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Conserved domains on  [gi|4757966|ref|NP_004671|]
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testis-specific chromodomain protein Y 1 isoform b [Homo sapiens]

Protein Classification

enoyl-CoA hydratase/isomerase family protein( domain architecture ID 13036092)

enoyl-CoA hydratase/isomerase family protein similar to enoyl-CoA hydratase, which catalyzes the second step in the beta-oxidation pathway of fatty acid metabolism, the syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA thioester, resulting in the formation of a beta-hydroxyacyl-CoA thioester

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 ...
 286-482 2.48e-46

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: 160.80  E-value: 2.48e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHlrNNRNTASLE 364
Cdd:cd06558   1 VLVERDGGVATITLN-RPEKRNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:cd06558  78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4757966  445 LIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKEL 482
Cdd:cd06558 158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 5-56 7.30e-29

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: 108.30  E-value: 7.30e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    5 EFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNR 56
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 ...
 286-482 2.48e-46

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: 160.80  E-value: 2.48e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHlrNNRNTASLE 364
Cdd:cd06558   1 VLVERDGGVATITLN-RPEKRNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:cd06558  78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4757966  445 LIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKEL 482
Cdd:cd06558 158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
 286-529 1.02e-44

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: 158.41  E-value: 1.02e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFvkhLRNNRNTASLE 364
Cdd:COG1024   1 VLVEREGGVATITLN-RPEKLNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKEL---AAAADPEEARA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:COG1024  77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKEL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  445 LIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQ 524
Cdd:COG1024 157 LLTGRRIDAEEALELGLVNRVVPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFASED 236


                ....*
gi 4757966  525 GIESM 529
Cdd:COG1024 237 AREGI 241
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
 284-519 1.55e-41

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 150.02  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   284 RDIVVKKEDGFTQIVLsTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHlrnnrNTAS 362
Cdd:PRK06688   5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGDIKDFPKA-----PPKP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   363 LEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASAN 442
Cdd:PRK06688  79 PDELAPVNRFLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757966   443 EMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKI 519
Cdd:PRK06688 159 EMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREAAGFGRL 235
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 5-56 7.30e-29

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: 108.30  E-value: 7.30e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    5 EFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNR 56
Cdd:cd18634   1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
 302-530 1.86e-20

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: 90.88  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    302 RSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGyfvKHLRNNRNTASlemvDTIKNFVNTFI--- 377
Cdd:pfam00378  13 RPEAVNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLK---EMYGEGPAHQA----LYRENVLDLWTlly 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    378 QFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREAC 457
Cdd:pfam00378  86 TCPKPVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEAL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4757966    458 AKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESML 530
Cdd:pfam00378 166 KWGLVDKVVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQ 238
CHROMO smart00298
Chromatin organization modifier domain;
5-58 5.60e-20

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 83.42  E-value: 5.60e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 4757966       5 EFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQ 58
Cdd:smart00298   1 EYEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKE 54
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
6-57 1.06e-19

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 82.63  E-value: 1.06e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4757966      6 FEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRR 57
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 286-465 1.09e-08

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: 57.92  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    286 IVVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS--KLVLFSAAGSVFCCGLDFGyFVKHLRNNRNTASL 363
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGADIQ-MIAACKTAQEVTQL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    364 -----EMVDTIKnfvntfiQFKKPIVVSVNGPAIGLGASILPLCDLVWA--NEKAWFQTPYTTFGQSPDGCSSITFPKMM 436
Cdd:TIGR02441  94 sqegqEMFERIE-------KSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLT 166

                         170       180
                  ....*....|....*....|....*....
gi 4757966    437 GKASANEMLIAGRKLTAREACAKGLVSQV 465
Cdd:TIGR02441 167 GVPAALDMMLTGKKIRADRAKKMGIVDQL 195
 
Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
 286-482 2.48e-46

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: 160.80  E-value: 2.48e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHlrNNRNTASLE 364
Cdd:cd06558   1 VLVERDGGVATITLN-RPEKRNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:cd06558  78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4757966  445 LIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKEL 482
Cdd:cd06558 158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
 286-529 1.02e-44

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: 158.41  E-value: 1.02e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFvkhLRNNRNTASLE 364
Cdd:COG1024   1 VLVEREGGVATITLN-RPEKLNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKEL---AAAADPEEARA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:COG1024  77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKEL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966  445 LIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQ 524
Cdd:COG1024 157 LLTGRRIDAEEALELGLVNRVVPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFASED 236


                ....*
gi 4757966  525 GIESM 529
Cdd:COG1024 237 AREGI 241
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
 284-519 1.55e-41

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 150.02  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   284 RDIVVKKEDGFTQIVLsTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHlrnnrNTAS 362
Cdd:PRK06688   5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGDIKDFPKA-----PPKP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   363 LEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASAN 442
Cdd:PRK06688  79 PDELAPVNRFLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757966   443 EMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKI 519
Cdd:PRK06688 159 EMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREAAGFGRL 235
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 5-56 7.30e-29

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: 108.30  E-value: 7.30e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    5 EFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNR 56
Cdd:cd18634   1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
PRK05981 PRK05981
enoyl-CoA hydratase/isomerase;
282-484 2.21e-24

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235661  Cd Length: 266  Bit Score: 102.50  E-value: 2.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   282 TYRDIVVKKEDGFTQIVLSTRSTeKNALNTEVIKEIVNALNSAAADDSKL--VLFSAAGSVFCCGLDFGYfvkhlRNNRN 359
Cdd:PRK05981   2 QFKKVTLDFDGGVAILTLDHPEV-MNAVSIDMLGGLAEALDAIEDGKAEVrcLVLTGAGRGFCTGANLQG-----RGSGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   360 TASLEMVD---TIKNFVNTFI----QFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITF 432
Cdd:PRK05981  76 RESDSGGDagaALETAYHPFLrrlrNLPCPIVTAVNGPAAGVGMSFALMGDLILCARSAYFLQAFRRIGLVPDGGSTWLL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4757966   433 PKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELAS 484
Cdd:PRK05981 156 PRLVGKARAMELSLLGEKLPAETALQWGLVNRVVDDAELMAEAMKLAHELAN 207
PRK06023 PRK06023
crotonase/enoyl-CoA hydratase family protein;
296-498 6.99e-24

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 168351  Cd Length: 251  Bit Score: 100.64  E-value: 6.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   296 QIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLrnnrnTASLEMVDTIKNFVN 374
Cdd:PRK06023  17 QVIRFNRPEKKNAITRAMYATMAKALKAADADDAiRAHVFLGTEGCFSAGNDMQDFLAAA-----MGGTSFGSEILDFLI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   375 TFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAR 454
Cdd:PRK06023  92 ALAEAEKPIVSGVDGLAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALVPEAGSSLLAPRLMGHQRAFALLALGEGFSAE 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4757966   455 EACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVR 498
Cdd:PRK06023 172 AAQEAGLIWKIVDEEAVEAETLKAAEELAAKPPQALQIARDLMR 215
PRK09674 PRK09674
enoyl-CoA hydratase-isomerase; Provisional
 285-498 3.99e-21

enoyl-CoA hydratase-isomerase; Provisional


Pssm-ID: 182026 [Multi-domain]  Cd Length: 255  Bit Score: 92.91  E-value: 3.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   285 DIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFgyfvkhlrnnRNTASL 363
Cdd:PRK09674   3 ELLVSRQQRVLLLTLN-RPEARNALNNALLTQLVNELEAAATDTSiGVCVITGNARFFAAGADL----------NEMAEK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   364 EMVDTIKNFVNTFIQ----FKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKA 439
Cdd:PRK09674  72 DLAATLNDPRPQLWQrlqaFNKPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGGTQRLIRSVGKS 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4757966   440 SANEMLIAGRKLTAREACAKGLVSQVF---LTGTFTQEVMIQIkelASYNPIVLEECKALVR 498
Cdd:PRK09674 152 LASQMVLTGESITAQQAQQAGLVSEVFppeLTLERALQLASKI---ARHSPLALRAAKQALR 210
PRK07854 PRK07854
enoyl-CoA hydratase; Provisional
 302-527 1.07e-20

enoyl-CoA hydratase; Provisional


Pssm-ID: 236115 [Multi-domain]  Cd Length: 243  Bit Score: 91.24  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   302 RSTEKNALNTEVIKEIVNALNSAAADDSKLVLFSAAGSVFCCGLDFG---YFVKHLRnnRNTASLEMVDTIknfvntfiq 378
Cdd:PRK07854  17 RPERRNALNAELCEELREAVRKAVDESARAIVLTGQGTVFCAGADLSgdvYADDFPD--ALIEMLHAIDAA--------- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   379 fKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACA 458
Cdd:PRK07854  86 -PVPVIAAINGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDNWTIRRLSSLVGGGRARAMLLGAEKLTAEQALA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4757966   459 KGLVSQVfltGTFT--QEVMIQIKELAsynPIVLEECKALVrcNIKLELEQANERECEVLRKIWSSAQGIE 527
Cdd:PRK07854 165 TGMANRI---GTLAdaQAWAAEIAGLA---PLALQHAKRVL--NDDGAIEEAWPAHKELFDKAWASQDAIE 227
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
 302-530 1.86e-20

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: 90.88  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    302 RSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGyfvKHLRNNRNTASlemvDTIKNFVNTFI--- 377
Cdd:pfam00378  13 RPEAVNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLK---EMYGEGPAHQA----LYRENVLDLWTlly 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    378 QFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREAC 457
Cdd:pfam00378  86 TCPKPVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEAL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4757966    458 AKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESML 530
Cdd:pfam00378 166 KWGLVDKVVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQ 238
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
 6-56 2.89e-20

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: 84.07  E-value: 2.89e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNR 56
Cdd:cd00024   1 YEVEKILDHRVRK-GKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
CHROMO smart00298
Chromatin organization modifier domain;
5-58 5.60e-20

