NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2077081831|ref|XP_042689617|]
View 

LOW QUALITY PROTEIN: chromodomain Y-like protein [Centrocercus urophasianus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
619-815 8.56e-47

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


:

Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 165.43  E-value: 8.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRltDDRKKESTK 697
Cdd:cd06558     1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 698 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEM 777
Cdd:cd06558    78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2077081831 778 LFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKEL 815
Cdd:cd06558   158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
335-386 2.10e-32

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: 119.47  E-value: 2.10e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 335 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 386
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 ...
619-815 8.56e-47

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


Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 165.43  E-value: 8.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRltDDRKKESTK 697
Cdd:cd06558     1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 698 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEM 777
Cdd:cd06558    78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2077081831 778 LFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKEL 815
Cdd:cd06558   158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
619-869 1.32e-42

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: 155.71  E-value: 1.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDrkkESTK 697
Cdd:COG1024     1 VLVEREGGVATITLNRPEK-LNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPE---EARA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 698 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEM 777
Cdd:COG1024    77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 778 LFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIWGSAQ 857
Cdd:COG1024   157 LLTGRRIDAEEALELGLVNRVVPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFASED 236
                         250
                  ....*....|..
gi 2077081831 858 GMDSMLKYLQRK 869
Cdd:COG1024   237 AREGIAAFLEKR 248
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
617-848 3.98e-36

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 137.31  E-value: 3.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 617 RDIVVRKQDGFTHILLsTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES 695
Cdd:PRK06688    5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD----IKDFPKAPPKPP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 696 TKMAEAIRnFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASAN 775
Cdd:PRK06688   80 DELAPVNR-FLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077081831 776 EMLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEV 848
Cdd:PRK06688  159 EMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREAAG 231
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
335-386 2.10e-32

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: 119.47  E-value: 2.10e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 335 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 386
Cdd:cd18634     1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
336-387 2.98e-23

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 93.03  E-value: 2.98e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 336 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRR 387
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
336-389 4.86e-21

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 86.88  E-value: 4.86e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831  336 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRRHN 389
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKER 55
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
639-868 1.15e-19

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: 89.34  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 639 NNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRR---LTDDRKKESTKMAEAIRnfvntfiQFKK 714
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLKEMYGEgpaHQALYRENVLDLWTLLY-------TCPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 715 PIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGL 794
Cdd:pfam00378  90 PVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEALKWGL 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 795 VSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIWGSAQGMDSMLKYLQR 868
Cdd:pfam00378 170 VDKVVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQAFLEK 243
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
619-801 7.13e-09

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


Pssm-ID: 131494 [Multi-domain]  Cd Length: 737  Bit Score: 59.47  E-value: 7.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDfIYFIRrlTDDRKKEST 696
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD-IQMIA--ACKTAQEVT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 697 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWA--NEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASA 774
Cdd:TIGR02441  92 QLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGVPAA 171
                         170       180
                  ....*....|....*....|....*..
gi 2077081831 775 NEMLFSGRKLTAQEACAKGLVSQVFWP 801
Cdd:TIGR02441 172 LDMMLTGKKIRADRAKKMGIVDQLVDP 198
 
Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
619-815 8.56e-47

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


Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 165.43  E-value: 8.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRltDDRKKESTK 697
Cdd:cd06558     1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 698 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEM 777
Cdd:cd06558    78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2077081831 778 LFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKEL 815
Cdd:cd06558   158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
619-869 1.32e-42

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: 155.71  E-value: 1.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDrkkESTK 697
Cdd:COG1024     1 VLVEREGGVATITLNRPEK-LNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPE---EARA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 698 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEM 777
Cdd:COG1024    77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 778 LFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIWGSAQ 857
Cdd:COG1024   157 LLTGRRIDAEEALELGLVNRVVPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFASED 236
                         250
                  ....*....|..
gi 2077081831 858 GMDSMLKYLQRK 869
Cdd:COG1024   237 AREGIAAFLEKR 248
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
617-848 3.98e-36

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 137.31  E-value: 3.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 617 RDIVVRKQDGFTHILLsTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES 695
Cdd:PRK06688    5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD----IKDFPKAPPKPP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 696 TKMAEAIRnFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASAN 775
Cdd:PRK06688   80 DELAPVNR-FLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077081831 776 EMLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEV 848
Cdd:PRK06688  159 EMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREAAG 231
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
335-386 2.10e-32

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: 119.47  E-value: 2.10e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 335 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 386
Cdd:cd18634     1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
PRK08260 PRK08260
enoyl-CoA hydratase; Provisional
616-834 1.19e-23

enoyl-CoA hydratase; Provisional


Pssm-ID: 236206 [Multi-domain]  Cd Length: 296  Bit Score: 102.01  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 616 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLD-------FIYFIRRL 687
Cdd:PRK08260    3 YETIRYDVADGIATITLN-RPDKLNAFTVTMARELIEAFDAADADDAvRAVIVTGAGRAFCAGADlsaggntFDLDAPRT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 688 TDDRKKEST--KMAEAIRN----FVNTFIQFKKPIIVAVNGPAIGLGASI-LPLcDVVWANEKAWFQTPYTTFGQSPDGC 760
Cdd:PRK08260   82 PVEADEEDRadPSDDGVRDgggrVTLRIFDSLKPVIAAVNGPAVGVGATMtLAM-DIRLASTAARFGFVFGRRGIVPEAA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 761 SSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVleeSKALVRNIM 834
Cdd:PRK08260  161 SSWFLPRLVGLQTALEWVYSGRVFDAQEALDGGLVRSVHPPDELLPAARALAREIADNTSPV---SVALTRQMM 231
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
336-386 1.48e-23

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: 94.08  E-value: 1.48e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 386
Cdd:cd00024     1 YEVEKILDHRV-RKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
336-387 2.98e-23

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 93.03  E-value: 2.98e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 336 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRR 387
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
PRK05809 PRK05809
short-chain-enoyl-CoA hydratase;
616-873 1.26e-22

short-chain-enoyl-CoA hydratase;


Pssm-ID: 180270 [Multi-domain]  Cd Length: 260  Bit Score: 98.28  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 616 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKK 693
Cdd:PRK05809    3 LKNVILEKEGHIAVVTIN-RPKALNALNSETLKELDTVLDDIENDDNvyAVILTGAGEKAFVAGAD----ISEMKDLNEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 694 ESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLAS 773
Cdd:PRK05809   78 EGRKFGLLGNKVFRKLENLDKPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGITPGFGGTQRLARIVGPGK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 774 ANEMLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIW 853
Cdd:PRK05809  158 AKELIYTGDMINAEEALRIGLVNKVVEPEKLMEEAKALANKIAANAPIAVKLCKDAINRGMQVDIDTAVAIEAEDFGECF 237
                         250       260
                  ....*....|....*....|
gi 2077081831 854 GSAQGMDSMLKYLQRKIDEF 873
Cdd:PRK05809  238 STEDQTEGMTAFVEKREKNF 257
PRK07511 PRK07511
enoyl-CoA hydratase; Provisional
640-845 2.65e-21

enoyl-CoA hydratase; Provisional


Pssm-ID: 181009 [Multi-domain]  Cd Length: 260  Bit Score: 94.29  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEAI---RNFVNTFIQFKKP 715
Cdd:PRK07511   25 NALHPDMYAAGIEALNTAERDPSiRAVVLTGAGGFFCAGGN----LNRLLENRAKPPSVQAASIdglHDWIRAIRAFPKP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 716 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLV 795
Cdd:PRK07511  101 VIAAVEGAAAGAGFSLALACDLLVAARDAKFVMAYVKVGLTPDGGGSWFLARALPRQLATELLLEGKPISAERLHALGVV 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077081831 796 SQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKE 845
Cdd:PRK07511  181 NRLAEPGQALAEALALADQLAAGSPNALARIKSLIADAPEATLAAQLEAE 230
CHROMO smart00298
Chromatin organization modifier domain;
336-389 4.86e-21

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 86.88  E-value: 4.86e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831  336 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRRHN 389
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKER 55
PRK05981 PRK05981
enoyl-CoA hydratase/isomerase;
640-873 3.77e-20

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235661  Cd Length: 266  Bit Score: 91.33  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSKL--VLFSAVGSIFCCGLDFIyfiRRLTDDRKKESTKMA-EAIRNFVNTFI----QF 712
Cdd:PRK05981   26 NAVSIDMLGGLAEALDAIEDGKAEVrcLVLTGAGRGFCTGANLQ---GRGSGGRESDSGGDAgAALETAYHPFLrrlrNL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 713 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAK 792
Cdd:PRK05981  103 PCPIVTAVNGPAAGVGMSFALMGDLILCARSAYFLQAFRRIGLVPDGGSTWLLPRLVGKARAMELSLLGEKLPAETALQW 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 793 GLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEvLKKIWGSAQGM-DSMLKYLQRKID 871
Cdd:PRK05981  183 GLVNRVVDDAELMAEAMKLAHELANGPTVALGLIRKLYWDSPENDFEEQLNLERE-AQRIAGKTEDFkEGVGAFLQKRPA 261

                  ..
gi 2077081831 872 EF 873
Cdd:PRK05981  262 QF 263
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
639-868 1.15e-19

