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Conserved domains on  [gi|334188190|ref|NP_001190470|]
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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
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 515-570 1.34e-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: 83.71  E-value: 1.34e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   515 ENVANLLMVWRFLITFADVLGLWPFTLDEFAQAFHDYDP--RLMGEIHIVLLKTIIKD 570
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEEpsELLDEIHCALLKALVRD 58
Homeodomain pfam00046
Homeodomain;
18-74 2.39e-17

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.16  E-value: 2.39e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188190    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 4.75e-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: 71.18  E-value: 4.75e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188190   696 GTVKFAAFHVLSLEGeKGLNILEVAEKIQKSGLRDlTTSRTPEASVAAALSRDTK---LFERVAPSTYCVRAS 765
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRSW 71
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1071-1138 2.58e-13

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: 66.02  E-value: 2.58e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334188190  1071 YRSLPLGQDRRRNRYWRFsasasrnDPGCGRIFVELQ-DGRWRLIDSEE------ASLPPEGL-EAFWTENLRKSW 1138
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVESPsDGEWGVYSSKEqldaliASLNPRGVrESALKEALEKIK 69
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 322-457 1.16e-09

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: 63.22  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   322 LQLERHRKNEeaRIAREVEAHEKRIRRELEKQDMLRRKREE--QIRKEMERqdrerrkeeerllrEKQREEERYLKEQMR 399
Cdd:pfam17380  383 LQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEmeQIRAEQEE--------------ARQREVRRLEEERAR 446

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   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 2.49e-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: 2.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 334188190   899 GEQWVQGLVEGDYSNLSSEERLNALVALIGIATEGNTIRIALE 941
Cdd:pfam15612    4 LPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
 
Name Accession Description Interval E-value
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 515-570 1.34e-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: 83.71  E-value: 1.34e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   515 ENVANLLMVWRFLITFADVLGLWPFTLDEFAQAFHDYDP--RLMGEIHIVLLKTIIKD 570
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEEpsELLDEIHCALLKALVRD 58
DDT smart00571
domain in different transcription and chromosome remodeling factors;
514-572 1.97e-17

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 77.67  E-value: 1.97e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334188190    514 DENVANLLMVWRFLITFADVLGLWPF--TLDEFAQAFHDYDPR-LMGEIHIVLLKTIIKDIE 572
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSPFraTLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEG 62
Homeodomain pfam00046
Homeodomain;
18-74 2.39e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.16  E-value: 2.39e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188190    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 4.75e-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: 71.18  E-value: 4.75e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188190   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 2.38e-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: 66.11  E-value: 2.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   18 KSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERKS 75
Cdd:cd00086     1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1071-1138 2.58e-13

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: 66.02  E-value: 2.58e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334188190  1071 YRSLPLGQDRRRNRYWRFsasasrnDPGCGRIFVELQ-DGRWRLIDSEE------ASLPPEGL-EAFWTENLRKSW 1138
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVESPsDGEWGVYSSKEqldaliASLNPRGVrESALKEALEKIK 69
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 17-73 9.80e-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: 64.19  E-value: 9.80e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188190     17 SKSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKER 73
Cdd:smart00389    1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
16-83 5.88e-12

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 65.15  E-value: 5.88e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   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 1.16e-09

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: 63.22  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   322 LQLERHRKNEeaRIAREVEAHEKRIRRELEKQDMLRRKREE--QIRKEMERqdrerrkeeerllrEKQREEERYLKEQMR 399
Cdd:pfam17380  383 LQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEmeQIRAEQEE--------------ARQREVRRLEEERAR 446

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   400 ELQR-REKFLKKETiRAEKMRQKEEMRKEKEVARLKAANERAIA----RKIAKESME-----LIEDER 457
Cdd:pfam17380  447 EMERvRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAeeqrRKILEKELEerkqaMIEEER 513
PTZ00121 PTZ00121
MAEBL; Provisional
 319-468 1.86e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  319 DDALQLERHRKNEEARIAREV-EAHEKR----IRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR----E 389
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELkKAEEKKkaeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaE 1616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  390 EERYLKEQMR-ELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTK 468
Cdd:PTZ00121 1617 EAKIKAEELKkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-492 1.29e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  308 SEREVGNEDEDDDALQLERhRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQirKEMERQDRERRKEEERLLREKQ 387
Cdd:COG1196   302 QDIARLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  388 REEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALT 467
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                         170       180
                  ....*....|....*....|....*.
gi 334188190  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 2.49e-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: 2.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 334188190   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 8.05e-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: 43.33  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  336 AREVEAHEKRIRRELEKQdmlRRKREEQIRKEMERQDrerrkeeerllrekqREEERYLKEQMRELQRREKfLKKETIRA 415
Cdd:cd16269   195 EKEKEIEAERAKAEAAEQ---ERKLLEEQQRELEQKL---------------EDQERSYEEHLRQLKEKME-EERENLLK 255

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 334188190  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 2.63e-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: 42.36  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   325 ERHRKNEEARIAREVEAHEKRIRREL---EKQDMLRRKREEQIRKEMERQdreRRKEEERLLREKQREEERYlKEQMREL 401
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYlekEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEEL-EAALRDL 880

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   402 QRREKFLKKETIRAEKmrQKEEMRKEKEVARLKA------ANERAIARKIAKESMELIEDERLELMEVAALTKGLP---- 471
Cdd:TIGR02169  881 ESRLGDLKKERDELEA--QLRELERKIEELEAQIekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdvqa 958

