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Conserved domains on  [gi|1063736012|ref|NP_001318738|]
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Homeodomain-like transcriptional regulator [Arabidopsis thaliana]

Protein Classification

homeobox domain-containing protein( domain architecture ID 11079024)

homeobox domain-containing protein similar to double homeobox protein that may act as a transcription factor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1071-1145 2.05e-25

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


:

Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 100.69  E-value: 2.05e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063736012 1071 YRSLPLGQDRRRNRYWRFsasasrnDPGCGRIFVELQ-DGRWRLIDSEEAFDYLVKSLDVRGVRESHLHFMLLKIE 1145
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVESPsDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 515-570 1.97e-19

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


:

Pssm-ID: 460696  Cd Length: 58  Bit Score: 83.32  E-value: 1.97e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  515 ENVANLLMVWRFLITFADVLGLWPFTLDEFAQAFHDYDP--RLMGEIHIVLLKTIIKD 570
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEEpsELLDEIHCALLKALVRD 58
Homeodomain pfam00046
Homeodomain;
18-74 1.88e-17

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.54  E-value: 1.88e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063736012   18 KSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERK 74
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 696-765 4.44e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


:

Pssm-ID: 461541  Cd Length: 71  Bit Score: 71.57  E-value: 4.44e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063736012  696 GTVKFAAFHVLSLEGeKGLNILEVAEKIQKSGLRDlTTSRTPEASVAAALSRDTK---LFERVAPSTYCVRAS 765
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRSW 71
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 322-457 3.56e-10

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 64.76  E-value: 3.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  322 LQLERHRKNEeaRIAREVEAHEKRIRRELEKQDMLRRKREE--QIRKEMERqdrerrkeeerllrEKQREEERYLKEQMR 399
Cdd:pfam17380  383 LQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEmeQIRAEQEE--------------ARQREVRRLEEERAR 446

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  400 ELQR-REKFLKKETiRAEKMRQKEEMRKEKEVARLKAANERAIA----RKIAKESME-----LIEDER 457
Cdd:pfam17380  447 EMERvRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAeeqrRKILEKELEerkqaMIEEER 513
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 899-941 3.05e-05

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


:

Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 42.87  E-value: 3.05e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1063736012  899 GEQWVQGLVEGDYSNLSSEERLNALVALIGIATEGNTIRIALE 941
Cdd:pfam15612    4 LPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
 
Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1071-1145 2.05e-25

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 100.69  E-value: 2.05e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063736012 1071 YRSLPLGQDRRRNRYWRFsasasrnDPGCGRIFVELQ-DGRWRLIDSEEAFDYLVKSLDVRGVRESHLHFMLLKIE 1145
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVESPsDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 515-570 1.97e-19

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


Pssm-ID: 460696  Cd Length: 58  Bit Score: 83.32  E-value: 1.97e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  515 ENVANLLMVWRFLITFADVLGLWPFTLDEFAQAFHDYDP--RLMGEIHIVLLKTIIKD 570
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEEpsELLDEIHCALLKALVRD 58
Homeodomain pfam00046
Homeodomain;
18-74 1.88e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.54  E-value: 1.88e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063736012   18 KSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERK 74
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
DDT smart00571
domain in different transcription and chromosome remodeling factors;
514-572 3.72e-17

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 76.90  E-value: 3.72e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063736012   514 DENVANLLMVWRFLITFADVLGLWPF--TLDEFAQAFHDYDPR-LMGEIHIVLLKTIIKDIE 572
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSPFraTLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEG 62
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 696-765 4.44e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 71.57  E-value: 4.44e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063736012  696 GTVKFAAFHVLSLEGeKGLNILEVAEKIQKSGLRDlTTSRTPEASVAAALSRDTK---LFERVAPSTYCVRAS 765
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRSW 71
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 18-75 1.94e-13

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 66.50  E-value: 1.94e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012   18 KSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERKS 75
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 17-73 8.06e-13

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 64.58  E-value: 8.06e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063736012    17 SKSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKER 73
Cdd:smart00389    1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
16-83 4.15e-12

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 65.92  E-value: 4.15e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012   16 ESKSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERKSTTPSKRQR 83
Cdd:COG5576     50 PPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQR 117
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 322-457 3.56e-10

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 64.76  E-value: 3.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  322 LQLERHRKNEeaRIAREVEAHEKRIRRELEKQDMLRRKREE--QIRKEMERqdrerrkeeerllrEKQREEERYLKEQMR 399
Cdd:pfam17380  383 LQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEmeQIRAEQEE--------------ARQREVRRLEEERAR 446

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  400 ELQR-REKFLKKETiRAEKMRQKEEMRKEKEVARLKAANERAIA----RKIAKESME-----LIEDER 457
Cdd:pfam17380  447 EMERvRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAeeqrRKILEKELEerkqaMIEEER 513
PTZ00121 PTZ00121
MAEBL; Provisional
 319-468 8.21e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  319 DDALQLERHRKNEEARIAREV-EAHEKR----IRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR----E 389
Cdd:PTZ00121  1537 DEAKKAEEKKKADELKKAEELkKAEEKKkaeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaE 1616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  390 EERYLKEQMR-ELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTK 468
Cdd:PTZ00121  1617 EAKIKAEELKkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-492 1.12e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  308 SEREVGNEDEDDDALQLERhRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQirKEMERQDRERRKEEERLLREKQ 387
Cdd:COG1196    302 QDIARLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  388 REEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALT 467
Cdd:COG1196    379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                          170       180
                   ....*....|....*....|....*.
gi 1063736012  468 KGL-PSMLALDFETLQNLDEYRDKQA 492
Cdd:COG1196    459 EALlELLAELLEEAALLEAALAELLE 484
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 899-941 3.05e-05

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 42.87  E-value: 3.05e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1063736012  899 GEQWVQGLVEGDYSNLSSEERLNALVALIGIATEGNTIRIALE 941
Cdd:pfam15612    4 LPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 336-452 6.60e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  336 AREVEAHEKRIRRELEKQdmlRRKREEQIRKEMERQDrerrkeeerllrekqREEERYLKEQMRELQRREKfLKKETIRA 415
Cdd:cd16269    195 EKEKEIEAERAKAEAAEQ---ERKLLEEQQRELEQKL---------------EDQERSYEEHLRQLKEKME-EERENLLK 255

