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Conserved domains on  [gi|37590660|gb|AAH58956|]
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Chromodomain protein, Y chromosome-like 2 [Mus musculus]

Protein Classification

CD_CDY and crotonase-like domain-containing protein( domain architecture ID 13036092)

CD_CDY and crotonase-like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
249-445 8.84e-47

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


:

Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 161.19  E-value: 8.84e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 249 IVVRKEEGFTHILLSSQtSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGrlSSDRRKESTR 327
Cdd:cd06558   1 VLVERDGGVATITLNRP-EKRNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAA--LSDAGEEARA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 328 IAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEM 407
Cdd:cd06558  78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 37590660 408 LFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEM 445
Cdd:cd06558 158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 5.19e-31

chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain found in the mammalian chromodomain Y-like (CDY) protein family, and similar proteins. The human CDY family includes 6 proteins: the genes encoding four of these: two copies of CDY1 (CDY1a, CDY1a) and two copies of CDY2(CDY2a and CDY2b), are located on chromosome Y, and the genes encoding the other two members (CDYL and CDYL2) are located on autosomes. The chromosomal genes are only present in primates, whereas the CDYL and CDYL2 genes exist in most mammalian species. The CDY family proteins contain two functional domains: a chromodomain involved in chromatin binding and a catalytic domain found in many coenzyme A (CoA)- dependent acylation enzymes. CDYL is ubiquitously expressed, whereas CDYL2 shows selective expression in tissues of testis, prostate, spleen, and leukocyte. The CDYL genes are ubiquitously expressed, the CDY genes are only expressed in the testis. Deletion of the CDY1b gene has been shown to be a risk factor for male infertility. Impairments in CDY2 expression could be implicated in the pathogenesis of maturation arrest (a failure of germ cell development).


:

Pssm-ID: 349284  Cd Length: 52  Bit Score: 114.08  E-value: 5.19e-31
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 37590660   6 LYEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEFNG 57
Cdd:cd18634   1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
 
Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
249-445 8.84e-47

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 161.19  E-value: 8.84e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 249 IVVRKEEGFTHILLSSQtSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGrlSSDRRKESTR 327
Cdd:cd06558   1 VLVERDGGVATITLNRP-EKRNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAA--LSDAGEEARA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 328 IAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEM 407
Cdd:cd06558  78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 37590660 408 LFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEM 445
Cdd:cd06558 158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
270-485 4.14e-43

Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440647 [Multi-domain]  Cd Length: 249  Bit Score: 153.01  E-value: 4.14e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKestRIAEAIRDFVKAFIQFKKPIVV 348
Cdd:COG1024  21 NALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPEEAR---AFARGLQRLFRALRRLPKPVIA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:COG1024  98 AVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKELLLTGRRIDAEEALELGLVNRV 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 37590660 429 FWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKECVMLKQLWSS 485
Cdd:COG1024 178 VPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFAS 234
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
247-476 1.79e-35

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 132.68  E-value: 1.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  247 RDIVVRKEEGFTHIllssqTSDN----NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDysyligrLSSD- 320
Cdd:PRK06688   5 TDLLVELEDGVLTI-----TINRpdkkNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD-------IKDFp 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  321 -RRKESTRIAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQIL 399
Cdd:PRK06688  73 kAPPKPPDELAPVNRFLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590660  400 GVALANEMLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKEC 476
Cdd:PRK06688 153 GRARAAEMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREA 229
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 5.19e-31

chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain found in the mammalian chromodomain Y-like (CDY) protein family, and similar proteins. The human CDY family includes 6 proteins: the genes encoding four of these: two copies of CDY1 (CDY1a, CDY1a) and two copies of CDY2(CDY2a and CDY2b), are located on chromosome Y, and the genes encoding the other two members (CDYL and CDYL2) are located on autosomes. The chromosomal genes are only present in primates, whereas the CDYL and CDYL2 genes exist in most mammalian species. The CDY family proteins contain two functional domains: a chromodomain involved in chromatin binding and a catalytic domain found in many coenzyme A (CoA)- dependent acylation enzymes. CDYL is ubiquitously expressed, whereas CDYL2 shows selective expression in tissues of testis, prostate, spleen, and leukocyte. The CDYL genes are ubiquitously expressed, the CDY genes are only expressed in the testis. Deletion of the CDY1b gene has been shown to be a risk factor for male infertility. Impairments in CDY2 expression could be implicated in the pathogenesis of maturation arrest (a failure of germ cell development).


Pssm-ID: 349284  Cd Length: 52  Bit Score: 114.08  E-value: 5.19e-31
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 37590660   6 LYEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEFNG 57
Cdd:cd18634   1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
269-497 2.69e-24

Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.


Pssm-ID: 395302 [Multi-domain]  Cd Length: 251  Bit Score: 101.67  E-value: 2.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   269 NNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRlsSDRRKESTRiaEAIRDFVKAFIQFKKPIV 347
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLKEMYGE--GPAHQALYR--ENVLDLWTLLYTCPKPVI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   348 VAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQ 427
Cdd:pfam00378  93 AAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEALKWGLVDK 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   428 VFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKECVMLKQLWSSSKGLDSLFSYLQ 497
Cdd:pfam00378 173 VVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQAFLE 242
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
7-56 2.02e-19

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 81.47  E-value: 2.02e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 37590660     7 YEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEFN 56
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFK 50
CHROMO smart00298
Chromatin organization modifier domain;
7-55 2.68e-18

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 78.41  E-value: 2.68e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 37590660      7 YEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNY 50
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
260-431 2.36e-09

fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).


Pssm-ID: 131494 [Multi-domain]  Cd Length: 737  Bit Score: 59.85  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   260 ILLSSQTSDNNALTPEIMKEVRRALCNAATDDS--KLLLLSAVGSVFCSGLDysylIGRLSSDRR-KESTRIAEAIRDFV 336
Cdd:TIGR02441  26 VKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD----IQMIAACKTaQEVTQLSQEGQEMF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   337 KAFIQFKKPIVVAINGPALGLGASILPLCD--IVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKL 414
Cdd:TIGR02441 102 ERIEKSQKPIVAAISGSCLGGGLELALACHyrIATKDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGVPAALDMMLTGKKI 181
                         170
                  ....*....|....*..
gi 37590660   415 TAQEACSRGLVSQVFWP 431
Cdd:TIGR02441 182 RADRAKKMGIVDQLVDP 198
 
Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
249-445 8.84e-47

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 161.19  E-value: 8.84e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 249 IVVRKEEGFTHILLSSQtSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGrlSSDRRKESTR 327
Cdd:cd06558   1 VLVERDGGVATITLNRP-EKRNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAA--LSDAGEEARA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 328 IAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEM 407
Cdd:cd06558  78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 37590660 408 LFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEM 445
Cdd:cd06558 158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
270-485 4.14e-43

Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440647 [Multi-domain]  Cd Length: 249  Bit Score: 153.01  E-value: 4.14e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKestRIAEAIRDFVKAFIQFKKPIVV 348
Cdd:COG1024  21 NALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPEEAR---AFARGLQRLFRALRRLPKPVIA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660 349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:COG1024  98 AVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKELLLTGRRIDAEEALELGLVNRV 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 37590660 429 FWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKECVMLKQLWSS 485
Cdd:COG1024 178 VPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFAS 234
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
247-476 1.79e-35

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 132.68  E-value: 1.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  247 RDIVVRKEEGFTHIllssqTSDN----NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDysyligrLSSD- 320
Cdd:PRK06688   5 TDLLVELEDGVLTI-----TINRpdkkNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD-------IKDFp 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  321 -RRKESTRIAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQIL 399
Cdd:PRK06688  73 kAPPKPPDELAPVNRFLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590660  400 GVALANEMLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKEC 476
Cdd:PRK06688 153 GRARAAEMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREA 229
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 5.19e-31

chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain found in the mammalian chromodomain Y-like (CDY) protein family, and similar proteins. The human CDY family includes 6 proteins: the genes encoding four of these: two copies of CDY1 (CDY1a, CDY1a) and two copies of CDY2(CDY2a and CDY2b), are located on chromosome Y, and the genes encoding the other two members (CDYL and CDYL2) are located on autosomes. The chromosomal genes are only present in primates, whereas the CDYL and CDYL2 genes exist in most mammalian species. The CDY family proteins contain two functional domains: a chromodomain involved in chromatin binding and a catalytic domain found in many coenzyme A (CoA)- dependent acylation enzymes. CDYL is ubiquitously expressed, whereas CDYL2 shows selective expression in tissues of testis, prostate, spleen, and leukocyte. The CDYL genes are ubiquitously expressed, the CDY genes are only expressed in the testis. Deletion of the CDY1b gene has been shown to be a risk factor for male infertility. Impairments in CDY2 expression could be implicated in the pathogenesis of maturation arrest (a failure of germ cell development).


Pssm-ID: 349284  Cd Length: 52  Bit Score: 114.08  E-value: 5.19e-31
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 37590660   6 LYEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEFNG 57
Cdd:cd18634   1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
PRK07511 PRK07511
enoyl-CoA hydratase; Provisional
255-428 9.59e-25

enoyl-CoA hydratase; Provisional


Pssm-ID: 181009 [Multi-domain]  Cd Length: 260  Bit Score: 103.15  E-value: 9.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  255 EGFTHILLSSQTSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIaEAIR 333
Cdd:PRK07511  10 EGSTLVLTLSNPGARNALHPDMYAAGIEALNTAERDPSiRAVVLTGAGGFFCAGGNLNRLLENRAKPPSVQAASI-DGLH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  334 DFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRK 413
Cdd:PRK07511  89 DWIRAIRAFPKPVIAAVEGAAAGAGFSLALACDLLVAARDAKFVMAYVKVGLTPDGGGSWFLARALPRQLATELLLEGKP 168
                        170
                 ....*....|....*
gi 37590660  414 LTAQEACSRGLVSQV 428
Cdd:PRK07511 169 ISAERLHALGVVNRL 183
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
269-497 2.69e-24

Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.


