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Conserved domains on  [gi|1491390975|ref|XP_026646013|]
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chromodomain Y-like protein isoform X6 [Zonotrichia albicollis]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
302-455 2.19e-33

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: 124.60  E-value: 2.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRltDDRKKESTK 380
Cdd:cd06558     1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 381 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:cd06558    78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPA 152
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 3.85e-33

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: 119.09  E-value: 3.85e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd18634     1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
 
Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
302-455 2.19e-33

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: 124.60  E-value: 2.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRltDDRKKESTK 380
Cdd:cd06558     1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 381 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:cd06558    78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPA 152
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 3.85e-33

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: 119.09  E-value: 3.85e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd18634     1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
302-455 2.03e-24

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: 101.40  E-value: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDrkkESTK 380
Cdd:COG1024     1 VLVEREGGVATITLNRPEK-LNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPE---EARA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 381 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:COG1024    77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLA 151
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
300-453 9.74e-24

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 99.94  E-value: 9.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 300 RDIVVRKQDGFTHILLsTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES 378
Cdd:PRK06688    5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD----IKDFPKAPPKPP 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 379 TKMAEAIRnFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PRK06688   80 DELAPVNR-FLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIG 153
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
7-58 1.70e-23

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 92.64  E-value: 1.70e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRR 58
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
7-60 2.18e-21

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 86.88  E-value: 2.18e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975    7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRRHN 60
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKER 55
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
322-453 2.47e-10

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: 60.84  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 322 NNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRR---LTDDRKKESTKMAEAIRnfvntfiQFKK 397
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLKEMYGEgpaHQALYRENVLDLWTLLY-------TCPK 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1491390975 398 PIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:pfam00378  90 PVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIG 145
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
302-454 2.63e-03

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: 40.21  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDfIYFIRrlTDDRKKEST 379
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD-IQMIA--ACKTAQEVT 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491390975 380 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWA--NEKAWFQTPYTTFGQSPDGCSSLTFPRIMGL 454
Cdd:TIGR02441  92 QLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGV 168
 
Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
302-455 2.19e-33

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: 124.60  E-value: 2.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRltDDRKKESTK 380
Cdd:cd06558     1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 381 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:cd06558    78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPA 152
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 3.85e-33

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: 119.09  E-value: 3.85e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd18634     1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
302-455 2.03e-24

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: 101.40  E-value: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSeNNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDrkkESTK 380
Cdd:COG1024     1 VLVEREGGVATITLNRPEK-LNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPE---EARA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 381 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:COG1024    77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLA 151
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
7-57 5.78e-24

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: 5.78e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd00024     1 YEVEKILDHRV-RKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
300-453 9.74e-24

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 99.94  E-value: 9.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 300 RDIVVRKQDGFTHILLsTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES 378
Cdd:PRK06688    5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD----IKDFPKAPPKPP 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 379 TKMAEAIRnFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PRK06688   80 DELAPVNR-FLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIG 153
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
7-58 1.70e-23

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 92.64  E-value: 1.70e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRR 58
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
7-60 2.18e-21

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 86.88  E-value: 2.18e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975    7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRRHN 60
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKER 55
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
6-57 3.25e-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: 3.25e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   6 LYEVERIVDKrKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd18633     1 VFEVEKILDM-KTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
PRK07511 PRK07511
enoyl-CoA hydratase; Provisional
323-442 9.09e-17

enoyl-CoA hydratase; Provisional


Pssm-ID: 181009 [Multi-domain]  Cd Length: 260  Bit Score: 80.04  E-value: 9.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEAI---RNFVNTFIQFKKP 398
Cdd:PRK07511   25 NALHPDMYAAGIEALNTAERDPSiRAVVLTGAGGFFCAGGN----LNRLLENRAKPPSVQAASIdglHDWIRAIRAFPKP 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1491390975 399 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDG 442
Cdd:PRK07511  101 VIAAVEGAAAGAGFSLALACDLLVAARDAKFVMAYVKVGLTPDG 144
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-55 1.75e-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: 1.75e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975   7 YEVE-----RIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18968     2 YEVEvilaaRVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
7-55 1.11e-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: 1.11e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975   7 YEVERIVDKR----KNKKGKTEYL-VRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18635     2 FEVEKLVGICygdpKKTGERGLYFkVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
7-55 1.53e-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: 67.46  E-value: 1.53e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 55
Cdd:cd18631     2 YVVEKVLDRRV-VKGKVEYLLKWKGYPDEDNTWEPEENL-DCPDLIAEF 48
PRK08260 PRK08260
enoyl-CoA hydratase; Provisional
299-455 3.38e-14

enoyl-CoA hydratase; Provisional


Pssm-ID: 236206 [Multi-domain]  Cd Length: 296  Bit Score: 72.73  E-value: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 299 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLD-------FIYFIRRL 370
Cdd:PRK08260    3 YETIRYDVADGIATITLN-RPDKLNAFTVTMARELIEAFDAADADDAvRAVIVTGAGRAFCAGADlsaggntFDLDAPRT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 371 TDDRKKEST--KMAEAIRN----FVNTFIQFKKPIIVAVNGPAIGLGASI-LPLcDVVWANEKAWFQTPYTTFGQSPDGC 443
Cdd:PRK08260   82 PVEADEEDRadPSDDGVRDgggrVTLRIFDSLKPVIAAVNGPAVGVGATMtLAM-DIRLASTAARFGFVFGRRGIVPEAA 160
                         170
                  ....*....|..
gi 1491390975 444 SSLTFPRIMGLA 455
Cdd:PRK08260  161 SSWFLPRLVGLQ 172
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
4-57 5.30e-14