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1063736012  416 EKMRQKEEMRKEKEvaRLKAANERAIARKIAKESMEL 452
Cdd:cd16269    256 EQERALESKLKEQE--ALLEEGFKEQAELLQEEIRSL 290
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 325-492 1.50e-03

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: 43.52  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVEAHEKRIRREL---EKQDMLRRKREEQIRKEMERQdreRRKEEERLLREKQREEERYlKEQMREL 401
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYlekEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEEL-EAALRDL 880

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  402 QRREKFLKKETIRAEKmrQKEEMRKEKEVARLKA------ANERAIARKIAKESMELIEDERLELMEVAALTKGLP---- 471
Cdd:TIGR02169  881 ESRLGDLKKERDELEA--QLRELERKIEELEAQIekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdvqa 958

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1063736012  472 ---------------SMLALD--FETLQNLDEYRDKQA 492
Cdd:TIGR02169  959 elqrveeeiralepvNMLAIQeyEEVLKRLDELKEKRA 996
 
Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1071-1145 2.05e-25

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 100.69  E-value: 2.05e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063736012 1071 YRSLPLGQDRRRNRYWRFsasasrnDPGCGRIFVELQ-DGRWRLIDSEEAFDYLVKSLDVRGVRESHLHFMLLKIE 1145
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVESPsDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 515-570 1.97e-19

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


Pssm-ID: 460696  Cd Length: 58  Bit Score: 83.32  E-value: 1.97e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  515 ENVANLLMVWRFLITFADVLGLWPFTLDEFAQAFHDYDP--RLMGEIHIVLLKTIIKD 570
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEEpsELLDEIHCALLKALVRD 58
Homeodomain pfam00046
Homeodomain;
18-74 1.88e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.54  E-value: 1.88e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063736012   18 KSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERK 74
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
DDT smart00571
domain in different transcription and chromosome remodeling factors;
514-572 3.72e-17

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 76.90  E-value: 3.72e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063736012   514 DENVANLLMVWRFLITFADVLGLWPF--TLDEFAQAFHDYDPR-LMGEIHIVLLKTIIKDIE 572
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSPFraTLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEG 62
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 696-765 4.44e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 71.57  E-value: 4.44e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063736012  696 GTVKFAAFHVLSLEGeKGLNILEVAEKIQKSGLRDlTTSRTPEASVAAALSRDTK---LFERVAPSTYCVRAS 765
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRSW 71
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 18-75 1.94e-13

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 66.50  E-value: 1.94e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012   18 KSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERKS 75
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 17-73 8.06e-13

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 64.58  E-value: 8.06e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063736012    17 SKSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKER 73
Cdd:smart00389    1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
16-83 4.15e-12

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 65.92  E-value: 4.15e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012   16 ESKSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERKSTTPSKRQR 83
Cdd:COG5576     50 PPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQR 117
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 322-457 3.56e-10

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 64.76  E-value: 3.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  322 LQLERHRKNEeaRIAREVEAHEKRIRRELEKQDMLRRKREE--QIRKEMERqdrerrkeeerllrEKQREEERYLKEQMR 399
Cdd:pfam17380  383 LQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEmeQIRAEQEE--------------ARQREVRRLEEERAR 446

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  400 ELQR-REKFLKKETiRAEKMRQKEEMRKEKEVARLKAANERAIA----RKIAKESME-----LIEDER 457
Cdd:pfam17380  447 EMERvRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAeeqrRKILEKELEerkqaMIEEER 513
PTZ00121 PTZ00121
MAEBL; Provisional
 319-468 8.21e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  319 DDALQLERHRKNEEARIAREV-EAHEKR----IRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR----E 389
Cdd:PTZ00121  1537 DEAKKAEEKKKADELKKAEELkKAEEKKkaeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaE 1616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  390 EERYLKEQMR-ELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTK 468
Cdd:PTZ00121  1617 EAKIKAEELKkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
PTZ00121 PTZ00121
MAEBL; Provisional
 307-451 2.98e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.47  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  307 KSEREVGNEDE---DDDALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKRE----EQIRKEMERQDRERRKE 378
Cdd:PTZ00121  1504 KAAEAKKKADEakkAEEAKKADEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEkkkaEEAKKAEEDKNMALRKA 1583

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063736012  379 EERLLREKQREEERYLKEQMRELQRREKFLKKET--IRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESME 451
Cdd:PTZ00121  1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
PTZ00121 PTZ00121
MAEBL; Provisional
 307-456 2.86e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  307 KSEREVGNEDEDDDALQLERHRKNEEARI-AREV--EAHEKRIRRELEKQDMLRRKREEQIRKEMER------QDRERRK 377
Cdd:PTZ00121  1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIkAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaEEAKKAE 1671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  378 EEERLLREKQREEERYLKEQMRELQRREKFLKKETIR---AEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIE 454
Cdd:PTZ00121  1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751


                   ..
gi 1063736012  455 DE 456
Cdd:PTZ00121  1752 DE 1753
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 323-461 2.91e-07

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 54.54  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  323 QLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeerllrEKQREEERylkEQMRELQ 402
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ-------------IEEREQKR---QEEYEEK 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  403 RREKFLKKETIRAEKM-RQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELM 461
Cdd:pfam13868   97 LQEREQMDEIVERIQEeDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER 156
PTZ00121 PTZ00121
MAEBL; Provisional
 319-457 7.32e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 7.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  319 DDALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQ 397
Cdd:PTZ00121  1197 EDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  398 MRELQrrekflkkETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDER 457
Cdd:PTZ00121  1277 ARKAD--------ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 320-462 8.19e-07

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 53.00  E-value: 8.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  320 DALQLERHR-KNEEARIAREVEAHEKRIRRELEkqdmLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQM 398
Cdd:pfam13868  204 DELRAKLYQeEQERKERQKEREEAEKKARQRQE----LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE 279

