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Conserved domains on  [gi|221307494|ref|NP_004815|]
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chromodomain Y-like protein isoform a [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
290-486 2.32e-48

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: 166.20  E-value: 2.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLSTKSSeNNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRltDDRKRESTK 368
Cdd:cd06558    1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEM 448
Cdd:cd06558   78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 221307494 449 LLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKEL 486
Cdd:cd06558  158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 1.73e-32

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


:

Pssm-ID: 349284  Cd Length: 52  Bit Score: 118.32  E-value: 1.73e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNR 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 ...
290-486 2.32e-48

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: 166.20  E-value: 2.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLSTKSSeNNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRltDDRKRESTK 368
Cdd:cd06558    1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEM 448
Cdd:cd06558   78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 221307494 449 LLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKEL 486
Cdd:cd06558  158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
290-534 7.65e-47

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: 163.80  E-value: 7.65e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLSTKSSeNNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRLTDDRKREstk 368
Cdd:COG1024    1 VLVEREGGVATITLNRPEK-LNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPEEARA--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEM 448
Cdd:COG1024   77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 449 LLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQ 528
Cdd:COG1024  157 LLTGRRIDAEEALELGLVNRVVPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFASED 236

                 ....*....
gi 221307494 529 ---GMDSML 534
Cdd:COG1024  237 areGIAAFL 245
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
288-519 3.18e-38

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 141.16  E-value: 3.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 288 RDIVVRKQDGFTHILLsTKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRES 366
Cdd:PRK06688   5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD----IKDFPKAPPKPP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 367 TKMAEAIRnFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASAN 446
Cdd:PRK06688  80 DELAPVNR-FLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221307494 447 EMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEV 519
Cdd:PRK06688 159 EMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREAAG 231
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 1.73e-32

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


Pssm-ID: 349284  Cd Length: 52  Bit Score: 118.32  E-value: 1.73e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNR 57
Cdd:cd18634    1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
310-539 2.09e-23

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: 99.36  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  310 NNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFiyfiRRLTDDRKRESTKMAEAIRNFVNTFIQFKKPII 388
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADL----KEMYGEGPAHQALYRENVLDLWTLLYTCPKPVI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  389 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQ 468
Cdd:pfam00378  93 AAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEALKWGLVDK 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221307494  469 VFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQGMDSMLKYLQR 539
Cdd:pfam00378 173 VVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQAFLEK 243
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
7-58 1.43e-22

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 90.71  E-value: 1.43e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221307494    7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRR 58
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
7-59 9.43e-21

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 85.73  E-value: 9.43e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 221307494     7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRRH 59
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKE 54
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
290-472 9.17e-10

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: 61.39  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  290 IVVRKQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAADDS--KLVLLSAVGSVFCCGLDfIYFIRrlTDDRKREST 367
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD-IQMIA--ACKTAQEVT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  368 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWA--NEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASA 445
Cdd:TIGR02441  92 QLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGVPAA 171
                         170       180
                  ....*....|....*....|....*..
gi 221307494  446 NEMLLSGRKLTAQEACGKGLVSQVFWP 472
Cdd:TIGR02441 172 LDMMLTGKKIRADRAKKMGIVDQLVDP 198
 
Name Accession Description Interval E-value
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
290-486 2.32e-48

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: 166.20  E-value: 2.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLSTKSSeNNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRltDDRKRESTK 368
Cdd:cd06558    1 VLVERDGGVATITLNRPEK-RNALSLEMLDELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAL--SDAGEEARA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEM 448
Cdd:cd06558   78 FIRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARAREL 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 221307494 449 LLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKEL 486
Cdd:cd06558  158 LLTGRRISAEEALELGLVDEVVPDEELLAAALELARRL 195
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
290-534 7.65e-47