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: 5.30e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975   4 EELYEVERIVDKRKNKKGkTEYLVRWKGYDSEDDTWEPeQHLVNCEEYIHEFNR 57
Cdd:cd18978     1 DESYEVEKIINHRGEKNR-RKYLVKWKGYDDTDNSWVT-QEDFNDKDMIDEYEN 52
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
7-57 1.58e-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: 64.97  E-value: 1.58e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   7 YEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHL-VNCEEYIHEFNR 57
Cdd:cd18638     2 FEVEKIV-KKKTVKGGTEYFVKWKGYSAKENTWETEDNLeKSYKEMIDEFEK 52
PRK06023 PRK06023
crotonase/enoyl-CoA hydratase family protein;
323-453 2.34e-13

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 168351  Cd Length: 251  Bit Score: 69.82  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDrkkesTKMAEAIRNFVNTFIQFKKPIIV 401
Cdd:PRK06023   28 NAITRAMYATMAKALKAADADDAiRAHVFLGTEGCFSAGNDMQDFLAAAMGG-----TSFGSEILDFLIALAEAEKPIVS 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975 402 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PRK06023  103 GVDGLAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALVPEAGSSLLAPRLMG 154
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
6-57 2.44e-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: 64.39  E-value: 2.44e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd18636     1 VYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
PRK08140 PRK08140
enoyl-CoA hydratase; Provisional
323-455 3.71e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 236163  Cd Length: 262  Bit Score: 69.17  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDSKLVLFSAVGSIFCCGLDfiyfirrLTD---DRKKESTKMAEAIRNFVNTFIQ----F 395
Cdd:PRK08140   26 NSFTREMHRELREALDQVEDDGARALLLTGAGRGFCAGQD-------LADrdvTPGGAMPDLGESIETFYNPLVRrlraL 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 396 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:PRK08140   99 PLPVIAAVNGVAAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLPRLVGMA 158
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
7-58 7.14e-13

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: 62.91  E-value: 7.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1491390975   7 YEVERIVD-KRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNRR 58
Cdd:cd18632     2 YEVEKIVDeKTDRNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRK 54
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
7-55 9.25e-13

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: 9.25e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 55
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 ...
7-55 9.94e-13

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: 62.65  E-value: 9.94e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18973     1 YVVEAILDNKR-RKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKY 48
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
4-58 1.10e-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: 62.48  E-value: 1.10e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975   4 EELYEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHEFNRR 58
Cdd:cd18644     1 DLVYAAEKILKKRV-RKGKVEYLVKWKGWSNKHNTWEPEENILD-RRLIEIFERT 53
PRK05981 PRK05981
enoyl-CoA hydratase/isomerase;
323-455 1.54e-12

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235661  Cd Length: 266  Bit Score: 67.45  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDSKL--VLFSAVGSIFCCGLDFIyfiRRLTDDRKKESTKMA-EAIRNFVNTFI----QF 395
Cdd:PRK05981   26 NAVSIDMLGGLAEALDAIEDGKAEVrcLVLTGAGRGFCTGANLQ---GRGSGGRESDSGGDAgAALETAYHPFLrrlrNL 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 396 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:PRK05981  103 PCPIVTAVNGPAAGVGMSFALMGDLILCARSAYFLQAFRRIGLVPDGGSTWLLPRLVGKA 162
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
7-57 1.75e-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: 1.75e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd18974     1 WEVEEIVDEKM-IDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
7-55 1.94e-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: 1.94e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 55
Cdd:cd18653     2 YAVEKICDRRV-RKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
7-55 2.86e-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: 2.86e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491390975   7 YEVERIVDKRKNKKGKTE--YLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18980     4 YEVEAILDHKVDRRYRDPnfYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
6-57 4.13e-12

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


Pssm-ID: 349316  Cd Length: 51  Bit Score: 60.65  E-value: 4.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEFNR 57
Cdd:cd18960     1 VFVVERILDKRLGRNGGEEFLIKWQGFPESDSSWEPRENL-QCDEMLEEFEK 51
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
7-49 9.53e-12

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: 59.76  E-value: 9.53e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1491390975   7 YEVERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCE 49
Cdd:cd18970     1 FFVERILDERRRGRGW-QYLVRWLGYGPSDDSWLPRRELEECE 42
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
7-55 1.02e-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: 1.02e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 55
Cdd:cd18651     2 YVVEKVLDRRV-VKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEF 48
PRK07854 PRK07854
enoyl-CoA hydratase; Provisional
323-442 3.22e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 236115 [Multi-domain]  Cd Length: 243  Bit Score: 63.12  E-value: 3.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDSKLVLFSAVGSIFCCGLDF---IY---FIRRLTDdrkkestkMAEAIrnfVNTFIqfk 396
Cdd:PRK07854   22 NALNAELCEELREAVRKAVDESARAIVLTGQGTVFCAGADLsgdVYaddFPDALIE--------MLHAI---DAAPV--- 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1491390975 397 kPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDG 442
Cdd:PRK07854   88 -PVIAAINGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDN 132
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
7-55 3.95e-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: 3.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1491390975   7 YEVERIVDKRKNKKGKT-EYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18640     1 EPVEKIVAKRFNPRKKTwEYLVKWENRSHHENTWEPMANLERCKYLLQMF 50
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-45 4.56e-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: 4.56e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKNKkGKTEYLVRWKGYDSEDDTWEPEQHL 45
Cdd:cd18966     1 YEVERILAERRDD-GGKRYLVKWEGYPLEEATWEPEENI 38
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-55 8.41e-11