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  399 RELQRREkflKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELME 462
Cdd:pfam13868  280 EAEKRRM---KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 315-468 8.69e-07

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 50.84  E-value: 8.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRElEKQDMLRRKREEQIRKemerqdrerrkeeerllrekqREEERYL 394
Cdd:pfam11600    9 SQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKE-EAKAEKERAKEEARRK---------------------KEEEKEL 66

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  395 KEQmrelQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERaiaRKiAKESMELIEDERLELMEVAALTK 468
Cdd:pfam11600   67 KEK----ERREKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEK---RK-KEEEKRLKEEEKRIKAEKAEITR 132
PTZ00121 PTZ00121
MAEBL; Provisional
 295-451 9.26e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 9.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  295 DTAAQVHDDPFVKSEREVGNEDEDDDALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKREEQIRKEMER-QD 372
Cdd:PTZ00121  1143 EEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKaED 1222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  373 RERRKEEERLLREKQREEERYLKEQMRELQRREKF---------LKKETIRAEKMRQKEEMRKEKEVAR---LKAANERA 440
Cdd:PTZ00121  1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFeearmahfaRRQAAIKAEEARKADELKKAEEKKKadeAKKAEEKK 1302

                          170
                   ....*....|.
gi 1063736012  441 IARKIAKESME 451
Cdd:PTZ00121  1303 KADEAKKKAEE 1313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-492 1.12e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  308 SEREVGNEDEDDDALQLERhRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQirKEMERQDRERRKEEERLLREKQ 387
Cdd:COG1196    302 QDIARLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  388 REEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALT 467
Cdd:COG1196    379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                          170       180
                   ....*....|....*....|....*.
gi 1063736012  468 KGL-PSMLALDFETLQNLDEYRDKQA 492
Cdd:COG1196    459 EALlELLAELLEEAALLEAALAELLE 484
PTZ00121 PTZ00121
MAEBL; Provisional
 309-451 3.08e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  309 EREVGNEDEDDDALQLERHRKNEEARIAREVEAHE--KRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREK 386
Cdd:PTZ00121  1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEeeKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063736012  387 QREEERYLKEQMR----ELQRREKFLKKetiRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESME 451
Cdd:PTZ00121  1648 KAEELKKAEEENKikaaEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 323-490 4.14e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 50.69  E-value: 4.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  323 QLERHRKNEEARIAREVEAHEKRIRRELEK-------QDMLRRKR--EEQIRKEMER-QDRERRKEEERLLREKQREEER 392
Cdd:pfam13868  166 EREEEREAEREEIEEEKEREIARLRAQQEKaqdekaeRDELRAKLyqEEQERKERQKeREEAEKKARQRQELQQAREEQI 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  393 YLKEQMRELQRREKflkketiRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIED-ERLELMEVAAltkglp 471
Cdd:pfam13868  246 ELKERRLAEEAERE-------EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEErEEQRAAEREE------ 312

                          170
                   ....*....|....*....
gi 1063736012  472 smLALDFETLQNLDEYRDK 490
Cdd:pfam13868  313 --ELEEGERLREEEAERRE 329
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 323-470 4.56e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 50.69  E-value: 4.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  323 QLERHRKNEEARI-AREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYL------- 394
Cdd:pfam13868   86 EQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeylkeka 165

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063736012  395 -KEQMRELQRREKFLKKETIRAeKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTKGL 470
Cdd:pfam13868  166 eREEEREAEREEIEEEKEREIA-RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 322-459 4.91e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.11  E-value: 4.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  322 LQLERHRKN--EEARIAREVEAHEKRIRRELEkQDMLRRKREEQIRKEMERQDRERRkeeerllreKQREEERYLKEQM- 398
Cdd:pfam15709  348 LEVERKRREqeEQRRLQQEQLERAEKMREELE-LEQQRRFEEIRLRKQRLEEERQRQ---------EEEERKQRLQLQAa 417

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063736012  399 --RELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKiaKESMELIEDERLE 459
Cdd:pfam15709  418 qeRARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ--KRLMEMAEEERLE 478
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 309-509 4.96e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 4.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  309 EREVGNEDEDDDALQLERHRKNEearIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMErqdrerrkeeerllrekQR 388
Cdd:pfam17380  441 EEERAREMERVRLEEQERQQQVE---RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE-----------------KE 500

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  389 EEERylKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKaANERAIARKIAKESMELIEDE-RLELMEvaalt 467
Cdd:pfam17380  501 LEER--KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK-QQEMEERRRIQEQMRKATEERsRLEAME----- 572

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1063736012  468 kglpsmlaLDFETLQNLDEYRDKQAIFPPTSvklkKPFAVKP 509
Cdd:pfam17380  573 --------REREMMRQIVESEKARAEYEATT----PITTIKP 602
PTZ00121 PTZ00121
MAEBL; Provisional
 325-490 5.24e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 5.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeeRLLREKQREEERYLKEQMR--E 400
Cdd:PTZ00121  1461 EAKKKAEEAKKADEAKkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---------KKADEAKKAEEAKKADEAKkaE 1531

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  401 LQRREKFLKK--ETIRAEKMRQKEEMRKEKEVARL----KAANERAIARKIAKESMElIEDERLElmEVAALTKGLPSML 474
Cdd:PTZ00121  1532 EAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAeeakKAEEDKNMALRKAEEAKK-AEEARIE--EVMKLYEEEKKMK 1608

                          170
                   ....*....|....*.
gi 1063736012  475 AldfETLQNLDEYRDK 490
Cdd:PTZ00121  1609 A---EEAKKAEEAKIK 1621
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 329-457 5.73e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 50.30  E-value: 5.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  329 KNEEARI---AREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQMRELQRRE 405
Cdd:pfam13868  151 REEDERIleyLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  406 KFLKKETIRA--EKMRQKEEMRkEKEVARLKAANERAIARKIAKESMELIEDER 457
Cdd:pfam13868  231 ARQRQELQQAreEQIELKERRL-AEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 325-459 7.14e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 47.73  E-value: 7.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeerllrekQREEERYLKEQMRELQRR 404
Cdd:pfam05672   18 EKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEAR---------------RLEEERRREEEERQRKAE 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063736012  405 EKFLKKETIRAEKMrqkEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:pfam05672   83 EEAEEREQREQEEQ---ERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLE 134
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 319-462 9.41e-06