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: 89.34  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 639 NNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRR---LTDDRKKESTKMAEAIRnfvntfiQFKK 714
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLKEMYGEgpaHQALYRENVLDLWTLLY-------TCPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 715 PIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGL 794
Cdd:pfam00378  90 PVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEALKWGL 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 795 VSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIWGSAQGMDSMLKYLQR 868
Cdd:pfam00378 170 VDKVVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQAFLEK 243
PRK06023 PRK06023
crotonase/enoyl-CoA hydratase family protein;
640-831 4.13e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 168351  Cd Length: 251  Bit Score: 87.93  E-value: 4.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDrkkesTKMAEAIRNFVNTFIQFKKPIIV 718
Cdd:PRK06023   28 NAITRAMYATMAKALKAADADDAiRAHVFLGTEGCFSAGNDMQDFLAAAMGG-----TSFGSEILDFLIALAEAEKPIVS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 719 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK06023  103 GVDGLAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALVPEAGSSLLAPRLMGHQRAFALLALGEGFSAEAAQEAGLIWKI 182
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2077081831 799 FWPGTFTQEVMVRIKELVTCNSVVLEESKALVR 831
Cdd:PRK06023  183 VDEEAVEAETLKAAEELAAKPPQALQIARDLMR 215
PRK09245 PRK09245
crotonase/enoyl-CoA hydratase family protein;
618-803 4.74e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181723  Cd Length: 266  Bit Score: 88.10  E-value: 4.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 618 DIVVRKQDGFTHILLSTKSSENNSLN-PEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES 695
Cdd:PRK09245    3 DFLLVERDGHIVTLTMNRPETRNALSdNDAVDALVAACAAINADRSvRAVILTGAGTAFSSGGN----VKDMRARVGAFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 696 TKMAEA-------IRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP-DGCSSLtFPR 767
Cdd:PRK09245   79 GSPADIrqgyrhgIQRIPLALYNLEVPVIAAVNGPAIGAGCDLACMCDIRIASETARFAESFVKLGLIPgDGGAWL-LPR 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2077081831 768 IMGLASANEMLFSGRKLTAQEACAKGLVSQVFWPGT 803
Cdd:PRK09245  158 IIGMARAAEMAFTGDAIDAATALEWGLVSRVVPADQ 193
PRK06210 PRK06210
enoyl-CoA hydratase; Provisional
640-801 7.97e-18

enoyl-CoA hydratase; Provisional


Pssm-ID: 180472  Cd Length: 272  Bit Score: 84.37  E-value: 7.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDF-------IYFIRRLTDDRKKESTKMAEAIRNFvNTFIQ 711
Cdd:PRK06210   28 NAWTPVMEAEVYAAMDRAEADPAvRVIVLTGAGRGFCAGADMgelqtidPSDGRRDTDVRPFVGNRRPDYQTRY-HFLTA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 712 FKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACA 791
Cdd:PRK06210  107 LRKPVIAAINGACAGIGLTHALMCDVRFAADGAKFTTAFARRGLIAEHGISWILPRLVGHANALDLLLSARTFYAEEALR 186
                         170
                  ....*....|
gi 2077081831 792 KGLVSQVFWP 801
Cdd:PRK06210  187 LGLVNRVVPP 196
PRK07659 PRK07659
enoyl-CoA hydratase; Provisional
619-845 3.29e-17

enoyl-CoA hydratase; Provisional


Pssm-ID: 236073 [Multi-domain]  Cd Length: 260  Bit Score: 82.39  E-value: 3.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDSKLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKM 698
Cdd:PRK07659    8 VVVKYEGRVATIMLN-RPEALNALDEPMLKELLQALKEVAESSAHIVVLRGNGRGFSAGGD----IKMMLSSNDESKFDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 699 A-EAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEM 777
Cdd:PRK07659   83 VmNTISEIVVTLYTMPKLTISAIHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGLIPDGGGHFFLQKRVGENKAKQI 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077081831 778 LFSGRKLTAQEACAKGLVSQVFwPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKE 845
Cdd:PRK07659  163 IWEGKKLSATEALDLGLIDEVI-GGDFQTAAKQKISEWLQKPLKAMIETKQIYCELNRSQLEQVLQLE 229
PLN02600 PLN02600
enoyl-CoA hydratase
640-846 3.49e-17

enoyl-CoA hydratase


Pssm-ID: 178210 [Multi-domain]  Cd Length: 251  Bit Score: 82.16  E-value: 3.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSK--LVLFSAVGSIFCCGLDFiyfirrltddrkKESTKMAEA-IRNFVN----TFIQF 712
Cdd:PLN02600   17 NAIGKEMLRGLRSAFEKIQADASArvVMLRSSVPGVFCAGADL------------KERRKMSPSeVQKFVNslrsTFSSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 713 KK---PIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEA 789
Cdd:PLN02600   85 EAlsiPTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVGRSRAKELIFTGRRIGAREA 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2077081831 790 CAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQAN--EKEC 846
Cdd:PLN02600  165 ASMGLVNYCVPAGEAYEKALELAQEINQKGPLAIKMAKKAINEGSEVDMASGLeiEEEC 223
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
335-386 6.39e-17

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: 75.40  E-value: 6.39e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 335 LYEVERIVDKrKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 386
Cdd:cd18633     1 VFEVEKILDM-KTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
PLN02664 PLN02664
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
614-799 6.90e-17

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


Pssm-ID: 178269 [Multi-domain]  Cd Length: 275  Bit Score: 81.87  E-value: 6.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 614 YRYRDIVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVGSIFCCGLDFIYF----IRRLT 688
Cdd:PLN02664    4 YKTLEIIQKSPNSSVFHLNLNRPSQRNALSLDFFTEFPKALSSLDQNpNVSVIILSGAGDHFCSGIDLKTLnsisEQSSS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 689 DDRKKESTKMAEAIRNF---VNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTF 765
Cdd:PLN02664   84 GDRGRSGERLRRKIKFLqdaITAIEQCRKPVIAAIHGACIGGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTLQRL 163
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2077081831 766 PRIMGLASANEMLFSGRKLTAQEACAKGLVSQVF 799
Cdd:PLN02664  164 PSIVGYGNAMELALTGRRFSGSEAKELGLVSRVF 197
PRK08140 PRK08140
enoyl-CoA hydratase; Provisional
640-798 7.72e-17

enoyl-CoA hydratase; Provisional


Pssm-ID: 236163  Cd Length: 262  Bit Score: 81.50  E-value: 7.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSKLVLFSAVGSIFCCGLDfiyfirrLTD---DRKKESTKMAEAIRNFVNTFIQ----F 712
Cdd:PRK08140   26 NSFTREMHRELREALDQVEDDGARALLLTGAGRGFCAGQD-------LADrdvTPGGAMPDLGESIETFYNPLVRrlraL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 713 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAK 792
Cdd:PRK08140   99 PLPVIAAVNGVAAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLPRLVGMARALGLALLGEKLSAEQAEQW 178

                  ....*.
gi 2077081831 793 GLVSQV 798
Cdd:PRK08140  179 GLIWRV 184
PLN02888 PLN02888
enoyl-CoA hydratase
619-847 1.17e-16

enoyl-CoA hydratase


Pssm-ID: 215480  Cd Length: 265  Bit Score: 80.95  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSENnSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfirrLT--DDRKKES 695
Cdd:PLN02888   12 LVPKSRNGIATITINRPKALN-ALTRPMMVELAAAFKRLDEDDSvKVIILTGSGRAFCSGVD-------LTaaEEVFKGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 696 TKMAEAirnfvNTFIQF---KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 772
Cdd:PLN02888   84 VKDVET-----DPVAQMercRKPIIGAINGFAITAGFEIALACDILVASRGAKFIDTHAKFGIFPSWGLSQKLSRIIGAN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077081831 773 SANEMLFSGRKLTAQEACAKGLVSQVFWPGtftqEVMVRIKEL----VTCNSVVLEESKALVRNIMKVDLEQANEKECE 847
Cdd:PLN02888  159 RAREVSLTAMPLTAETAERWGLVNHVVEES----ELLKKAREVaeaiIKNNQGMVLRYKSVINDGLKLDLGHALQLEKE 233
PRK09674 PRK09674
enoyl-CoA hydratase-isomerase; Provisional
618-873 1.53e-16

enoyl-CoA hydratase-isomerase; Provisional


Pssm-ID: 182026 [Multi-domain]  Cd Length: 255  Bit Score: 80.20  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 618 DIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRR-----LTDDR 691
Cdd:PRK09674    3 ELLVSRQQRVLLLTLN-RPEARNALNNALLTQLVNELEAAATDTSiGVCVITGNARFFAAGADLNEMAEKdlaatLNDPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 692 KKESTKMAeairnfvntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGL 771
Cdd:PRK09674   82 PQLWQRLQ-----------AFNKPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGGTQRLIRSVGK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 772 ASANEMLFSGRKLTAQEACAKGLVSQVFwPGTFTQEVMVRIKELVTCNS-VVLEESKALVRNIMKVDLEQANEKECEVLK 850
Cdd:PRK09674  151 SLASQMVLTGESITAQQAQQAGLVSEVF-PPELTLERALQLASKIARHSpLALRAAKQALRQSQEVDLQAGLAQERQLFT 229
                         250       260
                  ....*....|....*....|...
gi 2077081831 851 KIWGSAQGMDSMLKYLQRKIDEF 873
Cdd:PRK09674  230 LLAATEDRHEGISAFLEKRTPDF 252
PRK07657 PRK07657
enoyl-CoA hydratase; Provisional
640-839 1.80e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 181069 [Multi-domain]  Cd Length: 260  Bit Score: 80.16  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVG-SIFCCGLDFiyfirrltddrkKESTKMAEA--------IRNFVNTF 709
Cdd:PRK07657   26 NALSLALLEELQNILTQINEEaNVRVVILTGAGeKAFCAGADL------------KERAGMNEEqvrhavslIRTTMEMV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 710 IQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEA 789
Cdd:PRK07657   94 EQLPQPVIAAINGIALGGGLELALACDFRIAAESASLGLTETTLAIIPGAGGTQRLPRLIGVGRAKELIYTGRRISAQEA 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 790 CAKGLVSQVFwPGTFTQEVMVRIKELVTCNS-VVLEESKALVRNIMKVDLE 839
Cdd:PRK07657  174 KEIGLVEFVV-PAHLLEEKAIEIAEKIASNGpIAVRQAKEAISNGIQVDLH 223
PRK07468 PRK07468
crotonase/enoyl-CoA hydratase family protein;
640-869 2.42e-16