Pssm-ID: 395302 [Multi-domain]  Cd Length: 251  Bit Score: 101.67  E-value: 2.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   269 NNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRlsSDRRKESTRiaEAIRDFVKAFIQFKKPIV 347
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLKEMYGE--GPAHQALYR--ENVLDLWTLLYTCPKPVI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   348 VAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQ 427
Cdd:pfam00378  93 AAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEALKWGLVDK 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   428 VFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKECVMLKQLWSSSKGLDSLFSYLQ 497
Cdd:pfam00378 173 VVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQAFLE 242
PRK05981 PRK05981
enoyl-CoA hydratase/isomerase;
270-477 2.11e-23

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235661  Cd Length: 266  Bit Score: 99.42  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDSKL--LLLSAVGSVFCSGLDysyLIGRLSSDRRKESTRIAEAIRD-----FVKAFIQF 342
Cdd:PRK05981  26 NAVSIDMLGGLAEALDAIEDGKAEVrcLVLTGAGRGFCTGAN---LQGRGSGGRESDSGGDAGAALEtayhpFLRRLRNL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  343 KKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSR 422
Cdd:PRK05981 103 PCPIVTAVNGPAAGVGMSFALMGDLILCARSAYFLQAFRRIGLVPDGGSTWLLPRLVGKARAMELSLLGEKLPAETALQW 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37590660  423 GLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKECV 477
Cdd:PRK05981 183 GLVNRVVDDAELMAEAMKLAHELANGPTVALGLIRKLYWDSPENDFEEQLNLERE 237
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
7-56 2.94e-22

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 89.46  E-value: 2.94e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEFN 56
Cdd:cd00024   1 YEVEKILDHRV-RKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYE 49
PRK08260 PRK08260
enoyl-CoA hydratase; Provisional
270-431 3.61e-22

enoyl-CoA hydratase; Provisional


Pssm-ID: 236206 [Multi-domain]  Cd Length: 296  Bit Score: 96.61  E-value: 3.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLD---------YSYLIGRLSSDRRKESTRIAEAIRD----F 335
Cdd:PRK08260  26 NAFTVTMARELIEAFDAADADDAvRAVIVTGAGRAFCAGADlsaggntfdLDAPRTPVEADEEDRADPSDDGVRDgggrV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  336 VKAFIQFKKPIVVAINGPALGLGASI-LPLcDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKL 414
Cdd:PRK08260 106 TLRIFDSLKPVIAAVNGPAVGVGATMtLAM-DIRLASTAARFGFVFGRRGIVPEAASSWFLPRLVGLQTALEWVYSGRVF 184
                        170
                 ....*....|....*..
gi 37590660  415 TAQEACSRGLVSQVFWP 431
Cdd:PRK08260 185 DAQEALDGGLVRSVHPP 201
PRK06190 PRK06190
enoyl-CoA hydratase; Provisional
270-428 8.43e-21

enoyl-CoA hydratase; Provisional


Pssm-ID: 235733  Cd Length: 258  Bit Score: 91.96  E-value: 8.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLiGRLSSDRRKEStriaeAIRDFVKAFIQFKKPIVV 348
Cdd:PRK06190  26 NALSAALRRALFAALAEADADDDvDVVVLTGADPAFCAGLDLKEL-GGDGSAYGAQD-----ALPNPSPAWPAMRKPVIG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK06190 100 AINGAAVTGGLELALACDILIASERARFADTHARVGILPGWGLSVRLPQKVGIGRARRMSLTGDFLDAADALRAGLVTEV 179
PRK07468 PRK07468
crotonase/enoyl-CoA hydratase family protein;
270-495 1.19e-20

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180987 [Multi-domain]  Cd Length: 262  Bit Score: 91.27  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRrkeSTRIAEAIR--DFVKAFIQFKKPI 346
Cdd:PRK07468  27 NALSARMIAELTTAARRLAADAAvRVVVLTGAGKSFCAGGDLGWMRAQMTADR---ATRIEEARRlaMMLKALNDLPKPL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  347 VVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQIlGVALANEMLFCGRKLTAQEACSRGLVS 426
Cdd:PRK07468 104 IGRIQGQAFGGGVGLISVCDVAIAVSGARFGLTETRLGLIPATISPYVVARM-GEANARRVFMSARLFDAEEAVRLGLLS 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37590660  427 QVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKECVMLKQLWSSSKGLDSLFSY 495
Cdd:PRK07468 183 RVVPAERLDAAVEAEVTPYLSCAPGAVAAAKALVRALGAPIDEAVIDATIEALADTWETEEAREGIAAF 251
PRK06210 PRK06210
enoyl-CoA hydratase; Provisional
270-446 9.04e-20

enoyl-CoA hydratase; Provisional


Pssm-ID: 180472  Cd Length: 272  Bit Score: 88.99  E-value: 9.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTriaeaIRDFVKA---------- 338
Cdd:PRK06210  28 NAWTPVMEAEVYAAMDRAEADPAvRVIVLTGAGRGFCAGADMGELQTIDPSDGRRDTD-----VRPFVGNrrpdyqtryh 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  339 -FIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQ 417
Cdd:PRK06210 103 fLTALRKPVIAAINGACAGIGLTHALMCDVRFAADGAKFTTAFARRGLIAEHGISWILPRLVGHANALDLLLSARTFYAE 182
                        170       180
                 ....*....|....*....|....*....
gi 37590660  418 EACSRGLVSQVFWPttfsQEVMLRVKEMA 446
Cdd:PRK06210 183 EALRLGLVNRVVPP----DELMERTLAYA 207
PRK06495 PRK06495
enoyl-CoA hydratase/isomerase family protein;
270-457 1.38e-19

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 168580 [Multi-domain]  Cd Length: 257  Bit Score: 88.21  E-value: 1.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCN-AATDDSKLLLLSAVGSVFCSGLDysyLIGRLS-----SDRRKESTRIaeaiRDFVKAFIQFK 343
Cdd:PRK06495  25 NALSRELRDELIAVFDEiSERPDVRVVVLTGAGKVFCAGAD---LKGRPDvikgpGDLRAHNRRT----RECFHAIRECA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  344 KPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLtpAGCSSYTFpQILGVALANEMLFCGRKLTAQEACSRG 423
Cdd:PRK06495  98 KPVIAAVNGPALGAGLGLVASCDIIVASENAVFGLPEIDVGL--AGGGKHAM-RLFGHSLTRRMMLTGYRVPAAELYRRG 174
                        170       180       190
                 ....*....|....*....|....*....|....
gi 37590660  424 LVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESK 457
Cdd:PRK06495 175 VIEACLPPEELMPEAMEIAREIASKSPLATRLAK 208
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
7-56 2.02e-19

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 81.47  E-value: 2.02e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 37590660     7 YEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEFN 56
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFK 50
PRK09245 PRK09245
crotonase/enoyl-CoA hydratase family protein;
248-431 5.16e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181723  Cd Length: 266  Bit Score: 86.95  E-value: 5.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  248 DIVVRKEEGFTHILLSSQTSDNNALT-PEIMKEVRrALCNAATDDS--KLLLLSAVGSVFCSGLDYSYLIGR-----LSS 319
Cdd:PRK09245   3 DFLLVERDGHIVTLTMNRPETRNALSdNDAVDALV-AACAAINADRsvRAVILTGAGTAFSSGGNVKDMRARvgafgGSP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  320 DRRKESTRiaEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQIL 399
Cdd:PRK09245  82 ADIRQGYR--HGIQRIPLALYNLEVPVIAAVNGPAIGAGCDLACMCDIRIASETARFAESFVKLGLIPGDGGAWLLPRII 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 37590660  400 GVALANEMLFCGRKLTAQEACSRGLVSQVFWP 431
Cdd:PRK09245 160 GMARAAEMAFTGDAIDAATALEWGLVSRVVPA 191
PLN02664 PLN02664
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
250-429 8.85e-19

enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase


Pssm-ID: 178269 [Multi-domain]  Cd Length: 275  Bit Score: 86.49  E-value: 8.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  250 VVRK--EEGFTHILLSsQTSDNNALTPEIMKEVRRALCNAATD-DSKLLLLSAVGSVFCSGLDYSYLIG----RLSSDRR 322
Cdd:PLN02664   9 IIQKspNSSVFHLNLN-RPSQRNALSLDFFTEFPKALSSLDQNpNVSVIILSGAGDHFCSGIDLKTLNSiseqSSSGDRG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  323 KESTRIAEAIR---DFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQIL 399
Cdd:PLN02664  88 RSGERLRRKIKflqDAITAIEQCRKPVIAAIHGACIGGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTLQRLPSIV 167
                        170       180       190
                 ....*....|....*....|....*....|
gi 37590660  400 GVALANEMLFCGRKLTAQEACSRGLVSQVF 429
Cdd:PLN02664 168 GYGNAMELALTGRRFSGSEAKELGLVSRVF 197
PRK06023 PRK06023
crotonase/enoyl-CoA hydratase family protein;
270-474 8.99e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 168351  Cd Length: 251  Bit Score: 85.61  E-value: 8.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKEStriaeAIRDFVKAFIQFKKPIVV 348
Cdd:PRK06023  28 NAITRAMYATMAKALKAADADDAiRAHVFLGTEGCFSAGNDMQDFLAAAMGGTSFGS-----EILDFLIALAEAEKPIVS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK06023 103 GVDGLAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALVPEAGSSLLAPRLMGHQRAFALLALGEGFSAEAAQEAGLIWKI 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 37590660  429 FWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEK 474
Cdd:PRK06023 183 VDEEAVEAETLKAAEELAAKPPQALQIARDLMRGPREDILARIDEE 228
CHROMO smart00298
Chromatin organization modifier domain;
7-55 2.68e-18

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 78.41  E-value: 2.68e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 37590660      7 YEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNY 50
PRK08140 PRK08140
enoyl-CoA hydratase; Provisional
270-428 5.25e-18

enoyl-CoA hydratase; Provisional


Pssm-ID: 236163  Cd Length: 262  Bit Score: 83.81  E-value: 5.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDSKLLLLSAVGSVFCSGLDysylIGRLSSDRRKESTRIAEAIRDFVKAFIQ----FKKP 345
Cdd:PRK08140  26 NSFTREMHRELREALDQVEDDGARALLLTGAGRGFCAGQD----LADRDVTPGGAMPDLGESIETFYNPLVRrlraLPLP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  346 IVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLV 425
Cdd:PRK08140 102 VIAAVNGVAAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLPRLVGMARALGLALLGEKLSAEQAEQWGLI 181

                 ...
gi 37590660  426 SQV 428
Cdd:PRK08140 182 WRV 184
PRK08258 PRK08258
enoyl-CoA hydratase family protein;
270-428 1.48e-17

enoyl-CoA hydratase family protein;


Pssm-ID: 181329  Cd Length: 277  Bit Score: 82.71  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVR---RALCNAatDDSKLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAIRDFVKAFIQFKKPI 346
Cdd:PRK08258  39 NPLTFESYAELRdlfRELVYA--DDVKAVVLTGAGGNFCSGGDVHEIIGPLTKMDMPELLAFTRMTGDLVKAMRACPQPI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  347 VVAINGPALGLGASILPLCDIVWASEKAwfQTPYATIRLTPAGC---SSYTFPQILGVALANEMLFCGRKLTAQEACSRG 423
Cdd:PRK08258 117 IAAVDGVCAGAGAILAMASDLRLGTPSA--KTAFLFTRVGLAGAdmgACALLPRIIGQGRASELLYTGRSMSAEEGERWG 194

                 ....*
gi 37590660  424 LVSQV 428
Cdd:PRK08258 195 FFNRL 199
PRK07659 PRK07659
enoyl-CoA hydratase; Provisional
270-475 2.60e-17

enoyl-CoA hydratase; Provisional


Pssm-ID: 236073 [Multi-domain]  Cd Length: 260  Bit Score: 81.62  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDSKLLLLSAVGSVFCSGLDYSYLigrLSSDRRKESTRIAEAIRDFVKAFIQFKKPIVVA 349
Cdd:PRK07659  28 NALDEPMLKELLQALKEVAESSAHIVVLRGNGRGFSAGGDIKMM---LSSNDESKFDGVMNTISEIVVTLYTMPKLTISA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  350 INGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQVF 429
Cdd:PRK07659 105 IHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGLIPDGGGHFFLQKRVGENKAKQIIWEGKKLSATEALDLGLIDEVI 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 37590660  430 wPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKE 475
Cdd:PRK07659 185 -GGDFQTAAKQKISEWLQKPLKAMIETKQIYCELNRSQLEQVLQLE 229
PRK05809 PRK05809
short-chain-enoyl-CoA hydratase;
246-457 6.62e-17

short-chain-enoyl-CoA hydratase;