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 46.79  E-value: 9.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  319 DDALQLERHRKneEARIAREVEAHEKRIRR---ELEKQDMLRRKRE-EQIRKEMERQDRERRKEeerllrekQREEERYL 394
Cdd:pfam12474    9 KDRFEQERQQL--KKRYEKELEQLERQQKQqieKLEQRQTQELRRLpKRIRAEQKKRLKMFRES--------LKQEKKEL 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063736012  395 K---EQMRELQRREKFLKketiRAEKMRQKEEMRKEKEVARLKAANERAIARkiakesmeLIEDERLELME 462
Cdd:pfam12474   79 KqevEKLPKFQRKEAKRQ----RKEELELEQKHEELEFLQAQSEALERELQQ--------LQNEKRKELAE 137
PTZ00121 PTZ00121
MAEBL; Provisional
 315-457 1.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYL 394
Cdd:PTZ00121  1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063736012  395 KEqmrELQRREKFLKK--ETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIakESMELIEDER 457
Cdd:PTZ00121  1165 KA---EEARKAEDAKKaeAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA--EEARKAEDAK 1224
PTZ00121 PTZ00121
MAEBL; Provisional
 321-463 1.53e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  321 ALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKREEQiRKEMERQDRERRKEEERLLREKQREEERYLKEQMR 399
Cdd:PTZ00121  1271 AIKAEEARKADELKKAEEKkKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  400 elqRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEV 463
Cdd:PTZ00121  1350 ---AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
325-486 1.71e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.10  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVEAHEKRI---RRELE-KQDMLRRKRE------------EQIRKEMERQDRERRKEEERLLREKQR 388
Cdd:COG2268    218 QANREAEEAELEQEREIETARIaeaEAELAkKKAEERREAEtaraeaeaayeiAEANAEREVQRQLEIAEREREIELQEK 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  389 EEERYLKEQMRELqrrekflkKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAkESMELIEDERLELMevaaLTK 468
Cdd:COG2268    298 EAEREEAELEADV--------RKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALA-EAWNKLGDAAILLM----LIE 364

                          170
                   ....*....|....*...
gi 1063736012  469 GLPSMLALDFETLQNLDE 486
Cdd:COG2268    365 KLPEIAEAAAKPLEKIDK 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-465 1.99e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRR------ELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR 388
Cdd:COG1196    238 EAELEELEAELEELEAELEELEAELAELEAELEElrleleELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  389 EEEryLKEQMRELQRREKFLKKETIRAEKMRQK-EEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAA 465
Cdd:COG1196    318 LEE--LEEELAELEEELEELEEELEELEEELEEaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 317-463 2.07e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 48.76  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  317 EDDDALQLERHRKNEEAR--IAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQ-DRERRkeEERLLREKQREEERY 393
Cdd:pfam13868  112 EEDQAEAEEKLEKQRQLReeIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREeEREAE--REEIEEEKEREIARL 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  394 LKEQMRELQRREkflKKETIRA--------EKMRQKEEM---RKEKEVARLKAANERAIARKIAKESMElIEDERLELME 462
Cdd:pfam13868  190 RAQQEKAQDEKA---ERDELRAklyqeeqeRKERQKEREeaeKKARQRQELQQAREEQIELKERRLAEE-AEREEEEFER 265


                   .
gi 1063736012  463 V 463
Cdd:pfam13868  266 M 266
PTZ00121 PTZ00121
MAEBL; Provisional
 306-456 2.07e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  306 VKSEREVGNEDEDDDALQLERHRKNEE----ARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeER 381
Cdd:PTZ00121  1646 KKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK--------KK 1717

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063736012  382 LLREKQREEERYLKEQmrELQRREKFLKKetiRAEKMRQKEEmrKEKEVARLKAANERAiARKIAKESMELIEDE 456
Cdd:PTZ00121  1718 AEELKKAEEENKIKAE--EAKKEAEEDKK---KAEEAKKDEE--EKKKIAHLKKEEEKK-AEEIRKEKEAVIEEE 1784
PTZ00121 PTZ00121
MAEBL; Provisional
 325-488 2.57e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeerllrekqREEERYLKEQMR--ELQ 402
Cdd:PTZ00121  1125 EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARK----------------AEDAKKAEAARKaeEVR 1188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  403 RREKFLKKETIR-AEKMRQKEEMRKEKEVARLKAANERAIARKI---------AKESMELIEDERLELMEVAALTKGLPS 472
Cdd:PTZ00121  1189 KAEELRKAEDARkAEAARKAEEERKAEEARKAEDAKKAEAVKKAeeakkdaeeAKKAEEERNNEEIRKFEEARMAHFARR 1268

                          170
                   ....*....|....*.
gi 1063736012  473 MLALDFETLQNLDEYR 488
Cdd:PTZ00121  1269 QAAIKAEEARKADELK 1284
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 899-941 3.05e-05

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 42.87  E-value: 3.05e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1063736012  899 GEQWVQGLVEGDYSNLSSEERLNALVALIGIATEGNTIRIALE 941
Cdd:pfam15612    4 LPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 309-459 5.66e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.22  E-value: 5.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  309 EREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKreEQIRKEMERQDRERRKEEERLLREKQR 388
Cdd:pfam13868   50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER--EQMDEIVERIQEEDQAEAEEKLEKQRQ 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  389 ---------EEERYLKEQMRELQRRE-----KFLK-KETIRAEKMRQKEEMR--KEKEVARLKAANERAIARKIAKESM- 450
Cdd:pfam13868  128 lreeidefnEEQAEWKELEKEEEREEderilEYLKeKAEREEEREAEREEIEeeKEREIARLRAQQEKAQDEKAERDELr 207