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 83.42  E-value: 5.60e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 4757966       5 EFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQ 58
Cdd:smart00298   1 EYEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKE 54
PRK07659 PRK07659
enoyl-CoA hydratase; Provisional
 286-482 7.06e-20

enoyl-CoA hydratase; Provisional


Pssm-ID: 236073 [Multi-domain]  Cd Length: 260  Bit Score: 89.32  E-value: 7.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDSKLVLFSAAGSVFCCGLDFGYFvkhLRNNRNTASLEM 365
Cdd:PRK07659   8 VVVKYEGRVATIMLN-RPEALNALDEPMLKELLQALKEVAESSAHIVVLRGNGRGFSAGGDIKMM---LSSNDESKFDGV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   366 VDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEML 445
Cdd:PRK07659  84 MNTISEIVVTLYTMPKLTISAIHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGLIPDGGGHFFLQKRVGENKAKQII 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4757966   446 IAGRKLTAREACAKGLVSQVFlTGTFTQEVMIQIKEL 482
Cdd:PRK07659 164 WEGKKLSATEALDLGLIDEVI-GGDFQTAAKQKISEW 199
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
6-57 1.06e-19

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 82.63  E-value: 1.06e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4757966      6 FEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRR 57
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
PRK07511 PRK07511
enoyl-CoA hydratase; Provisional
 306-498 2.98e-19

enoyl-CoA hydratase; Provisional


Pssm-ID: 181009 [Multi-domain]  Cd Length: 260  Bit Score: 87.74  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   306 KNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDfgyfVKHLRNNRNTA---SLEMVDTIKNFVNTFIQFKK 381
Cdd:PRK07511  24 RNALHPDMYAAGIEALNTAERDPSiRAVVLTGAGGFFCAGGN----LNRLLENRAKPpsvQAASIDGLHDWIRAIRAFPK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   382 PIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGL 461
Cdd:PRK07511 100 PVIAAVEGAAAGAGFSLALACDLLVAARDAKFVMAYVKVGLTPDGGGSWFLARALPRQLATELLLEGKPISAERLHALGV 179

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4757966   462 VSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVR 498
Cdd:PRK07511 180 VNRLAEPGQALAEALALADQLAAGSPNALARIKSLIA 216
PRK09245 PRK09245
crotonase/enoyl-CoA hydratase family protein;
285-498 3.58e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181723  Cd Length: 266  Bit Score: 87.33  E-value: 3.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   285 DIVVKKEDGFTQIVLSTRSTEKNALN-TEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDfgyfVKHLRNNRNTAS 362
Cdd:PRK09245   3 DFLLVERDGHIVTLTMNRPETRNALSdNDAVDALVAACAAINADRSvRAVILTGAGTAFSSGGN----VKDMRARVGAFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   363 LEMVD-------TIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSP-DGCSSItFPK 434
Cdd:PRK09245  79 GSPADirqgyrhGIQRIPLALYNLEVPVIAAVNGPAIGAGCDLACMCDIRIASETARFAESFVKLGLIPgDGGAWL-LPR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4757966   435 MMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVR 498
Cdd:PRK09245 158 IIGMARAAEMAFTGDAIDAATALEWGLVSRVVPADQLLPAARALAERIAANPPHALRLTKRLLR 221
PRK08260 PRK08260
enoyl-CoA hydratase; Provisional
 282-465 3.60e-19

enoyl-CoA hydratase; Provisional


Pssm-ID: 236206 [Multi-domain]  Cd Length: 296  Bit Score: 88.14  E-value: 3.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   282 TYRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLD-------FGYFVKH 353
Cdd:PRK08260   2 TYETIRYDVADGIATITLN-RPDKLNAFTVTMARELIEAFDAADADDAvRAVIVTGAGRAFCAGADlsaggntFDLDAPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   354 LRNNRNTASLEMV------DTIKNFVNTFIQFKKPIVVSVNGPAIGLGASI-LPLcDLVWANEKAWFQTPYTTFGQSPDG 426
Cdd:PRK08260  81 TPVEADEEDRADPsddgvrDGGGRVTLRIFDSLKPVIAAVNGPAVGVGATMtLAM-DIRLASTAARFGFVFGRRGIVPEA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4757966   427 CSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQV 465
Cdd:PRK08260 160 ASSWFLPRLVGLQTALEWVYSGRVFDAQEALDGGLVRSV 198
PRK05809 PRK05809
short-chain-enoyl-CoA hydratase;
283-529 4.44e-18

short-chain-enoyl-CoA hydratase;


Pssm-ID: 180270 [Multi-domain]  Cd Length: 260  Bit Score: 84.03  E-value: 4.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   283 YRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGS-VFCCGLD-------------- 346
Cdd:PRK05809   3 LKNVILEKEGHIAVVTIN-RPKALNALNSETLKELDTVLDDIENDDNvYAVILTGAGEkAFVAGADisemkdlneeegrk 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   347 FGyfvkhLRNNRNTASLEMVDtiknfvntfiqfkKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDG 426
Cdd:PRK05809  82 FG-----LLGNKVFRKLENLD-------------KPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGITPGF 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   427 CSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELE 506
Cdd:PRK05809 144 GGTQRLARIVGPGKAKELIYTGDMINAEEALRIGLVNKVVEPEKLMEEAKALANKIAANAPIAVKLCKDAINRGMQVDID 223

                        250       260
                 ....*....|....*....|...
gi 4757966   507 QANERECEVLRKIWSSAQGIESM 529
Cdd:PRK05809 224 TAVAIEAEDFGECFSTEDQTEGM 246
PRK07799 PRK07799
crotonase/enoyl-CoA hydratase family protein;
290-513 2.66e-17

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181122 [Multi-domain]  Cd Length: 263  Bit Score: 82.07  E-value: 2.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   290 KEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLRNNRNTASLEMVDT 368
Cdd:PRK07799  10 EQRGHTLIVTMNRPEARNALSTEMLRIMVDAWDRVDNDPDiRSCILTGAGGAFCAGMDLKAATKKPPGDSFKDGSYDPSR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   369 IKNFVNTFiQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAG 448
Cdd:PRK07799  90 IDALLKGR-RLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLFPMGGSAVRLVRQIPYTVACDLLLTG 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757966   449 RKLTAREACAKGLVSQVFLTGTFTQEVmIQIKELASYN-PIVLEECKALVRcniklELEQANEREC 513
Cdd:PRK07799 169 RHITAAEAKEIGLIGHVVPDGQALDKA-LELAELINANgPLAVQAILRTIR-----ETEGMHENEA 228
PRK08140 PRK08140
enoyl-CoA hydratase; Provisional
 282-465 8.33e-17

enoyl-CoA hydratase; Provisional


Pssm-ID: 236163  Cd Length: 262  Bit Score: 80.34  E-value: 8.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   282 TYRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDSKLVLFSAAGSVFCCGLDFgyfvkhlrNNRN-T 360
Cdd:PRK08140   2 MYETILLAIEAGVATLTLN-RPDKLNSFTREMHRELREALDQVEDDGARALLLTGAGRGFCAGQDL--------ADRDvT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   361 ASLEMVD---TIKNFVNTFIQ----FKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFP 433
Cdd:PRK08140  73 PGGAMPDlgeSIETFYNPLVRrlraLPLPVIAAVNGVAAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLP 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4757966   434 KMMGKASANEMLIAGRKLTAREACAKGLVSQV 465
Cdd:PRK08140 153 RLVGMARALGLALLGEKLSAEQAEQWGLIWRV 184
PLN02664 PLN02664
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
 302-507 8.76e-17

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


Pssm-ID: 178269 [Multi-domain]  Cd Length: 275  Bit Score: 80.72  E-value: 8.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   302 RSTEKNALNTEVIKEIVNALNSAAAD-DSKLVLFSAAGSVFCCGLDFGYF----VKHLRNNRNTASLEMVDTIKNF---V 373
Cdd:PLN02664  25 RPSQRNALSLDFFTEFPKALSSLDQNpNVSVIILSGAGDHFCSGIDLKTLnsisEQSSSGDRGRSGERLRRKIKFLqdaI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   374 NTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTA 453
Cdd:PLN02664 105 TAIEQCRKPVIAAIHGACIGGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTLQRLPSIVGYGNAMELALTGRRFSG 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4757966   454 REACAKGLVSQVFLTGTFTQEVMIQIKE-LASYNPIVLEECKALVRCNIKLELEQ 507
Cdd:PLN02664 185 SEAKELGLVSRVFGSKEDLDEGVRLIAEgIAAKSPLAVTGTKAVLLRSRELSVEQ 239
PRK05980 PRK05980
crotonase/enoyl-CoA hydratase family protein;
286-465 1.55e-16

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180335 [Multi-domain]  Cd Length: 260  Bit Score: 79.80  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGS-VFCCGLDFGYFVKHLRNNRNTASL 363
Cdd:PRK05980   5 VLIEIRDGIALLTLN-RPEKLNALNYALIDRLLARLDAIEVDESvRAVILTGAGDrAFSAGADIHEFSASVAAGADVALR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   364 EMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANE 443
Cdd:PRK05980  84 DFVRRGQAMTARLEAFPKPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPTFGGTQRLPRLAGRKRALE 163