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: 163.80  E-value: 7.65e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLSTKSSeNNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRLTDDRKREstk 368
Cdd:COG1024    1 VLVEREGGVATITLNRPEK-LNALSLEMLAELAAALDEAEADPDvRVVVLTGAGKAFCAGADLKELAAAADPEEARA--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 MAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEM 448
Cdd:COG1024   77 FARGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 449 LLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQ 528
Cdd:COG1024  157 LLTGRRIDAEEALELGLVNRVVPDDELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELFASED 236

                 ....*....
gi 221307494 529 ---GMDSML 534
Cdd:COG1024  237 areGIAAFL 245
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
288-519 3.18e-38

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 141.16  E-value: 3.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 288 RDIVVRKQDGFTHILLsTKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRES 366
Cdd:PRK06688   5 TDLLVELEDGVLTITI-NRPDKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRAFSAGGD----IKDFPKAPPKPP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 367 TKMAEAIRnFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASAN 446
Cdd:PRK06688  80 DELAPVNR-FLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221307494 447 EMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEV 519
Cdd:PRK06688 159 EMLLLGEPLSAEEALRIGLVNRVVPAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEALAREAAG 231
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
6-57 1.73e-32

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


Pssm-ID: 349284  Cd Length: 52  Bit Score: 118.32  E-value: 1.73e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNR 57
Cdd:cd18634    1 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
ECH_1 pfam00378
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
310-539 2.09e-23

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: 99.36  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  310 NNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFiyfiRRLTDDRKRESTKMAEAIRNFVNTFIQFKKPII 388
Cdd:pfam00378  17 VNALSAELITELIQALEKLRTDPSvRAVVLTGGDKAFCAGADL----KEMYGEGPAHQALYRENVLDLWTLLYTCPKPVI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  389 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQ 468
Cdd:pfam00378  93 AAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEALKWGLVDK 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221307494  469 VFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQGMDSMLKYLQR 539
Cdd:pfam00378 173 VVPEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQAFLEK 243
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
7-57 2.09e-23

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 92.93  E-value: 2.09e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNR 57
Cdd:cd00024    1 YEVEKILDHRV-RKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
7-58 1.43e-22

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 90.71  E-value: 1.43e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221307494    7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRR 58
Cdd:pfam00385   1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
PRK07854 PRK07854
enoyl-CoA hydratase; Provisional
311-526 2.83e-22

enoyl-CoA hydratase; Provisional


Pssm-ID: 236115 [Multi-domain]  Cd Length: 243  Bit Score: 95.86  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDSKLVLLSAVGSVFCCGLDF---IY---FIRRLTDdrkrestkMAEAIrnfVNTFIqfk 384
Cdd:PRK07854  22 NALNAELCEELREAVRKAVDESARAIVLTGQGTVFCAGADLsgdVYaddFPDALIE--------MLHAI---DAAPV--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 385 kPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKG 464
Cdd:PRK07854  88 -PVIAAINGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDNWTIRRLSSLVGGGRARAMLLGAEKLTAEQALATG 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221307494 465 LVSQVfwpGTFT--QEVMVRIKELAscnPVVLEESKALVrcNMKMELEQANERECEVLKKIWGS 526
Cdd:PRK07854 167 MANRI---GTLAdaQAWAAEIAGLA---PLALQHAKRVL--NDDGAIEEAWPAHKELFDKAWAS 222
PRK05981 PRK05981
enoyl-CoA hydratase/isomerase;
311-544 2.90e-22

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235661  Cd Length: 266  Bit Score: 96.34  E-value: 2.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDSKL--VLLSAVGSVFCCGLDFIyfiRRLTDDRKRESTKMA-EAIRNFVNTFI----QF 383
Cdd:PRK05981  26 NAVSIDMLGGLAEALDAIEDGKAEVrcLVLTGAGRGFCTGANLQ---GRGSGGRESDSGGDAgAALETAYHPFLrrlrNL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 384 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGK 463
Cdd:PRK05981 103 PCPIVTAVNGPAAGVGMSFALMGDLILCARSAYFLQAFRRIGLVPDGGSTWLLPRLVGKARAMELSLLGEKLPAETALQW 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 464 GLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEvLKKIWGSAQGM-DSMLKYLQRKID 542
Cdd:PRK05981 183 GLVNRVVDDAELMAEAMKLAHELANGPTVALGLIRKLYWDSPENDFEEQLNLERE-AQRIAGKTEDFkEGVGAFLQKRPA 261