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180987 [Multi-domain]  Cd Length: 262  Bit Score: 79.72  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDD---RKKESTKMAEAIRNfVNTFiqfKKP 715
Cdd:PRK07468   27 NALSARMIAELTTAARRLAADAAvRVVVLTGAGKSFCAGGDLGWMRAQMTADratRIEEARRLAMMLKA-LNDL---PKP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 716 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRiMGLASANEMLFSGRKLTAQEACAKGLV 795
Cdd:PRK07468  103 LIGRIQGQAFGGGVGLISVCDVAIAVSGARFGLTETRLGLIPATISPYVVAR-MGEANARRVFMSARLFDAEEAVRLGLL 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 796 SQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIWGSAQGMDSMLKYLQRK 869
Cdd:PRK07468  182 SRVVPAERLDAAVEAEVTPYLSCAPGAVAAAKALVRALGAPIDEAVIDATIEALADTWETEEAREGIAAFFDKR 255
PRK06494 PRK06494
enoyl-CoA hydratase; Provisional
640-841 2.44e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 180591 [Multi-domain]  Cd Length: 259  Bit Score: 79.70  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSKLV--LFSAVGSIFCCGLDFIYFIRRltDDRKKESTKMAEAIRNFvntfiQFKKPII 717
Cdd:PRK06494   26 NALHLDAHFELEEVFDDFAADPEQWVaiVTGAGDKAFSAGNDLKEQAAG--GKRGWPESGFGGLTSRF-----DLDKPII 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 718 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQ 797
Cdd:PRK06494   99 AAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGLKRAMGMILTGRRVTAREGLELGFVNE 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2077081831 798 VFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQA 841
Cdd:PRK06494  179 VVPAGELLAAAERWADDILACSPLSIRASKQAVYRGLEVSLEEA 222
PRK07854 PRK07854
enoyl-CoA hydratase; Provisional
640-855 2.78e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 236115 [Multi-domain]  Cd Length: 243  Bit Score: 79.30  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSKLVLFSAVGSIFCCGLDF---IY---FIRRLTDdrkkestkMAEAIrnfVNTFIqfk 713
Cdd:PRK07854   22 NALNAELCEELREAVRKAVDESARAIVLTGQGTVFCAGADLsgdVYaddFPDALIE--------MLHAI---DAAPV--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 714 kPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKG 793
Cdd:PRK07854   88 -PVIAAINGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDNWTIRRLSSLVGGGRARAMLLGAEKLTAEQALATG 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 794 LVSQVfwpGTFT--QEVMVRIKELVtcnSVVLEESKALVRNIMkvDLEQANEKECEVLKKIWGS 855
Cdd:PRK07854  167 MANRI---GTLAdaQAWAAEIAGLA---PLALQHAKRVLNDDG--AIEEAWPAHKELFDKAWAS 222
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
336-384 3.40e-15

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: 70.45  E-value: 3.40e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 336 YEVE-----RIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18968     2 YEVEvilaaRVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
PRK07658 PRK07658
enoyl-CoA hydratase; Provisional
640-858 9.60e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 181070 [Multi-domain]  Cd Length: 257  Bit Score: 75.06  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTD-DRKKESTKMAEAIRNFVNTFIQFKKPII 717
Cdd:PRK07658   23 NALSSQVLHELSELLDQVEKDDNvRVVVIHGEGRFFSAGAD----IKEFTSvTEAEQATELAQLGQVTFERVEKFSKPVI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 718 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQ 797
Cdd:PRK07658   99 AAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGFAGTQRLPRYVGKAKALEMMLTSEPITGAEALKWGLVNG 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 798 VFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIWGSAQG 858
Cdd:PRK07658  179 VFPEETLLDDAKKLAKKIAGKSPATTRAVLELLQTTKSSSYYEGVKREAKIFGEVFTSEDA 239
PRK07799 PRK07799
crotonase/enoyl-CoA hydratase family protein;
623-803 1.46e-14

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181122 [Multi-domain]  Cd Length: 263  Bit Score: 74.75  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 623 KQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEA 701
Cdd:PRK07799   10 EQRGHTLIVTMNRPEARNALSTEMLRIMVDAWDRVDNDPDiRSCILTGAGGAFCAGMDLKAATKKPPGDSFKDGSYDPSR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 702 IRNFVNTFiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSG 781
Cdd:PRK07799   90 IDALLKGR-RLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLFPMGGSAVRLVRQIPYTVACDLLLTG 168
                         170       180
                  ....*....|....*....|..
gi 2077081831 782 RKLTAQEACAKGLVSQVFWPGT 803
Cdd:PRK07799  169 RHITAAEAKEIGLIGHVVPDGQ 190
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
336-384 2.14e-14

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: 68.11  E-value: 2.14e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 336 YEVERIVDKR----KNKKGKTEYL-VRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18635     2 FEVEKLVGICygdpKKTGERGLYFkVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
336-384 2.45e-14

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: 67.85  E-value: 2.45e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 384
Cdd:cd18631     2 YVVEKVLDRRV-VKGKVEYLLKWKGYPDEDNTWEPEENL-DCPDLIAEF 48
PRK03580 PRK03580
crotonobetainyl-CoA hydratase;
714-841 4.43e-14

crotonobetainyl-CoA hydratase;


Pssm-ID: 179599 [Multi-domain]  Cd Length: 261  Bit Score: 73.19  E-value: 4.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 714 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKG 793
Cdd:PRK03580   95 KPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRLPPAIANEMVMTGRRMDAEEALRWG 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 794 LVSQVFwPGtftQEVMVRIKEL----VTCNSVVLEESKALVRNIMKVDLEQA 841
Cdd:PRK03580  175 IVNRVV-PQ---AELMDRARELaqqlVNSAPLAIAALKEIYRETSEMPVEEA 222
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
333-386 1.02e-13

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: 66.19  E-value: 1.02e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 333 EELYEVERIVDKRKNKKGkTEYLVRWKGYDSEDDTWEPeQHLVNCEEYIHEFNR 386
Cdd:cd18978     1 DESYEVEKIINHRGEKNR-RKYLVKWKGYDDTDNSWVT-QEDFNDKDMIDEYEN 52
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
336-386 1.17e-13

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: 66.13  E-value: 1.17e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 336 YEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHL-VNCEEYIHEFNR 386
Cdd:cd18638     2 FEVEKIV-KKKTVKGGTEYFVKWKGYSAKENTWETEDNLeKSYKEMIDEFEK 52
PRK06190 PRK06190
enoyl-CoA hydratase; Provisional
640-798 1.52e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 235733  Cd Length: 258  Bit Score: 71.54  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEaiRNFVNTFIQFKKPIIV 718
Cdd:PRK06190   26 NALSAALRRALFAALAEADADDDvDVVVLTGADPAFCAGLD----LKELGGDGSAYGAQDAL--PNPSPAWPAMRKPVIG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 719 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK06190  100 AINGAAVTGGLELALACDILIASERARFADTHARVGILPGWGLSVRLPQKVGIGRARRMSLTGDFLDAADALRAGLVTEV 179
PRK05862 PRK05862
enoyl-CoA hydratase; Provisional
640-809 3.05e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 180295 [Multi-domain]  Cd Length: 257  Bit Score: 70.46  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDsklvlfsAVGSI--------FCCGLDfiyfIRRLTDDRKKESTKmAEAIRNFvNTFIQ 711
Cdd:PRK05862   26 NALNDALMDELGAALAAFDADE-------GIGAIvitgsekaFAAGAD----IKEMADLSFMDVYK-GDYITNW-EKVAR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 712 FKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACA 791
Cdd:PRK05862   93 IRKPVIAAVAGYALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGMGGSQRLTRAVGKAKAMDLCLTGRMMDAAEAER 172
                         170
                  ....*....|....*...
gi 2077081831 792 KGLVSQVFWPGTFTQEVM 809
Cdd:PRK05862  173 AGLVSRVVPADKLLDEAL 190
PRK07260 PRK07260
enoyl-CoA hydratase; Provisional
640-798 4.62e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 180910 [Multi-domain]  Cd Length: 255  Bit Score: 70.15  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEAIRNFVNTFIQFKKPIIV 718
Cdd:PRK07260   24 NGFNIPMCQEILEALRLAEEDPSvRFLLINANGKVFSVGGDLVEMKRAVDEDDVQSLVKIAELVNEISFAIKQLPKPVIM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 719 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK07260  104 CVDGAVAGAAANMAVAADFCIASTKTKFIQAFVGVGLAPDAGGLFLLTRAIGLNRATHLAMTGEALTAEKALEYGFVYRV 183
PRK05995 PRK05995
enoyl-CoA hydratase; Provisional
640-841 4.75e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 235664 [Multi-domain]  Cd Length: 262  Bit Score: 69.95  E-value: 4.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfIYFIRRLTDDRKKESTKMAEAIRNFVNTFIQFKKPIIV 718
Cdd:PRK05995   26 NAFNETVIAELTAAFRALDADDSvRAVVLAGAGKAFCAGAD-LNWMKKMAGYSDDENRADARRLADMLRAIYRCPKPVIA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 719 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFpRIMGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK05995  105 RVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLGLIPATISPYVI-RAMGERAARRYFLTAERFDAAEALRLGLVHEV 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2077081831 799 FWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQA 841
Cdd:PRK05995  184 VPAEALDAKVDELLAALVANSPQAVRAGKRLVRDVAGRPIDAA 226
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
335-386 6.70e-13

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: 64.01  E-value: 6.70e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 335 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 386
Cdd:cd18636     1 VYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
PRK06495 PRK06495
enoyl-CoA hydratase/isomerase family protein;
640-833 1.16e-12

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 168580 [Multi-domain]  Cd Length: 257  Bit Score: 68.95  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNT-AAADDSKLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEA--IRNFVNTFIQFKKPI 716
Cdd:PRK06495   25 NALSRELRDELIAVFDEiSERPDVRVVVLTGAGKVFCAGAD----LKGRPDVIKGPGDLRAHNrrTRECFHAIRECAKPV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 717 IVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSpDGCSSLTfpRIMGLASANEMLFSGRKLTAQEACAKGLVS 796
Cdd:PRK06495  101 IAAVNGPALGAGLGLVASCDIIVASENAVFGLPEIDVGLA-GGGKHAM--RLFGHSLTRRMMLTGYRVPAAELYRRGVIE 177
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2077081831 797 QVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNI 833
Cdd:PRK06495  178 ACLPPEELMPEAMEIAREIASKSPLATRLAKDALNTI 214
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
336-387 1.29e-12