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 334188190   472 ---------------SMLALD--FETLQNLDEYRDKQA 492
Cdd:TIGR02169  959 elqrveeeiralepvNMLAIQeyEEVLKRLDELKEKRA 996
 
Name Accession Description Interval E-value
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 515-570 1.34e-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: 83.71  E-value: 1.34e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   515 ENVANLLMVWRFLITFADVLGLWPFTLDEFAQAFHDYDP--RLMGEIHIVLLKTIIKD 570
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEEpsELLDEIHCALLKALVRD 58
DDT smart00571
domain in different transcription and chromosome remodeling factors;
514-572 1.97e-17

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 77.67  E-value: 1.97e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334188190    514 DENVANLLMVWRFLITFADVLGLWPF--TLDEFAQAFHDYDPR-LMGEIHIVLLKTIIKDIE 572
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSPFraTLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEG 62
Homeodomain pfam00046
Homeodomain;
18-74 2.39e-17

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 77.16  E-value: 2.39e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188190    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 4.75e-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: 71.18  E-value: 4.75e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188190   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 2.38e-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: 66.11  E-value: 2.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   18 KSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKERKS 75
Cdd:cd00086     1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1071-1138 2.58e-13

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: 66.02  E-value: 2.58e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334188190  1071 YRSLPLGQDRRRNRYWRFsasasrnDPGCGRIFVELQ-DGRWRLIDSEE------ASLPPEGL-EAFWTENLRKSW 1138
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVESPsDGEWGVYSSKEqldaliASLNPRGVrESALKEALEKIK 69
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 17-73 9.80e-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: 64.19  E-value: 9.80e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188190     17 SKSKRKMKTAAQLEVLENTYSAEPYPSEAIRADLSVKLNLSDRQLQMWFCHRRLKER 73
Cdd:smart00389    1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
16-83 5.88e-12

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 65.15  E-value: 5.88e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   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 1.16e-09

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: 63.22  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   322 LQLERHRKNEeaRIAREVEAHEKRIRRELEKQDMLRRKREE--QIRKEMERqdrerrkeeerllrEKQREEERYLKEQMR 399
Cdd:pfam17380  383 LQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEmeQIRAEQEE--------------ARQREVRRLEEERAR 446

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   400 ELQR-REKFLKKETiRAEKMRQKEEMRKEKEVARLKAANERAIA----RKIAKESME-----LIEDER 457
Cdd:pfam17380  447 EMERvRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAeeqrRKILEKELEerkqaMIEEER 513
PTZ00121 PTZ00121
MAEBL; Provisional
 319-468 1.86e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  319 DDALQLERHRKNEEARIAREV-EAHEKR----IRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR----E 389
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELkKAEEKKkaeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaE 1616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  390 EERYLKEQMR-ELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTK 468
Cdd:PTZ00121 1617 EAKIKAEELKkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 289-462 4.60e-09

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: 61.29  E-value: 4.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   289 YQKSYMDTAAQvhdDPFVKSEREVGNEDEDDDALQLERHRKNEEARIAREVE--------AHEKRIRRELEKQdmLRRKR 360
Cdd:pfam17380  280 HQKAVSERQQQ---EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmdrqaaiyAEQERMAMERERE--LERIR 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   361 EEQIRKEMER---QDRERRKEEERLLREKQREEERYLKEQMRELQ--RREKFLKKETIRA--EKMRQKEEMRKEKEVARL 433
Cdd:pfam17380  355 QEERKRELERirqEEIAMEISRMRELERLQMERQQKNERVRQELEaaRKVKILEEERQRKiqQQKVEMEQIRAEQEEARQ 434

                          170       180
                   ....*....|....*....|....*....
gi 334188190   434 KAANERAIARKIAKESMELIEDERLELME 462
Cdd:pfam17380  435 REVRRLEEERAREMERVRLEEQERQQQVE 463
PTZ00121 PTZ00121
MAEBL; Provisional
 307-451 6.38e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 6.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  307 KSEREVGNEDE---DDDALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKRE----EQIRKEMERQDRERRKE 378
Cdd:PTZ00121 1504 KAAEAKKKADEakkAEEAKKADEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEkkkaEEAKKAEEDKNMALRKA 1583

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334188190  379 EERLLREKQREEERYLKEQMRELQRREKFLKKET--IRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESME 451
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
PTZ00121 PTZ00121
MAEBL; Provisional
 307-456 5.51e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  307 KSEREVGNEDEDDDALQLERHRKNEEARI-AREV--EAHEKRIRRELEKQDMLRRKREEQIRKEMER------QDRERRK 377
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIkAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaEEAKKAE 1671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  378 EEERLLREKQREEERYLKEQMRELQRREKFLKKETIR---AEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIE 454
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751


                  ..
gi 334188190  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 9.27e-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: 52.61  E-value: 9.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   323 QLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeerllrEKQREEERylkEQMRELQ 402
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ-------------IEEREQKR---QEEYEEK 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   403 RREKFLKKETIRAEKM-RQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELM 461
Cdd:pfam13868   97 LQEREQMDEIVERIQEeDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER 156
PTZ00121 PTZ00121
MAEBL; Provisional
 319-457 1.19e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  319 DDALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQ 397
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  398 MRELQrrekflkkETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDER 457
Cdd:PTZ00121 1277 ARKAD--------ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-492 1.29e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  308 SEREVGNEDEDDDALQLERhRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQirKEMERQDRERRKEEERLLREKQ 387
Cdd:COG1196   302 QDIARLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  388 REEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALT 467
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                         170       180
                  ....*....|....*....|....*.
gi 334188190  468 KGL-PSMLALDFETLQNLDEYRDKQA 492
Cdd:COG1196   459 EALlELLAELLEEAALLEAALAELLE 484
PTZ00121 PTZ00121
MAEBL; Provisional
 295-451 1.67e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  295 DTAAQVHDDPFVKSEREVGNEDEDDDALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKREEQIRKEMER-QD 372
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKaED 1222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  373 RERRKEEERLLREKQREEERYLKEQMRELQRREKF---------LKKETIRAEKMRQKEEMRKEKEVAR---LKAANERA 440
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFeearmahfaRRQAAIKAEEARKADELKKAEEKKKadeAKKAEEKK 1302