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


Pssm-ID: 349320  Cd Length: 54  Bit Score: 56.96  E-value: 8.41e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   7 YEVERIVDKR---KNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18964     1 FFVERIIGRRpsaRDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDF 52
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
7-55 1.77e-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: 56.34  E-value: 1.77e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1491390975   7 YEVERIVD----KRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18977     4 YEVEKIVGekwkKRKNRRVK-LYKVRFKGYGPEEDEWLTKEELKNAPEILAEW 55
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
4-55 2.10e-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: 2.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975   4 EELYEVERIVDKRKN--KKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18969     1 EEEYEIEEILDVKKGgfEDGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEY 54
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
7-47 2.12e-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: 55.86  E-value: 2.12e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18627     1 FAAECILKKRI-RKGKVEYLVKWKGWSQKYNTWEPEENILD 40
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
322-453 2.47e-10

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: 60.84  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 322 NNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRR---LTDDRKKESTKMAEAIRnfvntfiQFKK 397
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADLKEMYGEgpaHQALYRENVLDLWTLLY-------TCPK 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1491390975 398 PIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:pfam00378  90 PVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIG 145
PRK06495 PRK06495
enoyl-CoA hydratase/isomerase family protein;
323-432 2.64e-10

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 168580 [Multi-domain]  Cd Length: 257  Bit Score: 60.86  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNT-AAADDSKLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEA--IRNFVNTFIQFKKPI 399
Cdd:PRK06495   25 NALSRELRDELIAVFDEiSERPDVRVVVLTGAGKVFCAGAD----LKGRPDVIKGPGDLRAHNrrTRECFHAIRECAKPV 100
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1491390975 400 IVAVNGPAIGLGASILPLCDVVWANEKAWFQTP 432
Cdd:PRK06495  101 IAAVNGPALGAGLGLVASCDIIVASENAVFGLP 133
PRK09245 PRK09245
crotonase/enoyl-CoA hydratase family protein;
301-455 5.24e-10

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181723  Cd Length: 266  Bit Score: 59.98  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 301 DIVVRKQDGFTHILLSTKSSENNSLN-PEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES 378
Cdd:PRK09245    3 DFLLVERDGHIVTLTMNRPETRNALSdNDAVDALVAACAAINADRSvRAVILTGAGTAFSSGGN----VKDMRARVGAFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 379 TKMAEA-------IRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP-DGCSSLtFPR 450
Cdd:PRK09245   79 GSPADIrqgyrhgIQRIPLALYNLEVPVIAAVNGPAIGAGCDLACMCDIRIASETARFAESFVKLGLIPgDGGAWL-LPR 157

                  ....*
gi 1491390975 451 IMGLA 455
Cdd:PRK09245  158 IIGMA 162
PLN02888 PLN02888
enoyl-CoA hydratase
302-453 7.27e-10

enoyl-CoA hydratase


Pssm-ID: 215480  Cd Length: 265  Bit Score: 59.38  E-value: 7.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSENnSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfirrLT--DDRKKES 378
Cdd:PLN02888   12 LVPKSRNGIATITINRPKALN-ALTRPMMVELAAAFKRLDEDDSvKVIILTGSGRAFCSGVD-------LTaaEEVFKGD 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491390975 379 TKMAEAirnfvNTFIQF---KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PLN02888   84 VKDVET-----DPVAQMercRKPIIGAINGFAITAGFEIALACDILVASRGAKFIDTHAKFGIFPSWGLSQKLSRIIG 156
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
4-58 1.06e-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: 53.91  E-value: 1.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975   4 EELYEVERIVDKRkNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHEFNRR 58
Cdd:cd18647     1 EQVFAAECILSKR-LRKGKLEYLVKWRGWSSKHNSWEPEENILD-PRLLLAFQKK 53
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
7-55 1.07e-09

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


Pssm-ID: 349299  Cd Length: 50  Bit Score: 53.86  E-value: 1.07e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 55
Cdd:cd18652     2 FVVEKVLDRRV-VNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
7-55 1.23e-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: 1.23e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18972     1 YEVEAIVGHKPKKKPR-QFLVSWLGYDSSHNEWKQKEELENARELLQDY 48
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
8-43 1.34e-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: 1.34e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1491390975   8 EVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQ 43
Cdd:cd18659     4 IVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEE 39
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
7-55 1.40e-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: 1.40e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHEF 55
Cdd:cd18639     1 YEVEYLCDYKK-IREQEYYLVKWKGYPDSENTWEPRQNL-KCSRLLKQF 47
PRK07659 PRK07659
enoyl-CoA hydratase; Provisional
302-442 2.45e-09

enoyl-CoA hydratase; Provisional


Pssm-ID: 236073 [Multi-domain]  Cd Length: 260  Bit Score: 57.74  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDSKLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKM 381
Cdd:PRK07659    8 VVVKYEGRVATIMLN-RPEALNALDEPMLKELLQALKEVAESSAHIVVLRGNGRGFSAGGD----IKMMLSSNDESKFDG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491390975 382 A-EAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDG 442
Cdd:PRK07659   83 VmNTISEIVVTLYTMPKLTISAIHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGLIPDG 144
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
7-55 2.81e-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: 2.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491390975   7 YEVERIVDKRKNKKGKT-EYLVRWKGYDSEDD-TWEPEQHLVNCEEYIHEF 55
Cdd:cd18637     2 YVVEKILKHRMARKGGGyEYLLKWEGYDDPSDnTWSSEADCAGCKDLIEAY 52
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
7-57 3.56e-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: 3.56e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491390975   7 YEVERIVDKRkNKKGKTEYLVRWKGYDSEDDTWEPEQHlVNCEEYIHEFNR 57
Cdd:cd18975     1 YEVESILNSR-LHRGKLQYLIQWKGYPLEEASWELEDN-IKNPRLIEEFHK 49
PRK06210 PRK06210
enoyl-CoA hydratase; Provisional
323-455 3.62e-09

enoyl-CoA hydratase; Provisional


Pssm-ID: 180472  Cd Length: 272  Bit Score: 57.41  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDF-------IYFIRRLTDDRKKESTKMAEAIRNFvNTFIQ 394
Cdd:PRK06210   28 NAWTPVMEAEVYAAMDRAEADPAvRVIVLTGAGRGFCAGADMgelqtidPSDGRRDTDVRPFVGNRRPDYQTRY-HFLTA 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491390975 395 FKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:PRK06210  107 LRKPVIAAINGACAGIGLTHALMCDVRFAADGAKFTTAFARRGLIAEHGISWILPRLVGHA 167
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
4-47 3.75e-09