                        170       180
                 ....*....|....*....|..
gi 4757966   444 MLIAGRKLTAREACAKGLVSQV 465
Cdd:PRK05980 164 LLLTGDAFSAERALEIGLVNAV 185
PLN02600 PLN02600
enoyl-CoA hydratase
 302-529 5.46e-16

enoyl-CoA hydratase


Pssm-ID: 178210 [Multi-domain]  Cd Length: 251  Bit Score: 77.92  E-value: 5.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   302 RSTEKNALNTEVIKEIVNALNSAAADDSK--LVLFSAAGSVFCCGLDfgyfvkhLRNNRNTASLEMVDTIKNFVNTFIQF 379
Cdd:PLN02600  12 RPEAKNAIGKEMLRGLRSAFEKIQADASArvVMLRSSVPGVFCAGAD-------LKERRKMSPSEVQKFVNSLRSTFSSL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   380 KK---PIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREA 456
Cdd:PLN02600  85 EAlsiPTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVGRSRAKELIFTGRRIGAREA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4757966   457 CAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESM 529
Cdd:PLN02600 165 ASMGLVNYCVPAGEAYEKALELAQEINQKGPLAIKMAKKAINEGSEVDMASGLEIEEECYEQVLKTKDRLEGL 237
PRK07658 PRK07658
enoyl-CoA hydratase; Provisional
 286-527 1.04e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 181070 [Multi-domain]  Cd Length: 257  Bit Score: 76.98  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStrSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHlrnNRNTASLE 364
Cdd:PRK07658   4 LSVRVEDHVAVITLN--HPPANALSSQVLHELSELLDQVEKDDNvRVVVIHGEGRFFSAGADIKEFTSV---TEAEQATE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:PRK07658  79 LAQLGQVTFERVEKFSKPVIAAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGFAGTQRLPRYVGKAKALEM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   445 LIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQ 524
Cdd:PRK07658 159 MLTSEPITGAEALKWGLVNGVFPEETLLDDAKKLAKKIAGKSPATTRAVLELLQTTKSSSYYEGVKREAKIFGEVFTSED 238


                 ...
gi 4757966   525 GIE 527
Cdd:PRK07658 239 AKE 241
PRK06190 PRK06190
enoyl-CoA hydratase; Provisional
 286-465 1.22e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 235733  Cd Length: 258  Bit Score: 76.94  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDfgyfVKHLrnNRNTASLE 364
Cdd:PRK06190   6 LLVETHDRVRTLTLN-RPEARNALSAALRRALFAALAEADADDDvDVVVLTGADPAFCAGLD----LKEL--GGDGSAYG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:PRK06190  79 AQDALPNPSPAWPAMRKPVIGAINGAAVTGGLELALACDILIASERARFADTHARVGILPGWGLSVRLPQKVGIGRARRM 158

                        170       180
                 ....*....|....*....|.
gi 4757966   445 LIAGRKLTAREACAKGLVSQV 465
Cdd:PRK06190 159 SLTGDFLDAADALRAGLVTEV 179
PRK05862 PRK05862
enoyl-CoA hydratase; Provisional
 282-490 1.28e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 180295 [Multi-domain]  Cd Length: 257  Bit Score: 77.00  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   282 TYRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS--KLVLfsaAGS--VFCCGLDFGyfvkhlrnn 357
Cdd:PRK05862   2 AYETILVETRGRVGLITLN-RPKALNALNDALMDELGAALAAFDADEGigAIVI---TGSekAFAAGADIK--------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   358 rNTASLEMVDTIKN--FVN--TFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFP 433
Cdd:PRK05862  69 -EMADLSFMDVYKGdyITNweKVARIRKPVIAAVAGYALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGMGGSQRLT 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4757966   434 KMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYN-PIVL 490
Cdd:PRK05862 148 RAVGKAKAMDLCLTGRMMDAAEAERAGLVSRVVPADKLLDEALAAATTIASFSlPAVM 205
PRK06495 PRK06495
enoyl-CoA hydratase/isomerase family protein;
307-495 2.11e-15

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 168580 [Multi-domain]  Cd Length: 257  Bit Score: 76.27  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   307 NALNTEVIKEIVNALNS-AAADDSKLVLFSAAGSVFCCGLDF----------GYFVKHLRNNRNTAslemvdtiknfvNT 375
Cdd:PRK06495  25 NALSRELRDELIAVFDEiSERPDVRVVVLTGAGKVFCAGADLkgrpdvikgpGDLRAHNRRTRECF------------HA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   376 FIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSpDGCSSITfpKMMGKASANEMLIAGRKLTARE 455
Cdd:PRK06495  93 IRECAKPVIAAVNGPALGAGLGLVASCDIIVASENAVFGLPEIDVGLA-GGGKHAM--RLFGHSLTRRMMLTGYRVPAAE 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4757966   456 ACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKA 495
Cdd:PRK06495 170 LYRRGVIEACLPPEELMPEAMEIAREIASKSPLATRLAKD 209
PRK08138 PRK08138
enoyl-CoA hydratase; Provisional
 286-508 2.71e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 236162 [Multi-domain]  Cd Length: 261  Bit Score: 75.86  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVK------HLRNN- 357
Cdd:PRK08138  10 LLERPADGVALLRLN-RPEARNALNMEVRQQLAEHFTELSEDPDiRAIVLTGGEKVFAAGADIKEFATagaiemYLRHTe 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   358 RNTASLEmvdtiknfvntfiQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMG 437
Cdd:PRK08138  89 RYWEAIA-------------QCPKPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGLMPGAGGTQRLVRAVG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4757966   438 KASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQA 508
Cdd:PRK08138 156 KFKAMRMALTGCMVPAPEALAIGLVSEVVEDEQTLPRALELAREIARMPPLALAQIKEVVLAGADAPLDAA 226
PRK07657 PRK07657
enoyl-CoA hydratase; Provisional
 302-506 2.87e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 181069 [Multi-domain]  Cd Length: 260  Bit Score: 75.93  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   302 RSTEKNALNTEVIKEIVNALNSAAAD-DSKLVLFSAAG-SVFCCGLDfgyfVKHLRNNRNTASLEMVDTIKNFVNTFIQF 379
Cdd:PRK07657  21 RPRAANALSLALLEELQNILTQINEEaNVRVVILTGAGeKAFCAGAD----LKERAGMNEEQVRHAVSLIRTTMEMVEQL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   380 KKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAK 459
Cdd:PRK07657  97 PQPVIAAINGIALGGGLELALACDFRIAAESASLGLTETTLAIIPGAGGTQRLPRLIGVGRAKELIYTGRRISAQEAKEI 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4757966   460 GLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELE 506
Cdd:PRK07657 177 GLVEFVVPAHLLEEKAIEIAEKIASNGPIAVRQAKEAISNGIQVDLH 223
PRK05995 PRK05995
enoyl-CoA hydratase; Provisional
 281-498 1.25e-14

enoyl-CoA hydratase; Provisional


Pssm-ID: 235664 [Multi-domain]  Cd Length: 262  Bit Score: 74.19  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   281 STYRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLD-------FGYFvk 352
Cdd:PRK05995   1 MMYETLEIEQRGQVATVTLN-RPDVRNAFNETVIAELTAAFRALDADDSvRAVVLAGAGKAFCAGADlnwmkkmAGYS-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   353 HLRNNRNTASL-EMVDTIKNFvntfiqfKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSIT 431
Cdd:PRK05995  78 DDENRADARRLaDMLRAIYRC-------PKPVIARVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLGLIPATISPYV 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757966   432 FpKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVR 498
Cdd:PRK05995 151 I-RAMGERAARRYFLTAERFDAAEALRLGLVHEVVPAEALDAKVDELLAALVANSPQAVRAGKRLVR 216
PRK08139 PRK08139
enoyl-CoA hydratase; Validated
 291-516 1.99e-14

enoyl-CoA hydratase; Validated


Pssm-ID: 181249  Cd Length: 266  Bit Score: 73.44  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   291 EDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDfgyfVKHLRNNRNTASLE-MVDT 368
Cdd:PRK08139  18 RDGVATLTLN-RPQAFNALSEAMLAALQAALDAIAADPSvRVVVLAAAGKAFCAGHD----LKEMRAARGLAYFRaLFAR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   369 IKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSpdgCS--SITFPKMMGKASANEMLI 446
Cdd:PRK08139  93 CSRVMQAIVALPQPVIARVHGIATAAGCQLVASCDLAVAADTARFAVPGVNIGLF---CStpMVALSRNVPRKQAMEMLL 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   447 AGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVL 516
Cdd:PRK08139 170 TGEFIDAATAREWGLVNRVVPADALDAAVARLAAVIAAKSPAAVRIGKEAFYRQAEMPLADAYAYAGDVM 239
PRK07468 PRK07468
crotonase/enoyl-CoA hydratase family protein;
302-527 2.59e-14

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180987 [Multi-domain]  Cd Length: 262  Bit Score: 73.17  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   302 RSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLRNNRNTASLEmVDTIKNFVNTFIQFK 380
Cdd:PRK07468  22 RPEKHNALSARMIAELTTAARRLAADAAvRVVVLTGAGKSFCAGGDLGWMRAQMTADRATRIEE-ARRLAMMLKALNDLP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   381 KPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMmGKASANEMLIAGRKLTAREACAKG 460
Cdd:PRK07468 101 KPLIGRIQGQAFGGGVGLISVCDVAIAVSGARFGLTETRLGLIPATISPYVVARM-GEANARRVFMSARLFDAEEAVRLG 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757966   461 LVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIE 527
Cdd:PRK07468 180 LLSRVVPAERLDAAVEAEVTPYLSCAPGAVAAAKALVRALGAPIDEAVIDATIEALADTWETEEARE 246
PLN02921 PLN02921
naphthoate synthase
 278-495 4.67e-14

naphthoate synthase


Pssm-ID: 178509 [Multi-domain]  Cd Length: 327  Bit Score: 73.28  E-value: 4.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   278 ESASTYRDIVVKK--EDGFTQIVLStRSTEKNALNTEVIKEIVNALNsAAADDSKL--VLFSAAGS-VFCCGLDfgyfvK 352
Cdd:PLN02921  59 GSGKEFTDIIYEKavGEGIAKITIN-RPERRNAFRPRTVKELQRAFN-DARDDSSVgvIILTGKGTkAFCSGGD-----Q 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   353 HLRNNRNTASLEMVDTIkNFVNTFIQFK---KPIVVSVNGPAIGlGASILPL-CDLVWANEKAWFQTPYTTFGQSPDGCS 428
Cdd:PLN02921 132 AVRGKDGYVGPDDAGRL-NVLDLQIQIRrlpKPVIAMVAGYAVG-GGHILHMvCDLTIAADNAVFGQTGPKVGSFDAGYG 209

