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Conserved domains on  [gi|392887325|ref|NP_493018|]
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Zinc finger PHD-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

DUF1280 domain-containing protein( domain architecture ID 10536504)

DUF1280 domain-containing protein similar to Caenorhabditis elegans enhanced RNAi (RNA interference)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF1280 pfam06918
Protein of unknown function (DUF1280); This family represents a conserved region approximately ...
152-367 3.34e-68

Protein of unknown function (DUF1280); This family represents a conserved region approximately 200 residues long within a number of proteins of unknown function that seem to be specific to C. elegans.


:

Pssm-ID: 369136  Cd Length: 219  Bit Score: 225.52  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  152 SRSEKFRRIEIARAELQRcgekylqiqlfkvILGGESSE-FYRLLLGRLSKLGLLKWK--MSKREGLYLYHASNLTRRRF 228
Cdd:pfam06918   1 NRETKKNRCERVIEAIQE-------------IVGEEDVDaFLTDFVKFLDKSGEFKFKlkLSPWETFVLKHKFHLSDGFL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  229 TKLKQMLRGSGCIDPLPSIHEIKKLEKVVGSSDQFKVTEHTVDGKS--------VVAVHLLDVVKMLTERINELVANGKM 300
Cdd:pfam06918  68 KKFKKFLKEFLGFDVFPSRKSICELEKKVSSIDLYEISVEKVVKKTsgrevkkkVTVVQCKDVEKLLSRRLEELAASGRL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  301 VVG---DDPIWLTILGDKGSEEFKLCLSIGNVSQPNSCFHLIPLGIFNDDESSENIRKYLGPIVEQLNRL 367
Cdd:pfam06918 148 IFDestGDDIVLGIGGDKGGDETKLCLIIGNVEKPNSPHNLLLLGMYTGDDDYENLKKYLGPVFEQLNNL 217
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
14-178 1.98e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    14 SLSSDLKRALQDNEKLTRDVS-DAKLLKEDAE----------IKLKKIRDKLNGEHSE------KLGKLNDKYKAVQEEL 76
Cdd:TIGR02169  702 NRLDELSQELSDASRKIGEIEkEIEQLEQEEEklkerleeleEDLSSLEQEIENVKSElkeleaRIEELEEDLHKLEEAL 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    77 KTMKQS-----WTQLKREKGVLETENRRLETAKRELDRQLSGKNDELRMADVEKVEDVKMIRDLKAgKRPPFKTEFKNLI 151
Cdd:TIGR02169  782 NDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-QIKSIEKEIENLN 860
                          170       180
                   ....*....|....*....|....*...
gi 392887325   152 SRSEKF-RRIEIARAELQRCGEKYLQIQ 178
Cdd:TIGR02169  861 GKKEELeEELEELEAALRDLESRLGDLK 888
 
Name Accession Description Interval E-value
DUF1280 pfam06918
Protein of unknown function (DUF1280); This family represents a conserved region approximately ...
152-367 3.34e-68

Protein of unknown function (DUF1280); This family represents a conserved region approximately 200 residues long within a number of proteins of unknown function that seem to be specific to C. elegans.


Pssm-ID: 369136  Cd Length: 219  Bit Score: 225.52  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  152 SRSEKFRRIEIARAELQRcgekylqiqlfkvILGGESSE-FYRLLLGRLSKLGLLKWK--MSKREGLYLYHASNLTRRRF 228
Cdd:pfam06918   1 NRETKKNRCERVIEAIQE-------------IVGEEDVDaFLTDFVKFLDKSGEFKFKlkLSPWETFVLKHKFHLSDGFL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  229 TKLKQMLRGSGCIDPLPSIHEIKKLEKVVGSSDQFKVTEHTVDGKS--------VVAVHLLDVVKMLTERINELVANGKM 300
Cdd:pfam06918  68 KKFKKFLKEFLGFDVFPSRKSICELEKKVSSIDLYEISVEKVVKKTsgrevkkkVTVVQCKDVEKLLSRRLEELAASGRL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  301 VVG---DDPIWLTILGDKGSEEFKLCLSIGNVSQPNSCFHLIPLGIFNDDESSENIRKYLGPIVEQLNRL 367
Cdd:pfam06918 148 IFDestGDDIVLGIGGDKGGDETKLCLIIGNVEKPNSPHNLLLLGMYTGDDDYENLKKYLGPVFEQLNNL 217
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
14-178 1.98e-06