                         170
                  ....*....|.
gi 334188190  441 IARKIAKESME 451
Cdd:PTZ00121 1303 KADEAKKKAEE 1313
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 320-462 2.00e-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: 51.84  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   320 DALQLERHR-KNEEARIAREVEAHEKRIRRELEkqdmLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQM 398
Cdd:pfam13868  204 DELRAKLYQeEQERKERQKEREEAEKKARQRQE----LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE 279

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188190   399 RELQRREkflKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELME 462
Cdd:pfam13868  280 EAEKRRM---KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
PTZ00121 PTZ00121
MAEBL; Provisional
 309-451 5.20e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  309 EREVGNEDEDDDALQLERHRKNEEARIAREVEAHE--KRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREK 386
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEeeKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334188190  387 QREEERYLKEQMR----ELQRREKFLKKetiRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESME 451
Cdd:PTZ00121 1648 KAEELKKAEEENKikaaEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 315-468 6.76e-06

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: 47.76  E-value: 6.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRElEKQDMLRRKREEQIRKemerqdrerrkeeerllrekqREEERYL 394
Cdd:pfam11600    9 SQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKE-EAKAEKERAKEEARRK---------------------KEEEKEL 66

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188190   395 KEQmrelQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERaiaRKiAKESMELIEDERLELMEVAALTK 468
Cdd:pfam11600   67 KEK----ERREKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEK---RK-KEEEKRLKEEEKRIKAEKAEITR 132
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 323-470 1.13e-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: 49.15  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   323 QLERHRKNEEARI-AREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYL------- 394
Cdd:pfam13868   86 EQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeylkeka 165

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334188190   395 -KEQMRELQRREKFLKKETIRAeKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTKGL 470
Cdd:pfam13868  166 eREEEREAEREEIEEEKEREIA-RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241
PTZ00121 PTZ00121
MAEBL; Provisional
 325-490 1.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  325 ERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeeRLLREKQREEERYLKEQMR--E 400
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---------KKADEAKKAEEAKKADEAKkaE 1531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  401 LQRREKFLKK--ETIRAEKMRQKEEMRKEKEVARL---KAANERAIARKIAKESMELIEDERLElmEVAALTKGLPSMLA 475
Cdd:PTZ00121 1532 EAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAeeaKKAEEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKA 1609

                         170
                  ....*....|....*
gi 334188190  476 ldfETLQNLDEYRDK 490
Cdd:PTZ00121 1610 ---EEAKKAEEAKIK 1621
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 323-490 1.37e-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: 49.15  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   323 QLERHRKNEEARIAREVEAHEKRIRRELEK-------QDMLRRKR--EEQIRKEMER-QDRERRKEEERLLREKQREEER 392
Cdd:pfam13868  166 EREEEREAEREEIEEEKEREIARLRAQQEKaqdekaeRDELRAKLyqEEQERKERQKeREEAEKKARQRQELQQAREEQI 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   393 YLKEQMRELQRREKflkketiRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIED-ERLELMEVAAltkglp 471
Cdd:pfam13868  246 ELKERRLAEEAERE-------EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEErEEQRAAEREE------ 312

                          170
                   ....*....|....*....
gi 334188190   472 smLALDFETLQNLDEYRDK 490
Cdd:pfam13868  313 --ELEEGERLREEEAERRE 329
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 309-509 1.40e-05

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: 49.74  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   309 EREVGNEDEDDDALQLERHRKNEearIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMErqdrerrkeeerllrekQR 388
Cdd:pfam17380  441 EEERAREMERVRLEEQERQQQVE---RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE-----------------KE 500

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   389 EEERylKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKaANERAIARKIAKESMELIEDE-RLELMEvaalt 467
Cdd:pfam17380  501 LEER--KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK-QQEMEERRRIQEQMRKATEERsRLEAME----- 572

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 334188190   468 kglpsmlaLDFETLQNLDEYRDKQAIFPPTSvklkKPFAVKP 509
Cdd:pfam17380  573 --------REREMMRQIVESEKARAEYEATT----PITTIKP 602
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 322-459 1.49e-05

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: 49.56  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   322 LQLERHRKN--EEARIAREVEAHEKRIRRELEkQDMLRRKREEQIRKEMERQDRERRkeeerllreKQREEERYLKEQM- 398
Cdd:pfam15709  348 LEVERKRREqeEQRRLQQEQLERAEKMREELE-LEQQRRFEEIRLRKQRLEEERQRQ---------EEEERKQRLQLQAa 417

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188190   399 --RELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKiaKESMELIEDERLE 459
Cdd:pfam15709  418 qeRARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ--KRLMEMAEEERLE 478
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 329-457 1.58e-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: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   329 KNEEARI---AREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQMRELQRRE 405
Cdd:pfam13868  151 REEDERIleyLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 334188190   406 KFLKKETIRA--EKMRQKEEMRkEKEVARLKAANERAIARKIAKESMELIEDER 457
Cdd:pfam13868  231 ARQRQELQQAreEQIELKERRL-AEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
PTZ00121 PTZ00121
MAEBL; Provisional
 315-457 2.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYL 394
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334188190  395 KEqmrELQRREKFLKK--ETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIakESMELIEDER 457
Cdd:PTZ00121 1165 KA---EEARKAEDAKKaeAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA--EEARKAEDAK 1224
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 319-462 2.13e-05