Pssm-ID: 180270 [Multi-domain]  Cd Length: 260  Bit Score: 80.56  E-value: 6.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  246 FRDIVVRKEEGFTHILLSSQTSdNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGS-VFCSGLDysylIGRLSSDRRK 323
Cdd:PRK05809   3 LKNVILEKEGHIAVVTINRPKA-LNALNSETLKELDTVLDDIENDDNvYAVILTGAGEkAFVAGAD----ISEMKDLNEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  324 ESTRIAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVAL 403
Cdd:PRK05809  78 EGRKFGLLGNKVFRKLENLDKPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGITPGFGGTQRLARIVGPGK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 37590660  404 ANEMLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESK 457
Cdd:PRK05809 158 AKELIYTGDMINAEEALRIGLVNKVVEPEKLMEEAKALANKIAANAPIAVKLCK 211
PRK07854 PRK07854
enoyl-CoA hydratase; Provisional
270-428 1.59e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 236115 [Multi-domain]  Cd Length: 243  Bit Score: 78.91  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDSKLLLLSAVGSVFCSGLDysyligrLSSDRRKEStrIAEAIRDFVKAFIQFKKPIVVA 349
Cdd:PRK07854  22 NALNAELCEELREAVRKAVDESARAIVLTGQGTVFCAGAD-------LSGDVYADD--FPDALIEMLHAIDAAPVPVIAA 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37590660  350 INGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK07854  93 INGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDNWTIRRLSSLVGGGRARAMLLGAEKLTAEQALATGMANRI 171
PRK09674 PRK09674
enoyl-CoA hydratase-isomerase; Provisional
270-457 2.08e-16

enoyl-CoA hydratase-isomerase; Provisional


Pssm-ID: 182026 [Multi-domain]  Cd Length: 255  Bit Score: 79.04  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSY-----LIGRLSSDRRKESTRIAeairdfvkafiQFK 343
Cdd:PRK09674  24 NALNNALLTQLVNELEAAATDTSiGVCVITGNARFFAAGADLNEmaekdLAATLNDPRPQLWQRLQ-----------AFN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  344 KPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRG 423
Cdd:PRK09674  93 KPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGGTQRLIRSVGKSLASQMVLTGESITAQQAQQAG 172
                        170       180       190
                 ....*....|....*....|....*....|....
gi 37590660  424 LVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESK 457
Cdd:PRK09674 173 LVSEVFPPELTLERALQLASKIARHSPLALRAAK 206
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-55 3.28e-16

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349324  Cd Length: 57  Bit Score: 72.76  E-value: 3.28e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 37590660   7 YEVE-----RIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18968   2 YEVEvilaaRVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
PRK05870 PRK05870
enoyl-CoA hydratase; Provisional
270-428 3.61e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 180298  Cd Length: 249  Bit Score: 78.23  E-value: 3.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATD-DSKLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAirdFVkAFIQFKKPIVV 348
Cdd:PRK05870  25 NAVTAEMSAQLRAAVAAAEADpDVHALVVTGAGKAFCAGADLTALGAAPGRPAEDGLRRIYDG---FL-AVASCPLPTIA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK05870 101 AVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLGLHPGGGATWMLQRAVGPQVARAALLFGMRFDAEAAVRHGLALMV 180
PRK07799 PRK07799
crotonase/enoyl-CoA hydratase family protein;
248-428 5.86e-16

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181122 [Multi-domain]  Cd Length: 263  Bit Score: 77.84  E-value: 5.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  248 DIVVRKEeGFTHILLSSQTSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKEST 326
Cdd:PRK07799   6 HALVEQR-GHTLIVTMNRPEARNALSTEMLRIMVDAWDRVDNDPDiRSCILTGAGGAFCAGMDLKAATKKPPGDSFKDGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  327 RIAEAIRDFVKAFiQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANE 406
Cdd:PRK07799  85 YDPSRIDALLKGR-RLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLFPMGGSAVRLVRQIPYTVACD 163
                        170       180
                 ....*....|....*....|..
gi 37590660  407 MLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK07799 164 LLLTGRHITAAEAKEIGLIGHV 185
PRK07658 PRK07658
enoyl-CoA hydratase; Provisional
249-475 1.72e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 181070 [Multi-domain]  Cd Length: 257  Bit Score: 76.21  E-value: 1.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  249 IVVRKEEGFTHILLSSQTSdnNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDysylIGRLSS-DRRKEST 326
Cdd:PRK07658   4 LSVRVEDHVAVITLNHPPA--NALSSQVLHELSELLDQVEKDDNvRVVVIHGEGRFFSAGAD----IKEFTSvTEAEQAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  327 RIAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANE 406
Cdd:PRK07658  78 ELAQLGQVTFERVEKFSKPVIAAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGFAGTQRLPRYVGKAKALE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37590660  407 MLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLKSVLEEVNEKE 475
Cdd:PRK07658 158 MMLTSEPITGAEALKWGLVNGVFPEETLLDDAKKLAKKIAGKSPATTRAVLELLQTTKSSSYYEGVKRE 226
PLN02888 PLN02888
enoyl-CoA hydratase
270-470 3.94e-15

enoyl-CoA hydratase


Pssm-ID: 215480  Cd Length: 265  Bit Score: 75.56  E-value: 3.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYligrlSSDRRKESTRIAEAirDFVKAFIQFKKPIVV 348
Cdd:PLN02888  32 NALTRPMMVELAAAFKRLDEDDSvKVIILTGSGRAFCSGVDLTA-----AEEVFKGDVKDVET--DPVAQMERCRKPIIG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PLN02888 105 AINGFAITAGFEIALACDILVASRGAKFIDTHAKFGIFPSWGLSQKLSRIIGANRAREVSLTAMPLTAETAERWGLVNHV 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 37590660  429 FWPTtfsqEVMLRVKEMAscSAVVLEESKCLVRsfLKSVLEE 470
Cdd:PLN02888 185 VEES----ELLKKAREVA--EAIIKNNQGMVLR--YKSVIND 218
PRK07657 PRK07657
enoyl-CoA hydratase; Provisional
270-446 5.60e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 181069 [Multi-domain]  Cd Length: 260  Bit Score: 74.77  E-value: 5.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATD-DSKLLLLSAVG-SVFCSGLDysyligrLSSDRRKESTRIAEA---IRDFVKAFIQFKK 344
Cdd:PRK07657  26 NALSLALLEELQNILTQINEEaNVRVVILTGAGeKAFCAGAD-------LKERAGMNEEQVRHAvslIRTTMEMVEQLPQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  345 PIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGL 424
Cdd:PRK07657  99 PVIAAINGIALGGGLELALACDFRIAAESASLGLTETTLAIIPGAGGTQRLPRLIGVGRAKELIYTGRRISAQEAKEIGL 178
                        170       180
                 ....*....|....*....|..
gi 37590660  425 VSQVFWPttfsQEVMLRVKEMA 446
Cdd:PRK07657 179 VEFVVPA----HLLEEKAIEIA 196
PLN02600 PLN02600
enoyl-CoA hydratase
270-425 1.03e-14

enoyl-CoA hydratase


Pssm-ID: 178210 [Multi-domain]  Cd Length: 251  Bit Score: 74.07  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDSK--LLLLSAVGSVFCSGLDYSyligrlssDRRK----ESTRIAEAIRDFVKAFIQFK 343
Cdd:PLN02600  17 NAIGKEMLRGLRSAFEKIQADASArvVMLRSSVPGVFCAGADLK--------ERRKmspsEVQKFVNSLRSTFSSLEALS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  344 KPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRG 423
Cdd:PLN02600  89 IPTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVGRSRAKELIFTGRRIGAREAASMG 168

                 ..
gi 37590660  424 LV 425
Cdd:PLN02600 169 LV 170
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
7-55 1.09e-14

chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1 (Tf2-1), and similar proteins. It belongs to the Ty3/gypsy family of long terminal repeat (LTR) retrotransposons. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349329  Cd Length: 50  Bit Score: 68.04  E-value: 1.09e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18973   1 YVVEAILDNKR-RKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKY 48
PRK07827 PRK07827
enoyl-CoA hydratase family protein;
248-460 4.28e-14

enoyl-CoA hydratase family protein;


Pssm-ID: 236109 [Multi-domain]  Cd Length: 260  Bit Score: 72.41  E-value: 4.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  248 DIVVRKEE--GFTHILLSSqTSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKE 324
Cdd:PRK07827   5 DTLVRYAVdgGVATLTLDS-PHNRNALSARLVAQLHDGLRAAAADPAvRAVVLTHTGGTFCAGADLSEAGGGGGDPYDAA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  325 STRiAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVAlA 404
Cdd:PRK07827  84 VAR-AREMTALLRAIVELPKPVIAAIDGHVRAGGFGLVGACDIVVAGPESTFALTEARIGVAPAIISLTLLPRLSPRA-A 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 37590660  405 NEMLFCGRKLTAQEACSRGLVSQVFWPTTfsQEVMLRVKEMASCSAVVLEESKCLV 460
Cdd:PRK07827 162 ARYYLTGEKFGAAEAARIGLVTAAADDVD--AAVAALLADLRRGSPQGLAESKALT 215
PRK05995 PRK05995
enoyl-CoA hydratase; Provisional
270-428 6.15e-14

enoyl-CoA hydratase; Provisional


Pssm-ID: 235664 [Multi-domain]  Cd Length: 262  Bit Score: 71.88  E-value: 6.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLD---------YSYligrlsSDRRKESTRIAEAIRdfvkAF 339
Cdd:PRK05995  26 NAFNETVIAELTAAFRALDADDSvRAVVLAGAGKAFCAGADlnwmkkmagYSD------DENRADARRLADMLR----AI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  340 IQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFpQILGVALANEMLFCGRKLTAQEA 419
Cdd:PRK05995  96 YRCPKPVIARVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLGLIPATISPYVI-RAMGERAARRYFLTAERFDAAEA 174