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: 63.29  E-value: 1.29e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077081831 336 YEVERIVD-KRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRR 387
Cdd:cd18632     2 YEVEKIVDeKTDRNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRK 54
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
336-384 1.76e-12

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: 62.65  E-value: 1.76e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 384
Cdd:cd18650     2 YVVEKVLDRRV-VKGKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEF 48
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
336-384 2.19e-12

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: 62.26  E-value: 2.19e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18973     1 YVVEAILDNKR-RKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKY 48
PRK05864 PRK05864
enoyl-CoA hydratase; Provisional
640-796 2.30e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 168278 [Multi-domain]  Cd Length: 276  Bit Score: 68.32  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDF-----IYFIRRLTddRKKESTKMAEAIRNFVNTFIQFK 713
Cdd:PRK05864   32 NSMAFDVMVPLKEALAEVSYDNSvRVVVLTGAGRGFSSGADHksagvVPHVEGLT--RPTYALRSMELLDDVILALRRLH 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 714 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFG--QSPDGCSSLtFPRIMGLASANEMLFSGRKLTAQEACA 791
Cdd:PRK05864  110 QPVIAAVNGPAIGGGLCLALAADIRVASSSAYFRAAGINNGltASELGLSYL-LPRAIGSSRAFEIMLTGRDVDAEEAER 188

                  ....*
gi 2077081831 792 KGLVS 796
Cdd:PRK05864  189 IGLVS 193
PRK05980 PRK05980
crotonase/enoyl-CoA hydratase family protein;
618-798 2.53e-12

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180335 [Multi-domain]  Cd Length: 260  Bit Score: 67.86  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 618 DIVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKes 695
Cdd:PRK05980    3 DTVLIEIRDGIALLTLNRPEKLNALNYALIDRLLARLDAIEVDESvrAVILTGAGDRAFSAGADIHEFSASVAAGADV-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 696 tkmaeAIRNFV-------NTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRI 768
Cdd:PRK05980   81 -----ALRDFVrrgqamtARLEAFPKPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPTFGGTQRLPRL 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 2077081831 769 MGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK05980  156 AGRKRALELLLTGDAFSAERALEIGLVNAV 185
PRK05870 PRK05870
enoyl-CoA hydratase; Provisional
640-798 2.54e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 180298  Cd Length: 249  Bit Score: 67.83  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVGSIFCCGLDfiyfirrLTDDRKKESTKMAEAIRNFVNTFI---QFKKP 715
Cdd:PRK05870   25 NAVTAEMSAQLRAAVAAAEADpDVHALVVTGAGKAFCAGAD-------LTALGAAPGRPAEDGLRRIYDGFLavaSCPLP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 716 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLV 795
Cdd:PRK05870   98 TIAAVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLGLHPGGGATWMLQRAVGPQVARAALLFGMRFDAEAAVRHGLA 177

                  ...
gi 2077081831 796 SQV 798
Cdd:PRK05870  178 LMV 180
PRK08139 PRK08139
enoyl-CoA hydratase; Validated
640-808 2.68e-12

enoyl-CoA hydratase; Validated


Pssm-ID: 181249  Cd Length: 266  Bit Score: 68.04  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES--------TKMAEAIRnfvntfi 710
Cdd:PRK08139   33 NALSEAMLAALQAALDAIAADPSvRVVVLAAAGKAFCAGHD----LKEMRAARGLAYfralfarcSRVMQAIV------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 711 QFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSpdgCS--SLTFPRIMGLASANEMLFSGRKLTAQE 788
Cdd:PRK08139  102 ALPQPVIARVHGIATAAGCQLVASCDLAVAADTARFAVPGVNIGLF---CStpMVALSRNVPRKQAMEMLLTGEFIDAAT 178
                         170       180
                  ....*....|....*....|
gi 2077081831 789 ACAKGLVSQVFWPGTFTQEV 808
Cdd:PRK08139  179 AREWGLVNRVVPADALDAAV 198
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
333-387 3.25e-12

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: 62.10  E-value: 3.25e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077081831 333 EELYEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHEFNRR 387
Cdd:cd18644     1 DLVYAAEKILKKRV-RKGKVEYLVKWKGWSNKHNTWEPEENILD-RRLIEIFERT 53
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
336-386 3.33e-12

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: 61.73  E-value: 3.33e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 386
Cdd:cd18974     1 WEVEEIVDEKM-IDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
336-384 3.70e-12

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: 61.59  E-value: 3.70e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 384
Cdd:cd18653     2 YAVEKICDRRV-RKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
336-384 5.48e-12

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: 61.43  E-value: 5.48e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 336 YEVERIVDKRKNKKGKTE--YLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18980     4 YEVEAILDHKVDRRYRDPnfYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
335-386 1.19e-11

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


Pssm-ID: 349316  Cd Length: 51  Bit Score: 60.26  E-value: 1.19e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 335 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEFNR 386
Cdd:cd18960     1 VFVVERILDKRLGRNGGEEFLIKWQGFPESDSSWEPRENL-QCDEMLEEFEK 51
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
336-384 1.95e-11

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: 59.62  E-value: 1.95e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 384
Cdd:cd18651     2 YVVEKVLDRRV-VKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEF 48
PRK07827 PRK07827
enoyl-CoA hydratase family protein;
625-869 2.51e-11

enoyl-CoA hydratase family protein;


Pssm-ID: 236109 [Multi-domain]  Cd Length: 260  Bit Score: 65.09  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 625 DGFTHILLStkSSEN-NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEAI 702
Cdd:PRK07827   14 GGVATLTLD--SPHNrNALSARLVAQLHDGLRAAAADPAvRAVVLTHTGGTFCAGAD----LSEAGGGGGDPYDAAVARA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 703 RNFVNTF---IQFKKPIIVAVNG--PAIGLGasILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRiMGLASANEM 777
Cdd:PRK07827   88 REMTALLraiVELPKPVIAAIDGhvRAGGFG--LVGACDIVVAGPESTFALTEARIGVAPAIISLTLLPR-LSPRAAARY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 778 LFSGRKLTAQEACAKGLVSQVfwpgtfTQEVMVRIKELVT----CNSVVLEESKALVRNIMKVDLEQANEKECEVLKKIW 853
Cdd:PRK07827  165 YLTGEKFGAAEAARIGLVTAA------ADDVDAAVAALLAdlrrGSPQGLAESKALTTAAVLAGFDRDAEELTEESARLF 238
                         250
                  ....*....|....*.
gi 2077081831 854 GSAQGMDSMLKYLQRK 869
Cdd:PRK07827  239 VSDEAREGMTAFLQKR 254
PRK06072 PRK06072
enoyl-CoA hydratase; Provisional
619-795 3.82e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 168377 [Multi-domain]  Cd Length: 248  Bit Score: 64.41  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTK 697
Cdd:PRK06072    2 IKVESREGYAIVTMS-RPDKLNALNLEMRNEFISKLKQINADpKIRVVIVTGEGRAFCVGADLSEFAPDFAIDLRETFYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 698 MAEAIRNFvntfiqfKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGlASANEM 777
Cdd:PRK06072   81 IIREIRFS-------DKIYISAINGVTAGACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYFLLKLTG-QRFYEI 152
                         170
                  ....*....|....*...
gi 2077081831 778 LFSGRKLTAQEACAKGLV 795
Cdd:PRK06072  153 LVLGGEFTAEEAERWGLL 170
PRK08258 PRK08258
enoyl-CoA hydratase family protein;
659-798 5.36e-11

enoyl-CoA hydratase family protein;


Pssm-ID: 181329  Cd Length: 277  Bit Score: 64.22  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 659 ADDSKLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVV 738
Cdd:PRK08258   59 ADDVKAVVLTGAGGNFCSGGDVHEIIGPLTKMDMPELLAFTRMTGDLVKAMRACPQPIIAAVDGVCAGAGAILAMASDLR 138
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077081831 739 WANEKAWFQTPYTTFGQSpdGC---SSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK08258  139 LGTPSAKTAFLFTRVGLA--GAdmgACALLPRIIGQGRASELLYTGRSMSAEEGERWGFFNRL 199
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
336-384 7.54e-11

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: 58.07  E-value: 7.54e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077081831 336 YEVERIVDKRKNKKGKT-EYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18640     1 EPVEKIVAKRFNPRKKTwEYLVKWENRSHHENTWEPMANLERCKYLLQMF 50
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
336-374 8.68e-11

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


Pssm-ID: 349322  Cd Length: 49  Bit Score: 57.68  E-value: 8.68e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKNKkGKTEYLVRWKGYDSEDDTWEPEQHL 374
Cdd:cd18966     1 YEVERILAERRDD-GGKRYLVKWEGYPLEEATWEPEENI 38
PRK08138 PRK08138
enoyl-CoA hydratase; Provisional
640-798 8.89e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 236162 [Multi-domain]  Cd Length: 261  Bit Score: 63.53  E-value: 8.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRL-----TDDRKKESTKMAEAIRnfvntfiQFK 713
Cdd:PRK08138   30 NALNMEVRQQLAEHFTELSEDPDiRAIVLTGGEKVFAAGAD----IKEFatagaIEMYLRHTERYWEAIA-------QCP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 714 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP--DGCSSLTfpRIMGLASANEMLFSGRKLTAQEACA 791
Cdd:PRK08138   99 KPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGLMPgaGGTQRLV--RAVGKFKAMRMALTGCMVPAPEALA 176

                  ....*..
gi 2077081831 792 KGLVSQV 798
Cdd:PRK08138  177 IGLVSEV 183
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
336-378 9.66e-11

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: 57.45  E-value: 9.66e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2077081831 336 YEVERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCE 378
Cdd:cd18970     1 FFVERILDERRRGRGW-QYLVRWLGYGPSDDSWLPRRELEECE 42
PRK07327 PRK07327
enoyl-CoA hydratase/isomerase family protein;
615-796 1.13e-10

