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Conserved domains on  [gi|1370455298|ref|XP_024306818|]
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chromodomain-helicase-DNA-binding protein 1-like isoform X1 [Homo sapiens]

Protein Classification

DEXHc_CHD1L and Macro_Poa1p_like_SNF2 domain-containing protein (domain architecture ID 13327344)

protein containing domains DEXHc_CHD1L, SF2_C_SNF, and Macro_Poa1p_like_SNF2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Macro_Poa1p_like_SNF2 cd03331
Macro domain, Poa1p_like family, SNF2 subfamily. The macro domain is a high-affinity ...
289-439 2.45e-99

Macro domain, Poa1p_like family, SNF2 subfamily. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ADP-ribose as a ligand. Previously identified as displaying an Appr-1"-p (ADP-ribose-1"-monophosphate) processing activity, the macro domain may play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation of proteins, an important post-translational modification which occurs in DNA repair, transcription, chromatin biology, and long-term memory formation, among other processes. Members of this subfamily contain a C-terminal macro domain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


:

Pssm-ID: 239447  Cd Length: 152  Bit Score: 294.39  E-value: 2.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 289 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 367
Cdd:cd03331     1 SVRYVYGDVTHPSAvCAEDAIIVHCVDDSGHWGRGGLFTALEKRSDQPRKAYELAGKMKDLHLGDLHLFPIDDKNSRLKG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370455298 368 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd03331    81 PDWVALIVAQHRDKSNPLSGIKLSALEKGLKKIYFAAKQKSASVHLPRIGHSTKSFNWYGTERLIRKYLATR 152
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
1-272 2.94e-21

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 97.18  E-value: 2.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPA 80
Cdd:PLN03142   554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKT 630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298   81 ADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGK 142
Cdd:PLN03142   631 VNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENK 709
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298  143 NHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDR 216
Cdd:PLN03142   710 LDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYL 783
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370455298  217 QKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 272
Cdd:PLN03142   784 MQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
 
Name Accession Description Interval E-value
Macro_Poa1p_like_SNF2 cd03331
Macro domain, Poa1p_like family, SNF2 subfamily. The macro domain is a high-affinity ...
289-439 2.45e-99

Macro domain, Poa1p_like family, SNF2 subfamily. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ADP-ribose as a ligand. Previously identified as displaying an Appr-1"-p (ADP-ribose-1"-monophosphate) processing activity, the macro domain may play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation of proteins, an important post-translational modification which occurs in DNA repair, transcription, chromatin biology, and long-term memory formation, among other processes. Members of this subfamily contain a C-terminal macro domain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 239447  Cd Length: 152  Bit Score: 294.39  E-value: 2.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 289 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 367
Cdd:cd03331     1 SVRYVYGDVTHPSAvCAEDAIIVHCVDDSGHWGRGGLFTALEKRSDQPRKAYELAGKMKDLHLGDLHLFPIDDKNSRLKG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370455298 368 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd03331    81 PDWVALIVAQHRDKSNPLSGIKLSALEKGLKKIYFAAKQKSASVHLPRIGHSTKSFNWYGTERLIRKYLATR 152
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1-272 2.94e-21

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 97.18  E-value: 2.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPA 80
Cdd:PLN03142   554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKT 630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298   81 ADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGK 142
Cdd:PLN03142   631 VNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENK 709
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298  143 NHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDR 216
Cdd:PLN03142   710 LDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYL 783
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370455298  217 QKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 272
Cdd:PLN03142   784 MQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
2-43 2.88e-18

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: 80.60  E-value: 2.88e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370455298   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 43
Cdd:cd18793    94 NLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
2-69 1.23e-12

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627 [Multi-domain]  Cd Length: 866  Bit Score: 70.15  E-value: 1.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370455298   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEG 69
Cdd:COG0553   778 NLTGADTVILFDPWWNPAVELQAIDRAHRIGQKRPVKVYRLITRGTIEEKILELQEKKQELLDSLIDA 845
HELICc smart00490
helicase superfamily c-terminal domain;
1-32 1.58e-06