                 ....*....
gi 37590660  420 CSRGLVSQV 428
Cdd:PRK05995 175 LRLGLVHEV 183
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
6-55 9.09e-14

chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), a component of the RanBPM-containing large protein complex, binds methylated H3K9. This may in turn recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promoting tumor cell motility and invasion. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349283  Cd Length: 51  Bit Score: 65.77  E-value: 9.09e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 37590660   6 LYEVERIVDKrKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18633   1 VFEVEKILDM-KTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEF 49
PRK06494 PRK06494
enoyl-CoA hydratase; Provisional
270-470 1.10e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 180591 [Multi-domain]  Cd Length: 259  Bit Score: 70.84  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDSK-LLLLSAVGS-VFCSGLDYSYLIGRLssDRRKESTRIAEAIRDFvkafiQFKKPIV 347
Cdd:PRK06494  26 NALHLDAHFELEEVFDDFAADPEQwVAIVTGAGDkAFSAGNDLKEQAAGG--KRGWPESGFGGLTSRF-----DLDKPII 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  348 VAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQ 427
Cdd:PRK06494  99 AAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGLKRAMGMILTGRRVTAREGLELGFVNE 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 37590660  428 VfwptTFSQEVMLRVKEMA----SCSAVVLEESKCLVRSFLKSVLEE 470
Cdd:PRK06494 179 V----VPAGELLAAAERWAddilACSPLSIRASKQAVYRGLEVSLEE 221
PRK07110 PRK07110
polyketide biosynthesis enoyl-CoA hydratase; Validated
254-446 1.25e-13

polyketide biosynthesis enoyl-CoA hydratase; Validated


Pssm-ID: 235936  Cd Length: 249  Bit Score: 70.77  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  254 EEGFTHILLSSQTSDNnALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIgRLSSDRRKestrIAEAi 332
Cdd:PRK07110  12 EEGIAQVTMQDRVNKN-AFSDELCDQLHEAFDTIAQDPRyKVVILTGYPNYFATGGTQEGLL-SLQTGKGT----FTEA- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  333 rDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGR 412
Cdd:PRK07110  85 -NLYSLALNCPIPVIAAMQGHAIGGGLVLGLYADIVVLSRESVYTANFMKYGFTPGMGATAILPEKLGLALGQEMLLTAR 163
                        170       180       190
                 ....*....|....*....|....*....|....
gi 37590660  413 KLTAQEACSRGlvsqVFWPTTFSQEVMLRVKEMA 446
Cdd:PRK07110 164 YYRGAELKKRG----VPFPVLPRAEVLEKALELA 193
PRK05864 PRK05864
enoyl-CoA hydratase; Provisional
270-426 1.86e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 168278 [Multi-domain]  Cd Length: 276  Bit Score: 70.63  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYL-----IGRLSsdRRKESTRIAEAIRDFVKAFIQFK 343
Cdd:PRK05864  32 NSMAFDVMVPLKEALAEVSYDNSvRVVVLTGAGRGFSSGADHKSAgvvphVEGLT--RPTYALRSMELLDDVILALRRLH 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  344 KPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCS-SYTFPQILGVALANEMLFCGRKLTAQEACSR 422
Cdd:PRK05864 110 QPVIAAVNGPAIGGGLCLALAADIRVASSSAYFRAAGINNGLTASELGlSYLLPRAIGSSRAFEIMLTGRDVDAEEAERI 189

                 ....
gi 37590660  423 GLVS 426
Cdd:PRK05864 190 GLVS 193
PRK03580 PRK03580
crotonobetainyl-CoA hydratase;
344-473 2.34e-13

crotonobetainyl-CoA hydratase;


Pssm-ID: 179599 [Multi-domain]  Cd Length: 261  Bit Score: 70.11  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  344 KPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRG 423
Cdd:PRK03580  95 KPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRLPPAIANEMVMTGRRMDAEEALRWG 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 37590660  424 LVSQVFwPttfSQEVMLRVKEMAScsavVLEESKCLVRSFLKSVLEEVNE 473
Cdd:PRK03580 175 IVNRVV-P---QAELMDRARELAQ----QLVNSAPLAIAALKEIYRETSE 216
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
7-55 4.45e-13

chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. HP1a is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. In Drosophila, there are at least five HP1 family proteins, this subgroup includes the CD of Drosophila melanogaster HP1a.


Pssm-ID: 349300  Cd Length: 50  Bit Score: 63.51  E-value: 4.45e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEF 55
Cdd:cd18653   2 YAVEKICDRRV-RKGKVEYYLKWKGYPETENTWEPEEN-LDCQDLIQQY 48
PLN02921 PLN02921
naphthoate synthase
241-449 4.51e-13

naphthoate synthase


Pssm-ID: 178509 [Multi-domain]  Cd Length: 327  Bit Score: 70.20  E-value: 4.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  241 ESNCRFRDIVVRK--EEGFTHILLSsQTSDNNALTPEIMKEVRRALcNAATDDSK---LLLLSAVGSVFCSGLDYS---- 311
Cdd:PLN02921  59 GSGKEFTDIIYEKavGEGIAKITIN-RPERRNAFRPRTVKELQRAF-NDARDDSSvgvIILTGKGTKAFCSGGDQAvrgk 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  312 --YL----IGRLSsdrrkestriaeaIRDFVKAFIQFKKPIVVAINGPALGlGASILPL-CDIVWASEKAWFQTPYATIR 384
Cdd:PLN02921 137 dgYVgpddAGRLN-------------VLDLQIQIRRLPKPVIAMVAGYAVG-GGHILHMvCDLTIAADNAVFGQTGPKVG 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37590660  385 LTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCS 449
Cdd:PLN02921 203 SFDAGYGSSIMARLVGQKKAREMWFLARFYTASEALKMGLVNTVVPLDELEGETVKWCREILRNS 267
PRK06127 PRK06127
enoyl-CoA hydratase; Provisional
249-465 5.75e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 235705  Cd Length: 269  Bit Score: 68.96  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  249 IVVRKEEGFTHILLSsQTSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGS-VFCSGLDYSYLiGRLSSDRrKEST 326
Cdd:PRK06127  13 LLAEKTGGLGRITFN-NPARHNAMSLDMWEALPQALAAAEDDDAiRVVVLTGAGEkAFVSGADISQF-EESRSDA-EAVA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  327 RIAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANE 406
Cdd:PRK06127  90 AYEQAVEAAQAALADYAKPTIACIRGYCIGGGMGIALACDIRIAAEDSRFGIPAARLGLGYGYDGVKNLVDLVGPSAAKD 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 37590660  407 MLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVRSFLK 465
Cdd:PRK06127 170 LFYTARRFDAAEALRIGLVHRVTAADDLETALADYAATIAGNAPLTLRAAKRAIAELLK 228
PRK07260 PRK07260
enoyl-CoA hydratase; Provisional
270-428 1.32e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 180910 [Multi-domain]  Cd Length: 255  Bit Score: 67.84  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAIRDFVKAFIQFKKPIVV 348
Cdd:PRK07260  24 NGFNIPMCQEILEALRLAEEDPSvRFLLINANGKVFSVGGDLVEMKRAVDEDDVQSLVKIAELVNEISFAIKQLPKPVIM 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK07260 104 CVDGAVAGAAANMAVAADFCIASTKTKFIQAFVGVGLAPDAGGLFLLTRAIGLNRATHLAMTGEALTAEKALEYGFVYRV 183
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
7-55 1.86e-12

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349281  Cd Length: 50  Bit Score: 61.68  E-value: 1.86e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEF 55
Cdd:cd18631   2 YVVEKVLDRRV-VKGKVEYLLKWKGYPDEDNTWEPEEN-LDCPDLIAEF 48
PRK05980 PRK05980
crotonase/enoyl-CoA hydratase family protein;
248-428 2.08e-12

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180335 [Multi-domain]  Cd Length: 260  Bit Score: 67.09  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  248 DIVVRKEEGFTHILLSSQTSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGS-VFCSGLDysylIGRLSSDRRKES 325
Cdd:PRK05980   3 DTVLIEIRDGIALLTLNRPEKLNALNYALIDRLLARLDAIEVDESvRAVILTGAGDrAFSAGAD----IHEFSASVAAGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  326 TriaEAIRDFVKA-------FIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQI 398
Cdd:PRK05980  79 D---VALRDFVRRgqamtarLEAFPKPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPTFGGTQRLPRL 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 37590660  399 LGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK05980 156 AGRKRALELLLTGDAFSAERALEIGLVNAV 185
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
7-55 3.28e-12

chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in chromodomain of Drosophila melanogaster chromator (also known as Chriz/Chro) chromodomain protein, and similar proteins. Chromator is a nuclear protein that plays a role in proper spindle dynamics during mitosis. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349290  Cd Length: 52  Bit Score: 61.15  E-value: 3.28e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 37590660   7 YEVERIVDKRKNKKGK-WEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18640   1 EPVEKIVAKRFNPRKKtWEYLVKWENRSHHENTWEPMANLERCKYLLQMF 50
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
7-56 4.58e-12

chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This subgroup includes the N-terminal CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 (HP1)-like protein from Entamoeba histolytica, and similar proteins. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349288  Cd Length: 52  Bit Score: 60.73  E-value: 4.58e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   7 YEVERIVdKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHL-LHCEEFIDEFN 56
Cdd:cd18638   2 FEVEKIV-KKKTVKGGTEYFVKWKGYSAKENTWETEDNLeKSYKEMIDEFE 51
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
6-55 5.23e-12

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; uncharacterized subgroup; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349316  Cd Length: 51  Bit Score: 60.65  E-value: 5.23e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 37590660   6 LYEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEF 55
Cdd:cd18960   1 VFVVERILDKRLGRNGGEEFLIKWQGFPESDSSWEPREN-LQCDEMLEEF 49
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
7-55 5.63e-12

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349285  Cd Length: 57  Bit Score: 60.79  E-value: 5.63e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37590660   7 YEVERIVD------KRKNKKGkWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18635   2 FEVEKLVGicygdpKKTGERG-LYFKVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
PRK06142 PRK06142
crotonase/enoyl-CoA hydratase family protein;
270-457 5.90e-12

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235714  Cd Length: 272  Bit Score: 66.15  E-value: 5.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNA-ATDDSKLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAIRDFVK-------AFIQ 341
Cdd:PRK06142  28 NAMNPAFWSELPEIFRWLdADPEVRAVVLSGSGKHFSYGIDLPAMAGVFGQLGKDGLARPRTDLRREILrlqaainAVAD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  342 FKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACS 421
Cdd:PRK06142 108 CRKPVIAAVQGWCIGGGVDLISACDMRYASADAKFSVREVDLGMVADVGSLQRLPRIIGDGHLRELALTGRDIDAAEAEK 187
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 37590660  422 RGLVSQVFW-PTTFSQEVMLRVKEMASCSAVVLEESK 457
Cdd:PRK06142 188 IGLVNRVYDdADALLAAAHATAREIAAKSPLAVRGTK 224
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-55 1.00e-11

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349320  Cd Length: 54  Bit Score: 59.65  E-value: 1.00e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 37590660   7 YEVERIVDKR---KNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18964   1 FFVERIIGRRpsaRDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDF 52
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
4-55 1.88e-11