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: 52.40  E-value: 3.75e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1491390975   4 EELYEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18646     2 EQVFAVESIRKKRV-RKGKVEYLVKWKGWPPKYSTWEPEEHILD 44
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
7-55 4.49e-09

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


Pssm-ID: 349280  Cd Length: 51  Bit Score: 52.14  E-value: 4.49e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVDKRKNKkGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHEF 55
Cdd:cd18630     2 YVVEKILGKRFVN-GRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
PRK05870 PRK05870
enoyl-CoA hydratase; Provisional
323-453 5.94e-09

enoyl-CoA hydratase; Provisional


Pssm-ID: 180298  Cd Length: 249  Bit Score: 56.66  E-value: 5.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVGSIFCCGLDfiyfirrLTDDRKKESTKMAEAIRNFVNTFI---QFKKP 398
Cdd:PRK05870   25 NAVTAEMSAQLRAAVAAAEADpDVHALVVTGAGKAFCAGAD-------LTALGAAPGRPAEDGLRRIYDGFLavaSCPLP 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1491390975 399 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PRK05870   98 TIAAVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLGLHPGGGATWMLQRAVG 152
PRK06072 PRK06072
enoyl-CoA hydratase; Provisional
302-453 7.69e-09

enoyl-CoA hydratase; Provisional


Pssm-ID: 168377 [Multi-domain]  Cd Length: 248  Bit Score: 56.33  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTK 380
Cdd:PRK06072    2 IKVESREGYAIVTMS-RPDKLNALNLEMRNEFISKLKQINADpKIRVVIVTGEGRAFCVGADLSEFAPDFAIDLRETFYP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491390975 381 MAEAIRNFvntfiqfKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PRK06072   81 IIREIRFS-------DKIYISAINGVTAGACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYFLLKLTG 146
PRK05809 PRK05809
short-chain-enoyl-CoA hydratase;
299-455 8.14e-09

short-chain-enoyl-CoA hydratase;


Pssm-ID: 180270 [Multi-domain]  Cd Length: 260  Bit Score: 56.29  E-value: 8.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 299 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKK 376
Cdd:PRK05809    3 LKNVILEKEGHIAVVTIN-RPKALNALNSETLKELDTVLDDIENDDNvyAVILTGAGEKAFVAGAD----ISEMKDLNEE 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491390975 377 ESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:PRK05809   78 EGRKFGLLGNKVFRKLENLDKPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGITPGFGGTQRLARIVGPG 156
PLN02664 PLN02664
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
297-456 1.38e-08

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


Pssm-ID: 178269 [Multi-domain]  Cd Length: 275  Bit Score: 55.68  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 297 YRYRDIVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVGSIFCCGLDFIYF----IRRLT 371
Cdd:PLN02664    4 YKTLEIIQKSPNSSVFHLNLNRPSQRNALSLDFFTEFPKALSSLDQNpNVSVIILSGAGDHFCSGIDLKTLnsisEQSSS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 372 DDRKKESTKMAEAIRNF---VNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTF 448
Cdd:PLN02664   84 GDRGRSGERLRRKIKFLqdaITAIEQCRKPVIAAIHGACIGGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTLQRL 163

                  ....*...
gi 1491390975 449 PRIMGLAS 456
Cdd:PLN02664  164 PSIVGYGN 171
PRK09674 PRK09674
enoyl-CoA hydratase-isomerase; Provisional
301-440 1.77e-08

enoyl-CoA hydratase-isomerase; Provisional


Pssm-ID: 182026 [Multi-domain]  Cd Length: 255  Bit Score: 55.16  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 301 DIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRR-----LTDDR 374
Cdd:PRK09674    3 ELLVSRQQRVLLLTLN-RPEARNALNNALLTQLVNELEAAATDTSiGVCVITGNARFFAAGADLNEMAEKdlaatLNDPR 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491390975 375 KKESTKMAeairnfvntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP 440
Cdd:PRK09674   82 PQLWQRLQ-----------AFNKPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMP 136
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
9-57 1.78e-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: 1.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1491390975   9 VERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQ-HLVNCEEYIHEFNR 57
Cdd:cd18662     6 IHRIINHRVDKDGNTWYLVKWRDLPYDQSTWESEDdDIPDYEKHIQEYWD 55
PLN02600 PLN02600
enoyl-CoA hydratase
323-453 3.17e-08

enoyl-CoA hydratase


Pssm-ID: 178210 [Multi-domain]  Cd Length: 251  Bit Score: 54.42  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDSK--LVLFSAVGSIFCCGLDFiyfirrltddrkKESTKMAEA-IRNFVN----TFIQF 395
Cdd:PLN02600   17 NAIGKEMLRGLRSAFEKIQADASArvVMLRSSVPGVFCAGADL------------KERRKMSPSeVQKFVNslrsTFSSL 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491390975 396 KK---PIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PLN02600   85 EAlsiPTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVG 145
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
7-49 4.33e-08