                          170
                   ....*....|
gi 1063736012  451 -ELIEDERLE 459
Cdd:pfam13868  208 aKLYQEEQER 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-486 6.57e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  309 EREVGNEDEDDDALQLERHRKnEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEME-RQDRERRKEEERLLREKQ 387
Cdd:COG1196    324 ELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQL 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  388 REEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALT 467
Cdd:COG1196    403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                          170
                   ....*....|....*....
gi 1063736012  468 KGLPSMLALDFETLQNLDE 486
Cdd:COG1196    483 LEELAEAAARLLLLLEAEA 501
PTZ00121 PTZ00121
MAEBL; Provisional
 306-448 6.60e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 6.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  306 VKSEREVGNEDEDDdalqlerhRKNEEARIAREVE--AHEKRIRRELEKQ--DMLRRKREEQIRKEMERQDRERRKEEER 381
Cdd:PTZ00121  1661 IKAAEEAKKAEEDK--------KKAEEAKKAEEDEkkAAEALKKEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKA 1732

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063736012  382 LLREKQREEERYLKEQMRELQRREKflKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKE 448
Cdd:PTZ00121  1733 EEAKKEAEEDKKKAEEAKKDEEEKK--KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-486 8.12e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 8.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEeRLLREKQREEERY- 393
Cdd:COG1196    319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-LAEELLEALRAAAe 397

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  394 LKEQMRELQRREKFLKKETIRAEkmRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTKGLPSM 473
Cdd:COG1196    398 LAAQLEELEEAEEALLERLERLE--EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                          170
                   ....*....|...
gi 1063736012  474 LALDFETLQNLDE 486
Cdd:COG1196    476 EAALAELLEELAE 488
PTZ00121 PTZ00121
MAEBL; Provisional
 325-503 8.64e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 8.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRRKREEQIRK--EMERQDRERRKEEERLLREKQREEERYLKEQMRE 400
Cdd:PTZ00121  1422 EAKKKAEEKKKADEAKkkAEEAKKADEAKKKAEEAKKAEEAKKKaeEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  401 LQRREKFLKK--ETIRAEKMRQKEEMRKEKEVAR---LKAANERAIARKIaKESMELIEDERLELMEVAALTKGLPSMLA 475
Cdd:PTZ00121  1502 AKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADEL-KKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580

                          170       180
                   ....*....|....*....|....*...
gi 1063736012  476 LDFETLQNLDEYRDKQAIFPPTSVKLKK 503
Cdd:PTZ00121  1581 RKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-466 8.99e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 8.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  309 EREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR 388
Cdd:COG1196    259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  389 EEEryLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAAnERAIARKIAKESMELIEDERLELMEVAAL 466
Cdd:COG1196    339 LEE--LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALL 413
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 307-435 9.08e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 44.68  E-value: 9.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  307 KSEREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEkqdmlRRKREEQIRKEMERQDrerrkeeerllREK 386
Cdd:pfam11600   13 KEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEAR-----RKKEEEKELKEKERRE-----------KKE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1063736012  387 QREEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKA 435
Cdd:pfam11600   77 KDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKA 125
PRK12704 PRK12704
phosphodiesterase; Provisional
 329-451 9.26e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 9.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  329 KNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDrerrkeeerllrekqrEEERYLKEQMRELQRREKFL 408
Cdd:PRK12704    63 KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE----------------KREEELEKKEKELEQKQQEL 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1063736012  409 KKETIRAEKMRQKEEMRKEkEVARLKAANeraiARKIAKESME 451
Cdd:PRK12704   127 EKKEEELEELIEEQLQELE-RISGLTAEE----AKEILLEKVE 164
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 321-474 1.39e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 46.18  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  321 ALQLERHRKNEEARIAREVEAHEkriRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQ--- 397
Cdd:pfam15558   11 ALMLARHKEEQRMRELQQQAALA---WEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRrek 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  398 ---MRELQRREKFLKKETIRAEKM---RQKEEMRKEKEVARLKAANEraiARKIAKESMELIEDERLelmEVAALTKGLP 471
Cdd:pfam15558   88 qviEKESRWREQAEDQENQRQEKLeraRQEAEQRKQCQEQRLKEKEE---ELQALREQNSLQLQERL---EEACHKRQLK 161


                   ...
gi 1063736012  472 SML 474
Cdd:pfam15558  162 ERE 164
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 314-464 2.47e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 44.31  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  314 NEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRElEKQDMLRRKREEQIRKEMERQdrerrkeeerllrekQREEERY 393
Cdd:pfam13904   34 QSSSLTYARKLEGLKLERQPLEAYENWLAAKQRQRQ-KELQAQKEEREKEEQEAELRK---------------RLAKEKY 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  394 L-----KEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVAR----------LKAANERAIARKIAKESMELIEDERL 458
Cdd:pfam13904   98 QewlqrKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKevlqewerkkLEQQQRKREEEQREQLKKEEEEQERK 177


                   ....*.
gi 1063736012  459 ELMEVA 464
Cdd:pfam13904  178 QLAEKA 183
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 347-448 2.78e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 42.17  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  347 RRELEK-QDMLRRKREEqIRKEMERQDrerrkeeerllrekQREEERYLKEQM--RELQRREKFLK---KETIRAEKMRQ 420
Cdd:pfam13863    5 KREMFLvQLALDAKREE-IERLEELLK--------------QREEELEKKEQElkEDLIKFDKFLKendAKRRRALKKAE 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1063736012  421 KEE---MRKEKEVARLKAANERAIARKIAKE 448
Cdd:pfam13863   70 EETklkKEKEKEIKKLTAQIEELKSEISKLE 100
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 331-462 2.88e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  331 EEARIAREVEAHEKRIRRELEKQdmlrRKREEQIRKEMERQdrerrkeeerllREKQREEERY-LKEQMRElQRREKFLK 409
Cdd:pfam13868   30 EKKRIKAEEKEEERRLDEMMEEE----RERALEEEEEKEEE------------RKEERKRYRQeLEEQIEE-REQKRQEE 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063736012  410 KETIRAEKMRQKEEMRKEKEvARLKAANERAIARKIAKESMELIEDERLELME 462
Cdd:pfam13868   93 YEEKLQEREQMDEIVERIQE-EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 333-459 2.96e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.11  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  333 ARIAREVEAheKRIRRELEKQDMLRRKREEQIRKEMErqdrerrkeeerllrekqrEEERYLKEQMR-----ELQRREkf 407
Cdd:pfam05672    4 AGTTDAEEA--ARILAEKRRQAREQREREEQERLEKE-------------------EEERLRKEELRrraeeERARRE-- 60