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 59.02  E-value: 1.88e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 37590660   4 GDLYEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHLLHcEEFIDEF 55
Cdd:cd18644   1 DLVYAAEKILKKRV-RKGKVEYLVKWKGWSNKHNTWEPEENILD-RRLIEIF 50
PRK06144 PRK06144
enoyl-CoA hydratase; Provisional
270-461 2.08e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 180424 [Multi-domain]  Cd Length: 262  Bit Score: 64.24  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEiMKEVRRALCNAATDDSK---LLLLSAVGSVFCSGLDysylIGRLSSDRRKESTRIAEAIRDFVKAFI-QFKKP 345
Cdd:PRK06144  30 NAMTWA-MYEGLAEICEAIAADPSiraVVLRGAGDKAFVAGTD----IAQFRAFSTAEDAVAYERRIDRVLGALeQLRVP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  346 IVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATirlTPAGC---SSYT-FPQILGVALANEMLFCGRKLTAQEACS 421
Cdd:PRK06144 105 TIAAIAGACVGGGAAIAAACDLRIATPSARFGFPIAR---TLGNClsmSNLArLVALLGAARVKDMLFTARLLEAEEALA 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 37590660  422 RGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVR 461
Cdd:PRK06144 182 AGLVNEVVEDAALDARADALAELLAAHAPLTLRATKEALR 221
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
7-55 2.19e-11

chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Trichosporon asahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349336  Cd Length: 56  Bit Score: 59.12  E-value: 2.19e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   7 YEVERIVDKRKNKKGK--WEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18980   4 YEVEAILDHKVDRRYRdpNFYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
PRK08138 PRK08138
enoyl-CoA hydratase; Provisional
270-428 2.52e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 236162 [Multi-domain]  Cd Length: 261  Bit Score: 63.92  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTpeimKEVRRALCNAAT-----DDSKLLLLSAVGSVFCSGLDYSYLIGRLSSD---RRKEstRIAEAIRdfvkafiQ 341
Cdd:PRK08138  30 NALN----MEVRQQLAEHFTelsedPDIRAIVLTGGEKVFAAGADIKEFATAGAIEmylRHTE--RYWEAIA-------Q 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  342 FKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACS 421
Cdd:PRK08138  97 CPKPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGLMPGAGGTQRLVRAVGKFKAMRMALTGCMVPAPEALA 176

                 ....*..
gi 37590660  422 RGLVSQV 428
Cdd:PRK08138 177 IGLVSEV 183
PRK06072 PRK06072
enoyl-CoA hydratase; Provisional
249-425 2.53e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 168377 [Multi-domain]  Cd Length: 248  Bit Score: 63.64  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  249 IVVRKEEGFTHILLSsQTSDNNALTPEIMKEVRRALCNAATD-DSKLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTR 327
Cdd:PRK06072   2 IKVESREGYAIVTMS-RPDKLNALNLEMRNEFISKLKQINADpKIRVVIVTGEGRAFCVGADLSEFAPDFAIDLRETFYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  328 IAEAIRDFVKAFIQfkkpivvAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVAlANEM 407
Cdd:PRK06072  81 IIREIRFSDKIYIS-------AINGVTAGACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYFLLKLTGQR-FYEI 152
                        170
                 ....*....|....*...
gi 37590660  408 LFCGRKLTAQEACSRGLV 425
Cdd:PRK06072 153 LVLGGEFTAEEAERWGLL 170
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
5-56 2.67e-11

chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizopus microsporus putative DDE transposases, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349334  Cd Length: 52  Bit Score: 58.48  E-value: 2.67e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 37590660   5 DLYEVERIVDKRKNKKGKwEYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEFN 56
Cdd:cd18978   2 ESYEVEKIINHRGEKNRR-KYLVKWKGYDDTDNSWVTQED-FNDKDMIDEYE 51
PRK05862 PRK05862
enoyl-CoA hydratase; Provisional
270-470 4.26e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 180295 [Multi-domain]  Cd Length: 257  Bit Score: 63.14  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDskllllsAVGSVFCSGLDYSYLIGrlsSDrrkestrIAE-AIRDFVKAFIQ------- 341
Cdd:PRK05862  26 NALNDALMDELGAALAAFDADE-------GIGAIVITGSEKAFAAG---AD-------IKEmADLSFMDVYKGdyitnwe 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  342 ----FKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQ 417
Cdd:PRK05862  89 kvarIRKPVIAAVAGYALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGMGGSQRLTRAVGKAKAMDLCLTGRMMDAA 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 37590660  418 EACSRGLVSQVFWPTTFSQEVMLRVKEMASCS-AVVLEESKCLVRSFlKSVLEE 470
Cdd:PRK05862 169 EAERAGLVSRVVPADKLLDEALAAATTIASFSlPAVMMAKEAVNRAY-ETTLAE 221
PRK08139 PRK08139
enoyl-CoA hydratase; Validated
270-459 4.29e-11

enoyl-CoA hydratase; Validated


Pssm-ID: 181249  Cd Length: 266  Bit Score: 63.42  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDysylIGRLSSDRRKES-TRIAEAIRDFVKAFIQFKKPIV 347
Cdd:PRK08139  33 NALSEAMLAALQAALDAIAADPSvRVVVLAAAGKAFCAGHD----LKEMRAARGLAYfRALFARCSRVMQAIVALPQPVI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  348 VAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTpagCSSytfPqilGVAL--------ANEMLFCGRKLTAQEA 419
Cdd:PRK08139 109 ARVHGIATAAGCQLVASCDLAVAADTARFAVPGVNIGLF---CST---P---MVALsrnvprkqAMEMLLTGEFIDAATA 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 37590660  420 CSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCL 459
Cdd:PRK08139 180 REWGLVNRVVPADALDAAVARLAAVIAAKSPAAVRIGKEA 219
PRK08150 PRK08150
crotonase/enoyl-CoA hydratase family protein;
270-425 1.48e-10

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181254  Cd Length: 255  Bit Score: 61.57  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALcNAATDDSKLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAirdFVKafIQFKK-PIVV 348
Cdd:PRK08150  24 NALNDGLIAALRAAF-ARLPEGVRAVVLHGEGDHFCAGLDLSELRERDAGEGMHHSRRWHRV---FDK--IQYGRvPVIA 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590660  349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLV 425
Cdd:PRK08150  98 ALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGIFVGGGGSVRVPRLIGVARMTDMMLTGRVYDAQEGERLGLA 174
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
7-55 2.26e-10

chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog beta (also known as HP1beta, CBX1, and chromobox 1), and related proteins. HP1beta is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta, and HP1gamma (also known as Cbx3).


Pssm-ID: 349297  Cd Length: 50  Bit Score: 56.11  E-value: 2.26e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEF 55
Cdd:cd18650   2 YVVEKVLDRRV-VKGKVEYLLKWKGFSDEDNTWEPEEN-LDCPDLIAEF 48
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
6-45 3.05e-10

chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of chromodomain-containing protein 1 (CHp1), and similar proteins. Chp1 is needed for RNA interference-dependent heterochromatin formation in fission yeast. Chp1 is a member of the RNA-induced transcriptional silencing (RITS) complex which maintains the heterochromatin regions. The chromodomain of the Chp1 component binds the histone H3 lysine 9 methylated tail (H3K9me) and the core of the nucleosome. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349286  Cd Length: 52  Bit Score: 55.53  E-value: 3.05e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 37590660   6 LYEVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHL 45
Cdd:cd18636   1 VYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNL 40
PRK11423 PRK11423
methylmalonyl-CoA decarboxylase; Provisional
270-428 3.18e-10

methylmalonyl-CoA decarboxylase; Provisional


Pssm-ID: 236908 [Multi-domain]  Cd Length: 261  Bit Score: 60.81  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDSKLLLLSA-VGS-VFCSGLDysylIGRLSSDRR------KESTRIAEAIRdfvkafiQ 341
Cdd:PRK11423  26 NALSKVLIDDLMQALSDLNRPEIRVVILRApSGSkVWSAGHD----IHELPSGGRdplsydDPLRQILRMIQ-------K 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  342 FKKPIVVAINGPALGlGASILPL-CDIVWAsekawfqTPYATIRLTPAGCS-SY------TFPQILGVALANEMLFCGRK 413
Cdd:PRK11423  95 FPKPVIAMVEGSVWG-GAFELIMsCDLIIA-------ASTSTFAMTPANLGvPYnlsgilNFTNDAGFHIVKEMFFTASP 166
                        170
                 ....*....|....*
gi 37590660  414 LTAQEACSRGLVSQV 428
Cdd:PRK11423 167 ITAQRALAVGILNHV 181
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
7-49 4.16e-10

chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Hypsizygus marmoreus TY3B-I_0 protein, a putative TY3/gypsy retrotransposon polyprotein, and similar proteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349326  Cd Length: 49  Bit Score: 55.14  E-value: 4.16e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 37590660   7 YEVERIVDKRKNKKGkWEYLIRWKGYGSTEDTWEPEHHLLHCE 49
Cdd:cd18970   1 FFVERILDERRRGRG-WQYLVRWLGYGPSDDSWLPRRELEECE 42
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
7-55 4.59e-10

chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349298  Cd Length: 50  Bit Score: 55.00  E-value: 4.59e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEF 55
Cdd:cd18651   2 YVVEKVLDRRV-VKGQVEYLLKWKGFSEEHNTWEPEKN-LDCPELISEF 48
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
7-55 7.42e-10

N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of cryptic loci regulator 4 (Clr4), a histone H3 lysine methyltransferase which targets H3K9. Clr4 regulates silencing and switching at the mating-type loci and affects chromatin structure at centromeres. Clr4 is a catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349282  Cd Length: 55  Bit Score: 54.43  E-value: 7.42e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 37590660   7 YEVERIVD-KRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18632   2 YEVEKIVDeKTDRNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKW 51
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
260-431 2.36e-09

fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).


Pssm-ID: 131494 [Multi-domain]  Cd Length: 737  Bit Score: 59.85  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   260 ILLSSQTSDNNALTPEIMKEVRRALCNAATDDS--KLLLLSAVGSVFCSGLDysylIGRLSSDRR-KESTRIAEAIRDFV 336
Cdd:TIGR02441  26 VKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD----IQMIAACKTaQEVTQLSQEGQEMF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660   337 KAFIQFKKPIVVAINGPALGLGASILPLCD--IVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKL 414
Cdd:TIGR02441 102 ERIEKSQKPIVAAISGSCLGGGLELALACHyrIATKDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGVPAALDMMLTGKKI 181
                         170
                  ....*....|....*..
gi 37590660   415 TAQEACSRGLVSQVFWP 431
Cdd:TIGR02441 182 RADRAKKMGIVDQLVDP 198
PRK06563 PRK06563
crotonase/enoyl-CoA hydratase family protein;
270-489 2.41e-09

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180625 [Multi-domain]  Cd Length: 255  Bit Score: 58.05  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSsdrrKESTRIAEAIRD-FVKAFIQFKKPIV 347
Cdd:PRK06563  21 NAFDSAMLDDLALALGEYEADDElRVAVLFAHGEHFTAGLDLADVAPKLA----AGGFPFPEGGIDpWGTVGRRLSKPLV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  348 VAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVsq 427
Cdd:PRK06563  97 VAVQGYCLTLGIELMLAADIVVAADNTRFAQLEVQRGILPFGGATLRFPQAAGWGNAMRYLLTGDEFDAQEALRLGLV-- 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590660  428 vfwpttfsQEVMLRVKEMAscSAVVLEESKCL-----VRSFLKSVLEEVNEKECVMLKQLWSSSKGL 489
Cdd:PRK06563 175 --------QEVVPPGEQLE--RAIELAERIARaaplgVQATLASARAAVREGEAAAAAQLPPELRPL 231
PRK09076 PRK09076
enoyl-CoA hydratase; Provisional
270-428 3.02e-09

enoyl-CoA hydratase; Provisional


Pssm-ID: 236373 [Multi-domain]  Cd Length: 258  Bit Score: 57.62  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALC--NAATDDSKLLLLSAVGSVFCSGLDysyLIGRLSSDRrkesTRIAEAIRDFVKAF---IQFKK 344
Cdd:PRK09076  24 NTWTADSLQALKQLVLelNADKDVYALVITGDGEKFFSAGAD---LNLFADGDK----AVAREMARRFGEAFealSAFRG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  345 PIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGL 424
Cdd:PRK09076  97 VSIAAINGYAMGGGLECALACDIRIAEEQAQMALPEASVGLLPCAGGTQNLPWLVGEGWAKRMILCGERVDAATALRIGL 176