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 45.67  E-value: 1.58e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1370455298    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:smart00490  51 LDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1-32 2.45e-06

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 333970 [Multi-domain]  Cd Length: 111  Bit Score: 46.05  E-value: 2.45e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370455298   1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:pfam00271  80 LDLPDVNLVINYDLPWNPASYIQRIGRAGRAG 111
 
Name Accession Description Interval E-value
Macro_Poa1p_like_SNF2 cd03331
Macro domain, Poa1p_like family, SNF2 subfamily. The macro domain is a high-affinity ...
289-439 2.45e-99

Macro domain, Poa1p_like family, SNF2 subfamily. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ADP-ribose as a ligand. Previously identified as displaying an Appr-1"-p (ADP-ribose-1"-monophosphate) processing activity, the macro domain may play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation of proteins, an important post-translational modification which occurs in DNA repair, transcription, chromatin biology, and long-term memory formation, among other processes. Members of this subfamily contain a C-terminal macro domain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 239447  Cd Length: 152  Bit Score: 294.39  E-value: 2.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 289 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 367
Cdd:cd03331     1 SVRYVYGDVTHPSAvCAEDAIIVHCVDDSGHWGRGGLFTALEKRSDQPRKAYELAGKMKDLHLGDLHLFPIDDKNSRLKG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370455298 368 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd03331    81 PDWVALIVAQHRDKSNPLSGIKLSALEKGLKKIYFAAKQKSASVHLPRIGHSTKSFNWYGTERLIRKYLATR 152
Macro_Poa1p_like cd02901
Macro domain, Poa1p_like family. The macro domain is a high-affinity ADP-ribose binding module ...
290-439 1.34e-31

Macro domain, Poa1p_like family. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ADP-ribose as a ligand. Previously identified as displaying an Appr-1"-p (ADP-ribose-1"-monophosphate) processing activity, the macro domain may play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation of proteins, an important post-translational modification which occurs in DNA repair, transcription, chromatin biology, and long-term memory formation, among other processes. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 239230  Cd Length: 140  Bit Score: 117.77  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 290 LKYVSGDVTHPqagAEDALIVHCVDDSGHWGRGGLFTALEKRsAEPRKIYELAGKMKDLSLGGVLLFPVDDkesrNKGQD 369
Cdd:cd02901     2 ITYVKGDLLHA---PEAAALAHAVNCDGVMGKGIALQFKEKF-PEFVEEYRAACKKKELLLGGVAVLERGS----SLVSR 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370455298 370 LLALIVAQHRDRSnvlsGIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd02901    74 YIYNLPTKVHYGP----KSRYEAIEKSLRELRaHARDNGIKSVAMPRIGCGLGGLDWEEVEPLIEKALADR 140
Macro cd02749
Macro domain, a high-affinity ADP-ribose binding module found in a variety of proteins as a ...
289-437 7.61e-25

Macro domain, a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ADP-ribose as a ligand. Previously identified as displaying an Appr-1"-p (ADP-ribose-1"-monophosphate) processing activity, the macro domain may play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation of proteins, an important post-translational modification which occurs in DNA repair, transcription, chromatin biology, and long-term memory formation, among other processes.


Pssm-ID: 239150  Cd Length: 147  Bit Score: 99.75  E-value: 7.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 289 SLKYVSGDVTHPQagaEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKEsrnkGQ 368
Cdd:cd02749     1 KIKVVSGDITKPL---GSDAIVNAANSSGRDGGGVNLAISKKAGKELEEESKKLRKELELQVGEAVLTKGYNLD----GA 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370455298 369 DLLALIVAQHRDRSN--VLSGIKMAALEEGLKKiflAAKKKKASVHLPRIGHATKGF------NWYGTERLIRKHLA 437
Cdd:cd02749    74 KYLIHIVGPKYNQGNnkAAFELLKNAYENCLKE---AEEKGIKSIAFPLIGTGPAGFpkderePWEDAIKIALEAAI 147
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1-272 2.94e-21