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 235991  Cd Length: 268  Bit Score: 63.12  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 615 RYRDIVVRKQDGftHILLSTKSSEN--NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFiYFIRRLTDDR 691
Cdd:PRK07327    9 DYPALRFDRPPP--GVLEIVLNGPGalNAADARMHRELADIWRDVDRDPDvRVVLIRGEGKAFSAGGDL-ALVEEMADDF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 692 KKESTKMAEAiRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGL 771
Cdd:PRK07327   86 EVRARVWREA-RDLVYNVINCDKPIVSAIHGPAVGAGLVAALLADISIAAKDARIIDGHTRLGVAAGDHAAIVWPLLCGM 164
                         170       180
                  ....*....|....*....|....*
gi 2077081831 772 ASANEMLFSGRKLTAQEACAKGLVS 796
Cdd:PRK07327  165 AKAKYYLLLCEPVSGEEAERIGLVS 189
PRK08150 PRK08150
crotonase/enoyl-CoA hydratase family protein;
640-803 1.47e-10

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181254  Cd Length: 255  Bit Score: 62.73  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSKLVLFsAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEAIRNfvntfIQFKK-PIIV 718
Cdd:PRK08150   24 NALNDGLIAALRAAFARLPEGVRAVVLH-GEGDHFCAGLDLSELRERDAGEGMHHSRRWHRVFDK-----IQYGRvPVIA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 719 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK08150   98 ALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGIFVGGGGSVRVPRLIGVARMTDMMLTGRVYDAQEGERLGLAQYL 177

                  ....*
gi 2077081831 799 FWPGT 803
Cdd:PRK08150  178 VPAGE 182
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
336-384 1.61e-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: 349320  Cd Length: 54  Bit Score: 56.96  E-value: 1.61e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 336 YEVERIVDKR---KNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18964     1 FFVERIIGRRpsaRDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDF 52
PLN02921 PLN02921
naphthoate synthase
611-816 2.00e-10

naphthoate synthase


Pssm-ID: 178509 [Multi-domain]  Cd Length: 327  Bit Score: 63.27  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 611 ESAYRYRDIVVRKQ--DGFTHILLStKSSENNSLNPEVMKEVQSALNtAAADDSK---LVLFSAVGSIFCCGLDfiyfir 685
Cdd:PLN02921   59 GSGKEFTDIIYEKAvgEGIAKITIN-RPERRNAFRPRTVKELQRAFN-DARDDSSvgvIILTGKGTKAFCSGGD------ 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 686 rlTDDRKKESTKMAEAIR--NFVNTFIQFK---KPIIVAVNGPAIGlGASILPL-CDVVWANEKAWFQTPYTTFGQSPDG 759
Cdd:PLN02921  131 --QAVRGKDGYVGPDDAGrlNVLDLQIQIRrlpKPVIAMVAGYAVG-GGHILHMvCDLTIAADNAVFGQTGPKVGSFDAG 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2077081831 760 CSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELV 816
Cdd:PLN02921  208 YGSSIMARLVGQKKAREMWFLARFYTASEALKMGLVNTVVPLDELEGETVKWCREIL 264
PRK08290 PRK08290
enoyl-CoA hydratase; Provisional
639-799 2.21e-10

enoyl-CoA hydratase; Provisional


Pssm-ID: 236220 [Multi-domain]  Cd Length: 288  Bit Score: 62.67  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 639 NNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTK-------------------- 697
Cdd:PRK08290   25 RNAQNRQMLYELDAAFRRAEADDAvRVIVLAGAGKHFSAGHD----LGSGTPGRDRDPGPdqhptlwwdgatkpgveqry 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 698 ---------MAEAIRNFvntfiqfKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSpdGCSSLTFPRI 768
Cdd:PRK08290  101 arewevylgMCRRWRDL-------PKPTIAQVQGACIAGGLMLAWVCDLIVASDDAFFSDPVVRMGIP--GVEYFAHPWE 171
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2077081831 769 MGLASANEMLFSGRKLTAQEACAKGLVSQVF 799
Cdd:PRK08290  172 LGPRKAKELLFTGDRLTADEAHRLGMVNRVV 202
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
333-384 4.02e-10

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: 55.99  E-value: 4.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 333 EELYEVERIVDKRKN--KKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18969     1 EEEYEIEEILDVKKGgfEDGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEY 54
PRK06127 PRK06127
enoyl-CoA hydratase; Provisional
619-835 5.34e-10

enoyl-CoA hydratase; Provisional


Pssm-ID: 235705  Cd Length: 269  Bit Score: 61.26  E-value: 5.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDFIYFIRRLTDDrkKEST 696
Cdd:PRK06127   13 LLAEKTGGLGRITFN-NPARHNAMSLDMWEALPQALAAAEDDDAirVVVLTGAGEKAFVSGADISQFEESRSDA--EAVA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 697 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFG--QSPDGCSSLTfpRIMGLASA 774
Cdd:PRK06127   90 AYEQAVEAAQAALADYAKPTIACIRGYCIGGGMGIALACDIRIAAEDSRFGIPAARLGlgYGYDGVKNLV--DLVGPSAA 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 775 NEMLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMK 835
Cdd:PRK06127  168 KDLFYTARRFDAAEALRIGLVHRVTAADDLETALADYAATIAGNAPLTLRAAKRAIAELLK 228
PRK06142 PRK06142
crotonase/enoyl-CoA hydratase family protein;
616-799 5.82e-10

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235714  Cd Length: 272  Bit Score: 61.14  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 616 YRDIVVRKQDGFTHILLsTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFI----YFIRRLTDD 690
Cdd:PRK06142    5 YESFTVELADHVAQVTL-NRPGKGNAMNPAFWSELPEIFRWLDADPEvRAVVLSGSGKHFSYGIDLPamagVFGQLGKDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 691 RKKESTKMAEAIRNF---VNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPR 767
Cdd:PRK06142   84 LARPRTDLRREILRLqaaINAVADCRKPVIAAVQGWCIGGGVDLISACDMRYASADAKFSVREVDLGMVADVGSLQRLPR 163
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2077081831 768 IMGLASANEMLFSGRKLTAQEACAKGLVSQVF 799
Cdd:PRK06142  164 IIGDGHLRELALTGRDIDAAEAEKIGLVNRVY 195
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
336-376 6.10e-10

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: 55.48  E-value: 6.10e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 376
Cdd:cd18627     1 FAAECILKKRI-RKGKVEYLVKWKGWSQKYNTWEPEENILD 40
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
336-384 7.48e-10

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: 55.18  E-value: 7.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077081831 336 YEVERIVD----KRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18977     4 YEVEKIVGekwkKRKNRRVK-LYKVRFKGYGPEEDEWLTKEELKNAPEILAEW 55
PRK08252 PRK08252
crotonase/enoyl-CoA hydratase family protein;
640-869 1.09e-09

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181325 [Multi-domain]  Cd Length: 254  Bit Score: 60.00  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADD--SKLVLFSAVGSiFCCGLDFIYFIRRltddrkkESTKMAEaiRNFVN-TFIQFKKPI 716
Cdd:PRK08252   25 NAVNAAVAQGLAAALDELDADPdlSVGILTGAGGT-FCAGMDLKAFARG-------ERPSIPG--RGFGGlTERPPRKPL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 717 IVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVS 796
Cdd:PRK08252   95 IAAVEGYALAGGFELALACDLIVAARDAKFGLPEVKRGLVAAGGGLLRLPRRIPYHIAMELALTGDMLTAERAHELGLVN 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 797 QVFWPGTfTQEVMVRIKELVTCNS-VVLEESKALVRNIMKVDLEQANEKECEVLKKIWGSAQGMDSMLKYLQRK 869
Cdd:PRK08252  175 RLTEPGQ-ALDAALELAERIAANGpLAVAASKRIVVESGDWSEDEMFARQRELIAPVFTSADAKEGATAFAEKR 247
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
336-384 2.03e-09

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: 53.67  E-value: 2.03e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 384
Cdd:cd18639     1 YEVEYLCDYKK-IREQEYYLVKWKGYPDSENTWEPRQNL-KCSRLLKQF 47
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
336-384 2.04e-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: 2.04e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 384
Cdd:cd18652     2 FVVEKVLDRRV-VNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
336-384 2.35e-09

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


Pssm-ID: 349328  Cd Length: 50  Bit Score: 53.67  E-value: 2.35e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18972     1 YEVEAIVGHKPKKKPR-QFLVSWLGYDSSHNEWKQKEELENARELLQDY 48
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
337-372 2.57e-09

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


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 53.73  E-value: 2.57e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2077081831 337 EVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQ 372
Cdd:cd18659     4 IVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEE 39
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
336-384 5.37e-09

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


Pssm-ID: 349287  Cd Length: 54  Bit Score: 52.90  E-value: 5.37e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 336 YEVERIVDKRKNKKGKT-EYLVRWKGYDSEDD-TWEPEQHLVNCEEYIHEF 384
Cdd:cd18637     2 YVVEKILKHRMARKGGGyEYLLKWEGYDDPSDnTWSSEADCAGCKDLIEAY 52
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
333-387 5.89e-09

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: 52.75  E-value: 5.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077081831 333 EELYEVERIVDKRkNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHEFNRR 387
Cdd:cd18647     1 EQVFAAECILSKR-LRKGKLEYLVKWRGWSSKHNSWEPEENILD-PRLLLAFQKK 53
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
336-386 6.78e-09

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


Pssm-ID: 349331  Cd Length: 49  Bit Score: 52.55  E-value: 6.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077081831 336 YEVERIVDKRkNKKGKTEYLVRWKGYDSEDDTWEPEQHlVNCEEYIHEFNR 386
Cdd:cd18975     1 YEVESILNSR-LHRGKLQYLIQWKGYPLEEASWELEDN-IKNPRLIEEFHK 49
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
619-801 7.13e-09

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


Pssm-ID: 131494 [Multi-domain]  Cd Length: 737  Bit Score: 59.47  E-value: 7.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 619 IVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDfIYFIRrlTDDRKKEST 696
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD-IQMIA--ACKTAQEVT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 697 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWA--NEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASA 774
Cdd:TIGR02441  92 QLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGVPAA 171
                         170       180
                  ....*....|....*....|....*..
gi 2077081831 775 NEMLFSGRKLTAQEACAKGLVSQVFWP 801
Cdd:TIGR02441 172 LDMMLTGKKIRADRAKKMGIVDQLVDP 198
PRK06563 PRK06563
crotonase/enoyl-CoA hydratase family protein;
620-803 7.76e-09