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: 45.63  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   319 DDALQLERHRKneEARIAREVEAHEKRIRR---ELEKQDMLRRKRE-EQIRKEMERQDRERRKEeerllrekQREEERYL 394
Cdd:pfam12474    9 KDRFEQERQQL--KKRYEKELEQLERQQKQqieKLEQRQTQELRRLpKRIRAEQKKRLKMFRES--------LKQEKKEL 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334188190   395 K---EQMRELQRREKFLKketiRAEKMRQKEEMRKEKEVARLKAANERAIARkiakesmeLIEDERLELME 462
Cdd:pfam12474   79 KqevEKLPKFQRKEAKRQ----RKEELELEQKHEELEFLQAQSEALERELQQ--------LQNEKRKELAE 137
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-465 2.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRR------ELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR 388
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEElrleleELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190  389 EEEryLKEQMRELQRREKFLKKETIRAEKMRQK-EEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAA 465
Cdd:COG1196   318 LEE--LEEELAELEEELEELEEELEELEEELEEaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
PTZ00121 PTZ00121
MAEBL; Provisional
 321-463 2.43e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  321 ALQLERHRKNEEARIAREV-EAHEKRIRRELEKQDMLRRKREEQiRKEMERQDRERRKEEERLLREKQREEERYLKEQMR 399
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKkKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188190  400 elqRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEV 463
Cdd:PTZ00121 1350 ---AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 899-941 2.49e-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: 2.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 334188190   899 GEQWVQGLVEGDYSNLSSEERLNALVALIGIATEGNTIRIALE 941
Cdd:pfam15612    4 LPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 325-459 2.56e-05

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: 45.80  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   325 ERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeerllrekQREEERYLKEQMRELQRR 404
Cdd:pfam05672   18 EKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEAR---------------RLEEERRREEEERQRKAE 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334188190   405 EKFLKKETIRAEKMrqkEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:pfam05672   83 EEAEEREQREQEEQ---ERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLE 134
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
325-486 2.74e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 48.33  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  325 ERHRKNEEARIAREVEAHEKRI---RRELE-KQDMLRRKRE------------EQIRKEMERQDRERRKEEERLLREKQR 388
Cdd:COG2268   218 QANREAEEAELEQEREIETARIaeaEAELAkKKAEERREAEtaraeaeaayeiAEANAEREVQRQLEIAEREREIELQEK 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  389 EEERYLKEQMRELqrrekflkKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAkESMELIEDERLELMevaaLTK 468
Cdd:COG2268   298 EAEREEAELEADV--------RKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALA-EAWNKLGDAAILLM----LIE 364

                         170
                  ....*....|....*...
gi 334188190  469 GLPSMLALDFETLQNLDE 486
Cdd:COG2268   365 KLPEIAEAAAKPLEKIDK 382
PTZ00121 PTZ00121
MAEBL; Provisional
 306-456 4.41e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  306 VKSEREVGNEDEDDDALQLERHRKNEE----ARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeER 381
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK--------KK 1717

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334188190  382 LLREKQREEERYLKEQmrELQRREKFLKKetiRAEKMRQKEEmrKEKEVARLKAANERAiARKIAKESMELIEDE 456
Cdd:PTZ00121 1718 AEELKKAEEENKIKAE--EAKKEAEEDKK---KAEEAKKDEE--EKKKIAHLKKEEEKK-AEEIRKEKEAVIEEE 1784
PTZ00121 PTZ00121
MAEBL; Provisional
 325-488 4.92e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  325 ERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQdrerrkeeerllrekqREEERYLKEQMR--ELQ 402
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARK----------------AEDAKKAEAARKaeEVR 1188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  403 RREKFLKKETIR-AEKMRQKEEMRKEKEVARLKAANERAIARKI---------AKESMELIEDERLELMEVAALTKGLPS 472
Cdd:PTZ00121 1189 KAEELRKAEDARkAEAARKAEEERKAEEARKAEDAKKAEAVKKAeeakkdaeeAKKAEEERNNEEIRKFEEARMAHFARR 1268

                         170
                  ....*....|....*.
gi 334188190  473 MLALDFETLQNLDEYR 488
Cdd:PTZ00121 1269 QAAIKAEEARKADELK 1284
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-486 7.23e-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: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  309 EREVGNEDEDDDALQLERHRKnEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEME-RQDRERRKEEERLLREKQ 387
Cdd:COG1196   324 ELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQL 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  388 REEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALT 467
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         170
                  ....*....|....*....
gi 334188190  468 KGLPSMLALDFETLQNLDE 486
Cdd:COG1196   483 LEELAEAAARLLLLLEAEA 501
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 317-457 7.56e-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: 46.84  E-value: 7.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   317 EDDDALQLERHRKNEEAR--IAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQ-DRERRkeEERLLREKQREEERY 393
Cdd:pfam13868  112 EEDQAEAEEKLEKQRQLReeIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREeEREAE--REEIEEEKEREIARL 189