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: 49.31  E-value: 4.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1491390975   7 YEVERIVD-KRKNKKGK-TEYLVRWKGYDseDDTWEPEQHLVNCE 49
Cdd:cd18971     1 YEVEEILAaRRRRIRGKgREVLVKWVGYA--EPTWEPLDNLADTA 43
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
4-47 5.12e-08

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: 49.29  E-value: 5.12e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1491390975   4 EELYEVERIvDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18645     1 EHVFAVESI-EKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILD 43
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
4-63 9.37e-08

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: 48.51  E-value: 9.37e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHEFNRRHNEKQ 63
Cdd:cd18648     1 ERVFAAESII-KRRIRKGRIEYLVKWKGWAIKYSTWEPEENILD-SRLIAAFEQKERERE 58
PRK07468 PRK07468
crotonase/enoyl-CoA hydratase family protein;
323-440 1.01e-07

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180987 [Multi-domain]  Cd Length: 262  Bit Score: 53.14  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDD---RKKESTKMAEAIRNfVNTFiqfKKP 398
Cdd:PRK07468   27 NALSARMIAELTTAARRLAADAAvRVVVLTGAGKSFCAGGDLGWMRAQMTADratRIEEARRLAMMLKA-LNDL---PKP 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491390975 399 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP 440
Cdd:PRK07468  103 LIGRIQGQAFGGGVGLISVCDVAIAVSGARFGLTETRLGLIP 144
PRK07327 PRK07327
enoyl-CoA hydratase/isomerase family protein;
298-427 2.16e-07

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 235991  Cd Length: 268  Bit Score: 51.95  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 298 RYRDIVVRKQDGftHILLSTKSSEN--NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFiYFIRRLTDDR 374
Cdd:PRK07327    9 DYPALRFDRPPP--GVLEIVLNGPGalNAADARMHRELADIWRDVDRDPDvRVVLIRGEGKAFSAGGDL-ALVEEMADDF 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1491390975 375 KKESTKMAEAiRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKA 427
Cdd:PRK07327   86 EVRARVWREA-RDLVYNVINCDKPIVSAIHGPAVGAGLVAALLADISIAAKDA 137
PRK06190 PRK06190
enoyl-CoA hydratase; Provisional
323-455 2.64e-07

enoyl-CoA hydratase; Provisional


Pssm-ID: 235733  Cd Length: 258  Bit Score: 51.90  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEaiRNFVNTFIQFKKPIIV 401
Cdd:PRK06190   26 NALSAALRRALFAALAEADADDDvDVVVLTGADPAFCAGLD----LKELGGDGSAYGAQDAL--PNPSPAWPAMRKPVIG 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975 402 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:PRK06190  100 AINGAAVTGGLELALACDILIASERARFADTHARVGILPGWGLSVRLPQKVGIG 153
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
4-57 2.77e-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: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWePEQHLVNCEEYIHEFNR 57
Cdd:cd18962     1 EGHYVVEAIV-NDVLIDGKHMYEVKWEGYPSDHNNW-VAEWDLNDKEILRKYNK 52
PRK08139 PRK08139
enoyl-CoA hydratase; Validated
323-432 2.95e-07

enoyl-CoA hydratase; Validated


Pssm-ID: 181249  Cd Length: 266  Bit Score: 51.48  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKES--------TKMAEAIRnfvntfi 393
Cdd:PRK08139   33 NALSEAMLAALQAALDAIAADPSvRVVVLAAAGKAFCAGHD----LKEMRAARGLAYfralfarcSRVMQAIV------- 101
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1491390975 394 QFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTP 432
Cdd:PRK08139  102 ALPQPVIARVHGIATAAGCQLVASCDLAVAADTARFAVP 140
PRK07799 PRK07799
crotonase/enoyl-CoA hydratase family protein;
306-450 2.99e-07

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181122 [Multi-domain]  Cd Length: 263  Bit Score: 51.64  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 306 KQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEA 384
Cdd:PRK07799   10 EQRGHTLIVTMNRPEARNALSTEMLRIMVDAWDRVDNDPDiRSCILTGAGGAFCAGMDLKAATKKPPGDSFKDGSYDPSR 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491390975 385 IRNFVNTFiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPR 450
Cdd:PRK07799   90 IDALLKGR-RLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLFPMGGSAVRLVR 154
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
4-47 3.45e-07

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: 47.02  E-value: 3.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1491390975   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18649     2 ERVFAAEALL-KRRIRKGRMEYLVKWKGWSQKYSTWEPEENILD 44
PRK07658 PRK07658
enoyl-CoA hydratase; Provisional
323-458 4.05e-07

enoyl-CoA hydratase; Provisional


Pssm-ID: 181070 [Multi-domain]  Cd Length: 257  Bit Score: 51.17  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTD-DRKKESTKMAEAIRNFVNTFIQFKKPII 400
Cdd:PRK07658   23 NALSSQVLHELSELLDQVEKDDNvRVVVIHGEGRFFSAGAD----IKEFTSvTEAEQATELAQLGQVTFERVEKFSKPVI 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1491390975 401 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASTC 458
Cdd:PRK07658   99 AAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGFAGTQRLPRYVGKAKAL 156
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
7-57 4.43e-07

