdd:TIGR02168  644 GYRIVTLDGDLVRpggvitggSAKTNSSILERRREIEELE---------EKIEELEEKIAELEK---ALAELRKELEELE 711

                          330       340       350
                   ....*....|....*....|....*....|.
gi 148839305  1928 SQLEYLRTpDMRKKKQELDEHEKNLKLIEEK 1958
Cdd:TIGR02168  712 EELEQLRK-ELEELSRQISALRKDLARLEAE 741
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 143-255 1.30e-07

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 52.33  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305   143 FALAELIDNSLSATSRNigvrrIQIKLLFDETQGKPaVAVIDNGRGMTSKQLNNWavYRLSKFTRQGDFESDhsgyvrpv 222
Cdd:pfam13589    3 GALAELIDNSIDADATN-----IKIEVNKNRGGGTE-IVIEDDGHGMSPEELINA--LRLATSAKEAKRGST-------- 66

                           90       100       110
                   ....*....|....*....|....*....|...
gi 148839305   223 pvprslnsDISYFGVGGKQAVFFVGQSARMISK 255
Cdd:pfam13589   67 --------DLGRYGIGLKLASLSLGAKLTVTSK 91
 
Name Accession Description Interval E-value
HATPase_SMCHD1-like cd16937
Histidine kinase-like ATPase domain of structural maintenance of chromosomes flexible hinge ...
 128-246 8.21e-84

Histidine kinase-like ATPase domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein; This family includes histidine kinase-like ATPase (HATPase) domain of structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) protein, which is involved in gene silencing and in DNA damage. It has critical roles in X-chromosome inactivation and is also an important regulator of autosomal gene clusters. Upon DNA damage, SMCHD1 promotes non-homologous end joining and inhibits homologous recombination repair. SMCHD1 is implicated in the pathogenesis of facioscapulohumeral muscular dystrophy.


Pssm-ID: 340414 [Multi-domain]  Cd Length: 119  Bit Score: 269.94  E-value: 8.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  128 GMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTR 207
Cdd:cd16937     1 GMYEYYASEGQNPLPFALAELIDNSLSATRRNTDIRRIQIKLLFDEAQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 148839305  208 QGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFV 246
Cdd:cd16937    81 QGDFESDHSGYVRPDPVPRSLNSDISYFGVGGKQAVFFV 119
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 1720-1846 1.51e-17

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 80.35  E-value: 1.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305   1720 GDVLGKIAHLAQIeDDRAAMVISWHLASDMDCVVTLTTDAARRIYDETQ----GRQQVLPLDSIYKKTLPDWKRSLPHFR 1795
Cdd:smart00968    1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKknrlGRATFLPLDKIKPRSPAGSKLREALLP 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 148839305   1796 NGklyfkpiGDPVFARDLLTFPDnveHCETVFGMLLGDTIILDNLDAANHY 1846
Cdd:smart00968   80 EP-------GFVGPAIDLVEYDP---ELRPALEYLLGNTLVVDDLETARRL 120
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 1721-1847 3.61e-14

SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 70.75  E-value: 3.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1721 DVLGKIAHLAQIEDD-RAAmvISWHLASDMDCVVTLTTDAARRIYDE----TQGRQQVLPLDSIykktLPDWKRSLPHFR 1795
Cdd:pfam06470    3 GVLGRLADLIEVDEGyEKA--VEAALGGRLQAVVVDDEDDAKRAIEFlkknKLGRATFLPLDRL----KPRPRRPGADLK 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 148839305  1796 NGklyfkpigdPVFARDLLTFPDNVEHcetVFGMLLGDTIILDNLDAANHYR 1847
Cdd:pfam06470   77 GG---------AGPLLDLVEYDDEYRK---ALRYLLGNTLVVDDLDEALELA 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1621-1958 7.86e-10

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: 64.31  E-value: 7.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1621 QQMAALTKEKDQLSQSIVMYKSLFEASQQLLNEMKCQVEEARLKEAQLRNELKIHNidipttQQVPHIEALLKRKLSEQE 1700
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ------ARLDSLERLQENLEGFSE 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1701 ELKkkprrscTLPNYTKGSGDVLGKIAHLAQI-EDDRAAMVISwhLASDMDCVVTLTTDAARRIYD----ETQGRQQVLP 1775
Cdd:TIGR02168  507 GVK-------ALLKNQSGLSGILGVLSELISVdEGYEAAIEAA--LGGRLQAVVVENLNAAKKAIAflkqNELGRVTFLP 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1776 LDSIYKKTLPDWKRSLPHFRNGKLyfkpigdpVFARDLLTFPDNVEhceTVFGMLLGDTIILDNLDAANHYRKevvKITH 1855
Cdd:TIGR02168  578 LDSIKGTEIQGNDREILKNIEGFL--------GVAKDLVKFDPKLR---KALSYLLGGVLVVDDLDNALELAK---KLRP 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305  1856 CPTLLTRDGDRIR--------SNGKFGGLQNKAPPMDKLRgmvfgapvpKQCLILGEQIDLLQQyrsAVCKLDSVNKDLN 1927
Cdd:TIGR02168  644 GYRIVTLDGDLVRpggvitggSAKTNSSILERRREIEELE---------EKIEELEEKIAELEK---ALAELRKELEELE 711

                          330       340       350
                   ....*....|....*....|....*....|.
gi 148839305  1928 SQLEYLRTpDMRKKKQELDEHEKNLKLIEEK 1958
Cdd:TIGR02168  712 EELEQLRK-ELEELSRQISALRKDLARLEAE 741
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 143-255 1.30e-07

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 52.33  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839305   143 FALAELIDNSLSATSRNigvrrIQIKLLFDETQGKPaVAVIDNGRGMTSKQLNNWavYRLSKFTRQGDFESDhsgyvrpv 222
Cdd:pfam13589    3 GALAELIDNSIDADATN-----IKIEVNKNRGGGTE-IVIEDDGHGMSPEELINA--LRLATSAKEAKRGST-------- 66

                           90       100       110
                   ....*....|....*....|....*....|...
gi 148839305   223 pvprslnsDISYFGVGGKQAVFFVGQSARMISK 255
Cdd:pfam13589   67 --------DLGRYGIGLKLASLSLGAKLTVTSK 91
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 142-194 3.73e-03

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 39.31  E-value: 3.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148839305  142 PF-ALAELIDNslsatSRNIGVRRIQIKLLFDET-QGKPAVAVIDNGRGMTSKQL 194
Cdd:cd16931    12 PFgAVAELVDN-----ARDADATRLDIFIDDINLlRGGFMLSFLDDGNGMTPEEA 61
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 147-216 7.02e-03

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 39.73  E-value: 7.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148839305  147 ELIDNSLSAtsrniGVRRIQIKLlfdETQGKPAVAVIDNGRGMTSKQLNNwAVYR--LSKFTRQGDFESDHS 216
Cdd:cd16926    20 ELVENSIDA-----GATRIDVEI---EEGGLKLIRVTDNGSGISREDLEL-AFERhaTSKISSFEDLFSITT 82
 
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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