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Conserved domains on  [gi|46852388|ref|NP_060707|]
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cell division cycle and apoptosis regulator protein 1 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 479-604 1.39e-64

DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.


:

Pssm-ID: 464175  Cd Length: 123  Bit Score: 214.13  E-value: 1.39e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388    479 QHPARLVKFLVGMKGKD-EAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRpeetH 557
Cdd:pfam14443    1 VHPCKLLKFLVGDRGKDnEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYR----P 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46852388    558 KGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGE 604
Cdd:pfam14443   77 KTDGFPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 148-204 7.83e-37

S1-like; S1-like RNA binding domain found in DBC1


:

Pssm-ID: 464176  Cd Length: 58  Bit Score: 132.49  E-value: 7.83e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 46852388    148 RVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQR 204
Cdd:pfam14444    2 RVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 723-790 3.40e-33

LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.


:

Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 122.35  E-value: 3.40e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852388    723 LPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSL 790
Cdd:pfam19256    1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 372-454 3.50e-28

BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.


:

Pssm-ID: 466013  Cd Length: 82  Bit Score: 108.56  E-value: 3.50e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388    372 DCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKN--MAILDPPDadhLYSAKV 449
Cdd:pfam19257    1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQpaEAALEPAD---RYNAKV 77


                   ....*
gi 46852388    450 MLMAS 454
Cdd:pfam19257   78 MLLSG 82
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
637-670 2.96e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 47.48  E-value: 2.96e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 46852388     637 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 670
Cdd:smart00513    2 AKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1010-1145 2.36e-05

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: 48.90  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388   1010 TVKQESKDVEENVGLIVY--NGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVK 1087
Cdd:TIGR02168  327 ELESKLDELAEELAELEEklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852388   1088 KDLSQLQENLK-----ISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKE 1145
Cdd:TIGR02168  407 ARLERLEDRRErlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
 
Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 479-604 1.39e-64

DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.


Pssm-ID: 464175  Cd Length: 123  Bit Score: 214.13  E-value: 1.39e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388    479 QHPARLVKFLVGMKGKD-EAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRpeetH 557
Cdd:pfam14443    1 VHPCKLLKFLVGDRGKDnEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYR----P 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46852388    558 KGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGE 604
Cdd:pfam14443   77 KTDGFPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 148-204 7.83e-37

S1-like; S1-like RNA binding domain found in DBC1


Pssm-ID: 464176  Cd Length: 58  Bit Score: 132.49  E-value: 7.83e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 46852388    148 RVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQR 204
Cdd:pfam14444    2 RVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 723-790 3.40e-33

LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 122.35  E-value: 3.40e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852388    723 LPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSL 790
Cdd:pfam19256    1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 372-454 3.50e-28

BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466013  Cd Length: 82  Bit Score: 108.56  E-value: 3.50e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388    372 DCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKN--MAILDPPDadhLYSAKV 449
Cdd:pfam19257    1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQpaEAALEPAD---RYNAKV 77


                   ....*
gi 46852388    450 MLMAS 454
Cdd:pfam19257   78 MLLSG 82
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
637-670 2.96e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 47.48  E-value: 2.96e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 46852388     637 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 670
Cdd:smart00513    2 AKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 637-670 3.37e-07

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 47.40  E-value: 3.37e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 46852388    637 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 670
Cdd:pfam02037    2 SKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1010-1145 2.36e-05

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: 48.90  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388   1010 TVKQESKDVEENVGLIVY--NGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVK 1087
Cdd:TIGR02168  327 ELESKLDELAEELAELEEklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852388   1088 KDLSQLQENLK-----ISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKE 1145
Cdd:TIGR02168  407 ARLERLEDRRErlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1041-1146 2.41e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 41.34  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388   1041 LEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREV---KKDLSQLQENLKISENMNLQFENQMNKTIRN 1117
Cdd:pfam15905  193 LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVekyKLDIAQLEELLKEKNDEIESLKQSLEEKEQE 272

                           90       100       110
                   ....*....|....*....|....*....|....
gi 46852388   1118 LSTVMDEIHTVLK-----KDNVKNEDKDQKSKEN 1146
Cdd:pfam15905  273 LSKQIKDLNEKCKlleseKEELLREYEEKEQTLN 306
secA PRK12903
preprotein translocase subunit SecA; Reviewed
 1037-1146 5.68e-03

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237258 [Multi-domain]  Cd Length: 925  Bit Score: 40.81  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388  1037 LLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIR 1116
Cdd:PRK12903  807 LIDQIIESEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNK 886

                          90       100       110
                  ....*....|....*....|....*....|
gi 46852388  1117 NLSTVMDEIHTVLKKDNVKNEDKDQKSKEN 1146
Cdd:PRK12903  887 LIIAKDVLIKLVISSDEIKQDEKTTKKKKK 916
 
Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 479-604 1.39e-64

DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.


Pssm-ID: 464175  Cd Length: 123  Bit Score: 214.13  E-value: 1.39e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388    479 QHPARLVKFLVGMKGKD-EAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRpeetH 557
Cdd:pfam14443    1 VHPCKLLKFLVGDRGKDnEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYR----P 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46852388    558 KGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGE 604
Cdd:pfam14443   77 KTDGFPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 148-204 7.83e-37

S1-like; S1-like RNA binding domain found in DBC1


Pssm-ID: 464176  Cd Length: 58  Bit Score: 132.49  E-value: 7.83e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 46852388    148 RVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQR 204
Cdd:pfam14444    2 RVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 723-790 3.40e-33

LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 122.35  E-value: 3.40e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852388    723 LPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSL 790
Cdd:pfam19256    1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 372-454 3.50e-28

BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466013  Cd Length: 82  Bit Score: 108.56  E-value: 3.50e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388    372 DCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKN--MAILDPPDadhLYSAKV 449
Cdd:pfam19257    1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQpaEAALEPAD---RYNAKV 77


                   ....*
gi 46852388    450 MLMAS 454
Cdd:pfam19257   78 MLLSG 82
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
637-670 2.96e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 47.48  E-value: 2.96e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 46852388     637 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 670
Cdd:smart00513    2 AKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 637-670 3.37e-07

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 47.40  E-value: 3.37e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 46852388    637 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 670
Cdd:pfam02037    2 SKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1010-1145 2.36e-05

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: 48.90  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388   1010 TVKQESKDVEENVGLIVY--NGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVK 1087
Cdd:TIGR02168  327 ELESKLDELAEELAELEEklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852388   1088 KDLSQLQENLK-----ISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKE 1145
Cdd:TIGR02168  407 ARLERLEDRRErlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 986-1145 3.83e-05

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: 48.09  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388    986 EENHEESESLQEDMLGNRLLLptptvKQESKDVEE--NVGLIVYNGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTD 1063
Cdd:TIGR04523  418 QQEKELLEKEIERLKETIIKN-----NSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388   1064 EDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQmnktIRNLSTVMDEIHTVLKKDNVKNEdKDQKS 1143
Cdd:TIGR04523  493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK----ISDLEDELNKDDFELKKENLEKE-IDEKN 567


                   ..
gi 46852388   1144 KE 1145
Cdd:TIGR04523  568 KE 569
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1041-1146 2.41e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 41.34  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388   1041 LEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREV---KKDLSQLQENLKISENMNLQFENQMNKTIRN 1117
Cdd:pfam15905  193 LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVekyKLDIAQLEELLKEKNDEIESLKQSLEEKEQE 272

                           90       100       110
                   ....*....|....*....|....*....|....
gi 46852388   1118 LSTVMDEIHTVLK-----KDNVKNEDKDQKSKEN 1146
Cdd:pfam15905  273 LSKQIKDLNEKCKlleseKEELLREYEEKEQTLN 306
secA PRK12903
preprotein translocase subunit SecA; Reviewed
 1037-1146 5.68e-03

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237258 [Multi-domain]  Cd Length: 925  Bit Score: 40.81  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852388  1037 LLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIR 1116
Cdd:PRK12903  807 LIDQIIESEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNK 886

                          90       100       110
                  ....*....|....*....|....*....|
gi 46852388  1117 NLSTVMDEIHTVLKKDNVKNEDKDQKSKEN 1146
Cdd:PRK12903  887 LIIAKDVLIKLVISSDEIKQDEKTTKKKKK 916
 
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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