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: 46.41  E-value: 4.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN-CEEYIHEFNR 57
Cdd:cd18976     1 YIVESLLDRRK-VRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAYDA 51
PRK06494 PRK06494
enoyl-CoA hydratase; Provisional
323-454 1.00e-06

enoyl-CoA hydratase; Provisional


Pssm-ID: 180591 [Multi-domain]  Cd Length: 259  Bit Score: 50.04  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDSKLV--LFSAVGSIFCCGLDFIYFIRRltDDRKKESTKMAEAIRNFvntfiQFKKPII 400
Cdd:PRK06494   26 NALHLDAHFELEEVFDDFAADPEQWVaiVTGAGDKAFSAGNDLKEQAAG--GKRGWPESGFGGLTSRF-----DLDKPII 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975 401 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGL 454
Cdd:PRK06494   99 AAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGL 152
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
7-57 1.04e-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: 1.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975   7 YEVERIVDKRKnKKGKTEYLVRWKGY-DSEDDTWEPEQHLVNCEEYIHEFNR 57
Cdd:cd18961     1 YEVEKILSHRI-VNGKPLYLVMWVGYpGPVENSEMWEEDLKNCGELLKAYKD 51
PRK07657 PRK07657
enoyl-CoA hydratase; Provisional
323-453 1.22e-06

enoyl-CoA hydratase; Provisional


Pssm-ID: 181069 [Multi-domain]  Cd Length: 260  Bit Score: 49.73  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAAD-DSKLVLFSAVG-SIFCCGLDFiyfirrltddrkKESTKMAEA--------IRNFVNTF 392
Cdd:PRK07657   26 NALSLALLEELQNILTQINEEaNVRVVILTGAGeKAFCAGADL------------KERAGMNEEqvrhavslIRTTMEMV 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491390975 393 IQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PRK07657   94 EQLPQPVIAAINGIALGGGLELALACDFRIAAESASLGLTETTLAIIPGAGGTQRLPRLIG 154
PRK05862 PRK05862
enoyl-CoA hydratase; Provisional
323-455 1.60e-06

enoyl-CoA hydratase; Provisional


Pssm-ID: 180295 [Multi-domain]  Cd Length: 257  Bit Score: 49.27  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDsklvlfsAVGSI--------FCCGLDfiyfIRRLTDDRKKESTKmAEAIRNFvNTFIQ 394
Cdd:PRK05862   26 NALNDALMDELGAALAAFDADE-------GIGAIvitgsekaFAAGAD----IKEMADLSFMDVYK-GDYITNW-EKVAR 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491390975 395 FKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:PRK05862   93 IRKPVIAAVAGYALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGMGGSQRLTRAVGKA 153
PLN02874 PLN02874
3-hydroxyisobutyryl-CoA hydrolase-like protein
323-453 3.83e-06

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178462 [Multi-domain]  Cd Length: 379  Bit Score: 49.03  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDR-KKESTKMAEAIRNFVNTFIQ-FKKPI 399
Cdd:PLN02874   33 NVISLSVVSLLAEFLEQWEKDDSvELIIIKGAGRAFSAGGD----LKMFYDGReSDDSCLEVVYRMYWLCYHIHtYKKTQ 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975 400 IVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PLN02874  109 VALVHGLVMGGGAGLMVPMKFRVVTEKTVFATPEASVGFHTDCGFSYILSRLPG 162
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-45 3.88e-06

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


Pssm-ID: 349321  Cd Length: 53  Bit Score: 44.00  E-value: 3.88e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1491390975   7 YEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHL 45
Cdd:cd18965     1 YIIEALL-KKRQFNRKLEYLVKWHGLPESENTWEREKDI 38
PRK05995 PRK05995
enoyl-CoA hydratase; Provisional
323-453 3.92e-06

enoyl-CoA hydratase; Provisional


Pssm-ID: 235664 [Multi-domain]  Cd Length: 262  Bit Score: 48.00  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfIYFIRRLTDDRKKESTKMAEAIRNFVNTFIQFKKPIIV 401
Cdd:PRK05995   26 NAFNETVIAELTAAFRALDADDSvRAVVLAGAGKAFCAGAD-LNWMKKMAGYSDDENRADARRLADMLRAIYRCPKPVIA 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975 402 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFpRIMG 453
Cdd:PRK05995  105 RVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLGLIPATISPYVI-RAMG 155
PRK05864 PRK05864
enoyl-CoA hydratase; Provisional
323-453 5.16e-06

enoyl-CoA hydratase; Provisional


Pssm-ID: 168278 [Multi-domain]  Cd Length: 276  Bit Score: 47.91  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDF-----IYFIRRLTddRKKESTKMAEAIRNFVNTFIQFK 396
Cdd:PRK05864   32 NSMAFDVMVPLKEALAEVSYDNSvRVVVLTGAGRGFSSGADHksagvVPHVEGLT--RPTYALRSMELLDDVILALRRLH 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1491390975 397 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFG--QSPDGCSSLtFPRIMG 453
Cdd:PRK05864  110 QPVIAAVNGPAIGGGLCLALAADIRVASSSAYFRAAGINNGltASELGLSYL-LPRAIG 167
PRK07827 PRK07827
enoyl-CoA hydratase family protein;
308-451 1.06e-05

enoyl-CoA hydratase family protein;


Pssm-ID: 236109 [Multi-domain]  Cd Length: 260  Bit Score: 46.98  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 308 DGFTHILLStkSSEN-NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRLTDDRKKESTKMAEAI 385
Cdd:PRK07827   14 GGVATLTLD--SPHNrNALSARLVAQLHDGLRAAAADPAvRAVVLTHTGGTFCAGAD----LSEAGGGGGDPYDAAVARA 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491390975 386 RNFVNTF---IQFKKPIIVAVNG--PAIGLGasILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRI 451
Cdd:PRK07827   88 REMTALLraiVELPKPVIAAIDGhvRAGGFG--LVGACDIVVAGPESTFALTEARIGVAPAIISLTLLPRL 156
CD_POL_like cd18979
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ...
10-46 1.26e-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: 42.48  E-value: 1.26e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1491390975  10 ERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLV 46
Cdd:cd18979     4 EKVLDIRQRDKGNKEFLVQWQGLSVEEATWEPYKDLV 40
PLN02851 PLN02851
3-hydroxyisobutyryl-CoA hydrolase-like protein
344-453 1.70e-05