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 97.18  E-value: 2.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPA 80
Cdd:PLN03142   554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKT 630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298   81 ADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGK 142
Cdd:PLN03142   631 VNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENK 709
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298  143 NHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDR 216
Cdd:PLN03142   710 LDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYL 783
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370455298  217 QKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 272
Cdd:PLN03142   784 MQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
2-43 2.88e-18

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: 80.60  E-value: 2.88e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370455298   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 43
Cdd:cd18793    94 NLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
2-69 1.23e-12

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627 [Multi-domain]  Cd Length: 866  Bit Score: 70.15  E-value: 1.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370455298   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEG 69
Cdd:COG0553   778 NLTGADTVILFDPWWNPAVELQAIDRAHRIGQKRPVKVYRLITRGTIEEKILELQEKKQELLDSLIDA 845
HELICc smart00490
helicase superfamily c-terminal domain;
1-32 1.58e-06

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 45.67  E-value: 1.58e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1370455298    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:smart00490  51 LDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1-32 2.45e-06

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 333970 [Multi-domain]  Cd Length: 111  Bit Score: 46.05  E-value: 2.45e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370455298   1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:pfam00271  80 LDLPDVNLVINYDLPWNPASYIQRIGRAGRAG 111
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
136-289 3.08e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 340095 [Multi-domain]  Cd Length: 756  Bit Score: 46.36  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 136 RDQEEgknhmylfEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEgrslrNKGSVLipglvegSTKRKRVLSPEELED 215
Cdd:pfam17380 493 RQQEE--------DQKKKKLEKDKEEREKAEAEEENKRKIIEKELEE-----NKQAII-------EEENKRKILEKEMED 552
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 216 RQKKRQEaaAKRRRLIEEKKRQKEEAEHKKKMawwesnNYQSFCLPSEESEPEDLE----------NGEESSAELDYQDP 285
Cdd:pfam17380 553 RQNAIYE--EEERRIAEEERRKQIEIEERKQI------QEQIMIASEERSRLDAMErerellrqiiENEKKQKEFERQEL 624

                  ....
gi 1370455298 286 DATS 289
Cdd:pfam17380 625 LATT 628
Caldesmon pfam02029
Caldesmon;
154-267 1.17e-03

Caldesmon;


Pssm-ID: 307930 [Multi-domain]  Cd Length: 263  Bit Score: 40.62  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 154 SKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRNK---GSVLIPGLVEGSTKRKRVLSPEEledrQKKRQEAAAKRRRL 230
Cdd:pfam02029   3 DEQDAEAFLEAEQKLEKIRRSHQEKESQEFEKLRQKqqeAEVELEELKRKREERRKIREEEE----QRRKQEEAERKLRE 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370455298 231 IEEKKRQKEEAEhKKKMAWWESNNYQSFCLPSEESEP 267
Cdd:pfam02029  79 EEEKRRMKEEIE-RRRMEAAEKRQKNLDTSSAEGKKP 114
DUF4207 pfam13904
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several ...
151-248 4.56e-03

Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 316426 [Multi-domain]  Cd Length: 250  Bit Score: 38.58  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370455298 151 KDYSKEPSKE--DRKSFEQlvnlQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRKRVLSPEeledrQKKRQEAAAKRR 228
Cdd:pfam13904 119 KRLAKEKYQEwlQRKARQQ----KKKREQSHKQKAAEKASSSLSSSVRNVSKEEIKRRLQEWE-----LKKLEQQQRKRE 189
                          90       100
                  ....*....|....*....|
gi 1370455298 229 RLIEEKKRQKEEAEHKKKMA 248
Cdd:pfam13904 190 EEQREQLKKEEEEQERKQLA 209
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
219-268 7.69e-03

Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.


Pssm-ID: 311093  Cd Length: 192  Bit Score: 37.48  E-value: 7.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370455298 219 KRQEA-AAKRRRLIE----------EKKRQKEEAEHKKKMAWWES----NNYQSFCLPSEESEPE 268
Cdd:pfam06936  80 KRQEAlEAARLRMQEeldaqaekfkEKQKQLEEEKRRQKIEMWESmqegKSYKGNAKLAQEETPE 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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