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    14 SLSSDLKRALQDNEKLTRDVS-DAKLLKEDAE----------IKLKKIRDKLNGEHSE------KLGKLNDKYKAVQEEL 76
Cdd:TIGR02169  702 NRLDELSQELSDASRKIGEIEkEIEQLEQEEEklkerleeleEDLSSLEQEIENVKSElkeleaRIEELEEDLHKLEEAL 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    77 KTMKQS-----WTQLKREKGVLETENRRLETAKRELDRQLSGKNDELRMADVEKVEDVKMIRDLKAgKRPPFKTEFKNLI 151
Cdd:TIGR02169  782 NDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-QIKSIEKEIENLN 860
                          170       180
                   ....*....|....*....|....*...
gi 392887325   152 SRSEKF-RRIEIARAELQRCGEKYLQIQ 178
Cdd:TIGR02169  861 GKKEELeEELEELEAALRDLESRLGDLK 888
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-168 7.09e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  19 LKRALQDNEKLTRDVSDAKLLKEDAEIKLKKIRDKLNgEHSEKLGKLNDKYKAVQEELKTM---KQSWTQLKREKGVLET 95
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEG 252
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392887325  96 ENRRLETAKRELDRQLSGKNDELRMADvEKVEDVKMIRDLKAG--KRPPFKTEFKNLISRSEKfrRIEIARAELQ 168
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEyiKLSEFYEEYLDELREIEK--RLSRLEEEIN 324
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
14-119 9.22e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 9.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  14 SLSSDLKRALQDNEKLTRDVSDAKLLKEDAEIKLKKIRDKLNgEHSEKLGKLNDKYKAVQEELKTMKQSWTQLKREKGVL 93
Cdd:COG4372   49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
                         90       100
                 ....*....|....*....|....*.
gi 392887325  94 ETENRRLETAKRELDRQLSGKNDELR 119
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELK 153
Caldesmon pfam02029
Caldesmon;
7-144 2.28e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    7 MTTPLGVSLssdlKRALQDNEKLTRDVSDAKLLKEdAEIKLKKIRDKLNGEHSEKLGKLNDKYKAVQEELKTMKQswtql 86
Cdd:pfam02029 215 EVTKLKVTT----KRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKK----- 284
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392887325   87 KRE--KGVLETENRRLETAkrELDRQLSGKNDELRMAD---------VEKVEdvKMIRDLKAGKRPPFK 144
Cdd:pfam02029 285 KREerRKLLEEEEQRRKQE--EAERKLREEEEKRRMKEeierrraeaAEKRQ--KLPEDSSSEGKKPFK 349
 
Name Accession Description Interval E-value
DUF1280 pfam06918
Protein of unknown function (DUF1280); This family represents a conserved region approximately ...
152-367 3.34e-68

Protein of unknown function (DUF1280); This family represents a conserved region approximately 200 residues long within a number of proteins of unknown function that seem to be specific to C. elegans.


Pssm-ID: 369136  Cd Length: 219  Bit Score: 225.52  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  152 SRSEKFRRIEIARAELQRcgekylqiqlfkvILGGESSE-FYRLLLGRLSKLGLLKWK--MSKREGLYLYHASNLTRRRF 228
Cdd:pfam06918   1 NRETKKNRCERVIEAIQE-------------IVGEEDVDaFLTDFVKFLDKSGEFKFKlkLSPWETFVLKHKFHLSDGFL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  229 TKLKQMLRGSGCIDPLPSIHEIKKLEKVVGSSDQFKVTEHTVDGKS--------VVAVHLLDVVKMLTERINELVANGKM 300
Cdd:pfam06918  68 KKFKKFLKEFLGFDVFPSRKSICELEKKVSSIDLYEISVEKVVKKTsgrevkkkVTVVQCKDVEKLLSRRLEELAASGRL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  301 VVG---DDPIWLTILGDKGSEEFKLCLSIGNVSQPNSCFHLIPLGIFNDDESSENIRKYLGPIVEQLNRL 367
Cdd:pfam06918 148 IFDestGDDIVLGIGGDKGGDETKLCLIIGNVEKPNSPHNLLLLGMYTGDDDYENLKKYLGPVFEQLNNL 217
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
14-178 1.98e-06