                 ....
gi 37590660  425 VSQV 428
Cdd:PRK09076 177 VEEV 180
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
7-55 3.33e-09

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349330  Cd Length: 50  Bit Score: 52.48  E-value: 3.33e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18974   1 WEVEEIVDEKM-IDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSY 48
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
7-56 4.06e-09

chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in uncharacterized putative retrotransposon proteins, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349332  Cd Length: 51  Bit Score: 52.57  E-value: 4.06e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHLLH-CEEFIDEFN 56
Cdd:cd18976   1 YIVESLLDRRK-VRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAYD 50
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
7-55 4.42e-09

chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a structural and functional homolog of mammalian HP1 (heterochromatin protein 1) and is involved in the chromatin structure by binding to centromeres, telomeres, and the silent mating-type locus. Swi6 contains a N-terminal chromo (CHRromatin Organization MOdifier) domain and a C-terminal chromo shadow domain (CSD). Swi6 binds histone H3 tails methylated at Lys- and the cohesion subunit Psc3, leading to silencing the genes and sister chromatid cohesion. It is also involved in the repression of the silent mating-type loci MAT2 and MAT3. Swi6 may compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes. chromodomains mediate the interaction of the heterochromatin with other heterochromatin proteins, thereby affecting chromatin structure (e.g. Drosophila and human heterochromatin protein (HP1) and mammalian modifier 1 and modifier 2). CSDs have only been found in proteins that also possess a chromodomain.


Pssm-ID: 349287  Cd Length: 54  Bit Score: 52.51  E-value: 4.42e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   7 YEVERIVDKRKNKKGK-WEYLIRWKGYGSTED-TWEPEHHLLHCEEFIDEF 55
Cdd:cd18637   2 YVVEKILKHRMARKGGgYEYLLKWEGYDDPSDnTWSSEADCAGCKDLIEAY 52
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
7-46 4.50e-09

chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349277  Cd Length: 49  Bit Score: 52.01  E-value: 4.50e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHLL 46
Cdd:cd18627   1 FAAECILKKRI-RKGKVEYLVKWKGWSQKYNTWEPEENIL 39
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
7-55 4.74e-09

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349331  Cd Length: 49  Bit Score: 52.16  E-value: 4.74e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRkNKKGKWEYLIRWKGYGSTEDTWEPEHHLLHcEEFIDEF 55
Cdd:cd18975   1 YEVESILNSR-LHRGKLQYLIQWKGYPLEEASWELEDNIKN-PRLIEEF 47
PRK08290 PRK08290
enoyl-CoA hydratase; Provisional
269-446 5.15e-09

enoyl-CoA hydratase; Provisional


Pssm-ID: 236220 [Multi-domain]  Cd Length: 288  Bit Score: 57.28  E-value: 5.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  269 NNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYliGRLSSDRRKESTRIAEAIRDFVKAFIQ------ 341
Cdd:PRK08290  25 RNAQNRQMLYELDAAFRRAEADDAvRVIVLAGAGKHFSAGHDLGS--GTPGRDRDPGPDQHPTLWWDGATKPGVeqryar 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  342 --------------FKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPyaTIRLTPAGCSSYTFPQILGVALANEM 407
Cdd:PRK08290 103 ewevylgmcrrwrdLPKPTIAQVQGACIAGGLMLAWVCDLIVASDDAFFSDP--VVRMGIPGVEYFAHPWELGPRKAKEL 180
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 37590660  408 LFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMlrvkEMA 446
Cdd:PRK08290 181 LFTGDRLTADEAHRLGMVNRVVPRDELEAETL----ELA 215
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
8-55 5.67e-09

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 52.19  E-value: 5.67e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   8 EVERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLL-HCEEFIDEF 55
Cdd:cd18659   4 IVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEEDISdIFQEAIDEY 52
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
7-55 8.66e-09

chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Moniliophthora perniciosa FA553 putative retrotelement polyprotein, which includes domains in the following order: a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related "chromo shadow" domain


Pssm-ID: 349328  Cd Length: 50  Bit Score: 51.36  E-value: 8.66e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKNKKGKWeYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18972   1 YEVEAIVGHKPKKKPRQ-FLVSWLGYDSSHNEWKQKEELENARELLQDY 48
PRK05869 PRK05869
enoyl-CoA hydratase; Validated
253-431 9.90e-09

enoyl-CoA hydratase; Validated


Pssm-ID: 235632 [Multi-domain]  Cd Length: 222  Bit Score: 55.62  E-value: 9.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  253 KEEGFTHILLSSQTSdnNALTPEIMKEVRRALCN-AATDDSKLLLLSAVGSVFCSGLDysylIGRLSSDRRKESTRIAEA 331
Cdd:PRK05869  14 QDAGLATLLLSRPPT--NALTRQVYREIVAAANElGRRDDVAAVILYGGHEIFSAGDD----MPELRTLSAQEADTAARV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  332 IRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCG 411
Cdd:PRK05869  88 RQQAVDAVAAIPKPTVAAITGYALGAGLTLALAADWRVSGDNVKFGATEILAGLAPSGDGMARLTRAAGPSRAKELVFSG 167
                        170       180
                 ....*....|....*....|
gi 37590660  412 RKLTAQEACSRGLVSQVFWP 431
Cdd:PRK05869 168 RFFDAEEALALGLIDEMVAP 187
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
7-55 1.67e-08

chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog gamma (also known as HP1gamma, Cbx3, and Chromobox 3), and related proteins. HP1gamma is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. In addition to being involved in transcriptional silencing in heterochromatin-like complexes, HP1gamma also binds lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the protein may explain the association of heterochromatin with the inner nuclear membrane. HP1gamma is also recruited to sites of ultraviolet-induced DNA damage and double-strand breaks. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma.


Pssm-ID: 349299  Cd Length: 50  Bit Score: 50.78  E-value: 1.67e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEF 55
Cdd:cd18652   2 FVVEKVLDRRV-VNGKVEYFLKWKGFTDADNTWEPEEN-LDCPELIEAF 48
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
7-55 2.10e-08

chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Rhizoctonia solani AG-3 Rhs1AP, a putative Ty3/Gypsy polyprotein/retrotransposon which includes a protease, a reverse transcriptase, a ribonuclease H, and an integrase domain, in that order, with a chromodomain at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349333  Cd Length: 57  Bit Score: 50.56  E-value: 2.10e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 37590660   7 YEVERIVD----KRKNKKGKwEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18977   4 YEVEKIVGekwkKRKNRRVK-LYKVRFKGYGPEEDEWLTKEELKNAPEILAEW 55
PRK07509 PRK07509
crotonase/enoyl-CoA hydratase family protein;
249-447 2.42e-08

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181008 [Multi-domain]  Cd Length: 262  Bit Score: 54.89  E-value: 2.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  249 IVVRKEEGFTHILLSsQTSDNNALTPEIMKEVRRA---LcnAATDDSKLLLLSAVGSVFCSGLDysylIGRLSSDRRKES 325
Cdd:PRK07509   5 VSVTIEDGIADVRLN-RPDKMNALDFAMFEELIATikrL--KKDRGIRAVILSGEGGAFCAGLD----VKSVASSPGNAV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  326 TRIAEAIR----DFVKAFIQFKK---PIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTP--AGCSSytFP 396
Cdd:PRK07509  78 KLLFKRLPgnanLAQRVSLGWRRlpvPVIAALEGVCFGGGLQIALGADIRIAAPDTKLSIMEAKWGLVPdmAGTVS--LR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37590660  397 QILGVALANEMLFCGRKLTAQEACSRGLVSQVfwpttfSQEVMLRVKEMAS 447
Cdd:PRK07509 156 GLVRKDVARELTYTARVFSAEEALELGLVTHV------SDDPLAAALALAR 200
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
7-55 2.92e-08

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members of this subgroup, the chromodomain is followed by a chromo shadow domain; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. For the majority of members of this subgroup, the chromodomain is followed by a chromo shadow domain (CSD).


Pssm-ID: 349325  Cd Length: 56  Bit Score: 50.21  E-value: 2.92e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   7 YEVERIVDKRKN--KKGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18969   4 YEIEEILDVKKGgfEDGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEY 54
PRK08252 PRK08252
crotonase/enoyl-CoA hydratase family protein;
279-428 4.22e-08

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181325 [Multi-domain]  Cd Length: 254  Bit Score: 54.23  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  279 EVRRALCNA-----ATDDSKLLLLSAVGSVFCSGLDY-SYLIGRLSSDRRKESTRIAEAirdfvkafiQFKKPIVVAING 352
Cdd:PRK08252  30 AVAQGLAAAldeldADPDLSVGILTGAGGTFCAGMDLkAFARGERPSIPGRGFGGLTER---------PPRKPLIAAVEG 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590660  353 PALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK08252 101 YALAGGFELALACDLIVAARDAKFGLPEVKRGLVAAGGGLLRLPRRIPYHIAMELALTGDMLTAERAHELGLVNRL 176
PRK08321 PRK08321
1,4-dihydroxy-2-naphthoyl-CoA synthase;
270-428 6.87e-08

1,4-dihydroxy-2-naphthoyl-CoA synthase;


Pssm-ID: 181386  Cd Length: 302  Bit Score: 54.26  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNA-ATDDSKLLLLSAVGS-------VFCSGLD--------YSYligrlSSDRRKESTRIAEAIR 333
Cdd:PRK08321  47 NAFRPHTVDELYRALDHArMSPDVGCVLLTGNGPspkdggwAFCSGGDqrirgrdgYQY-----AEGDEADTVDPARAGR 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  334 DF---VKAFIQF-KKPIVVAINGPALGLGASILPLCDIVWAS-EKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEML 408
Cdd:PRK08321 122 LHileVQRLIRFmPKVVIAVVPGWAAGGGHSLHVVCDLTLASrEHARFKQTDADVGSFDGGYGSAYLARQVGQKFAREIF 201
                        170       180
                 ....*....|....*....|
gi 37590660  409 FCGRKLTAQEACSRGLVSQV 428
Cdd:PRK08321 202 FLGRTYSAEEAHDMGAVNAV 221
PRK07396 PRK07396
dihydroxynaphthoic acid synthetase; Validated
246-428 1.09e-07

dihydroxynaphthoic acid synthetase; Validated


Pssm-ID: 180958 [Multi-domain]  Cd Length: 273  Bit Score: 53.36  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  246 FRDIVVRKEEGFTHILLSsQTSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVG-SVFCSGLDYS------YL---- 313
Cdd:PRK07396  12 YEDILYKSADGIAKITIN-RPEVRNAFRPKTVKEMIDAFADARDDDNiGVIILTGAGdKAFCSGGDQKvrgyggYVdddg 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  314 IGRLSsdrrkestriaeaIRDFVKAFIQFKKPIVVAINGPALGlGASILPL-CDIVWASEKAWF-QTpyatirlTP---- 387
Cdd:PRK07396  91 VPRLN-------------VLDLQRLIRTCPKPVIAMVAGYAIG-GGHVLHLvCDLTIAADNAIFgQT-------GPkvgs 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 37590660  388 --AGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVSQV 428
Cdd:PRK07396 150 fdGGYGASYLARIVGQKKAREIWFLCRQYDAQEALDMGLVNTV 192
PRK07327 PRK07327
enoyl-CoA hydratase/isomerase family protein;
288-426 1.19e-07