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757966   429 SITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKA 495
Cdd:PLN02921 210 SSIMARLVGQKKAREMWFLARFYTASEALKMGLVNTVVPLDELEGETVKWCREILRNSPTAIRVLKS 276
PRK06494 PRK06494
enoyl-CoA hydratase; Provisional
 286-508 1.21e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 180591 [Multi-domain]  Cd Length: 259  Bit Score: 71.23  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDSKLV-LFSAAGS-VFCCGLDFGYFVKhlRNNRNTASL 363
Cdd:PRK06494   6 STVERKGHVTIVTLN-RPEVMNALHLDAHFELEEVFDDFAADPEQWVaIVTGAGDkAFSAGNDLKEQAA--GGKRGWPES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   364 EMVDTIKNFvntfiQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANE 443
Cdd:PRK06494  83 GFGGLTSRF-----DLDKPIIAAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGLKRAMG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4757966   444 MLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQA 508
Cdd:PRK06494 158 MILTGRRVTAREGLELGFVNEVVPAGELLAAAERWADDILACSPLSIRASKQAVYRGLEVSLEEA 222
PRK03580 PRK03580
crotonobetainyl-CoA hydratase;
381-508 1.68e-13

crotonobetainyl-CoA hydratase;


Pssm-ID: 179599 [Multi-domain]  Cd Length: 261  Bit Score: 70.49  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   381 KPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKG 460
Cdd:PRK03580  95 KPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRLPPAIANEMVMTGRRMDAEEALRWG 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4757966   461 LVSQVFLtgtfTQEVMIQIKELA----SYNPIVLEECKALVRCNIKLELEQA 508
Cdd:PRK03580 175 IVNRVVP----QAELMDRARELAqqlvNSAPLAIAALKEIYRETSEMPVEEA 222
PRK05870 PRK05870
enoyl-CoA hydratase; Provisional
 306-528 2.99e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 180298  Cd Length: 249  Bit Score: 69.75  E-value: 2.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   306 KNALNTEVIKEIVNALNSAAAD-DSKLVLFSAAGSVFCCGLDfgyfvkhLRNNRNTASLEMVDTIKNFVNTFI---QFKK 381
Cdd:PRK05870  24 RNAVTAEMSAQLRAAVAAAEADpDVHALVVTGAGKAFCAGAD-------LTALGAAPGRPAEDGLRRIYDGFLavaSCPL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   382 PIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGL 461
Cdd:PRK05870  97 PTIAAVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLGLHPGGGATWMLQRAVGPQVARAALLFGMRFDAEAAVRHGL 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4757966   462 VSQVfltgtfTQEVMIQIKEL----ASYNPIVLEECKALVRCNIKLE-LEQANEREcevlrkIWSSAQGIES 528
Cdd:PRK05870 177 ALMV------ADDPVAAALELaagpAAAPRELVLATKASMRATASLAqHAAAVEFE------LGPQAASVQS 236
PLN02888 PLN02888
enoyl-CoA hydratase
 277-514 3.88e-13

enoyl-CoA hydratase


Pssm-ID: 215480  Cd Length: 265  Bit Score: 69.78  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   277 TESASTYRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDfgyfvkhLR 355
Cdd:PLN02888   3 TQTVSENLILVPKSRNGIATITIN-RPKALNALTRPMMVELAAAFKRLDEDDSvKVIILTGSGRAFCSGVD-------LT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   356 NNRNTASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKM 435
Cdd:PLN02888  75 AAEEVFKGDVKDVETDPVAQMERCRKPIIGAINGFAITAGFEIALACDILVASRGAKFIDTHAKFGIFPSWGLSQKLSRI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   436 MGKASANEMLIAGRKLTAREACAKGLVSQVFLTGtftqEVMIQIKELA----SYNPIVLEECKALVRCNIKLELEQANER 511
Cdd:PLN02888 155 IGANRAREVSLTAMPLTAETAERWGLVNHVVEES----ELLKKAREVAeaiiKNNQGMVLRYKSVINDGLKLDLGHALQL 230


                 ...
gi 4757966   512 ECE 514
Cdd:PLN02888 231 EKE 233
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 6-56 5.48e-13

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: 63.46  E-value: 5.48e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVDKRQDkNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNR 56
Cdd:cd18633   2 FEVEKILDMKTE-GGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 5-54 1.33e-12

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: 62.36  E-value: 1.33e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4757966    5 EFEVEAIV-----DKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18968   1 EYEVEVILaarvvKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
PRK06210 PRK06210
enoyl-CoA hydratase; Provisional
 280-466 2.49e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 180472  Cd Length: 272  Bit Score: 67.42  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   280 ASTYRDIVVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYF----VKHL 354
Cdd:PRK06210   1 DMAYDAVLYEVADSGVAVITLNRPDRLNAWTPVMEAEVYAAMDRAEADPAvRVIVLTGAGRGFCAGADMGELqtidPSDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   355 RNNRNTASLEM-----VDTIKNFvntFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSS 429
Cdd:PRK06210  81 RRDTDVRPFVGnrrpdYQTRYHF---LTALRKPVIAAINGACAGIGLTHALMCDVRFAADGAKFTTAFARRGLIAEHGIS 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4757966   430 ITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVF 466
Cdd:PRK06210 158 WILPRLVGHANALDLLLSARTFYAEEALRLGLVNRVV 194
PRK06072 PRK06072
enoyl-CoA hydratase; Provisional
 286-462 3.65e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 168377 [Multi-domain]  Cd Length: 248  Bit Score: 66.34  E-value: 3.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAAD-DSKLVLFSAAGSVFCCGLDFGYFVKHLrnnrnTASLE 364
Cdd:PRK06072   2 IKVESREGYAIVTMS-RPDKLNALNLEMRNEFISKLKQINADpKIRVVIVTGEGRAFCVGADLSEFAPDF-----AIDLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   365 mvdtiknfvNTF------IQFKKPIVVS-VNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMG 437
Cdd:PRK06072  76 ---------ETFypiireIRFSDKIYISaINGVTAGACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYFLLKLTG 146

                        170       180
                 ....*....|....*....|....*
gi 4757966   438 kASANEMLIAGRKLTAREACAKGLV 462
Cdd:PRK06072 147 -QRFYEILVLGGEFTAEEAERWGLL 170
PRK08252 PRK08252
crotonase/enoyl-CoA hydratase family protein;
285-530 3.75e-12

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181325 [Multi-domain]  Cd Length: 254  Bit Score: 66.55  E-value: 3.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   285 DIVVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADD--SKLVLfSAAGSVFCCGLDFGYFVKHLR---NNRN 359
Cdd:PRK08252   3 DEVLVERRGRVLIITINRPEARNAVNAAVAQGLAAALDELDADPdlSVGIL-TGAGGTFCAGMDLKAFARGERpsiPGRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   360 TASLemvdtiknfvnTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKA 439
Cdd:PRK08252  82 FGGL-----------TERPPRKPLIAAVEGYALAGGFELALACDLIVAARDAKFGLPEVKRGLVAAGGGLLRLPRRIPYH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   440 SANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKI 519
Cdd:PRK08252 151 IAMELALTGDMLTAERAHELGLVNRLTEPGQALDAALELAERIAANGPLAVAASKRIVVESGDWSEDEMFARQRELIAPV 230

                        250
                 ....*....|.
gi 4757966   520 WSSAQGIESML 530
Cdd:PRK08252 231 FTSADAKEGAT 241
PRK06144 PRK06144
enoyl-CoA hydratase; Provisional
 285-530 3.78e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 180424 [Multi-domain]  Cd Length: 262  Bit Score: 66.55  E-value: 3.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   285 DIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS--KLVLFSAAGSVFCCGLDFGYFVKhLRNNRNTAS 362
Cdd:PRK06144   9 ELLLEVRGGIARITFN-RPAARNAMTWAMYEGLAEICEAIAADPSirAVVLRGAGDKAFVAGTDIAQFRA-FSTAEDAVA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   363 LEMvdTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYT-TFGQ--SPDGCSSITfpKMMGKA 439
Cdd:PRK06144  87 YER--RIDRVLGALEQLRVPTIAAIAGACVGGGAAIAAACDLRIATPSARFGFPIArTLGNclSMSNLARLV--ALLGAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   440 SANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRcniklELEQANERECE-VLRK 518
Cdd:PRK06144 163 RVKDMLFTARLLEAEEALAAGLVNEVVEDAALDARADALAELLAAHAPLTLRATKEALR-----RLRREGLPDGDdLIRM 237

                        250
                 ....*....|....*
gi 4757966   519 IWSSA---QGIESML 530
Cdd:PRK06144 238 CYMSEdfrEGVEAFL 252
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
 5-54 4.33e-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: 61.17  E-value: 4.33e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4757966    5 EFEVEAIVDKRQDKNGNT-----QYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18635   1 EFEVEKLVGICYGDPKKTgerglYFKVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
PRK07260 PRK07260
enoyl-CoA hydratase; Provisional
 283-465 1.37e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 180910 [Multi-domain]  Cd Length: 255  Bit Score: 64.76  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   283 YRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYfVKHLRNNRNTA 361
Cdd:PRK07260   1 FEHIIYEVEDDLATLTLN-RPEVSNGFNIPMCQEILEALRLAEEDPSvRFLLINANGKVFSVGGDLVE-MKRAVDEDDVQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   362 SL----EMVDTIkNFvnTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMG 437
Cdd:PRK07260  79 SLvkiaELVNEI-SF--AIKQLPKPVIMCVDGAVAGAAANMAVAADFCIASTKTKFIQAFVGVGLAPDAGGLFLLTRAIG 155