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1063736012  408 lkketirAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:pfam05672   61 -------EEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEE 105
PRK12704 PRK12704
phosphodiesterase; Provisional
 331-468 3.07e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  331 EEARiaREVEAHEKRIrrELEKQDMLRRKREEqirkeMERQDrerrkeeerllrekqREEERYLKEQMRELQRREKFLKK 410
Cdd:PRK12704    45 EEAK--KEAEAIKKEA--LLEAKEEIHKLRNE-----FEKEL---------------RERRNELQKLEKRLLQKEENLDR 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  411 ETIRAEKMRQKEEMRKEKEVARLKAANERaiarkiAKESMELIEDERLELMEVAALTK 468
Cdd:PRK12704   101 KLELLEKREEELEKKEKELEQKQQELEKK------EEELEELIEEQLQELERISGLTA 152
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-468 3.14e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  309 EREVGNEDEDDDALQLERHRKNEEARIA-REVEAHEKRIRRELEK-QDMLRRKREEQIRKEMERQDRERRKEEERLLREK 386
Cdd:COG1196    266 EAELEELRLELEELELELEEAQAEEYELlAELARLEQDIARLEERrRELEERLEELEEELAELEEELEELEEELEELEEE 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  387 QREEERYLKE-QMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERA-IARKIAKESMELIEDERLELMEVA 464
Cdd:COG1196    346 LEEAEEELEEaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqLEELEEAEEALLERLERLEEELEE 425


                   ....
gi 1063736012  465 ALTK 468
Cdd:COG1196    426 LEEA 429
PTZ00121 PTZ00121
MAEBL; Provisional
 325-462 4.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 4.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRrKREEQIRKEMERQDRERRKEEERLLREKQR--EEERYLKEQMRE 400
Cdd:PTZ00121  1494 EAKKKADEAKKAAEAKkkADEAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKA 1572

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063736012  401 LQRREKFLKketiRAEKMRQKEEMRKEkEVARLKAANERAIARKIAKESMELIEDERLELME 462
Cdd:PTZ00121  1573 EEDKNMALR----KAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
PTZ00121 PTZ00121
MAEBL; Provisional
 306-448 4.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  306 VKSEREVGNEDEDDDALQLERH----RKNEEARIAR------EVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDrer 375
Cdd:PTZ00121  1229 VKKAEEAKKDAEEAKKAEEERNneeiRKFEEARMAHfarrqaAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD--- 1305

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063736012  376 rkEEERLLREKQREEEryLKEQMRELQRREKFLKKetiRAEKMRQKEEMRKEKEVA---RLKAANERAIARKIAKE 448
Cdd:PTZ00121  1306 --EAKKKAEEAKKADE--AKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAaadEAEAAEEKAEAAEKKKE 1374
PTZ00491 PTZ00491
major vault protein; Provisional
 329-469 5.60e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 44.62  E-value: 5.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  329 KNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRK---EMERQDRERRKEEERLLREKQREEERYLKEQmRELQRRE 405
Cdd:PTZ00491   662 KSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTkllELQAESAAVESSGQSRAEALAEAEARLIEAE-AEVEQAE 740

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  406 KFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARkiAKESMElIEDERLELMeVAALTKG 469
Cdd:PTZ00491   741 LRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAK--AKELAD-IEATKFERI-VEALGRE 800
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 336-452 6.60e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  336 AREVEAHEKRIRRELEKQdmlRRKREEQIRKEMERQDrerrkeeerllrekqREEERYLKEQMRELQRREKfLKKETIRA 415
Cdd:cd16269    195 EKEKEIEAERAKAEAAEQ---ERKLLEEQQRELEQKL---------------EDQERSYEEHLRQLKEKME-EERENLLK 255

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1063736012  416 EKMRQKEEMRKEKEvaRLKAANERAIARKIAKESMEL 452
Cdd:cd16269    256 EQERALESKLKEQE--ALLEEGFKEQAELLQEEIRSL 290
PTZ00121 PTZ00121
MAEBL; Provisional
 307-457 6.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  307 KSEREVGNEDEDDDALQLERHRKNEEARIAREVEAHEK-----RIRRELEKQDMLRRKREEQIRK--EMERQDRERRKEE 379
Cdd:PTZ00121  1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKAD 1421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  380 ERLLREKQREEERYLKEQMRELQRREKFLKK--ETIRAEKMRQKEEMRKEKEVARLKAANERAI--ARKIAKESMELIED 455
Cdd:PTZ00121  1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeAKKKAEEAKKKADE 1501


                   ..
gi 1063736012  456 ER 457
Cdd:PTZ00121  1502 AK 1503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-459 6.95e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRR--KREEQIRKEMER-QDRERRKEEERLLREKQREEE 391
Cdd:COG1196    361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERlEEELEELEEALAELEEEEEEE 440

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  392 RYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PTZ00121 PTZ00121
MAEBL; Provisional
 319-444 7.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 7.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  319 DDALQLERHRKNEEAR---IAREVE----AHEKRIRRELEKQDMLRR----KREEQIRK--EMERQDRERRKEEERLLRE 385
Cdd:PTZ00121  1137 EDARKAEEARKAEDAKrveIARKAEdarkAEEARKAEDAKKAEAARKaeevRKAEELRKaeDARKAEAARKAEEERKAEE 1216