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 235991  Cd Length: 268  Bit Score: 53.10  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  288 ATDDSKLLLLSAVGSVFCSGLDYSyLIGRLSSDRrKESTRIAEAIRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDI 367
Cdd:PRK07327  53 RDPDVRVVLIRGEGKAFSAGGDLA-LVEEMADDF-EVRARVWREARDLVYNVINCDKPIVSAIHGPAVGAGLVAALLADI 130
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 37590660  368 VWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLVS 426
Cdd:PRK07327 131 SIAAKDARIIDGHTRLGVAAGDHAAIVWPLLCGMAKAKYYLLLCEPVSGEEAERIGLVS 189
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
4-56 1.23e-07

chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Coemansia reversa NRRL 1564 SET (Su(var)3-9, enhancer-of-zeste, trithorax) domain-containing protein, and similar proteins. The SU(VAR)3-9 protein is the main chromocenter-specific histone H3-K9 methyltransferase (HMTase) in Drosophila where it plays a role in heterochromatic gene silencing. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349318  Cd Length: 52  Bit Score: 48.33  E-value: 1.23e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 37590660   4 GDLYEVERIVdKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLLhCEEFIDEFN 56
Cdd:cd18962   1 EGHYVVEAIV-NDVLIDGKHMYEVKWEGYPSDHNNWVAEWDLN-DKEILRKYN 51
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-45 1.41e-07

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349322  Cd Length: 49  Bit Score: 48.05  E-value: 1.41e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKNKkGKWEYLIRWKGYGSTEDTWEPEHHL 45
Cdd:cd18966   1 YEVERILAERRDD-GGKRYLVKWEGYPLEEATWEPEENI 38
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
7-55 1.52e-07

chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349289  Cd Length: 49  Bit Score: 47.90  E-value: 1.52e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKNKKGKWeYLIRWKGYGSTEDTWEPEHHlLHCEEFIDEF 55
Cdd:cd18639   1 YEVEYLCDYKKIREQEY-YLVKWKGYPDSENTWEPRQN-LKCSRLLKQF 47
PRK08272 PRK08272
crotonase/enoyl-CoA hydratase family protein;
270-447 1.97e-07

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 236213  Cd Length: 302  Bit Score: 52.74  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYS-YLIGRLSSDRRKESTRIAEAIRD------------- 334
Cdd:PRK08272  32 NAITADTPLELRAAVERADLDPGvHVILVSGAGKGFCAGYDLSaYAEGSSSGGGGGAYPGKRQAVNHlpddpwdpmidyq 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  335 ----FVKAFIQF---KKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPA-GCSSYTfpqiLGVALANE 406
Cdd:PRK08272 112 mmsrFVRGFMSLwhaHKPTVAKVHGYCVAGGTDIALHCDQVIAADDAKIGYPPTRVWGVPAtGMWAYR----LGPQRAKR 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 37590660  407 MLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMAS 447
Cdd:PRK08272 188 LLFTGDCITGAQAAEWGLAVEAVPPEELDERTERLVERIAA 228
PLN02851 PLN02851
3-hydroxyisobutyryl-CoA hydrolase-like protein
217-427 2.12e-07

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178443 [Multi-domain]  Cd Length: 407  Bit Score: 53.06  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  217 VKRKLETEKDYVFDKRLRYSVRQNES-NCRFRDIVVRKEEGFTHILLSSQTSDNNALTPEIMKEVRRaLCNAATDDSKL- 294
Cdd:PLN02851  10 VAVPLQWVRFGSVSYGRSFSALPNYAaNDDLQDQVLVEGRAKSRAAILNRPSSLNALTIPMVARLKR-LYESWEENPDIg 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  295 -LLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAIRDFVKAFIQFKKPIVVAINGPALGLGASI-LPLCDIVwASE 372
Cdd:PLN02851  89 fVLMKGSGRAFCSGADVVSLYHLINEGNVEECKLFFENLYKFVYLQGTYLKPNVAIMDGITMGCGAGIsIPGMFRV-VTD 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37590660  373 KAWFQTPYATIRLTP-AGCSSY--TFPQILGVALAnemlFCGRKLTAQEACSRGLVSQ 427
Cdd:PLN02851 168 KTVFAHPEVQMGFHPdAGASYYlsRLPGYLGEYLA----LTGQKLNGVEMIACGLATH 221
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
6-46 2.56e-07

chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 2 (CBX2), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349294  Cd Length: 53  Bit Score: 47.36  E-value: 2.56e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 37590660   6 LYEVERIVDKRkNKKGKWEYLIRWKGYGSTEDTWEPEHHLL 46
Cdd:cd18647   3 VFAAECILSKR-LRKGKLEYLVKWRGWSSKHNSWEPEENIL 42
PRK12478 PRK12478
crotonase/enoyl-CoA hydratase family protein;
270-460 3.68e-07

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 183548  Cd Length: 298  Bit Score: 51.88  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATD-DSKLLLLSAVGSVFCSGLDY----SYLIGRLSSDRRKE--------STRIAEAIRDFV 336
Cdd:PRK12478  27 NTIVPPMPDEIEAAIGLAERDqDIKVIVLRGAGRAFSGGYDFgggfQHWGEAMMTDGRWDpgkdfamvTARETGPTQKFM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  337 kAFIQFKKPIVVAINGPALGlGASILPLC-DIVWASEKAWFQTPYAtiRLTPAGCSSYTFPQiLGVALANEMLFCGRKLT 415
Cdd:PRK12478 107 -AIWRASKPVIAQVHGWCVG-GASDYALCaDIVIASDDAVIGTPYS--RMWGAYLTGMWLYR-LSLAKVKWHSLTGRPLT 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 37590660  416 AQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLV 460
Cdd:PRK12478 182 GVQAAEAELINEAVPFERLEARVAEVATELARIPLSQLQAQKLIV 226
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
6-46 4.67e-07

chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 7 (CBX7), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX7 has been shown to function as a tumor suppressor in lung carcinoma and an oncogene in gastric cancer and lymphoma.


Pssm-ID: 349293  Cd Length: 56  Bit Score: 46.62  E-value: 4.67e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 37590660   6 LYEVERIVDKRKnKKGKWEYLIRWKGYGSTEDTWEPEHHLL 46
Cdd:cd18646   4 VFAVESIRKKRV-RKGKVEYLVKWKGWPPKYSTWEPEEHIL 43
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
7-55 6.18e-07

chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Magnaporthe grisea putative retrotransposon polyprotein which includes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349327  Cd Length: 50  Bit Score: 46.23  E-value: 6.18e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   7 YEVERIVD-KRKNKKGK-WEYLIRWKGYgsTEDTWEPEHHLLHCEEFiDEF 55
Cdd:cd18971   1 YEVEEILAaRRRRIRGKgREVLVKWVGY--AEPTWEPLDNLADTAAL-DRF 48
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
6-46 1.60e-06

chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 4 (CBX4), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. In addition to a chromodomain with H3K27me3-binding activity, Cbx4 contains two SUMO-interacting motifs responsible for its small ubiquitin-related modifier (SUMO) E3 ligase activity. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX4 may serve as a tumor suppressor in colorectal carcinoma, and has been shown to be an oncogene in osteosarcoma and breast cancer.


Pssm-ID: 349292  Cd Length: 55  Bit Score: 45.05  E-value: 1.60e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 37590660   6 LYEVERIvDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLL 46
Cdd:cd18645   3 VFAVESI-EKKRIRKGRVEYLVKWRGWSPKYNTWEPEENIL 42
PRK05674 PRK05674
gamma-carboxygeranoyl-CoA hydratase; Validated
250-461 1.63e-06

gamma-carboxygeranoyl-CoA hydratase; Validated


Pssm-ID: 168168  Cd Length: 265  Bit Score: 49.42  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  250 VVRKEEGFTHILLSsQTSDNNALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYSYLIGRLSSDRrkeSTRI 328
Cdd:PRK05674   9 LIRDPRGFATLWLS-RADKNNAFNAQMIRELILALDQVQSDASlRFLLLRGRGRHFSAGADLAWMQQSADLDY---NTNL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  329 AEA--IRDFVKAFIQFKKPIVVAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFpQILGVALANE 406
Cdd:PRK05674  85 DDAreLAELMYNLYRLKIPTLAVVQGAAFGGALGLISCCDMAIGADDAQFCLSEVRIGLAPAVISPFVV-KAIGERAARR 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37590660  407 MLFCGRKLTAQEACSRGLVSQVFWPTTFSQEVMLRVKEMASCSAVVLEESKCLVR 461
Cdd:PRK05674 164 YALTAERFDGRRARELGLLAESYPAAELEAQVEAWIANLLLNSPQALRASKDLLR 218
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
7-55 2.79e-06

chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of Drosophila melanogaster Rhino (also known as heterochromatin protein 1-like), and similar proteins. Rhino is a female-specific protein that affects chromosome structure and egg polarity that is required for germline PIWI-interacting RNA (piRNA) production. In Drosophila the RDC (rhino, deadlock, and cutoff) complex, composed of rhino, the protein deadlock (Del) and the Rai1-like transcription termination cofactor cutoff (Cuff) binds to chromatin of dual-strand piRNA clusters, special genomic regions, which encode piRNA precursors. The RDC complex is anchored to H3K9me3-marked chromatin in part via the H3K9me3-binding activity of Rhino, and is required for transcription of piRNA precursors. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349280  Cd Length: 51  Bit Score: 44.43  E-value: 2.79e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   7 YEVERIVDKRKNKkGKWEYLIRWKGYGSTEDTWEPEHHLLHCEEFIDEF 55
Cdd:cd18630   2 YVVEKILGKRFVN-GRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
CD_POL_like cd18979
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ...
10-41 5.42e-06

chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins (Z195D10.9), and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Zea maize Z195D10.9 protein, and other putative TY3/gypsy retrotransposon polyproteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349335  Cd Length: 48  Bit Score: 43.63  E-value: 5.42e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 37590660  10 ERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEP 41
Cdd:cd18979   4 EKVLDIRQRDKGNKEFLVQWQGLSVEEATWEP 35
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-57 5.77e-06

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349321  Cd Length: 53  Bit Score: 43.62  E-value: 5.77e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 37590660   7 YEVERIVdKRKNKKGKWEYLIRWKGYGSTEDTWEPEH---HLLHCEEFIDEFNG 57
Cdd:cd18965   1 YIIEALL-KKRQFNRKLEYLVKWHGLPESENTWEREKdikHVSHWKQLLKDLRA 53
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
15-46 5.90e-06

chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression.