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180625 [Multi-domain]  Cd Length: 255  Bit Score: 57.28  E-value: 7.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 620 VVRKQDGftHILLST--KSSENNSLNPEVMKEVQSALnTAAADDSKL---VLFsAVGSIFCCGLDFIYFIRRLTDDRKKE 694
Cdd:PRK06563    1 VSRERRG--HVLLIGldRPAKRNAFDSAMLDDLALAL-GEYEADDELrvaVLF-AHGEHFTAGLDLADVAPKLAAGGFPF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 695 StkmAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKawfqtpyTTFGQ-------SPDGCSSLTFPR 767
Cdd:PRK06563   77 P---EGGIDPWGTVGRRLSKPLVVAVQGYCLTLGIELMLAADIVVAADN-------TRFAQlevqrgiLPFGGATLRFPQ 146
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2077081831 768 IMGLASANEMLFSGRKLTAQEACAKGLVSQVFWPGT 803
Cdd:PRK06563  147 AAGWGNAMRYLLTGDEFDAQEALRLGLVQEVVPPGE 182
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
336-384 1.36e-08

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: 51.75  E-value: 1.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVDKRKNKkGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 384
Cdd:cd18630     2 YVVEKILGKRFVN-GRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
333-376 1.46e-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: 51.63  E-value: 1.46e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2077081831 333 EELYEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 376
Cdd:cd18646     2 EQVFAVESIRKKRV-RKGKVEYLVKWKGWPPKYSTWEPEEHILD 44
PRK06144 PRK06144
enoyl-CoA hydratase; Provisional
618-863 1.61e-08

enoyl-CoA hydratase; Provisional


Pssm-ID: 180424 [Multi-domain]  Cd Length: 262  Bit Score: 56.54  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 618 DIVVRKQDGFTHILLSTKSSENnSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDFIYFiRRLTDDRkkES 695
Cdd:PRK06144    9 ELLLEVRGGIARITFNRPAARN-AMTWAMYEGLAEICEAIAADPSirAVVLRGAGDKAFVAGTDIAQF-RAFSTAE--DA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 696 TKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYT-TFGQspdgCSSL-TFPRI---MG 770
Cdd:PRK06144   85 VAYERRIDRVLGALEQLRVPTIAAIAGACVGGGAAIAAACDLRIATPSARFGFPIArTLGN----CLSMsNLARLvalLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 771 LASANEMLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVmVRIKELVTCNS-VVLEESKALVRNIMKVDLEQANekecEVL 849
Cdd:PRK06144  161 AARVKDMLFTARLLEAEEALAAGLVNEVVEDAALDARA-DALAELLAAHApLTLRATKEALRRLRREGLPDGD----DLI 235
                         250
                  ....*....|....*..
gi 2077081831 850 KKIWGSA---QGMDSML 863
Cdd:PRK06144  236 RMCYMSEdfrEGVEAFL 252
PRK05869 PRK05869
enoyl-CoA hydratase; Validated
623-801 1.79e-08

enoyl-CoA hydratase; Validated


Pssm-ID: 235632 [Multi-domain]  Cd Length: 222  Bit Score: 56.00  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 623 KQDGFTHILLSTKSSenNSLNPEVMKEVQSALNTAAA-DDSKLVLFSAVGSIFCCGLDfIYFIRRLTDDrkkESTKMAEA 701
Cdd:PRK05869   14 QDAGLATLLLSRPPT--NALTRQVYREIVAAANELGRrDDVAAVILYGGHEIFSAGDD-MPELRTLSAQ---EADTAARV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 702 IRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSG 781
Cdd:PRK05869   88 RQQAVDAVAAIPKPTVAAITGYALGAGLTLALAADWRVSGDNVKFGATEILAGLAPSGDGMARLTRAAGPSRAKELVFSG 167
                         170       180
                  ....*....|....*....|
gi 2077081831 782 RKLTAQEACAKGLVSQVFWP 801
Cdd:PRK05869  168 RFFDAEEALALGLIDEMVAP 187
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
338-386 3.42e-08

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: 50.73  E-value: 3.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077081831 338 VERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQ-HLVNCEEYIHEFNR 386
Cdd:cd18662     6 IHRIINHRVDKDGNTWYLVKWRDLPYDQSTWESEDdDIPDYEKHIQEYWD 55
PLN02851 PLN02851
3-hydroxyisobutyryl-CoA hydrolase-like protein
661-828 9.23e-08

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178443 [Multi-domain]  Cd Length: 407  Bit Score: 55.37  E-value: 9.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 661 DSKLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASI-LPLCDVVw 739
Cdd:PLN02851   86 DIGFVLMKGSGRAFCSGADVVSLYHLINEGNVEECKLFFENLYKFVYLQGTYLKPNVAIMDGITMGCGAGIsIPGMFRV- 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 740 ANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLAsANEMLFSGRKLTAQEACAKGLVSQVfwpgTFTQEVMV---RIKELV 816
Cdd:PLN02851  165 VTDKTVFAHPEVQMGFHPDAGASYYLSRLPGYL-GEYLALTGQKLNGVEMIACGLATHY----CLNARLPLieeRLGKLL 239
                         170
                  ....*....|..
gi 2077081831 817 TCNSVVLEESKA 828
Cdd:PLN02851  240 TDDPAVIEDSLA 251
PRK07110 PRK07110
polyketide biosynthesis enoyl-CoA hydratase; Validated
640-809 9.68e-08

polyketide biosynthesis enoyl-CoA hydratase; Validated


Pssm-ID: 235936  Cd Length: 249  Bit Score: 54.20  E-value: 9.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCG------LDFIYFIRRLTDDrkkestkmaeairNFVNTFIQF 712
Cdd:PRK07110   27 NAFSDELCDQLHEAFDTIAQDPRyKVVILTGYPNYFATGgtqeglLSLQTGKGTFTEA-------------NLYSLALNC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 713 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAK 792
Cdd:PRK07110   94 PIPVIAAMQGHAIGGGLVLGLYADIVVLSRESVYTANFMKYGFTPGMGATAILPEKLGLALGQEMLLTARYYRGAELKKR 173
                         170
                  ....*....|....*..
gi 2077081831 793 GlvsqVFWPGTFTQEVM 809
Cdd:PRK07110  174 G----VPFPVLPRAEVL 186
PRK05674 PRK05674
gamma-carboxygeranoyl-CoA hydratase; Validated
626-869 1.41e-07

gamma-carboxygeranoyl-CoA hydratase; Validated


Pssm-ID: 168168  Cd Length: 265  Bit Score: 53.66  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 626 GFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIY--------FIRRLTDDRKkest 696
Cdd:PRK05674   15 GFATLWLS-RADKNNAFNAQMIRELILALDQVQSDASlRFLLLRGRGRHFSAGADLAWmqqsadldYNTNLDDARE---- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 697 kMAEAIRNFVntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRImGLASANE 776
Cdd:PRK05674   90 -LAELMYNLY----RLKIPTLAVVQGAAFGGALGLISCCDMAIGADDAQFCLSEVRIGLAPAVISPFVVKAI-GERAARR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 777 MLFSGRKLTAQEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQANEKECE-VLKKIWGS 855
Cdd:PRK05674  164 YALTAERFDGRRARELGLLAESYPAAELEAQVEAWIANLLLNSPQALRASKDLLREVGDGELSPALRRYCEnAIARIRVS 243
                         250
                  ....*....|....
gi 2077081831 856 AQGMDSMLKYLQRK 869
Cdd:PRK05674  244 AEGQEGLRAFLEKR 257
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
333-376 2.26e-07

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: 48.13  E-value: 2.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2077081831 333 EELYEVERIvDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 376
Cdd:cd18645     1 EHVFAVESI-EKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILD 43
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
336-378 2.48e-07

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


Pssm-ID: 349327  Cd Length: 50  Bit Score: 48.16  E-value: 2.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2077081831 336 YEVERIVD-KRKNKKGK-TEYLVRWKGYDseDDTWEPEQHLVNCE 378
Cdd:cd18971     1 YEVEEILAaRRRRIRGKgREVLVKWVGYA--EPTWEPLDNLADTA 43
PRK06143 PRK06143
enoyl-CoA hydratase; Provisional
640-841 3.09e-07

enoyl-CoA hydratase; Provisional


Pssm-ID: 180423  Cd Length: 256  Bit Score: 52.73  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSK--LVLFSAVGSIFCCGLDF-----------IYFIRRLTDdrkkestkMAEAIRnfv 706
Cdd:PRK06143   29 NILGTPVILALTQALRWLAADPDVrvLVLRGAGEKAFIGGADIkematldqasaEAFISRLRD--------LCDAVR--- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 707 ntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGqSPDGCSSLTFPRIMGLASANEMLFSGRKLTA 786
Cdd:PRK06143   98 ----HFPVPVIARIPGWCLGGGLELAAACDLRIAAHDAQFGMPEVRVG-IPSVIHAALLPRLIGWARTRWLLLTGETIDA 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077081831 787 QEACAKGLVSQVFWPGTFTQEVMVRIKELVTCNSVVLEESKALVRNIMKVDLEQA 841
Cdd:PRK06143  173 AQALAWGLVDRVVPLAELDAAVERLAASLAGCGPQALRQQKRLLREWEDMPLDVA 227
PRK07396 PRK07396
dihydroxynaphthoic acid synthetase; Validated
611-798 3.57e-07

dihydroxynaphthoic acid synthetase; Validated


Pssm-ID: 180958 [Multi-domain]  Cd Length: 273  Bit Score: 52.59  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 611 ESAYRYRDIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVG-SIFCCG----------- 677
Cdd:PRK07396    7 QDCKEYEDILYKSADGIAKITIN-RPEVRNAFRPKTVKEMIDAFADARDDDNiGVIILTGAGdKAFCSGgdqkvrgyggy 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 678 -----------LDFIYFIRRLtddrkkestkmaeairnfvntfiqfKKPIIVAVNGPAIGlGASILPL-CDVVWANEKAw 745
Cdd:PRK07396   86 vdddgvprlnvLDLQRLIRTC-------------------------PKPVIAMVAGYAIG-GGHVLHLvCDLTIAADNA- 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 746 fqtpytTFGQ------SPD---GCSSLTfpRIMGLASANEMLFSGRKLTAQEACAKGLVSQV 798
Cdd:PRK07396  139 ------IFGQtgpkvgSFDggyGASYLA--RIVGQKKAREIWFLCRQYDAQEALDMGLVNTV 192
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
333-392 5.14e-07