                        170       180
                 ....*....|....*....|....*...
gi 4757966   438 KASANEMLIAGRKLTAREACAKGLVSQV 465
Cdd:PRK07260 156 LNRATHLAMTGEALTAEKALEYGFVYRV 183
PRK05864 PRK05864
enoyl-CoA hydratase; Provisional
 296-463 1.43e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 168278 [Multi-domain]  Cd Length: 276  Bit Score: 65.24  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   296 QIVLST--RSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLD--FGYFVKHLRN-NRNTASLEMVDTI 369
Cdd:PRK05864  19 EIALITlnRPERMNSMAFDVMVPLKEALAEVSYDNSvRVVVLTGAGRGFSSGADhkSAGVVPHVEGlTRPTYALRSMELL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   370 KNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFG--QSPDGCSSItFPKMMGKASANEMLIA 447
Cdd:PRK05864  99 DDVILALRRLHQPVIAAVNGPAIGGGLCLALAADIRVASSSAYFRAAGINNGltASELGLSYL-LPRAIGSSRAFEIMLT 177

                        170
                 ....*....|....*.
gi 4757966   448 GRKLTAREACAKGLVS 463
Cdd:PRK05864 178 GRDVDAEEAERIGLVS 193
PRK05674 PRK05674
gamma-carboxygeranoyl-CoA hydratase; Validated
 293-529 1.70e-11

gamma-carboxygeranoyl-CoA hydratase; Validated


Pssm-ID: 168168  Cd Length: 265  Bit Score: 64.83  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   293 GFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLRNNRNTaSLEMVDTIKN 371
Cdd:PRK05674  15 GFATLWLS-RADKNNAFNAQMIRELILALDQVQSDASlRFLLLRGRGRHFSAGADLAWMQQSADLDYNT-NLDDARELAE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   372 FVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFpKMMGKASANEMLIAGRKL 451
Cdd:PRK05674  93 LMYNLYRLKIPTLAVVQGAAFGGALGLISCCDMAIGADDAQFCLSEVRIGLAPAVISPFVV-KAIGERAARRYALTAERF 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757966   452 TAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECE-VLRKIWSSAQGIESM 529
Cdd:PRK05674 172 DGRRARELGLLAESYPAAELEAQVEAWIANLLLNSPQALRASKDLLREVGDGELSPALRRYCEnAIARIRVSAEGQEGL 250
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
 5-58 1.75e-11

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: 59.44  E-value: 1.75e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4757966    5 EFEVEAIVD-KRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQ 58
Cdd:cd18632   1 EYEVEKIVDeKTDRNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRKK 55
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 5-54 2.58e-11

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: 58.60  E-value: 2.58e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    5 EFEVEAIVDKRQdKNGNTQYLVRWKGYDKQDDTWEPEQHLmNCEKCVHDF 54
Cdd:cd18631   1 EYVVEKVLDRRV-VKGKVEYLLKWKGYPDEDNTWEPEENL-DCPDLIAEF 48
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
 5-54 3.47e-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: 58.35  E-value: 3.47e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    5 EFEVEAIVDKRQDK--NGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18980   3 EYEVEAILDHKVDRryRDPNFYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
PRK06142 PRK06142
crotonase/enoyl-CoA hydratase family protein;
279-498 5.57e-11

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235714  Cd Length: 272  Bit Score: 63.45  E-value: 5.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   279 SASTYRDIVVKKEDGFTQIVLsTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLD-------FGYF 350
Cdd:PRK06142   1 MMTTYESFTVELADHVAQVTL-NRPGKGNAMNPAFWSELPEIFRWLDADPEvRAVVLSGSGKHFSYGIDlpamagvFGQL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   351 VKHLRNNRNTASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSI 430
Cdd:PRK06142  80 GKDGLARPRTDLRREILRLQAAINAVADCRKPVIAAVQGWCIGGGVDLISACDMRYASADAKFSVREVDLGMVADVGSLQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757966   431 TFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTG-TFTQEVMIQIKELASYNPIVLEECKALVR 498
Cdd:PRK06142 160 RLPRIIGDGHLRELALTGRDIDAAEAEKIGLVNRVYDDAdALLAAAHATAREIAAKSPLAVRGTKEVLD 228
PRK07827 PRK07827
enoyl-CoA hydratase family protein;
306-530 1.40e-10

enoyl-CoA hydratase family protein;


Pssm-ID: 236109 [Multi-domain]  Cd Length: 260  Bit Score: 62.01  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   306 KNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLRNNRNTAS---LEMVDTIKNFVntfiQFKK 381
Cdd:PRK07827  27 RNALSARLVAQLHDGLRAAAADPAvRAVVLTHTGGTFCAGADLSEAGGGGGDPYDAAVaraREMTALLRAIV----ELPK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   382 PIVVSVNG--PAIGLGasILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKAsANEMLIAGRKLTAREACAK 459
Cdd:PRK07827 103 PVIAAIDGhvRAGGFG--LVGACDIVVAGPESTFALTEARIGVAPAIISLTLLPRLSPRA-AARYYLTGEKFGAAEAARI 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4757966   460 GLVSQVflTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESML 530
Cdd:PRK07827 180 GLVTAA--ADDVDAAVAALLADLRRGSPQGLAESKALTTAAVLAGFDRDAEELTEESARLFVSDEAREGMT 248
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
 6-54 2.18e-10

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: 56.10  E-value: 2.18e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 4757966    6 FEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18973   1 YVVEAILDNKRRK-GKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKY 48
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
 5-56 2.50e-10

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: 55.79  E-value: 2.50e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    5 EFEVEAIVDKRQDKNgNTQYLVRWKGYDKQDDTWEPeQHLMNCEKCVHDFNR 56
Cdd:cd18978   3 SYEVEKIINHRGEKN-RRKYLVKWKGYDDTDNSWVT-QEDFNDKDMIDEYEN 52
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 6-44 4.37e-10

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: 54.98  E-value: 4.37e-10
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4757966    6 FEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHL 44
Cdd:cd18966   1 YEVERILAERRDD-GGKRYLVKWEGYPLEEATWEPEENI 38
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
 6-56 5.31e-10

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: 54.96  E-value: 5.31e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    6 FEVEAIVDKRQdKNGNTQYLVRWKGYDKQDDTWEPEQHL-MNCEKCVHDFNR 56
Cdd:cd18638   2 FEVEKIVKKKT-VKGGTEYFVKWKGYSAKENTWETEDNLeKSYKEMIDEFEK 52
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
 6-56 6.29e-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: 54.76  E-value: 6.29e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNR 56
Cdd:cd18636   2 YEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
PRK06127 PRK06127
enoyl-CoA hydratase; Provisional
 307-506 6.63e-10

enoyl-CoA hydratase; Provisional


Pssm-ID: 235705  Cd Length: 269  Bit Score: 60.10  E-value: 6.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   307 NALNTEVIKEIVNALNSAAADDS-KLVLFSAAGS-VFCCGLDFGYFVKhLRNNRNtASLEMVDTIKNFVNTFIQFKKPIV 384
Cdd:PRK06127  33 NAMSLDMWEALPQALAAAEDDDAiRVVVLTGAGEkAFVSGADISQFEE-SRSDAE-AVAAYEQAVEAAQAALADYAKPTI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   385 VSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFG--QSPDGCSSITfpKMMGKASANEMLIAGRKLTAREACAKGLV 462
Cdd:PRK06127 111 ACIRGYCIGGGMGIALACDIRIAAEDSRFGIPAARLGlgYGYDGVKNLV--DLVGPSAAKDLFYTARRFDAAEALRIGLV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4757966   463 SQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELE 506
Cdd:PRK06127 189 HRVTAADDLETALADYAATIAGNAPLTLRAAKRAIAELLKDEPE 232
PLN02874 PLN02874
3-hydroxyisobutyryl-CoA hydrolase-like protein
 286-461 9.58e-10

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178462 [Multi-domain]  Cd Length: 379  Bit Score: 60.58  E-value: 9.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHlrNNRNTASLE 364
Cdd:PLN02874  12 VVLGEEKGRVRVITLNRPRQLNVISLSVVSLLAEFLEQWEKDDSvELIIIKGAGRAFSAGGDLKMFYDG--RESDDSCLE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   365 MVdTIKNFVNTFIQ-FKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASanE 443
Cdd:PLN02874  90 VV-YRMYWLCYHIHtYKKTQVALVHGLVMGGGAGLMVPMKFRVVTEKTVFATPEASVGFHTDCGFSYILSRLPGHLG--E 166

                        170
                 ....*....|....*....
gi 4757966   444 ML-IAGRKLTAREACAKGL 461
Cdd:PLN02874 167 YLaLTGARLNGKEMVACGL 185
PRK08150 PRK08150
crotonase/enoyl-CoA hydratase family protein;
285-462 1.22e-09

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181254  Cd Length: 255  Bit Score: 58.88  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   285 DIVVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDSKLVLFsAAGSVFCCGLDFGYFVKHLRNNRNTASL- 363
Cdd:PRK08150   2 SLVSYELDGGVATIGLNRPAKRNALNDGLIAALRAAFARLPEGVRAVVLH-GEGDHFCAGLDLSELRERDAGEGMHHSRr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   364 --EMVDTIknfvntfiQFKK-PIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKAS 440
Cdd:PRK08150  81 whRVFDKI--------QYGRvPVIAALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGIFVGGGGSVRVPRLIGVAR 152

                        170       180
                 ....*....|....*....|..
gi 4757966   441 ANEMLIAGRKLTAREACAKGLV 462
Cdd:PRK08150 153 MTDMMLTGRVYDAQEGERLGLA 174
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 6-56 1.39e-09

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: 53.72  E-value: 1.39e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLmNCEKCVHDFNR 56
Cdd:cd18960   2 FVVERILDKRLGRNGGEEFLIKWQGFPESDSSWEPRENL-QCDEMLEEFEK 51
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
 5-54 1.47e-09

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: 53.86  E-value: 1.47e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    5 EFEVEAIVDKRQdKNGNTQYLVRWKGYDKQDDTWEPEQHLmNCEKCVHDF 54
Cdd:cd18652   1 EFVVEKVLDRRV-VNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
 5-54 1.69e-09