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334188190   394 LKEQMRELQRREkflKKETIRA--------EKMRQKEEM---RKEKEVARLKAANERAIARKIAKESMELIEDER 457
Cdd:pfam13868  190 RAQQEKAQDEKA---ERDELRAklyqeeqeRKERQKEREeaeKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-486 9.98e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 9.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEeRLLREKQREEERY- 393
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-LAEELLEALRAAAe 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  394 LKEQMRELQRREKFLKKETIRAEkmRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLELMEVAALTKGLPSM 473
Cdd:COG1196   398 LAAQLEELEEAEEALLERLERLE--EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                         170
                  ....*....|...
gi 334188190  474 LALDFETLQNLDE 486
Cdd:COG1196   476 EAALAELLEELAE 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-466 1.01e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  309 EREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQR 388
Cdd:COG1196   259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190  389 EEEryLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAAnERAIARKIAKESMELIEDERLELMEVAAL 466
Cdd:COG1196   339 LEE--LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALL 413
PRK12704 PRK12704
phosphodiesterase; Provisional
 329-451 1.11e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  329 KNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDrerrkeeerllrekqrEEERYLKEQMRELQRREKFL 408
Cdd:PRK12704   63 KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE----------------KREEELEKKEKELEQKQQEL 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 334188190  409 KKETIRAEKMRQKEEMRKEkEVARLKAANeraiARKIAKESME 451
Cdd:PRK12704  127 EKKEEELEELIEEQLQELE-RISGLTAEE----AKEILLEKVE 164
PTZ00121 PTZ00121
MAEBL; Provisional
 306-448 1.18e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  306 VKSEREVGNEDEDDdalqlerhRKNEEARIAREVE--AHEKRIRRELEKQ--DMLRRKREEQIRKEMERQDRERRKEEER 381
Cdd:PTZ00121 1661 IKAAEEAKKAEEDK--------KKAEEAKKAEEDEkkAAEALKKEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKA 1732

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334188190  382 LLREKQREEERYLKEQMRELQRREKflKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKE 448
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKK--KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
PTZ00121 PTZ00121
MAEBL; Provisional
 325-457 1.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  325 ERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRRKREEqIRKEMERQDRERRKEEERLLREKQREEERYLKEQMR--- 399
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKkkAEEAKKAEEAKKKAEEAKKADE-AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkad 1513

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334188190  400 ELQRREKFLKKETIR-AEKMRQKEEMRKEKEVAR---LKAANERAIARKIAKESMELIEDER 457
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKkAEEAKKADEAKKAEEKKKadeLKKAEELKKAEEKKKAEEAKKAEED 1575
PTZ00121 PTZ00121
MAEBL; Provisional
 325-503 1.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  325 ERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRRKREEQIRK--EMERQDRERRKEEERLLREKQREEERYLKEQMRE 400
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKkkAEEAKKADEAKKKAEEAKKAEEAKKKaeEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  401 LQRREKFLKK--ETIRAEKMRQKEEMRKEKEVAR---LKAANERAIARKIaKESMELIEDERLELMEVAALTKGLPSMLA 475
Cdd:PTZ00121 1502 AKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADEL-KKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580

                         170       180
                  ....*....|....*....|....*...
gi 334188190  476 LDFETLQNLDEYRDKQAIFPPTSVKLKK 503
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 309-465 1.50e-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: 45.68  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   309 EREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKreEQIRKEMERQDRERRKEEeRLLREKQR 388
Cdd:pfam13868   50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER--EQMDEIVERIQEEDQAEA-EEKLEKQR 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   389 EEERYLKEQMRELQRREKFLKKETIRAE-------KMRQKEEMRKEKEVARLKAANERAIARKIAKesMELIEDERLELM 461
Cdd:pfam13868  127 QLREEIDEFNEEQAEWKELEKEEEREEDerileylKEKAEREEEREAEREEIEEEKEREIARLRAQ--QEKAQDEKAERD 204


                   ....
gi 334188190   462 EVAA 465
Cdd:pfam13868  205 ELRA 208
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 315-465 1.56e-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: 45.68  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   315 EDEDDDALQLERHRKNEEARIAREVEAHEKRI--RRELEKQdMLRRKREEQIRKEMERQDRERRKEEErllrekQREEER 392
Cdd:pfam13868   41 EERRLDEMMEEERERALEEEEEKEEERKEERKryRQELEEQ-IEEREQKRQEEYEEKLQEREQMDEIV------ERIQEE 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   393 YLKEQMRELQRREKFLK-----KETIRAEKMRQKEEMRKE----KEVARLKAANERAIARKIAkesmELIEDERLELMEV 463
Cdd:pfam13868  114 DQAEAEEKLEKQRQLREeidefNEEQAEWKELEKEEEREEderiLEYLKEKAEREEEREAERE----EIEEEKEREIARL 189


                   ..
gi 334188190   464 AA 465
Cdd:pfam13868  190 RA 191
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 321-474 2.23e-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: 45.41  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   321 ALQLERHRKNEEARIAREVEAHEkriRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQ--- 397
Cdd:pfam15558   11 ALMLARHKEEQRMRELQQQAALA---WEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRrek 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   398 ---MRELQRREKFLKKETIRAEKM---RQKEEMRKEKEVARLKAANEraiARKIAKESMELIEDERLelmEVAALTKGLP 471
Cdd:pfam15558   88 qviEKESRWREQAEDQENQRQEKLeraRQEAEQRKQCQEQRLKEKEE---ELQALREQNSLQLQERL---EEACHKRQLK 161


                   ...
gi 334188190   472 SML 474
Cdd:pfam15558  162 ERE 164
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 307-435 3.64e-04