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: 47.36  E-value: 5.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 333 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHEFNRRHNEKQ 392
Cdd:cd18648     1 ERVFAAESII-KRRIRKGRIEYLVKWKGWAIKYSTWEPEENILD-SRLIAAFEQKERERE 58
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
333-386 5.31e-07

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


Pssm-ID: 349318  Cd Length: 52  Bit Score: 47.18  E-value: 5.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 333 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWePEQHLVNCEEYIHEFNR 386
Cdd:cd18962     1 EGHYVVEAIV-NDVLIDGKHMYEVKWEGYPSDHNNW-VAEWDLNDKEILRKYNK 52
PRK07112 PRK07112
enoyl-CoA hydratase/isomerase;
616-795 6.26e-07

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235938  Cd Length: 255  Bit Score: 51.61  E-value: 6.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 616 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAaDDSKLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKES 695
Cdd:PRK07112    3 YQTIRVRQQGDVCFLQLH-RPEAQNTINDRLIAECMDVLDRCE-HAATIVVLEGLPEVFCFGADFSAIAEKPDAGRADLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 696 TkmAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPdGCSSLTFPRIMGLASAN 775
Cdd:PRK07112   81 D--AEPLYDLWHRLATGPYVTIAHVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIP-ACVLPFLIRRIGTQKAH 157
                         170       180
                  ....*....|....*....|
gi 2077081831 776 EMLFSGRKLTAQEACAKGLV 795
Cdd:PRK07112  158 YMTLMTQPVTAQQAFSWGLV 177
PLN02874 PLN02874
3-hydroxyisobutyryl-CoA hydrolase-like protein
640-815 8.65e-07

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178462 [Multi-domain]  Cd Length: 379  Bit Score: 52.11  E-value: 8.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDR-KKESTKMAEAIRNFVNTFIQ-FKKPI 716
Cdd:PLN02874   33 NVISLSVVSLLAEFLEQWEKDDSvELIIIKGAGRAFSAGGD----LKMFYDGReSDDSCLEVVYRMYWLCYHIHtYKKTQ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 717 IVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGlaSANEML-FSGRKLTAQEACAKGLV 795
Cdd:PLN02874  109 VALVHGLVMGGGAGLMVPMKFRVVTEKTVFATPEASVGFHTDCGFSYILSRLPG--HLGEYLaLTGARLNGKEMVACGLA 186
                         170       180
                  ....*....|....*....|
gi 2077081831 796 SQvFWPGTFTQEVMVRIKEL 815
Cdd:PLN02874  187 TH-FVPSEKLPELEKRLLNL 205
PRK11423 PRK11423
methylmalonyl-CoA decarboxylase; Provisional
640-829 8.92e-07

methylmalonyl-CoA decarboxylase; Provisional


Pssm-ID: 236908 [Multi-domain]  Cd Length: 261  Bit Score: 51.18  E-value: 8.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDSK-LVLFSAVGS-IFCCGLDfiyfIRRLTDDRKKE---STKMAEAIRNfvntfIQ-FK 713
Cdd:PRK11423   26 NALSKVLIDDLMQALSDLNRPEIRvVILRAPSGSkVWSAGHD----IHELPSGGRDPlsyDDPLRQILRM-----IQkFP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 714 KPIIVAVNGPAIGlGASILPL-CDVVWANEKAWFQ-------TPYTTFGQspdgcssLTFPRIMGLASANEMLFSGRKLT 785
Cdd:PRK11423   97 KPVIAMVEGSVWG-GAFELIMsCDLIIAASTSTFAmtpanlgVPYNLSGI-------LNFTNDAGFHIVKEMFFTASPIT 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2077081831 786 AQEACAKGLVSQVFWPG---TFTQEVMVRIKELVT-CNSVVLEESKAL 829
Cdd:PRK11423  169 AQRALAVGILNHVVEVEeleDFTLQMAHHISEKAPlAIAVIKEQLRVL 216
PRK12478 PRK12478
crotonase/enoyl-CoA hydratase family protein;
640-797 1.21e-06

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 183548  Cd Length: 298  Bit Score: 51.11  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVGSIFCCGLDF----IYFIRRLTDDRKKESTK---MAEA-----IRNFV 706
Cdd:PRK12478   27 NTIVPPMPDEIEAAIGLAERDqDIKVIVLRGAGRAFSGGYDFgggfQHWGEAMMTDGRWDPGKdfaMVTAretgpTQKFM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 707 NTFiQFKKPIIVAVNGPAIGlGASILPLC-DVVWANEKAWFQTPYTTFGqspdGC--SSLTFPRiMGLASANEMLFSGRK 783
Cdd:PRK12478  107 AIW-RASKPVIAQVHGWCVG-GASDYALCaDIVIASDDAVIGTPYSRMW----GAylTGMWLYR-LSLAKVKWHSLTGRP 179
                         170
                  ....*....|....
gi 2077081831 784 LTAQEACAKGLVSQ 797
Cdd:PRK12478  180 LTGVQAAEAELINE 193
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
336-386 1.98e-06

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: 45.56  E-value: 1.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGY-DSEDDTWEPEQHLVNCEEYIHEFNR 386
Cdd:cd18961     1 YEVEKILSHRI-VNGKPLYLVMWVGYpGPVENSEMWEEDLKNCGELLKAYKD 51
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
333-376 2.42e-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: 45.48  E-value: 2.42e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2077081831 333 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 376
Cdd:cd18649     2 ERVFAAEALL-KRRIRKGRMEYLVKWKGWSQKYSTWEPEENILD 44
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
336-386 3.58e-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: 44.87  E-value: 3.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 336 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN-CEEYIHEFNR 386
Cdd:cd18976     1 YIVESLLDRRK-VRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAYDA 51
PRK09120 PRK09120
p-hydroxycinnamoyl CoA hydratase/lyase; Validated
640-841 6.96e-06

p-hydroxycinnamoyl CoA hydratase/lyase; Validated


Pssm-ID: 236383  Cd Length: 275  Bit Score: 48.85  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNT-AAADDSKLVLFSAVGSIFCCGLDFI-YFirRLTDDRKKESTkmaEAIRNFVNTFIQ----FK 713
Cdd:PRK09120   30 NAMSPTLNREMIDVLDAlEFDDDAGVLVLTGAGDAWSAGMDLKeYF--RETDAQPEILQ---ERIRREAYGWWRrlrwYQ 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 714 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRKLTAQEACAKG 793
Cdd:PRK09120  105 KPTIAMVNGWCFGGGFSPLVACDLAIAADEAQFGLSEINWGIPPGGGVSKAMADTVGHRDALYYIMTGETFTGRKAAEMG 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077081831 794 LVSQVFwPgtfTQEVMVRIKELVTC----NSVVLEESKALVRNIMKVDLEQA 841
Cdd:PRK09120  185 LVNESV-P---LAQLRARTRELAAKllekNPVVLRAAKDGFKRVRELTWDQA 232
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
609-854 8.77e-06

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 49.51  E-value: 8.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 609 QTESAYRyrdiVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDfIYFIRR 686
Cdd:PRK11154    2 EMASAFT----LNVREDNIAVITIDVPGEKMNTLKAEFAEQVRAILKQLREDKElkGVVFISGKPDNFIAGAD-INMLAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 687 LTDdrKKESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCD--VVWANEKAWFQTPYTTFGQSPDGCSSLT 764
Cdd:PRK11154   77 CKT--AQEAEALARQGQQLFAEIEALPIPVVAAIHGACLGGGLELALACHyrVCTDDPKTVLGLPEVQLGLLPGSGGTQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 765 FPRIMGLASANEMLFSGRKLTAQEACAKGLVSQVFwPGTFTQEVMV-------RIKELVTCNSVVLEESkALVRNIMkvd 837
Cdd:PRK11154  155 LPRLIGVSTALDMILTGKQLRAKQALKLGLVDDVV-PHSILLEVAVelakkgkPARRPLPVRERLLEGN-PLGRALL--- 229
                         250
                  ....*....|....*..
gi 2077081831 838 LEQANEKeceVLKKIWG 854
Cdd:PRK11154  230 FKQARKK---TLAKTQG 243
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
336-374 1.17e-05

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


Pssm-ID: 349321  Cd Length: 53  Bit Score: 43.23  E-value: 1.17e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2077081831 336 YEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHL 374
Cdd:cd18965     1 YIIEALL-KKRQFNRKLEYLVKWHGLPESENTWEREKDI 38
CD_POL_like cd18979
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ...
339-375 3.04e-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: 42.09  E-value: 3.04e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2077081831 339 ERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLV 375
Cdd:cd18979     4 EKVLDIRQRDKGNKEFLVQWQGLSVEEATWEPYKDLV 40
PRK08788 PRK08788
enoyl-CoA hydratase; Validated
643-802 3.24e-05

enoyl-CoA hydratase; Validated


Pssm-ID: 236338  Cd Length: 287  Bit Score: 46.83  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 643 NPEVMKE-------VQSALNTAAADDSKLVLFSAVGSIFCCGLDFIYFiRRLTDDRKKESTKM-AEAIRNFVNTFIQ-FK 713
Cdd:PRK08788   41 NLELLDDimnlqraIRQRLDDSGLPVDFWVLASDVPGVFNLGGDLALF-AELIRAGDRDALLAyARACVDGVHAFHRgFG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 714 KPII-VA-VNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPD-GCSSLTFPRImGLASANEMLFSGRKLTAQEAC 790
Cdd:PRK08788  120 AGAIsIAlVQGDALGGGFEAALSHHTIIAERGAKMGFPEILFNLFPGmGAYSFLARRV-GPKLAEELILSGKLYTAEELH 198
                         170
                  ....*....|..
gi 2077081831 791 AKGLVSQVFWPG 802
Cdd:PRK08788  199 DMGLVDVLVEDG 210
CD2_cpSRP43_like cd18629
chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
334-374 4.57e-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: 41.72  E-value: 4.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2077081831 334 ELYEVERIVDKRkNKKGKTEYLVRWKgyDSEDDTWEPEQHL 374
Cdd:cd18629     1 EYAEVNEILESR-GKGKDMEYLIEWK--DGGDCEWVKGVHV 38
PRK08259 PRK08259
crotonase/enoyl-CoA hydratase family protein;
659-803 5.22e-05