Pssm-ID: 349296  Cd Length: 55  Bit Score: 43.55  E-value: 5.90e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 37590660  15 KRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLL 46
Cdd:cd18649  12 KRRIRKGRMEYLVKWKGWSQKYSTWEPEENIL 43
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
15-46 9.45e-06

chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349295  Cd Length: 58  Bit Score: 43.12  E-value: 9.45e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 37590660  15 KRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLL 46
Cdd:cd18648  11 KRRIRKGRIEYLVKWKGWAIKYSTWEPEENIL 42
PRK07938 PRK07938
enoyl-CoA hydratase family protein;
270-428 1.47e-05

enoyl-CoA hydratase family protein;


Pssm-ID: 181174  Cd Length: 249  Bit Score: 46.50  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATD-DSKLLLLSAVGSVFCSGLDYSYLigrlssDRRKESTRIAEAIRDFVKAF---IQFKKP 345
Cdd:PRK07938  23 NALPSAGWFALADAITAAGADpDTRVVVLRAEGRGFNAGVDIKEL------QATPGFTALIDANRGCFAAFravYECAVP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  346 IVVAINGPALGLGASILPLCDIVWASEKAWFQTPY--------AT--IRLTPagcssytfpqilgVALANEMLFCGRKLT 415
Cdd:PRK07938  97 VIAAVHGFCLGGGIGLVGNADVIVASDDATFGLPEvdrgalgaAThlQRLVP-------------QHLMRALFFTAATIT 163
                        170
                 ....*....|...
gi 37590660  416 AQEACSRGLVSQV 428
Cdd:PRK07938 164 AAELHHFGSVEEV 176
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
270-446 3.35e-05

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 46.43  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS--KLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAIRDFVKAFiqfKKPIV 347
Cdd:PRK11154  29 NTLKAEFAEQVRAILKQLREDKElkGVVFISGKPDNFIAGADINMLAACKTAQEAEALARQGQQLFAEIEAL---PIPVV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  348 VAINGPALGLGASILPLCD--IVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLV 425
Cdd:PRK11154 106 AAIHGACLGGGLELALACHyrVCTDDPKTVLGLPEVQLGLLPGSGGTQRLPRLIGVSTALDMILTGKQLRAKQALKLGLV 185
                        170       180
                 ....*....|....*....|..
gi 37590660  426 SQVFwPttfsQEVMLRV-KEMA 446
Cdd:PRK11154 186 DDVV-P----HSILLEVaVELA 202
PLN02874 PLN02874
3-hydroxyisobutyryl-CoA hydrolase-like protein
270-494 4.10e-05

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178462 [Multi-domain]  Cd Length: 379  Bit Score: 45.95  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  270 NALTPEIMKEVRRALCNAATDDS-KLLLLSAVGSVFCSGLDYS-YLIGRLSSDRRKESTRIAEAIRDFVKAFiqfKKPIV 347
Cdd:PLN02874  33 NVISLSVVSLLAEFLEQWEKDDSvELIIIKGAGRAFSAGGDLKmFYDGRESDDSCLEVVYRMYWLCYHIHTY---KKTQV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  348 VAINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAGCSSYTFPQILGvALANEMLFCGRKLTAQEACSRGLVSQ 427
Cdd:PLN02874 110 ALVHGLVMGGGAGLMVPMKFRVVTEKTVFATPEASVGFHTDCGFSYILSRLPG-HLGEYLALTGARLNGKEMVACGLATH 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37590660  428 vFWPttfSQEVMlrvkemascsavvlEESKCLV------RSFLKSVLEEVN-----EKECVMLKQLWssskgLDSLFS 494
Cdd:PLN02874 189 -FVP---SEKLP--------------ELEKRLLnlnsgdESAVQEAIEEFSkdvqaDEDSILNKQSW-----INECFS 243
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
7-56 5.54e-05

chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin Organization Modifier (chromo) domain of Caenorhabditis elegans CEC-4, and similar proteins. CEC-4 is a perinuclear heterochromatin anchor, it mediates the anchoring of H3K9 methylation-bearing chromatin at the nuclear periphery in early to mid-stage embryos. It is necessary for anchoring, but does not affect transcriptional repression. CEC-4 contributes to the efficiency with which muscle differentiation is induced following ectopic expression of the master regulator, HLH-1 (MyoD in mammals). A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349317  Cd Length: 51  Bit Score: 40.55  E-value: 5.54e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   7 YEVERIVDKRKnKKGKWEYLIRWKGY-GSTEDTWEPEHHLLHCEEFIDEFN 56
Cdd:cd18961   1 YEVEKILSHRI-VNGKPLYLVMWVGYpGPVENSEMWEEDLKNCGELLKAYK 50
PRK08788 PRK08788
enoyl-CoA hydratase; Validated
269-429 9.74e-05

enoyl-CoA hydratase; Validated


Pssm-ID: 236338  Cd Length: 287  Bit Score: 44.13  E-value: 9.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  269 NNALTPEIMK---EVRRALCNAATDDSKLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTRIAEAIRDFVKAFIQ-FKK 344
Cdd:PRK08788  41 NLELLDDIMNlqrAIRQRLDDSGLPVDFWVLASDVPGVFNLGGDLALFAELIRAGDRDALLAYARACVDGVHAFHRgFGA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  345 PIV-VA-INGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPaGCSSYTF-PQILGVALANEMLFCGRKLTAQEACS 421
Cdd:PRK08788 121 GAIsIAlVQGDALGGGFEAALSHHTIIAERGAKMGFPEILFNLFP-GMGAYSFlARRVGPKLAEELILSGKLYTAEELHD 199

                 ....*...
gi 37590660  422 RGLVSQVF 429
Cdd:PRK08788 200 MGLVDVLV 207
PRK07112 PRK07112
enoyl-CoA hydratase/isomerase;
269-425 1.84e-04

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235938  Cd Length: 255  Bit Score: 43.13  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  269 NNALTPEIMKEVRRALcNAATDDSKLLLLSAVGSVFCSGLDYSYLIGRLSSDRRKESTriAEAIRDFVKAFIQFKKPIVV 348
Cdd:PRK07112  25 QNTINDRLIAECMDVL-DRCEHAATIVVLEGLPEVFCFGADFSAIAEKPDAGRADLID--AEPLYDLWHRLATGPYVTIA 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590660  349 AINGPALGLGASILPLCDIVWASEKAWFQTPYATIRLTPAgCSSYTFPQILGVALANEMLFCGRKLTAQEACSRGLV 425
Cdd:PRK07112 102 HVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIPA-CVLPFLIRRIGTQKAHYMTLMTQPVTAQQAFSWGLV 177
CD2_cpSRP43_like cd18629
chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
8-45 3.32e-04

chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; This subgroup includes the chromodomain 2 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain.


Pssm-ID: 349279  Cd Length: 48  Bit Score: 38.25  E-value: 3.32e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 37590660   8 EVERIVDKRkNKKGKWEYLIRWKGYGstEDTWEPEHHL 45
Cdd:cd18629   4 EVNEILESR-GKGKDMEYLIEWKDGG--DCEWVKGVHV 38
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
9-56 5.79e-04

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 38.01  E-value: 5.79e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37590660   9 VERIVDKRKNKKGKWEYLIRWKGYGSTEDTWEPEHHLL-HCEEFIDEFN 56
Cdd:cd18662   6 IHRIINHRVDKDGNTWYLVKWRDLPYDQSTWESEDDDIpDYEKHIQEYW 54
CBD_MSL3_like cd18983
chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins; ...
4-53 6.33e-04

chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins; This subgroup includes human male-specific lethal (MSL) complex subunit 3 (MSL3, also known as MSL3L1). The MSL3 chromodomain specifically recognizes the H4K20 monomethyl mark, in a DNA-dependent manner, and may be involved in chromosomal targeting of the MSL complex. Also included is MORF-related gene on chromosome 15 (MRG15, also known as MORF4L1) which specifically binds to Lys36-methylated histone H3 and plays a role in transcriptional regulation and in DNA repair. This subgroup also includes Arabidopsis thaliana Morf Related Gene 2 (MRG2) which acts as a H3K4me3/H3K36me3 reader involved in the regulation of Arabidopsis flowering. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 350846  Cd Length: 57  Bit Score: 37.81  E-value: 6.33e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 37590660   4 GDLYEVERIVDKRKNKKGkWEYLIRWKGYGSTEDTWEPEHHLL-HCEEFID 53
Cdd:cd18983   8 GPLLYEAKILDVIPDKKE-WKYFIHYNGWNKSWDEWVPEDRVLkYTDENLR 57
PRK08259 PRK08259
crotonase/enoyl-CoA hydratase family protein;
282-428 1.33e-03

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 236205  Cd Length: 254  Bit Score: 40.65  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  282 RALCNA-----ATDDSKLLLLSAVGSVFCSGLDysylIGRLSSDRRKESTRIAEA----IRdfvkafIQFKKPIVVAING 352
Cdd:PRK08259  33 AALADAfrafdADDAASVAVLWGAGGTFCAGAD----LKAVGTGRGNRLHPSGDGpmgpSR------MRLSKPVIAAVSG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  353 PALGLGASILPLCDIVWASEKAWFQT-------PY---ATIRLtpagcssytfPQILGVALANEMLFCGRKLTAQEACSR 422
Cdd:PRK08259 103 YAVAGGLELALWCDLRVAEEDAVFGVfcrrwgvPLidgGTVRL----------PRLIGHSRAMDLILTGRPVDADEALAI 172

                 ....*.
gi 37590660  423 GLVSQV 428
Cdd:PRK08259 173 GLANRV 178
PRK06213 PRK06213
crotonase/enoyl-CoA hydratase family protein;
266-366 1.59e-03

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235744  Cd Length: 229  Bit Score: 39.96  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590660  266 TSDN---NALTPEIMKEVRRALcNAATDDSKLLLLSAVGSVFCSGLDYsyligrlssdrrKESTRIAEAIRDFVKA---- 338
Cdd:PRK06213  17 TLDDgkvNALSPAMIDALNAAL-DQAEDDRAVVVITGQPGIFSGGFDL------------KVMTSGAQAAIALLTAgstl 83
                         90       100       110
                 ....*....|....*....|....*....|.
gi 37590660  339 ---FIQFKKPIVVAINGPALGLGASILPLCD 366
Cdd:PRK06213  84 arrLLSHPKPVIVACTGHAIAKGAFLLLSAD 114
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
9-41 5.18e-03

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349312  Cd Length: 65  Bit Score: 35.44  E-value: 5.18e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 37590660   9 VERIVDKRKNK----------KGKWEYLIRWKGYGSTEDTWEP 41
Cdd:cd18665   5 IDIVLDHRLKEgleegelddpKENYEFLIKWTDESHLHNTWET 47
 
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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