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: 42.75  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   307 KSEREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEkqdmlRRKREEQIRKEMERQDrerrkeeerllREK 386
Cdd:pfam11600   13 KEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEAR-----RKKEEEKELKEKERRE-----------KKE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 334188190   387 QREEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKA 435
Cdd:pfam11600   77 KDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKA 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-468 3.70e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  308 SEREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQ 387
Cdd:COG1196   267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  388 REEERYLKE-QMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERA-IARKIAKESMELIEDERLELMEVAA 465
Cdd:COG1196   347 EEAEEELEEaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqLEELEEAEEALLERLERLEEELEEL 426


                  ...
gi 334188190  466 LTK 468
Cdd:COG1196   427 EEA 429
PRK12704 PRK12704
phosphodiesterase; Provisional
 331-468 3.76e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  331 EEARiaREVEAHEKRIrrELEKQDMLRRKREEqirkeMERQDrerrkeeerllrekqREEERYLKEQMRELQRREKFLKK 410
Cdd:PRK12704   45 EEAK--KEAEAIKKEA--LLEAKEEIHKLRNE-----FEKEL---------------RERRNELQKLEKRLLQKEENLDR 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190  411 ETIRAEKMRQKEEMRKEKEVARLKAANERaiarkiAKESMELIEDERLELMEVAALTK 468
Cdd:PRK12704  101 KLELLEKREEELEKKEKELEQKQQELEKK------EEELEELIEEQLQELERISGLTA 152
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 314-464 5.74e-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: 43.15  E-value: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   314 NEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRElEKQDMLRRKREEQIRKEMERQdrerrkeeerllrekQREEERY 393
Cdd:pfam13904   34 QSSSLTYARKLEGLKLERQPLEAYENWLAAKQRQRQ-KELQAQKEEREKEEQEAELRK---------------RLAKEKY 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   394 L-----KEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVAR----------LKAANERAIARKIAKESMELIEDERL 458
Cdd:pfam13904   98 QewlqrKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKevlqewerkkLEQQQRKREEEQREQLKKEEEEQERK 177


                   ....*.
gi 334188190   459 ELMEVA 464
Cdd:pfam13904  178 QLAEKA 183
PTZ00491 PTZ00491
major vault protein; Provisional
 329-469 6.02e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 44.62  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  329 KNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRK---EMERQDRERRKEEERLLREKQREEERYLKEQmRELQRRE 405
Cdd:PTZ00491  662 KSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTkllELQAESAAVESSGQSRAEALAEAEARLIEAE-AEVEQAE 740

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188190  406 KFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARkiAKESMElIEDERLELMeVAALTKG 469
Cdd:PTZ00491  741 LRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAK--AKELAD-IEATKFERI-VEALGRE 800
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 347-448 6.60e-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: 41.01  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   347 RRELEK-QDMLRRKREEqIRKEMERQDrerrkeeerllrekQREEERYLKEQM--RELQRREKFLK---KETIRAEKMRQ 420
Cdd:pfam13863    5 KREMFLvQLALDAKREE-IERLEELLK--------------QREEELEKKEQElkEDLIKFDKFLKendAKRRRALKKAE 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 334188190   421 KEE---MRKEKEVARLKAANERAIARKIAKE 448
Cdd:pfam13863   70 EETklkKEKEKEIKKLTAQIEELKSEISKLE 100
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-459 7.16e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  315 EDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRR--KREEQIRKEMER-QDRERRKEEERLLREKQREEE 391
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERlEEELEELEEALAELEEEEEEE 440

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190  392 RYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 336-452 8.05e-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: 43.33  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  336 AREVEAHEKRIRRELEKQdmlRRKREEQIRKEMERQDrerrkeeerllrekqREEERYLKEQMRELQRREKfLKKETIRA 415
Cdd:cd16269   195 EKEKEIEAERAKAEAAEQ---ERKLLEEQQRELEQKL---------------EDQERSYEEHLRQLKEKME-EERENLLK 255

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 334188190  416 EKMRQKEEMRKEKEvaRLKAANERAIARKIAKESMEL 452
Cdd:cd16269   256 EQERALESKLKEQE--ALLEEGFKEQAELLQEEIRSL 290
PTZ00121 PTZ00121
MAEBL; Provisional
 325-462 8.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  325 ERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRrKREEQIRKEMERQDRERRKEEERLLREKQR--EEERYLKEQMRE 400
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKkkADEAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKA 1572

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334188190  401 LQRREKFLKketiRAEKMRQKEEMRKEkEVARLKAANERAIARKIAKESMELIEDERLELME 462
Cdd:PTZ00121 1573 EEDKNMALR----KAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 331-462 8.81e-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: 43.37  E-value: 8.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   331 EEARIAREVEAHEKRIRRELEKQdmlrRKREEQIRKEMERQdrerrkeeerllREKQREEERY-LKEQMRElQRREKFLK 409
Cdd:pfam13868   30 EKKRIKAEEKEEERRLDEMMEEE----RERALEEEEEKEEE------------RKEERKRYRQeLEEQIEE-REQKRQEE 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334188190   410 KETIRAEKMRQKEEMRKEKEvARLKAANERAIARKIAKESMELIEDERLELME 462
Cdd:pfam13868   93 YEEKLQEREQMDEIVERIQE-EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
PTZ00121 PTZ00121
MAEBL; Provisional
 306-448 9.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  306 VKSEREVGNEDEDDDALQLERH----RKNEEARIAR------EVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDrer 375
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNneeiRKFEEARMAHfarrqaAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD--- 1305