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    14 SLSSDLKRALQDNEKLTRDVS-DAKLLKEDAE----------IKLKKIRDKLNGEHSE------KLGKLNDKYKAVQEEL 76
Cdd:TIGR02169  702 NRLDELSQELSDASRKIGEIEkEIEQLEQEEEklkerleeleEDLSSLEQEIENVKSElkeleaRIEELEEDLHKLEEAL 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    77 KTMKQS-----WTQLKREKGVLETENRRLETAKRELDRQLSGKNDELRMADVEKVEDVKMIRDLKAgKRPPFKTEFKNLI 151
Cdd:TIGR02169  782 NDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-QIKSIEKEIENLN 860
                          170       180
                   ....*....|....*....|....*...
gi 392887325   152 SRSEKF-RRIEIARAELQRCGEKYLQIQ 178
Cdd:TIGR02169  861 GKKEELeEELEELEAALRDLESRLGDLK 888
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-168 7.09e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  19 LKRALQDNEKLTRDVSDAKLLKEDAEIKLKKIRDKLNgEHSEKLGKLNDKYKAVQEELKTM---KQSWTQLKREKGVLET 95
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEG 252
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392887325  96 ENRRLETAKRELDRQLSGKNDELRMADvEKVEDVKMIRDLKAG--KRPPFKTEFKNLISRSEKfrRIEIARAELQ 168
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEyiKLSEFYEEYLDELREIEK--RLSRLEEEIN 324
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
14-119 9.22e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 9.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  14 SLSSDLKRALQDNEKLTRDVSDAKLLKEDAEIKLKKIRDKLNgEHSEKLGKLNDKYKAVQEELKTMKQSWTQLKREKGVL 93
Cdd:COG4372   49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
                         90       100
                 ....*....|....*....|....*.
gi 392887325  94 ETENRRLETAKRELDRQLSGKNDELR 119
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELK 153
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
11-173 1.75e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  11 LGVSLSSDLKRALQDNEKLTR---DVSDAKLLKEDAEIKLKKIRDKLNgEHSEKLGKLNDKYKAVQEELKTMKQSWTqlk 87
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKELEELEKKYS--- 657
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  88 rekgvlETENRRLETAKRELDRQLSGKNDELRMADVEKVEDVKMIRDLKAgkrppfktEFKNLISRSEKFRRIEIARAEL 167
Cdd:PRK03918 658 ------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE--------ELEEREKAKKELEKLEKALERV 723

                 ....*.
gi 392887325 168 QRCGEK 173
Cdd:PRK03918 724 EELREK 729
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
17-169 1.83e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    17 SDLKRALQDNEKLTRDVSDAKLLKEDAEIKLKKIRDKLNGEHSEkLGKLNDKYKAVQEELKTMKQSWTQLKREKGVLETE 96
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE-LEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    97 NRRLETAKRELDRQLSGKNDELR--MADVEKVEDVKMIRDLKAGK--------RPPFKTEFKNLISRSEKFRRIEIARAE 166
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAAIAgiEAKINELEEEKEDKALEIKKqewkleqlAADLSKYEQELYDLKEEYDRVEKELSK 487

                   ...
gi 392887325   167 LQR 169
Cdd:TIGR02169  488 LQR 490
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
15-132 2.00e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  15 LSSDLKRALQDNEKLTRDVSDAKLLKEDAEIKLKKIRDKLNGEHSEK---------------LGKLNDKYKAVQEELKTM 79
Cdd:COG1579   43 LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeieslkrrISDLEDEILELMERIEEL 122
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392887325  80 KQswtQLKREKGVLETENRRLETAKRELDRQLSGKNDELRMADVEKVEDVKMI 132
Cdd:COG1579  123 EE---ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
40-167 3.45e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325  40 KEDAEIKLKKIRDKLNgEHSEKLGKLNDKYKAVQEELKTMKQSWTQLKREKGVLETENRRLETAKRELDRQLSGKNDELr 119
Cdd:COG4942   22 AAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392887325 120 maDVEKVEDVKMIRDL-KAGKRPPFK-----TEFKNLISRSEKFRRIEIARAEL 167
Cdd:COG4942  100 --EAQKEELAELLRALyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQ 151
Caldesmon pfam02029
Caldesmon;
7-144 2.28e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    7 MTTPLGVSLssdlKRALQDNEKLTRDVSDAKLLKEdAEIKLKKIRDKLNGEHSEKLGKLNDKYKAVQEELKTMKQswtql 86
Cdd:pfam02029 215 EVTKLKVTT----KRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKK----- 284
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392887325   87 KRE--KGVLETENRRLETAkrELDRQLSGKNDELRMAD---------VEKVEdvKMIRDLKAGKRPPFK 144
Cdd:pfam02029 285 KREerRKLLEEEEQRRKQE--EAERKLREEEEKRRMKEeierrraeaAEKRQ--KLPEDSSSEGKKPFK 349
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
33-178 4.03e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    33 VSDAKLLKEDAEIKLKKIRDKLN------GEHSEKLGKLN------DKYKAVQEELKTMK-----QSWTQLKREKGVLET 95
Cdd:TIGR02168  167 ISKYKERRKETERKLERTRENLDrledilNELERQLKSLErqaekaERYKELKAELRELElallvLRLEELREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887325    96 ENRRLETAKRELDRQLSGKNDELRMADVEKVEDVKMIRDLKAGkrppFKtEFKNLISRSEkfRRIEIARAELQRCGEKYL 175
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LY-ALANEISRLE--QQKQILRERLANLERQLE 319

                   ...
gi 392887325   176 QIQ 178
Cdd:TIGR02168  320 ELE 322
 
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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