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178443 [Multi-domain]  Cd Length: 407  Bit Score: 46.90  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 344 DSKLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASI-LPLCDVVw 422
Cdd:PLN02851   86 DIGFVLMKGSGRAFCSGADVVSLYHLINEGNVEECKLFFENLYKFVYLQGTYLKPNVAIMDGITMGCGAGIsIPGMFRV- 164
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1491390975 423 ANEKAWFQTPYTTFGQSPDGCSSLTFPRIMG 453
Cdd:PLN02851  165 VTDKTVFAHPEVQMGFHPDAGASYYLSRLPG 195
CD2_cpSRP43_like cd18629
chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
5-45 2.40e-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: 2.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1491390975   5 ELYEVERIVDKRkNKKGKTEYLVRWKgyDSEDDTWEPEQHL 45
Cdd:cd18629     1 EYAEVNEILESR-GKGKDMEYLIEWK--DGGDCEWVKGVHV 38
PRK08150 PRK08150
crotonase/enoyl-CoA hydratase family protein;
323-458 4.15e-05

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181254  Cd Length: 255  Bit Score: 45.01  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDSKLVLFsAVGSIFCCGLDFIYFIRRLTDDRKKESTKMAEAIRNfvntfIQFKK-PIIV 401
Cdd:PRK08150   24 NALNDGLIAALRAAFARLPEGVRAVVLH-GEGDHFCAGLDLSELRERDAGEGMHHSRRWHRVFDK-----IQYGRvPVIA 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1491390975 402 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLASTC 458
Cdd:PRK08150   98 ALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGIFVGGGGSVRVPRLIGVARMT 154
PRK05980 PRK05980
crotonase/enoyl-CoA hydratase family protein;
301-453 4.49e-05

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180335 [Multi-domain]  Cd Length: 260  Bit Score: 45.13  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 301 DIVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKes 378
Cdd:PRK05980    3 DTVLIEIRDGIALLTLNRPEKLNALNYALIDRLLARLDAIEVDESvrAVILTGAGDRAFSAGADIHEFSASVAAGADV-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 379 tkmaeAIRNFV-------NTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRI 451
Cdd:PRK05980   81 -----ALRDFVrrgqamtARLEAFPKPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPTFGGTQRLPRL 155

                  ..
gi 1491390975 452 MG 453
Cdd:PRK05980  156 AG 157
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
8-58 1.21e-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: 1.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1491390975   8 EVERIVDKRK-----NKKGKTEYLVRWKGYDSEDDTWEPEQHlVNcEEYIHEFNRR 58
Cdd:cd18663     5 EVDRILDVSVstdpnTGEPVTHYLVKWCSLPYEDSTWELEED-VD-PAKIEEFEKL 58
PRK06213 PRK06213
crotonase/enoyl-CoA hydratase family protein;
323-419 3.06e-04

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235744  Cd Length: 229  Bit Score: 42.27  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALnTAAADDSKLVLFSAVGSIFCCGLDFIYFIRRltddrKKESTKMAEAIRNFVNTFIQFKKPIIVA 402
Cdd:PRK06213   24 NALSPAMIDALNAAL-DQAEDDRAVVVITGQPGIFSGGFDLKVMTSG-----AQAAIALLTAGSTLARRLLSHPKPVIVA 97
                          90
                  ....*....|....*..
gi 1491390975 403 VNGPAIGLGASILPLCD 419
Cdd:PRK06213   98 CTGHAIAKGAFLLLSAD 114
PRK06142 PRK06142
crotonase/enoyl-CoA hydratase family protein;
299-453 3.44e-04

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235714  Cd Length: 272  Bit Score: 42.27  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 299 YRDIVVRKQDGFTHILLsTKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFI----YFIRRLTDD 373
Cdd:PRK06142    5 YESFTVELADHVAQVTL-NRPGKGNAMNPAFWSELPEIFRWLDADPEvRAVVLSGSGKHFSYGIDLPamagVFGQLGKDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 374 RKKESTKMAEAIRNF---VNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPR 450
Cdd:PRK06142   84 LARPRTDLRREILRLqaaINAVADCRKPVIAAVQGWCIGGGVDLISACDMRYASADAKFSVREVDLGMVADVGSLQRLPR 163

                  ...
gi 1491390975 451 IMG 453
Cdd:PRK06142  164 IIG 166
PRK03580 PRK03580
crotonobetainyl-CoA hydratase;
397-452 3.97e-04

crotonobetainyl-CoA hydratase;


Pssm-ID: 179599 [Multi-domain]  Cd Length: 261  Bit Score: 41.99  E-value: 3.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1491390975 397 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIM 452
Cdd:PRK03580   95 KPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRL 150
CD3_cpSRP43_like cd18628
chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
11-56 5.55e-04

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: 5.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1491390975  11 RIVDKRKnkkgKTEYLVRWkgYDSEDDTWEPEQHLVNceEYIHEFN 56
Cdd:cd18628    13 RVGDDGK----TIEYLVKW--TDMSDATWEPQDNVDS--TLVLLYQ 50
CD_eEF3 cd18626
chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic ...
9-46 8.64e-04

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: 37.20  E-value: 8.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1491390975   9 VERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLV 46
Cdd:cd18626     4 IEKIVGRRKLKKSY-EYEVKWKGMSSKDNSWIPREELE 40
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-57 9.37e-04

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: 37.23  E-value: 9.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1491390975   7 YEVERIVDKR----KNKKGKTE---YLVRWKGYDseDDTWEPEQHLVNcEEYIHEFNR 57
Cdd:cd18967     1 WEIEAILAHHmsdpRTHPGKPAtmlYLTKWEGFP--DETWEPAESFDD-RKILHDYRR 55
PRK07112 PRK07112
enoyl-CoA hydratase/isomerase;
299-440 1.16e-03