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334188190  376 rkEEERLLREKQREEEryLKEQMRELQRREKFLKKetiRAEKMRQKEEMRKEKEVA---RLKAANERAIARKIAKE 448
Cdd:PTZ00121 1306 --EAKKKAEEAKKADE--AKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAaadEAEAAEEKAEAAEKKKE 1374
PTZ00121 PTZ00121
MAEBL; Provisional
 307-457 1.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  307 KSEREVGNEDEDDDALQLERHRKNEEARIAREVEAHEK-----RIRRELEKQDMLRRKREEQIRK--EMERQDRERRKEE 379
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKAD 1421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  380 ERLLREKQREEERYLKEQMRELQRREKFLKK--ETIRAEKMRQKEEMRKEKEVARLKAANERAI--ARKIAKESMELIED 455
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeAKKKAEEAKKKADE 1501


                  ..
gi 334188190  456 ER 457
Cdd:PTZ00121 1502 AK 1503
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 333-459 1.17e-03

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: 41.18  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   333 ARIAREVEAheKRIRRELEKQDMLRRKREEQIRKEMErqdrerrkeeerllrekqrEEERYLKEQMR-----ELQRREkf 407
Cdd:pfam05672    4 AGTTDAEEA--ARILAEKRRQAREQREREEQERLEKE-------------------EEERLRKEELRrraeeERARRE-- 60

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 334188190   408 lkketirAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:pfam05672   61 -------EEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEE 105
PTZ00121 PTZ00121
MAEBL; Provisional
 319-444 1.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  319 DDALQLERHRKNEEAR---IAREVE----AHEKRIRRELEKQDMLRR----KREEQIRK--EMERQDRERRKEEERLLRE 385
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKrveIARKAEdarkAEEARKAEDAKKAEAARKaeevRKAEELRKaeDARKAEAARKAEEERKAEE 1216

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188190  386 KQREEERYLKEQMRELQRREKfLKKETIRAEKMRQKEEMRKEKEV-----ARLKAANERAIARK 444
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKK-DAEEAKKAEEERNNEEIRKFEEArmahfARRQAAIKAEEARK 1279
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 334188190  307 KSEREVGNEDEDDDALQLERHRKNEEARIAREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREK 386
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750

                          90       100
                  ....*....|....*....|....*
gi 334188190  387 QREEERYLKEQMRELQRREKFLKKE 411
Cdd:COG1196   751 EALEELPEPPDLEELERELERLERE 775
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
311-469 1.47e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  311 EVGNEDEDDDALQLERHRKNEEARiaREVEAHEKRIRREL-EKQDMLRRKREEQIRKEMERQDRERRKEeerllrekqRE 389
Cdd:COG4717   378 EAGVEDEEELRAALEQAEEYQELK--EELEELEEQLEELLgELEELLEALDEEELEEELEELEEELEEL---------EE 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  390 EERYLKEQMRELQRREKFLKKETiRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERL-ELME-----V 463
Cdd:COG4717   447 ELEELREELAELEAELEQLEEDG-ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLEraseyF 525


                  ....*.
gi 334188190  464 AALTKG 469
Cdd:COG4717   526 SRLTDG 531
PTZ00121 PTZ00121
MAEBL; Provisional
 306-457 1.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  306 VKSEREVGNEDEDDDALQL----ERHRKNEEARIAREVE--AHE--------KRIRRELEKQDMLRRKREEQIRKEMERQ 371
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKkkadEAKKKAEEAKKADEAKkkAEEakkkadaaKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  372 DRERRKEEERLLREKQREEEryLKEQMRELQRREKFLKKetirAEKMRQKEEMRKEKEVARLKA--ANERAIARKIAKES 449
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADA--AKKKAEEKKKADEAKKK----AEEDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEA 1436


                  ....*...
gi 334188190  450 MELIEDER 457
Cdd:PTZ00121 1437 KKKAEEAK 1444
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 305-462 1.79e-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: 43.04  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   305 FVKSEREVGNEDEDDdalqlERHRKNEEARIAREVEAHEKrIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLR 384
Cdd:pfam02463  659 AEKSEVKASLSELTK-----ELLEIQELQEKAESELAKEE-ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD 732

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188190   385 EKQREEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESmeLIEDERLELME 462
Cdd:pfam02463  733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK--AQEEELRALEE 808
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 347-440 1.86e-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: 42.63  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   347 RRELEK--QDMLRRKREEQIRKEMERQdRERRKEEERLLREKQREEERYLKEQMRELQRR--EKFLKKETIRAEKMRQKE 422
Cdd:pfam15709  327 KREQEKasRDRLRAERAEMRRLEVERK-RREQEEQRRLQQEQLERAEKMREELELEQQRRfeEIRLRKQRLEEERQRQEE 405

                           90
                   ....*....|....*...
gi 334188190   423 EMRKEKevARLKAANERA 440
Cdd:pfam15709  406 EERKQR--LQLQAAQERA 421
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 339-452 2.00e-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: 42.28  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   339 VEAHEKRIRR--ELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLKEQMRElQRREKFLKKETIRAE 416
Cdd:pfam07767  194 FEDHQELLQKavEAEKKRLKEEEKLERVLEKIAESAATAEAREEKRKTKAQRNKEKRRKEEERE-AKEEKALKKKLAQLE 272

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 334188190   417 KMRQ--KEEMRKEKEVARLKAANERAiARKIAKESMEL 452
Cdd:pfam07767  273 RLKEiaKEIAEKEKEREEKAEARKRE-KRKKKKEEKKL 309
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 325-492 2.63e-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: 42.36  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   325 ERHRKNEEARIAREVEAHEKRIRREL---EKQDMLRRKREEQIRKEMERQdreRRKEEERLLREKQREEERYlKEQMREL 401
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYlekEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEEL-EAALRDL 880