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: 53.68  E-value: 1.69e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    5 EFEVEAIVDKRQdKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18630   1 EYVVEKILGKRF-VNGRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
PRK08258 PRK08258
enoyl-CoA hydratase family protein;
291-465 1.78e-09

enoyl-CoA hydratase family protein;


Pssm-ID: 181329  Cd Length: 277  Bit Score: 58.82  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   291 EDGFTQIVLStRSTEKNALNTEVIKEIVNALNS-AAADDSKLVLFSAAGSVFCCGLD----FGYFVK-----HLRNNRNT 360
Cdd:PRK08258  24 DDGVATITLN-RPERKNPLTFESYAELRDLFRElVYADDVKAVVLTGAGGNFCSGGDvheiIGPLTKmdmpeLLAFTRMT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   361 ASLemvdtiknfVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSpdGC---SSITFPKMMG 437
Cdd:PRK08258 103 GDL---------VKAMRACPQPIIAAVDGVCAGAGAILAMASDLRLGTPSAKTAFLFTRVGLA--GAdmgACALLPRIIG 171

                        170       180
                 ....*....|....*....|....*...
gi 4757966   438 KASANEMLIAGRKLTAREACAKGLVSQV 465
Cdd:PRK08258 172 QGRASELLYTGRSMSAEEGERWGFFNRL 199
PLN02157 PLN02157
3-hydroxyisobutyryl-CoA hydrolase-like protein
 273-519 2.09e-09

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 177817 [Multi-domain]  Cd Length: 401  Bit Score: 59.70  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   273 TIRLTESASTYRdiVVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFgYFV 351
Cdd:PLN02157  27 SLKLTPEDLDYQ--VLVEGSGCSRTAILNRPPALNALTTHMGYRLQKLYKNWEEDPNiGFVMMKGSGRAFCAGGDI-VSL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   352 KHLRNNRNTASL-EMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSI 430
Cdd:PLN02157 104 YHLRKRGSPDAIrEFFSSLYSFIYLLGTYLKPHVAILNGVTMGGGTGVSIPGTFRVATDRTIFATPETIIGFHPDAGASF 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   431 TFPKMMGKAsANEMLIAGRKLTAREACAKGLVSQVFLtgtfTQEVMI---QIKELASYNPIVLEECkaLVRCnikleLEQ 507
Cdd:PLN02157 184 NLSHLPGRL-GEYLGLTGLKLSGAEMLACGLATHYIR----SEEIPVmeeQLKKLLTDDPSVVESC--LEKC-----AEV 251

                        250
                 ....*....|..
gi 4757966   508 ANERECEVLRKI 519
Cdd:PLN02157 252 AHPEKTGVIRRI 263
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
 5-54 2.53e-09

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: 53.02  E-value: 2.53e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    5 EFEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLmNCEKCVHDF 54
Cdd:cd18650   1 EYVVEKVLDRRVVK-GKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEF 48
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
 5-54 3.16e-09

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: 52.73  E-value: 3.16e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    5 EFEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLmNCEKCVHDF 54
Cdd:cd18653   1 EYAVEKICDRRVRK-GKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
 6-48 4.40e-09

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: 52.44  E-value: 4.40e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4757966    6 FEVEAIVDKRQDKNGnTQYLVRWKGYDKQDDTWEPEQHLMNCE 48
Cdd:cd18970   1 FFVERILDERRRGRG-WQYLVRWLGYGPSDDSWLPRRELEECE 42
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
 6-56 4.60e-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: 4.60e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVDKRqDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNR 56
Cdd:cd18974   1 WEVEEIVDEK-MIDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
 3-58 8.86e-09

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: 51.70  E-value: 8.86e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4757966    3 SQEFEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMNcEKCVHDFNRRQ 58
Cdd:cd18644   1 DLVYAAEKILKKRVRK-GKVEYLVKWKGWSNKHNTWEPEENILD-RRLIEIFERTN 54
PRK06143 PRK06143
enoyl-CoA hydratase; Provisional
 307-498 8.88e-09

enoyl-CoA hydratase; Provisional


Pssm-ID: 180423  Cd Length: 256  Bit Score: 56.58  E-value: 8.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   307 NALNTEVIKEIVNALNSAAADDSK--LVLFSAAGSVFCCGLDFgyfvkhlrnnRNTASLE------MVDTIKNFVNTFIQ 378
Cdd:PRK06143  29 NILGTPVILALTQALRWLAADPDVrvLVLRGAGEKAFIGGADI----------KEMATLDqasaeaFISRLRDLCDAVRH 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   379 FKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGqSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACA 458
Cdd:PRK06143  99 FPVPVIARIPGWCLGGGLELAAACDLRIAAHDAQFGMPEVRVG-IPSVIHAALLPRLIGWARTRWLLLTGETIDAAQALA 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4757966   459 KGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVR 498
Cdd:PRK06143 178 WGLVDRVVPLAELDAAVERLAASLAGCGPQALRQQKRLLR 217
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
 5-54 1.04e-08

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: 51.53  E-value: 1.04e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    5 EFEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLmNCEKCVHDF 54
Cdd:cd18651   1 EYVVEKVLDRRVVK-GQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEF 48
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 286-465 1.09e-08

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: 57.92  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    286 IVVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS--KLVLFSAAGSVFCCGLDFGyFVKHLRNNRNTASL 363
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGADIQ-MIAACKTAQEVTQL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    364 -----EMVDTIKnfvntfiQFKKPIVVSVNGPAIGLGASILPLCDLVWA--NEKAWFQTPYTTFGQSPDGCSSITFPKMM 436
Cdd:TIGR02441  94 sqegqEMFERIE-------KSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLT 166

                         170       180
                  ....*....|....*....|....*....
gi 4757966    437 GKASANEMLIAGRKLTAREACAKGLVSQV 465
Cdd:TIGR02441 167 GVPAALDMMLTGKKIRADRAKKMGIVDQL 195
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 6-46 2.78e-08

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: 50.08  E-value: 2.78e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMN 46
Cdd:cd18627   1 FAAECILKKRIRK-GKVEYLVKWKGWSQKYNTWEPEENILD 40
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
 5-51 3.05e-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: 50.17  E-value: 3.05e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    5 EFEVEAIVDKRQDKNGN---TQYLVRWKGYDKQDDTWEPEQHLMNCEKCV 51
Cdd:cd18977   3 EYEVEKIVGEKWKKRKNrrvKLYKVRFKGYGPEEDEWLTKEELKNAPEIL 52
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
 5-50 3.13e-08

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: 50.20  E-value: 3.13e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4757966    5 EFEVEAIVDKRQDKNGNT-QYLVRWKGYDKQDD-TWEPEQhlmNCEKC 50
Cdd:cd18637   1 EYVVEKILKHRMARKGGGyEYLLKWEGYDDPSDnTWSSEA---DCAGC 45
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
 4-46 4.15e-08

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: 49.70  E-value: 4.15e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4757966    4 QEFEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMN 46
Cdd:cd18646   3 QVFAVESIRKKRVRK-GKVEYLVKWKGWPPKYSTWEPEEHILD 44
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
 6-54 4.31e-08

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: 49.43  E-value: 4.31e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 4757966    6 FEVEAIVDKRQdKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18972   1 YEVEAIVGHKP-KKKPRQFLVSWLGYDSSHNEWKQKEELENARELLQDY 48
PRK07509 PRK07509
crotonase/enoyl-CoA hydratase family protein;
286-465 4.47e-08

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181008 [Multi-domain]  Cd Length: 262  Bit Score: 54.50  E-value: 4.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLsTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFV-----------KH 353
Cdd:PRK07509   5 VSVTIEDGIADVRL-NRPDKMNALDFAMFEELIATIKRLKKDRGiRAVILSGEGGAFCAGLDVKSVAsspgnavkllfKR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   354 LRNNRNTAslemvdtiKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWAnekawfqTPYTTF-------GQSPDG 426
Cdd:PRK07509  84 LPGNANLA--------QRVSLGWRRLPVPVIAALEGVCFGGGLQIALGADIRIA-------APDTKLsimeakwGLVPDM 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4757966   427 CSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQV 465
Cdd:PRK07509 149 AGTVSLRGLVRKDVARELTYTARVFSAEEALELGLVTHV 187
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
 4-57 6.19e-08

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: 49.28  E-value: 6.19e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 4757966    4 QEFEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHdFNRR 57
Cdd:cd18647   2 QVFAAECILSKRLRK-GKLEYLVKWRGWSSKHNSWEPEENILDPRLLLA-FQKK 53
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
 6-54 6.47e-08

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: 49.05  E-value: 6.47e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 4757966    6 FEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLmNCEKCVHDF 54
Cdd:cd18639   1 YEVEYLCDYKKIR-EQEYYLVKWKGYPDSENTWEPRQNL-KCSRLLKQF 47
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
 6-56 1.83e-07

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: 47.92  E-value: 1.83e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMNcEKCVHDFNR 56
Cdd:cd18975   1 YEVESILNSRLHR-GKLQYLIQWKGYPLEEASWELEDNIKN-PRLIEEFHK 49
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 6-54 2.23e-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: 349320  Cd Length: 54  Bit Score: 47.71  E-value: 2.23e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    6 FEVEAIVDKRQDKN---GNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18964   1 FFVERIIGRRPSARdgpGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDF 52
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
 6-54 3.11e-07