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 236205  Cd Length: 254  Bit Score: 45.66  E-value: 5.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 659 ADDSKLV--LFSAVGSiFCCGLDfiyfIRRLTDDRKKES----------TKMaeairnfvntfiQFKKPIIVAVNGPAIG 726
Cdd:PRK08259   44 ADDAASVavLWGAGGT-FCAGAD----LKAVGTGRGNRLhpsgdgpmgpSRM------------RLSKPVIAAVSGYAVA 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077081831 727 LGASILPLCDVVWANEKAWFQTPYTTFGqSP--DGcSSLTFPRIMGLASANEMLFSGRKLTAQEACAKGLVSQVFWPGT 803
Cdd:PRK08259  107 GGLELALWCDLRVAEEDAVFGVFCRRWG-VPliDG-GTVRLPRLIGHSRAMDLILTGRPVDADEALAIGLANRVVPKGQ 183
PRK08321 PRK08321
1,4-dihydroxy-2-naphthoyl-CoA synthase;
706-798 7.49e-05

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


Pssm-ID: 181386  Cd Length: 302  Bit Score: 45.79  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 706 VNTFIQF-KKPIIVAVNGPAIGLGASILPLCDVVWAN-EKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEMLFSGRK 783
Cdd:PRK08321  127 VQRLIRFmPKVVIAVVPGWAAGGGHSLHVVCDLTLASrEHARFKQTDADVGSFDGGYGSAYLARQVGQKFAREIFFLGRT 206
                          90
                  ....*....|....*
gi 2077081831 784 LTAQEACAKGLVSQV 798
Cdd:PRK08321  207 YSAEEAHDMGAVNAV 221
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
337-387 2.33e-04

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, 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 CHD5, CHD6, CHD7, CHD8, and CHD9. 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. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. 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: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 39.96  E-value: 2.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2077081831 337 EVERIVDKRK-----NKKGKTEYLVRWKGYDSEDDTWEPEQHlVNcEEYIHEFNRR 387
Cdd:cd18663     5 EVDRILDVSVstdpnTGEPVTHYLVKWCSLPYEDSTWELEED-VD-PAKIEEFEKL 58
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
620-798 3.92e-04

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 44.08  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 620 VVRKQDGFTHILLSTKSSENnSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKM 698
Cdd:PRK11730   10 VDWLEDGIAELVFDAPGSVN-KLDRATLASLGEALDALEAQSDlKGLLLTSAKDAFIVGADITEFLSLFAAPEEELSQWL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 699 AEAIRNFvNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASANEML 778
Cdd:PRK11730   89 HFANSIF-NRLEDLPVPTVAAINGYALGGGCECVLATDYRVASPDARIGLPETKLGIMPGFGGTVRLPRLIGADNALEWI 167
                         170       180
                  ....*....|....*....|
gi 2077081831 779 FSGRKLTAQEACAKGLVSQV 798
Cdd:PRK11730  168 AAGKDVRAEDALKVGAVDAV 187
PLN02267 PLN02267
enoyl-CoA hydratase/isomerase family protein
630-814 4.21e-04

enoyl-CoA hydratase/isomerase family protein


Pssm-ID: 215151  Cd Length: 239  Bit Score: 42.78  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 630 ILLSTKSSENNsLNPEVMKEVQSALNTAAADDSK--LVLFSAVGSIFCCGLDFIYFIRRLTD-DRKKEstkMAEAIRNFV 706
Cdd:PLN02267   12 ILTLTGDGEHR-LNPTLIDSIRSALRQVKSQATPgsVLITTAEGKFFSNGFDLAWAQAAGSApSRLHL---MVAKLRPLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 707 NTFIQFKKPIIVAVNGPAIGLGAsILPLCD--VVWANEKAWFQTPYTTFGQS-PDGCSSLTFPRIMGLASANEMLFSGRK 783
Cdd:PLN02267   88 ADLISLPMPTIAAVTGHASAAGF-ILALSHdyVLMRKDRGVLYMSEVDIGLPlPDYFMALLRAKIGSPAARRDVLLRAAK 166
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2077081831 784 LTAQEACAKGLVSQVFWPGTFTQEVMVRIKE 814
Cdd:PLN02267  167 LTAEEAVEMGIVDSAHDSAEETVEAAVRLGE 197
PLN02157 PLN02157
3-hydroxyisobutyryl-CoA hydrolase-like protein
664-824 5.50e-04

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 177817 [Multi-domain]  Cd Length: 401  Bit Score: 43.13  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 664 LVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEK 743
Cdd:PLN02157   84 FVMMKGSGRAFCAGGDIVSLYHLRKRGSPDAIREFFSSLYSFIYLLGTYLKPHVAILNGVTMGGGTGVSIPGTFRVATDR 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 744 AWFQTPYTTFGQSPDGCSSLTFPRIMGlaSANEML-FSGRKLTAQEACAKGLVSQVFWpgtfTQEVMV---RIKELVTCN 819
Cdd:PLN02157  164 TIFATPETIIGFHPDAGASFNLSHLPG--RLGEYLgLTGLKLSGAEMLACGLATHYIR----SEEIPVmeeQLKKLLTDD 237

                  ....*
gi 2077081831 820 SVVLE 824
Cdd:PLN02157  238 PSVVE 242
PRK06213 PRK06213
crotonase/enoyl-CoA hydratase family protein;
640-736 7.55e-04

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235744  Cd Length: 229  Bit Score: 41.88  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALnTAAADDSKLVLFSAVGSIFCCGLDFIYFIRRltddrKKESTKMAEAIRNFVNTFIQFKKPIIVA 719
Cdd:PRK06213   24 NALSPAMIDALNAAL-DQAEDDRAVVVITGQPGIFSGGFDLKVMTSG-----AQAAIALLTAGSTLARRLLSHPKPVIVA 97
                          90
                  ....*....|....*..
gi 2077081831 720 VNGPAIGLGASILPLCD 736
Cdd:PRK06213   98 CTGHAIAKGAFLLLSAD 114
CD3_cpSRP43_like cd18628
chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
340-385 1.20e-03

chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; This subgroup includes the chromodomain 3 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: 349278  Cd Length: 51  Bit Score: 37.75  E-value: 1.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2077081831 340 RIVDKRKnkkgKTEYLVRWkgYDSEDDTWEPEQHLVNceEYIHEFN 385
Cdd:cd18628    13 RVGDDGK----TIEYLVKW--TDMSDATWEPQDNVDS--TLVLLYQ 50
CD_eEF3 cd18626
chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic ...
338-375 1.54e-03

chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic elongation factor eEF3 (also known as EF-3, YEF3, and TEF3), a member of the ATP-binding cassette (ABC) family of proteins, is a ribosomal binding ATPase essential for fungal translation machinery. Until recently it was considered fungal-specific and therefore an attractive target for antifungal therapy; however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes, and translation elongation factor 3 activity has been demonstrated from a non-fungal species, Phytophthora infestans. 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. Chromodomain mutations in the ABC2 domain of eEF3 have been shown to reduce ATPase activity, but not ribosome binding. Thus, the chromodomain-like insertion is critical to eEF3 function. In addition to its elongation function, eEF3 has been shown to interact with mRNA in a translation independent manner, suggesting an additional, non-elongation function for this factor.


Pssm-ID: 349276 [Multi-domain]  Cd Length: 56  Bit Score: 37.58  E-value: 1.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2077081831 338 VERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLV 375
Cdd:cd18626     4 IEKIVGRRKLKKSY-EYEVKWKGMSSKDNSWIPREELE 40
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
336-386 2.24e-03

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: 349323  Cd Length: 55  Bit Score: 36.84  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077081831 336 YEVERIVDKR----KNKKGKTE---YLVRWKGYDseDDTWEPEQHLVNcEEYIHEFNR 386
Cdd:cd18967     1 WEIEAILAHHmsdpRTHPGKPAtmlYLTKWEGFP--DETWEPAESFDD-RKILHDYRR 55
PRK05617 PRK05617
3-hydroxyisobutyryl-CoA hydrolase; Provisional
640-758 8.03e-03

3-hydroxyisobutyryl-CoA hydrolase; Provisional


Pssm-ID: 235533 [Multi-domain]  Cd Length: 342  Bit Score: 39.42  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077081831 640 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSI-FCCGLDfiyfIRRLTDDRKKEStkmAEAIRNF------VNTFI- 710
Cdd:PRK05617   25 NALSLEMIRAIDAALDAWEDDDAvAAVVIEGAGERgFCAGGD----IRALYEAARAGD---PLAADRFfreeyrLNALIa 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077081831 711 QFKKPIIVAVNGPAIG------LGASIlplcDVVwaNEKAWFQTPYTTFGQSPD 758
Cdd:PRK05617   98 RYPKPYIALMDGIVMGggvgisAHGSH----RIV--TERTKMAMPETGIGFFPD 145
chromodomain cd18963
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
333-374 8.30e-03

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: 349319  Cd Length: 57  Bit Score: 35.36  E-value: 8.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2077081831 333 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEddtwEPEQHL 374
Cdd:cd18963     1 ERVFAAECII-KRRVRKGRIEYLVKWKGWASK----EREREL 37
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
338-370 8.61e-03

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


Pssm-ID: 349312  Cd Length: 65  Bit Score: 35.44  E-value: 8.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2077081831 338 VERIVDKRKNK----------KGKTEYLVRWKGYDSEDDTWEP 370
Cdd:cd18665     5 IDIVLDHRLKEgleegelddpKENYEFLIKWTDESHLHNTWET 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH