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Conserved domains on  [gi|545478468|ref|NP_001269889|]
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cell division cycle and apoptosis regulator protein 1 isoform b [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 ...
 464-589 1.42e-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: 1.42e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468   464 QHPARLVKFLVGMKGKD-EAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRpeetH 542
Cdd:pfam14443    1 VHPCKLLKFLVGDRGKDnEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYR----P 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 545478468   543 KGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGE 589
Cdd:pfam14443   77 KTDGFPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 133-189 7.73e-37

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


:

Pssm-ID: 464176  Cd Length: 58  Bit Score: 132.49  E-value: 7.73e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 545478468   133 RVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQR 189
Cdd:pfam14444    2 RVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 708-775 3.36e-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: 3.36e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545478468   708 LPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSL 775
Cdd:pfam19256    1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 357-439 3.42e-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: 3.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468   357 DCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKN--MAILDPPDadhLYSAKV 434
Cdd:pfam19257    1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQpaEAALEPAD---RYNAKV 77


                   ....*
gi 545478468   435 MLMAS 439
Cdd:pfam19257   78 MLLSG 82
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
622-655 2.92e-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: 2.92e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 545478468    622 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 655
Cdd:smart00513    2 AKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 995-1130 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 545478468   995 TVKQESKDVEENVGLIVY--NGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVK 1072
Cdd:TIGR02168  327 ELESKLDELAEELAELEEklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545478468  1073 KDLSQLQENLK-----ISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKE 1130
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 ...
 464-589 1.42e-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: 1.42e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468   464 QHPARLVKFLVGMKGKD-EAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRpeetH 542
Cdd:pfam14443    1 VHPCKLLKFLVGDRGKDnEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYR----P 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 545478468   543 KGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGE 589
Cdd:pfam14443   77 KTDGFPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 133-189 7.73e-37

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


Pssm-ID: 464176  Cd Length: 58  Bit Score: 132.49  E-value: 7.73e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 545478468   133 RVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQR 189
Cdd:pfam14444    2 RVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 708-775 3.36e-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: 3.36e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545478468   708 LPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSL 775
Cdd:pfam19256    1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 357-439 3.42e-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: 3.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468   357 DCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKN--MAILDPPDadhLYSAKV 434
Cdd:pfam19257    1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQpaEAALEPAD---RYNAKV 77


                   ....*
gi 545478468   435 MLMAS 439
Cdd:pfam19257   78 MLLSG 82
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
622-655 2.92e-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: 2.92e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 545478468    622 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 655
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 ...
 622-655 3.36e-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: 3.36e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 545478468   622 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 655
Cdd:pfam02037    2 SKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 995-1130 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 545478468   995 TVKQESKDVEENVGLIVY--NGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVK 1072
Cdd:TIGR02168  327 ELESKLDELAEELAELEEklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545478468  1073 KDLSQLQENLK-----ISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKE 1130
Cdd:TIGR02168  407 ARLERLEDRRErlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1026-1131 2.44e-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: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468  1026 LEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREV---KKDLSQLQENLKISENMNLQFENQMNKTIRN 1102
Cdd:pfam15905  193 LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVekyKLDIAQLEELLKEKNDEIESLKQSLEEKEQE 272

                           90       100       110
                   ....*....|....*....|....*....|....
gi 545478468  1103 LSTVMDEIHTVLK-----KDNVKNEDKDQKSKEN 1131
Cdd:pfam15905  273 LSKQIKDLNEKCKlleseKEELLREYEEKEQTLN 306
secA PRK12903
preprotein translocase subunit SecA; Reviewed
 1022-1131 5.69e-03

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237258 [Multi-domain]  Cd Length: 925  Bit Score: 40.81  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468 1022 LLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIR 1101
Cdd:PRK12903  807 LIDQIIESEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNK 886

                          90       100       110
                  ....*....|....*....|....*....|
gi 545478468 1102 NLSTVMDEIHTVLKKDNVKNEDKDQKSKEN 1131
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 ...
 464-589 1.42e-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: 1.42e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468   464 QHPARLVKFLVGMKGKD-EAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRpeetH 542
Cdd:pfam14443    1 VHPCKLLKFLVGDRGKDnEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYR----P 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 545478468   543 KGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGE 589
Cdd:pfam14443   77 KTDGFPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 133-189 7.73e-37

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


Pssm-ID: 464176  Cd Length: 58  Bit Score: 132.49  E-value: 7.73e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 545478468   133 RVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQR 189
Cdd:pfam14444    2 RVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 708-775 3.36e-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: 3.36e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545478468   708 LPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSL 775
Cdd:pfam19256    1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 357-439 3.42e-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: 3.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468   357 DCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKN--MAILDPPDadhLYSAKV 434
Cdd:pfam19257    1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQpaEAALEPAD---RYNAKV 77


                   ....*
gi 545478468   435 MLMAS 439
Cdd:pfam19257   78 MLLSG 82
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
622-655 2.92e-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: 2.92e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 545478468    622 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 655
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 ...
 622-655 3.36e-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: 3.36e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 545478468   622 KTMKVNDLRKELESRALSSKGLKSQLIARLTKQL 655
Cdd:pfam02037    2 SKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 995-1130 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 545478468   995 TVKQESKDVEENVGLIVY--NGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVK 1072
Cdd:TIGR02168  327 ELESKLDELAEELAELEEklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545478468  1073 KDLSQLQENLK-----ISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKE 1130
Cdd:TIGR02168  407 ARLERLEDRRErlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1021-1130 4.21e-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: 47.71  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468  1021 SLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQmnktI 1100
Cdd:TIGR04523  465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK----I 540

                           90       100       110
                   ....*....|....*....|....*....|
gi 545478468  1101 RNLSTVMDEIHTVLKKDNVKNEdKDQKSKE 1130
Cdd:TIGR04523  541 SDLEDELNKDDFELKKENLEKE-IDEKNKE 569
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1026-1131 2.44e-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: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468  1026 LEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREV---KKDLSQLQENLKISENMNLQFENQMNKTIRN 1102
Cdd:pfam15905  193 LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVekyKLDIAQLEELLKEKNDEIESLKQSLEEKEQE 272

                           90       100       110
                   ....*....|....*....|....*....|....
gi 545478468  1103 LSTVMDEIHTVLK-----KDNVKNEDKDQKSKEN 1131
Cdd:pfam15905  273 LSKQIKDLNEKCKlleseKEELLREYEEKEQTLN 306
secA PRK12903
preprotein translocase subunit SecA; Reviewed
 1022-1131 5.69e-03

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237258 [Multi-domain]  Cd Length: 925  Bit Score: 40.81  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478468 1022 LLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIR 1101
Cdd:PRK12903  807 LIDQIIESEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNK 886

                          90       100       110
                  ....*....|....*....|....*....|
gi 545478468 1102 NLSTVMDEIHTVLKKDNVKNEDKDQKSKEN 1131
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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