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235938  Cd Length: 255  Bit Score: 40.44  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 299 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMKEVQSALNTAAaDDSKLVLFSAVGSIFCCGLDFIYFIRRLTDDRKKES 378
Cdd:PRK07112    3 YQTIRVRQQGDVCFLQLH-RPEAQNTINDRLIAECMDVLDRCE-HAATIVVLEGLPEVFCFGADFSAIAEKPDAGRADLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491390975 379 TkmAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP 440
Cdd:PRK07112   81 D--AEPLYDLWHRLATGPYVTIAHVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIP 140
PRK05674 PRK05674
gamma-carboxygeranoyl-CoA hydratase; Validated
309-429 1.30e-03

gamma-carboxygeranoyl-CoA hydratase; Validated


Pssm-ID: 168168  Cd Length: 265  Bit Score: 40.56  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 309 GFTHILLStKSSENNSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDFIY--------FIRRLTDDRKkest 379
Cdd:PRK05674   15 GFATLWLS-RADKNNAFNAQMIRELILALDQVQSDASlRFLLLRGRGRHFSAGADLAWmqqsadldYNTNLDDARE---- 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1491390975 380 kMAEAIRNFVntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWF 429
Cdd:PRK05674   90 -LAELMYNLY----RLKIPTLAVVQGAAFGGALGLISCCDMAIGADDAQF 134
PRK08138 PRK08138
enoyl-CoA hydratase; Provisional
323-440 1.31e-03

enoyl-CoA hydratase; Provisional


Pssm-ID: 236162 [Multi-domain]  Cd Length: 261  Bit Score: 40.42  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCGLDfiyfIRRL-----TDDRKKESTKMAEAIRnfvntfiQFK 396
Cdd:PRK08138   30 NALNMEVRQQLAEHFTELSEDPDiRAIVLTGGEKVFAAGAD----IKEFatagaIEMYLRHTERYWEAIA-------QCP 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1491390975 397 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP 440
Cdd:PRK08138   99 KPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGLMP 142
PRK07110 PRK07110
polyketide biosynthesis enoyl-CoA hydratase; Validated
323-455 1.59e-03

polyketide biosynthesis enoyl-CoA hydratase; Validated


Pssm-ID: 235936  Cd Length: 249  Bit Score: 39.95  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSIFCCG------LDFIYFIRRLTDDrkkestkmaeairNFVNTFIQF 395
Cdd:PRK07110   27 NAFSDELCDQLHEAFDTIAQDPRyKVVILTGYPNYFATGgtqeglLSLQTGKGTFTEA-------------NLYSLALNC 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 396 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSSLTFPRIMGLA 455
Cdd:PRK07110   94 PIPVIAAMQGHAIGGGLVLGLYADIVVLSRESVYTANFMKYGFTPGMGATAILPEKLGLA 153
chromodomain cd18963
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
4-45 1.92e-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: 36.51  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1491390975   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEddtwEPEQHL 45
Cdd:cd18963     1 ERVFAAECII-KRRVRKGRIEYLVKWKGWASK----EREREL 37
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
302-454 2.63e-03

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: 40.21  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 302 IVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALNTAAADDS--KLVLFSAVGSIFCCGLDfIYFIRrlTDDRKKEST 379
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD-IQMIA--ACKTAQEVT 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491390975 380 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWA--NEKAWFQTPYTTFGQSPDGCSSLTFPRIMGL 454
Cdd:TIGR02441  92 QLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGV 168
PRK05617 PRK05617
3-hydroxyisobutyryl-CoA hydrolase; Provisional
323-441 3.55e-03

3-hydroxyisobutyryl-CoA hydrolase; Provisional


Pssm-ID: 235533 [Multi-domain]  Cd Length: 342  Bit Score: 39.42  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGSI-FCCGLDfiyfIRRLTDDRKKEStkmAEAIRNF------VNTFI- 393
Cdd:PRK05617   25 NALSLEMIRAIDAALDAWEDDDAvAAVVIEGAGERgFCAGGD----IRALYEAARAGD---PLAADRFfreeyrLNALIa 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1491390975 394 QFKKPIIVAVNGPAIG------LGASIlplcDVVwaNEKAWFQTPYTTFGQSPD 441
Cdd:PRK05617   98 RYPKPYIALMDGIVMGggvgisAHGSH----RIV--TERTKMAMPETGIGFFPD 145
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
9-41 4.44e-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: 4.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1491390975   9 VERIVDKRKNK----------KGKTEYLVRWKGYDSEDDTWEP 41
Cdd:cd18665     5 IDIVLDHRLKEgleegelddpKENYEFLIKWTDESHLHNTWET 47
ECH_2 pfam16113
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
323-444 8.02e-03

Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase. This family differs from pfam00378 in the structure of it's C-terminus.


Pssm-ID: 465024 [Multi-domain]  Cd Length: 331  Bit Score: 38.22  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491390975 323 NSLNPEVMKEVQSALNTAAADDS-KLVLFSAVGS-IFCCGLDfiyfIRRLTDDRKKESTkmaEAIRNF------VNTFI- 393
Cdd:pfam16113  13 NALNLEMVRALLAALKAWEDDPAvKLVVLKGAGErAFCAGGD----VRALYEAAKAGGG---EAGRDFfreeyrLNYLIa 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491390975 394 QFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPD-GCS 444
Cdd:pfam16113  86 TYPKPYVALMDGIVMGGGVGLSVHGSFRVVTERTRFAMPETAIGLFPDvGGS 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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