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: 47.29  E-value: 3.11e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    6 FEVEAIVDKRQDKNGNT-QYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18640   1 EPVEKIVAKRFNPRKKTwEYLVKWENRSHHENTWEPMANLERCKYLLQMF 50
PRK09120 PRK09120
p-hydroxycinnamoyl CoA hydratase/lyase; Validated
 286-508 3.25e-07

p-hydroxycinnamoyl CoA hydratase/lyase; Validated


Pssm-ID: 236383  Cd Length: 275  Bit Score: 51.93  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNS-AAADDSKLVLFSAAGSVFCCGLDFG-YFvkhlrnnRNTASL 363
Cdd:PRK09120  10 VKVEVEDGIAWVTLN-RPEKRNAMSPTLNREMIDVLDAlEFDDDAGVLVLTGAGDAWSAGMDLKeYF-------RETDAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   364 EMVDTIKnfvntfIQ------------FKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSIT 431
Cdd:PRK09120  82 PEILQER------IRreaygwwrrlrwYQKPTIAMVNGWCFGGGFSPLVACDLAIAADEAQFGLSEINWGIPPGGGVSKA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757966   432 FPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKALVRCNIKLELEQA 508
Cdd:PRK09120 156 MADTVGHRDALYYIMTGETFTGRKAAEMGLVNESVPLAQLRARTRELAAKLLEKNPVVLRAAKDGFKRVRELTWDQA 232
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 8-56 4.20e-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: 349321  Cd Length: 53  Bit Score: 46.70  E-value: 4.20e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    8 VEAIVDKRQdKNGNTQYLVRWKGYDKQDDTWEPEQ---HLMNCEKCVHDFNR 56
Cdd:cd18965   3 IEALLKKRQ-FNRKLEYLVKWHGLPESENTWEREKdikHVSHWKQLLKDLRA 53
PRK07110 PRK07110
polyketide biosynthesis enoyl-CoA hydratase; Validated
 286-483 7.91e-07

polyketide biosynthesis enoyl-CoA hydratase; Validated


Pssm-ID: 235936  Cd Length: 249  Bit Score: 50.35  E-value: 7.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLSTRsTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLRNnrntaslE 364
Cdd:PRK07110   7 ELREVEEGIAQVTMQDR-VNKNAFSDELCDQLHEAFDTIAQDPRyKVVILTGYPNYFATGGTQEGLLSLQTG-------K 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   365 MVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:PRK07110  79 GTFTEANLYSLALNCPIPVIAAMQGHAIGGGLVLGLYADIVVLSRESVYTANFMKYGFTPGMGATAILPEKLGLALGQEM 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4757966   445 LIAGRKLTAREACAKGlvsqVFLTGTFTQEVMIQIKELA 483
Cdd:PRK07110 159 LLTARYYRGAELKKRG----VPFPVLPRAEVLEKALELA 193
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
 7-42 8.56e-07

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: 46.03  E-value: 8.56e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4757966    7 EVEAIVDKRQDKNGNTQYLVRWKG--YDkqDDTWEPEQ 42
Cdd:cd18659   4 IVERIIAHREDDEGVTEYLVKWKGlpYD--ECTWESEE 39
PRK07327 PRK07327
enoyl-CoA hydratase/isomerase family protein;
290-463 9.03e-07

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 235991  Cd Length: 268  Bit Score: 50.40  E-value: 9.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   290 KEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGyFVKHLRNN---RNTASLEM 365
Cdd:PRK07327  18 PPPGVLEIVLN-GPGALNAADARMHRELADIWRDVDRDPDvRVVLIRGEGKAFSAGGDLA-LVEEMADDfevRARVWREA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   366 VDTIKNFVNtfiqFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEML 445
Cdd:PRK07327  96 RDLVYNVIN----CDKPIVSAIHGPAVGAGLVAALLADISIAAKDARIIDGHTRLGVAAGDHAAIVWPLLCGMAKAKYYL 171

                        170
                 ....*....|....*...
gi 4757966   446 IAGRKLTAREACAKGLVS 463
Cdd:PRK07327 172 LLCEPVSGEEAERIGLVS 189
PRK12478 PRK12478
crotonase/enoyl-CoA hydratase family protein;
309-510 1.24e-06

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 183548  Cd Length: 298  Bit Score: 50.34  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   309 LNTEVI---KEIVNALNSAAAD-DSKLVLFSAAGSVFCCGLDFGYFVKHLRNNRNTASleMVDTIKNF----------VN 374
Cdd:PRK12478  26 LNTIVPpmpDEIEAAIGLAERDqDIKVIVLRGAGRAFSGGYDFGGGFQHWGEAMMTDG--RWDPGKDFamvtaretgpTQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   375 TFIQF---KKPIVVSVNGPAIGlGASILPLC-DLVWANEKAWFQTPYT-TFGQSPDGcssiTFPKMMGKASANEMLIAGR 449
Cdd:PRK12478 104 KFMAIwraSKPVIAQVHGWCVG-GASDYALCaDIVIASDDAVIGTPYSrMWGAYLTG----MWLYRLSLAKVKWHSLTGR 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4757966   450 KLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASynpIVLEECKALvrcniKLELEQANE 510
Cdd:PRK12478 179 PLTGVQAAEAELINEAVPFERLEARVAEVATELAR---IPLSQLQAQ-----KLIVNQAYE 231
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
 6-48 1.41e-06

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: 45.46  E-value: 1.41e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 4757966    6 FEVEAIVDKRQDK--NGNTQYLVRWKGYDKQddTWEPEQHLMNCE 48
Cdd:cd18971   1 YEVEEILAARRRRirGKGREVLVKWVGYAEP--TWEPLDNLADTA 43
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 6-62 1.47e-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: 45.43  E-value: 1.47e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4757966    6 FEVEAIVdKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNcEKCVHDFNRRQTEKQ 62
Cdd:cd18648   4 FAAESII-KRRIRKGRIEYLVKWKGWAIKYSTWEPEENILD-SRLIAAFEQKERERE 58
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
 6-46 2.21e-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: 45.10  E-value: 2.21e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 4757966    6 FEVEAIVdKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMN 46
Cdd:cd18649   5 FAAEALL-KRRIRKGRMEYLVKWKGWSQKYSTWEPEENILD 44
PRK08259 PRK08259
crotonase/enoyl-CoA hydratase family protein;
286-485 2.59e-06

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 236205  Cd Length: 254  Bit Score: 49.12  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   286 IVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAADDSKLV-LFSAAGSVFCCGLDFGYfVKHLRNNRNTASLE 364
Cdd:PRK08259   5 VRVERNGPVTTVILN-RPEVRNAVDGPTAAALADAFRAFDADDAASVaVLWGAGGTFCAGADLKA-VGTGRGNRLHPSGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   365 --MVDTiknfvntFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGqSP--DGcSSITFPKMMGKAS 440
Cdd:PRK08259  83 gpMGPS-------RMRLSKPVIAAVSGYAVAGGLELALWCDLRVAEEDAVFGVFCRRWG-VPliDG-GTVRLPRLIGHSR 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 4757966   441 ANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASY 485
Cdd:PRK08259 154 AMDLILTGRPVDADEALAIGLANRVVPKGQARAAAEELAAELAAF 198
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
 6-58 2.95e-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: 44.66  E-value: 2.95e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4757966    6 FEVEAIvDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQ 58
Cdd:cd18645   4 FAVESI-EKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRER 55
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
 8-56 3.28e-06

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: 44.48  E-value: 3.28e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4757966    8 VEAIVDKRQDKnGNTQYLVRWKGYDKQDDTWEPEQHLMN-CEKCVHDFNR 56
Cdd:cd18976   3 VESLLDRRKVR-GQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAYDA 51
PRK11423 PRK11423
methylmalonyl-CoA decarboxylase; Provisional
 301-465 3.49e-06

methylmalonyl-CoA decarboxylase; Provisional


Pssm-ID: 236908 [Multi-domain]  Cd Length: 261  Bit Score: 48.87  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   301 TRSTEKNALNTEVIKEIVNALNSAAADDSKLVLFSAAGS--VFCCGLDFGYFVKHLRNnrntaSLEMVDTIKNFVNTFIQ 378
Cdd:PRK11423  20 NNPAKRNALSKVLIDDLMQALSDLNRPEIRVVILRAPSGskVWSAGHDIHELPSGGRD-----PLSYDDPLRQILRMIQK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   379 FKKPIVVSVNGPAIGlGASILPL-CDLVWANEKAWFQ-------TPYTTFGQspdgcssITFPKMMGKASANEMLIAGRK 450
Cdd:PRK11423  95 FPKPVIAMVEGSVWG-GAFELIMsCDLIIAASTSTFAmtpanlgVPYNLSGI-------LNFTNDAGFHIVKEMFFTASP 166

                        170
                 ....*....|....*
gi 4757966   451 LTAREACAKGLVSQV 465
Cdd:PRK11423 167 ITAQRALAVGILNHV 181
PRK05869 PRK05869
enoyl-CoA hydratase; Validated
 290-495 5.56e-06

enoyl-CoA hydratase; Validated


Pssm-ID: 235632 [Multi-domain]  Cd Length: 222  Bit Score: 47.53  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   290 KEDGFTQIVLSTRSTekNALNTEVIKEIVNALNSAAA-DDSKLVLFSAAGSVFCCGLDfgyfVKHLRNNRNTASLEMVDT 368
Cdd:PRK05869  14 QDAGLATLLLSRPPT--NALTRQVYREIVAAANELGRrDDVAAVILYGGHEIFSAGDD----MPELRTLSAQEADTAARV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   369 IKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAG 448
Cdd:PRK05869  88 RQQAVDAVAAIPKPTVAAITGYALGAGLTLALAADWRVSGDNVKFGATEILAGLAPSGDGMARLTRAAGPSRAKELVFSG 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4757966   449 RKLTAREACAKGLVSQVFLTGTFTQEVMIQIKELASYNPIVLEECKA 495
Cdd:PRK05869 168 RFFDAEEALALGLIDEMVAPDDVYDAAAAWARRFLDGPPHALAAAKA 214
PRK07112 PRK07112
enoyl-CoA hydratase/isomerase;
281-462 8.21e-06

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235938  Cd Length: 255  Bit Score: 47.37  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   281 STYRDIVVKKEDGFTQIVLStRSTEKNALNTEVIKEIVNALNSAAaDDSKLVLFSAAGSVFCCGLDFGYFvkHLRNNRNT 360
Cdd:PRK07112   1 MDYQTIRVRQQGDVCFLQLH-RPEAQNTINDRLIAECMDVLDRCE-HAATIVVLEGLPEVFCFGADFSAI--AEKPDAGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   361 ASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPdGCSSITFPKMMGKAS 440
Cdd:PRK07112  77 ADLIDAEPLYDLWHRLATGPYVTIAHVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIP-ACVLPFLIRRIGTQK 155