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  386 KQREEERYLKEQMRELQRREKfLKKETIRAEKMRQKEEMRKEKEV-----ARLKAANERAIARK 444
Cdd:PTZ00121  1217 ARKAEDAKKAEAVKKAEEAKK-DAEEAKKAEEERNNEEIRKFEEArmahfARRQAAIKAEEARK 1279
PTZ00121 PTZ00121
MAEBL; Provisional
 306-457 8.44e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 8.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  306 VKSEREVGNEDEDDDALQL----ERHRKNEEARIAREVE--AHE--------KRIRRELEKQDMLRRKREEQIRKEMERQ 371
Cdd:PTZ00121  1283 LKKAEEKKKADEAKKAEEKkkadEAKKKAEEAKKADEAKkkAEEakkkadaaKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  372 DRERRKEEERLLREKQREEEryLKEQMRELQRREKFLKKetirAEKMRQKEEMRKEKEVARLKA--ANERAIARKIAKES 449
Cdd:PTZ00121  1363 EEKAEAAEKKKEEAKKKADA--AKKKAEEKKKADEAKKK----AEEDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEA 1436


                   ....*...
gi 1063736012  450 MELIEDER 457
Cdd:PTZ00121  1437 KKKAEEAK 1444
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 347-440 9.08e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.79  E-value: 9.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  347 RRELEK--QDMLRRKREEQIRKEMERQdRERRKEEERLLREKQREEERYLKEQMRELQRR--EKFLKKETIRAEKMRQKE 422
Cdd:pfam15709  327 KREQEKasRDRLRAERAEMRRLEVERK-RREQEEQRRLQQEQLERAEKMREELELEQQRRfeEIRLRKQRLEEERQRQEE 405

                           90
                   ....*....|....*...
gi 1063736012  423 EMRKEKevARLKAANERA 440
Cdd:pfam15709  406 EERKQR--LQLQAAQERA 421
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 305-462 1.06e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  305 FVKSEREVGNEDEDDdalqlERHRKNEEARIAREVEAHEKrIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLR 384
Cdd:pfam02463  659 AEKSEVKASLSELTK-----ELLEIQELQEKAESELAKEE-ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD 732

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063736012  385 EKQREEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESmeLIEDERLELME 462
Cdd:pfam02463  733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK--AQEEELRALEE 808
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
311-469 1.09e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  311 EVGNEDEDDDALQLERHRKNEEARiaREVEAHEKRIRREL-EKQDMLRRKREEQIRKEMERQDRERRKEeerllrekqRE 389
Cdd:COG4717    378 EAGVEDEEELRAALEQAEEYQELK--EELEELEEQLEELLgELEELLEALDEEELEEELEELEEELEEL---------EE 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  390 EERYLKEQMRELQRREKFLKKETiRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERL-ELME-----V 463
Cdd:COG4717    447 ELEELREELAELEAELEQLEEDG-ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLEraseyF 525


                   ....*.
gi 1063736012  464 AALTKG 469
Cdd:COG4717    526 SRLTDG 531
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-411 1.45e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  307 KSEREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREK 386
Cdd:COG1196    671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750

                           90       100
                   ....*....|....*....|....*
gi 1063736012  387 QREEERYLKEQMRELQRREKFLKKE 411
Cdd:COG1196    751 EALEELPEPPDLEELERELERLERE 775
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 325-492 1.50e-03

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: 43.52  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVEAHEKRIRREL---EKQDMLRRKREEQIRKEMERQdreRRKEEERLLREKQREEERYlKEQMREL 401
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYlekEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEEL-EAALRDL 880

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  402 QRREKFLKKETIRAEKmrQKEEMRKEKEVARLKA------ANERAIARKIAKESMELIEDERLELMEVAALTKGLP---- 471
Cdd:TIGR02169  881 ESRLGDLKKERDELEA--QLRELERKIEELEAQIekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdvqa 958

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1063736012  472 ---------------SMLALD--FETLQNLDEYRDKQA 492
Cdd:TIGR02169  959 elqrveeeiralepvNMLAIQeyEEVLKRLDELKEKRA 996
PTZ00121 PTZ00121
MAEBL; Provisional
 319-457 1.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  319 DDALQLERHRKNEEARIAREV--------EAHEKRIRRELEKQ-DMLRRKREEQIRK--EMERQDRERRKEEERLLREKQ 387
Cdd:PTZ00121  1281 DELKKAEEKKKADEAKKAEEKkkadeakkKAEEAKKADEAKKKaEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAE 1360

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  388 REEErylKEQMRELQRREKFLKKETI--RAEKMRQKEEMRKEKEVARLKA--ANERAIARKIAKESMELIEDER 457
Cdd:PTZ00121  1361 AAEE---KAEAAEKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKK 1431
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 339-452 1.68e-03

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 42.67  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  339 VEAHEKRIRR--ELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQMRElQRREKFLKKETIRAE 416
Cdd:pfam07767  194 FEDHQELLQKavEAEKKRLKEEEKLERVLEKIAESAATAEAREEKRKTKAQRNKEKRRKEEERE-AKEEKALKKKLAQLE 272

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1063736012  417 KMRQ--KEEMRKEKEVARLKAANERAiARKIAKESMEL 452
Cdd:pfam07767  273 RLKEiaKEIAEKEKEREEKAEARKRE-KRKKKKEEKKL 309
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 296-492 1.69e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  296 TAAQVHDDPFvksEREVGNEDEDDDALQLERHRKNEEARIAREveaHEKRI--------------RRELEKQDMlRRKRE 361
Cdd:pfam15921  359 TEARTERDQF---SQESGNLDDQLQKLLADLHKREKELSLEKE---QNKRLwdrdtgnsitidhlRRELDDRNM-EVQRL 431

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  362 EQIRKEMERQdrerrkeeerllreKQREEERylkeQMRELQRREKFLKK-ETIRAEKMRQKEEMRKEKEVARLKAANERA 440
Cdd:pfam15921  432 EALLKAMKSE--------------CQGQMER----QMAAIQGKNESLEKvSSLTAQLESTKEMLRKVVEELTAKKMTLES 493