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   402 QRREKFLKKETIRAEKmrQKEEMRKEKEVARLKA------ANERAIARKIAKESMELIEDERLELMEVAALTKGLP---- 471
Cdd:TIGR02169  881 ESRLGDLKKERDELEA--QLRELERKIEELEAQIekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdvqa 958

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 334188190   472 ---------------SMLALD--FETLQNLDEYRDKQA 492
Cdd:TIGR02169  959 elqrveeeiralepvNMLAIQeyEEVLKRLDELKEKRA 996
PTZ00121 PTZ00121
MAEBL; Provisional
 306-459 2.71e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  306 VKSEREVGNEDEDDDALQLERHRKNEEARIAREVE--AHEKRIRRELEKQDMLRRKREEQIRKEMERQdrERRKEEERLL 383
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAK--KAEEAKKKAE 1467

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334188190  384 REKQREEERYLKEQMRELQRREKFLKKETIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDERLE 459
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
PTZ00121 PTZ00121
MAEBL; Provisional
 319-457 2.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  319 DDALQLERHRKNEEARIAREV--------EAHEKRIRRELEKQ-DMLRRKREEQIRK--EMERQDRERRKEEERLLREKQ 387
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKkkadeakkKAEEAKKADEAKKKaEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAE 1360

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188190  388 REEErylKEQMRELQRREKFLKKETI--RAEKMRQKEEMRKEKEVARLKA--ANERAIARKIAKESMELIEDER 457
Cdd:PTZ00121 1361 AAEE---KAEAAEKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKK 1431
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 296-492 3.29e-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: 42.03  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   296 TAAQVHDDPFvksEREVGNEDEDDDALQLERHRKNEEARIAREveaHEKRI--------------RRELEKQDMlRRKRE 361
Cdd:pfam15921  359 TEARTERDQF---SQESGNLDDQLQKLLADLHKREKELSLEKE---QNKRLwdrdtgnsitidhlRRELDDRNM-EVQRL 431

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   362 EQIRKEMerqdrerrkeeerllrekQREEERYLKEQMRELQRREKFLKK-ETIRAEKMRQKEEMRKEKEVARLKAANERA 440
Cdd:pfam15921  432 EALLKAM------------------KSECQGQMERQMAAIQGKNESLEKvSSLTAQLESTKEMLRKVVEELTAKKMTLES 493

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 334188190   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 ...
 315-448 4.56e-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: 41.48  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   315 EDEDDDALQLERHRKNEEARI---------AREVEAHEKRIRRELEKQDMLRRKREEQIRKEMERQDRERRKEEERLLRE 385
Cdd:pfam15709  371 AEKMREELELEQQRRFEEIRLrkqrleeerQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAE 450

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334188190   386 KQREEEryLKEQMRELQRREKFLKKETiRAEKMRQK--EEMR----------KEKEVARLKAANERAIARKIAKE 448
Cdd:pfam15709  451 KQRQKE--LEMQLAEEQKRLMEMAEEE-RLEYQRQKqeAEEKarleaeerrqKEEEAARLALEEAMKQAQEQARQ 522
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 346-462 4.89e-03

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 41.54  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  346 IRRELEKQDmLRRKREEQIRKEMERQdrerrkeeerllrekQREeeRYLKEQMRELQrrekflkKEtiraekMRQKEEmr 425
Cdd:COG0466   203 LEKEIEVLE-LEKKIRSRVKEQMEKS---------------QRE--YYLREQLKAIQ-------KE------LGEKDD-- 249

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 334188190  426 KEKEVARLKaanERAIARKIAKESMELIEDE--RLELME 462
Cdd:COG0466   250 GEDEIEELR---EKIEKAKLPEEVKEKAEKElkKLERMP 285
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 325-448 5.70e-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: 40.60  E-value: 5.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   325 ERHRKNEEARIAREVE----AHEKRIRR-ELEKQDMLRRKREEQIRKEMERQdrerrkEEERLLREKQREEERYLK-EQM 398
Cdd:TIGR02794   66 EQERQKKLEQQAEEAEkqraAEQARQKElEQRAAAEKAAKQAEQAAKQAEEK------QKQAEEAKAKQAAEAKAKaEAE 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 334188190   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 7.23e-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: 38.62  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190   320 DALQLE----RHRKNEEARIAREVEAHEKRIRRELEKQdmlRRKREEQIRKEMERqdrerrkeeerllREKQREEERYLK 395
Cdd:pfam15236   40 DPAQLEererKRQKALEHQNAIKKQLEEKERQKKLEEE---RRRQEEQEEEERLR-------------REREEEQKQFEE 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 334188190   396 EQMRELQRREKFLKKETIRAEKMRQKEEM-RKEKEVARLK 434
Cdd:pfam15236  104 ERRKQKEKEEAMTRKTQALLQAMQKAQELaQRLKQEQRIR 143
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 320-456 9.61e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188190  320 DALQLERHRKNEEARIARE----VEAHEKRIRrELEKQdmlrRKREEQIRKEMERQDRERRKEEERLLREKQREEERYLK 395
Cdd:PRK09510   73 SAKRAEEQRKKKEQQQAEElqqkQAAEQERLK-QLEKE----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334188190  396 EQMRELQRREKFLKKetIRAEKMRQKEEMRKEKEVARLKAANERAIARKIAKESMELIEDE 456
Cdd:PRK09510  148 KAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE 206
 
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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