                        170       180
                 ....*....|....*....|..
gi 4757966   441 ANEMLIAGRKLTAREACAKGLV 462
Cdd:PRK07112 156 AHYMTLMTQPVTAQQAFSWGLV 177
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
 11-56 8.62e-06

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: 43.02  E-value: 8.62e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 4757966   11 IVDKRQDKNGNTQYLVRWK--GYDkqDDTWEPEQ-HLMNCEKCVHDFNR 56
Cdd:cd18662   9 IINHRVDKDGNTWYLVKWRdlPYD--QSTWESEDdDIPDYEKHIQEYWD 55
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
 4-54 1.48e-05

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: 42.51  E-value: 1.48e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4757966    4 QEFEVEAIVDKRQD--KNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDF 54
Cdd:cd18969   2 EEYEIEEILDVKKGgfEDGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEY 54
PLN02988 PLN02988
3-hydroxyisobutyryl-CoA hydrolase
 287-487 4.12e-05

3-hydroxyisobutyryl-CoA hydrolase


Pssm-ID: 178568 [Multi-domain]  Cd Length: 381  Bit Score: 45.86  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   287 VVKKEDGFTQIVLSTRSTEKNALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLR--NNRNTASL 363
Cdd:PLN02988  11 VLVEEKSSVRILTLNRPKQLNALSFHMISRLLQLFLAFEEDPSvKLVILKGHGRAFCAGGDVAAVVRDIEqgNWRLGANF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   364 EMVDTIKNFVntFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGkASANE 443
Cdd:PLN02988  91 FSDEYMLNYV--MATYSKAQVSILNGIVMGGGAGVSVHGRFRIATENTVFAMPETALGLFPDVGASYFLSRLPG-FFGEY 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4757966   444 MLIAGRKLTAREACAKGLVSQvFLTGTFTQEVMIQIKELASYNP 487
Cdd:PLN02988 168 VGLTGARLDGAEMLACGLATH-FVPSTRLTALEADLCRIGSNDP 210
CD_POL_like cd18979
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ...
 9-40 4.39e-05

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: 40.94  E-value: 4.39e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 4757966    9 EAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEP 40
Cdd:cd18979   4 EKVLDIRQRDKGNKEFLVQWQGLSVEEATWEP 35
CD2_cpSRP43_like cd18629
chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
 7-44 6.67e-05

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: 40.56  E-value: 6.67e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4757966    7 EVEAIVDKRQdKNGNTQYLVRWKgyDKQDDTWEPEQHL 44
Cdd:cd18629   4 EVNEILESRG-KGKDMEYLIEWK--DGGDCEWVKGVHV 38
PRK08321 PRK08321
1,4-dihydroxy-2-naphthoyl-CoA synthase;
373-465 7.74e-05

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


Pssm-ID: 181386  Cd Length: 302  Bit Score: 45.01  E-value: 7.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   373 VNTFIQF-KKPIVVSVNGPAIGLGASILPLCDLVWAN-EKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEMLIAGRK 450
Cdd:PRK08321 127 VQRLIRFmPKVVIAVVPGWAAGGGHSLHVVCDLTLASrEHARFKQTDADVGSFDGGYGSAYLARQVGQKFAREIFFLGRT 206

                         90
                 ....*....|....*
gi 4757966   451 LTAREACAKGLVSQV 465
Cdd:PRK08321 207 YSAEEAHDMGAVNAV 221
PLN02851 PLN02851
3-hydroxyisobutyryl-CoA hydrolase-like protein
 328-492 8.02e-05

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178443 [Multi-domain]  Cd Length: 407  Bit Score: 45.36  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   328 DSKLVLFSAAGSVFCCGLDFGYFVKHLRNNRNTASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASI-LPLCDLVw 406
Cdd:PLN02851  86 DIGFVLMKGSGRAFCSGADVVSLYHLINEGNVEECKLFFENLYKFVYLQGTYLKPNVAIMDGITMGCGAGIsIPGMFRV- 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   407 ANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKAsANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQeVMIQIKELASYN 486
Cdd:PLN02851 165 VTDKTVFAHPEVQMGFHPDAGASYYLSRLPGYL-GEYLALTGQKLNGVEMIACGLATHYCLNARLPL-IEERLGKLLTDD 242


                 ....*.
gi 4757966   487 PIVLEE 492
Cdd:PLN02851 243 PAVIED 248
ECH_2 pfam16113
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
 307-398 2.39e-04

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. This family differs from pfam00378 in the structure of it's C-terminus.


Pssm-ID: 465024 [Multi-domain]  Cd Length: 331  Bit Score: 43.23  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966    307 NALNTEVIKEIVNALNSAAADDS-KLVLFSAAGS-VFCCGLDfgyfVKHLRNNRNTASLEMVDTiknF------VNTFI- 377
Cdd:pfam16113  13 NALNLEMVRALLAALKAWEDDPAvKLVVLKGAGErAFCAGGD----VRALYEAAKAGGGEAGRD---FfreeyrLNYLIa 85

                          90       100
                  ....*....|....*....|....*
gi 4757966    378 QFKKPIVVSVNGpaI----GLGASI 398
Cdd:pfam16113  86 TYPKPYVALMDG--IvmggGVGLSV 108
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
291-465 3.57e-04

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 43.31  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   291 EDGFTQIVLstRSTEK-NALNTEVIKEIVNALNSAAADDS-KLVLFSAAGSVFCCGLDFGYFVKHLrnnrnTASLEMVDT 368
Cdd:PRK11730  14 EDGIAELVF--DAPGSvNKLDRATLASLGEALDALEAQSDlKGLLLTSAKDAFIVGADITEFLSLF-----AAPEEELSQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   369 IKNFVN-TFIQFKK---PIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGQSPDGCSSITFPKMMGKASANEM 444
Cdd:PRK11730  87 WLHFANsIFNRLEDlpvPTVAAINGYALGGGCECVLATDYRVASPDARIGLPETKLGIMPGFGGTVRLPRLIGADNALEW 166

                        170       180
                 ....*....|....*....|.
gi 4757966   445 LIAGRKLTAREACAKGLVSQV 465
Cdd:PRK11730 167 IAAGKDVRAEDALKVGAVDAV 187
PRK06213 PRK06213
crotonase/enoyl-CoA hydratase family protein;
307-403 4.68e-04

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235744  Cd Length: 229  Bit Score: 41.88  E-value: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   307 NALNTEVIKEIVNALNsAAADDSKLVLFSAAGSVFCCGLDFGYFVKhlrnnRNTASLEMVDTIKNFVNTFIQFKKPIVVS 386
Cdd:PRK06213  24 NALSPAMIDALNAALD-QAEDDRAVVVITGQPGIFSGGFDLKVMTS-----GAQAAIALLTAGSTLARRLLSHPKPVIVA 97

                         90
                 ....*....|....*..
gi 4757966   387 VNGPAIGLGASILPLCD 403
Cdd:PRK06213  98 CTGHAIAKGAFLLLSAD 114
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
 5-56 1.18e-03

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: 37.16  E-value: 1.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    5 EFEVEAIVdKRQDKNGNTQYLVRWKGYDKQDDTWePEQHLMNCEKCVHDFNR 56
Cdd:cd18962   3 HYVVEAIV-NDVLIDGKHMYEVKWEGYPSDHNNW-VAEWDLNDKEILRKYNK 52
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
 6-56 1.62e-03

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: 36.70  E-value: 1.62e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4757966    6 FEVEAIVDKRQdKNGNTQYLVRWKGYDKQDDTWE-PEQHLMNCEKCVHDFNR 56
Cdd:cd18961   1 YEVEKILSHRI-VNGKPLYLVMWVGYPGPVENSEmWEEDLKNCGELLKAYKD 51
PRK08788 PRK08788
enoyl-CoA hydratase; Validated
 310-466 4.79e-03

enoyl-CoA hydratase; Validated


Pssm-ID: 236338  Cd Length: 287  Bit Score: 39.12  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   310 NTEVIKEIVN-------ALNSAAADDSKLVLFSAAGSVFCCGLDFGYFVKHLRnNRNTASLEM-----VDTIKNFVNTFi 377
Cdd:PRK08788  41 NLELLDDIMNlqrairqRLDDSGLPVDFWVLASDVPGVFNLGGDLALFAELIR-AGDRDALLAyaracVDGVHAFHRGF- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   378 qfkKPIVVS---VNGPAIGLGASILPLCDLVWANEKAWFQTPYTTFGqspdgcssiTFPKM---------MGKASANEML 445
Cdd:PRK08788 119 ---GAGAISialVQGDALGGGFEAALSHHTIIAERGAKMGFPEILFN---------LFPGMgaysflarrVGPKLAEELI 186

                        170       180
                 ....*....|....*....|.
gi 4757966   446 IAGRKLTAREACAKGLVSQVF 466
Cdd:PRK08788 187 LSGKLYTAEELHDMGLVDVLV 207
PRK07938 PRK07938
enoyl-CoA hydratase family protein;
307-416 8.28e-03

enoyl-CoA hydratase family protein;


Pssm-ID: 181174  Cd Length: 249  Bit Score: 38.03  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757966   307 NALNTEVIKEIVNALNSAAAD-DSKLVLFSAAGSVFCCGLDfgyfVKHLRNNRNTASLemVDtiknfVN--TFIQFK--- 380
Cdd:PRK07938  23 NALPSAGWFALADAITAAGADpDTRVVVLRAEGRGFNAGVD----IKELQATPGFTAL--ID-----ANrgCFAAFRavy 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 4757966   381 ---KPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTP 416
Cdd:PRK07938  92 ecaVPVIAAVHGFCLGGGIGLVGNADVIVASDDATFGLP 130
 
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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