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063736012  441 IARKIAKESMELIEDERLELMEVAALTKgLPSMLALDFETLQNL----DEYRDKQA 492
Cdd:pfam15921  494 SERTVSDLTASLQEKERAIEATNAEITK-LRSRVDLKLQELQHLknegDHLRNVQT 548
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 307-448 1.72e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.02  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  307 KSEREVGNEDEdddaLQLERHRKNEEARIaREVEAHEKRIRRELEK----------QDMLRRKREEQIRKEMERQDRERR 376
Cdd:pfam15709  367 QLERAEKMREE----LELEQQRRFEEIRL-RKQRLEEERQRQEEEErkqrlqlqaaQERARQQQEEFRRKLQELQRKKQQ 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  377 KEEERLLREKQREEEryLKEQMRELQRREKFLKKETiRAEKMRQK--EEMR----------KEKEVARLKAANERAIARK 444
Cdd:pfam15709  442 EEAERAEAEKQRQKE--LEMQLAEEQKRLMEMAEEE-RLEYQRQKqeAEEKarleaeerrqKEEEAARLALEEAMKQAQE 518


                   ....
gi 1063736012  445 IAKE 448
Cdd:pfam15709  519 QARQ 522
PTZ00121 PTZ00121
MAEBL; Provisional
 306-459 1.96e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  306 VKSEREVGNEDEDDDALQLERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRRKREEQIRKEMERQdrERRKEEERLL 383
Cdd:PTZ00121  1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAK--KAEEAKKKAE 1467

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063736012  384 REKQREEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:PTZ00121  1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 325-448 2.86e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  325 ERHRKNEEARIAREVE----AHEKRIRR-ELEKQDMLRRKREEQIRKEMERQdrerrkEEERLLREKQREEERYLK-EQM 398
Cdd:TIGR02794   66 EQERQKKLEQQAEEAEkqraAEQARQKElEQRAAAEKAAKQAEQAAKQAEEK------QKQAEEAKAKQAAEAKAKaEAE 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1063736012  399 RELQRREKFLKKETIRAEKMRQkEEMRKEKEVARLKAANErAIARKIAKE 448
Cdd:TIGR02794  140 AERKAKEEAAKQAEEEAKAKAA-AEAKKKAEEAKKKAEAE-AKAKAEAEA 187
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 320-434 2.89e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 40.16  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  320 DALQLE----RHRKNEEARIAREVEAHEKRIRRELEKQdmlRRKREEQIRKEMERqdrerrkeeerllREKQREEERYLK 395
Cdd:pfam15236   40 DPAQLEererKRQKALEHQNAIKKQLEEKERQKKLEEE---RRRQEEQEEEERLR-------------REREEEQKQFEE 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1063736012  396 EQMRELQRREKFLKKETIRAEKMRQKEEM-RKEKEVARLK 434
Cdd:pfam15236  104 ERRKQKEKEEAMTRKTQALLQAMQKAQELaQRLKQEQRIR 143
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 346-462 4.14e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 41.93  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  346 IRRELEKQDmLRRKREEQIRKEMERQdrerrkeeerllrekQREeeRYLKEQMRELQrrekflkKEtiraekMRQKEEmr 425
Cdd:COG0466    203 LEKEIEVLE-LEKKIRSRVKEQMEKS---------------QRE--YYLREQLKAIQ-------KE------LGEKDD-- 249

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1063736012  426 KEKEVARLKaanERAIARKIAKESMELIEDE--RLELME 462
Cdd:COG0466    250 GEDEIEELR---EKIEKAKLPEEVKEKAEKElkKLERMP 285
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 315-447 5.28e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  315 EDEDDDALQLERHR--KNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQI-----RKEMERQDRERRKEEERLLREKQ 387
Cdd:pfam13868  194 EKAQDEKAERDELRakLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIelkerRLAEEAEREEEEFERMLRKQAED 273

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063736012  388 REEERYLKEQMRELQ--------------RREKFLKKETIRAEKMRQKEEMRKEKEVArlkaanERAIARKIAK 447
Cdd:pfam13868  274 EEIEQEEAEKRRMKRlehrrelekqieerEEQRAAEREEELEEGERLREEEAERRERI------EEERQKKLKE 341
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
310-486 5.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  310 REVGNEDEDDDALQLERhrKNEEARIARE----VEAHEKRIRRELEKQDMLRRKREEQIRK----EMERQDRERRKEEER 381
Cdd:PRK03918   506 KELEEKLKKYNLEELEK--KAEEYEKLKEklikLKGEIKSLKKELEKLEELKKKLAELEKKldelEEELAELLKELEELG 583

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  382 LLREKQREEE---------RY--LKEQMRELQRREKFLKKETIRAEKMRqKEEMRKEKEVARLKAANErAIARKIAKESM 450
Cdd:PRK03918   584 FESVEELEERlkelepfynEYleLKDAEKELEREEKELKKLEEELDKAF-EELAETEKRLEELRKELE-ELEKKYSEEEY 661

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1063736012  451 ELIEDERLEL-MEVAALTKGLPSMLALDFETLQNLDE 486
Cdd:PRK03918   662 EELREEYLELsRELAGLRAELEELEKRREEIKKTLEK 698
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 320-456 7.09e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  320 DALQLERHRKNEEARIARE----VEAHEKRIRrELEKQdmlrRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLK 395
Cdd:PRK09510    73 SAKRAEEQRKKKEQQQAEElqqkQAAEQERLK-QLEKE----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063736012  396 EQMRELQRREKFLKKetIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDE 456
Cdd:PRK09510   148 KAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE 206
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 351-452 8.07e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 40.35  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063736012  351 EKQDMLRRKREEQIRKEMERQdrerrkeeerllREKQREEERYLKEQMRELQRREKFLKK--ETIRAEKMRQKEEM--RK 426
Cdd:pfam02841  203 EKAIEAERAKAEAAEAEQELL------------REKQKEEEQMMEAQERSYQEHVKQLIEkmEAEREQLLAEQERMleHK 270

                           90       100
                   ....*....|....*....|....*.
gi 1063736012  427 EKEVARLKAANERAIARKIAKESMEL 452
Cdd:pfam02841  271 LQEQEELLKEGFKTEAESLQKEIQDL 296
 
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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