                 ..
gi 221307494 543 EF 544
Cdd:PRK05981 262 QF 263
PRK07511 PRK07511
enoyl-CoA hydratase; Provisional
311-502 1.16e-21

enoyl-CoA hydratase; Provisional


Pssm-ID: 181009 [Multi-domain]  Cd Length: 260  Bit Score: 94.68  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRESTKMAEAI---RNFVNTFIQFKKP 386
Cdd:PRK07511  25 NALHPDMYAAGIEALNTAERDPSiRAVVLTGAGGFFCAGGN----LNRLLENRAKPPSVQAASIdglHDWIRAIRAFPKP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 387 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLV 466
Cdd:PRK07511 101 VIAAVEGAAAGAGFSLALACDLLVAARDAKFVMAYVKVGLTPDGGGSWFLARALPRQLATELLLEGKPISAERLHALGVV 180
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221307494 467 SQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVR 502
Cdd:PRK07511 181 NRLAEPGQALAEALALADQLAAGSPNALARIKSLIA 216
PRK05809 PRK05809
short-chain-enoyl-CoA hydratase;
287-544 7.13e-21

short-chain-enoyl-CoA hydratase;


Pssm-ID: 180270 [Multi-domain]  Cd Length: 260  Bit Score: 92.12  E-value: 7.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 287 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGS-VFCCGLDfiyfIRRLTDDRKR 364
Cdd:PRK05809   3 LKNVILEKEGHIAVVTIN-RPKALNALNSETLKELDTVLDDIENDDNvYAVILTGAGEkAFVAGAD----ISEMKDLNEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 365 ESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGAS 444
Cdd:PRK05809  78 EGRKFGLLGNKVFRKLENLDKPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGITPGFGGTQRLARIVGPGK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 445 ANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIW 524
Cdd:PRK05809 158 AKELIYTGDMINAEEALRIGLVNKVVEPEKLMEEAKALANKIAANAPIAVKLCKDAINRGMQVDIDTAVAIEAEDFGECF 237
                        250       260
                 ....*....|....*....|
gi 221307494 525 GSAQGMDSMLKYLQRKIDEF 544
Cdd:PRK05809 238 STEDQTEGMTAFVEKREKNF 257
PRK08260 PRK08260
enoyl-CoA hydratase; Provisional
287-472 9.30e-21

enoyl-CoA hydratase; Provisional


Pssm-ID: 236206 [Multi-domain]  Cd Length: 296  Bit Score: 92.76  E-value: 9.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 287 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLD-------FIYFIRRL 358
Cdd:PRK08260   3 YETIRYDVADGIATITLN-RPDKLNAFTVTMARELIEAFDAADADDAvRAVIVTGAGRAFCAGADlsaggntFDLDAPRT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 359 TDDR--KRESTKMAEAIRN----FVNTFIQFKKPIIVAVNGPAIGLGASI-LPLcDVVWANEKAWFQTPYTTFGQSPDGC 431
Cdd:PRK08260  82 PVEAdeEDRADPSDDGVRDgggrVTLRIFDSLKPVIAAVNGPAVGVGATMtLAM-DIRLASTAARFGFVFGRRGIVPEAA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 221307494 432 STVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQVFWP 472
Cdd:PRK08260 161 SSWFLPRLVGLQTALEWVYSGRVFDAQEALDGGLVRSVHPP 201
CHROMO smart00298
Chromatin organization modifier domain;
7-59 9.43e-21

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 85.73  E-value: 9.43e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 221307494     7 YEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRRH 59
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKE 54
PRK06210 PRK06210
enoyl-CoA hydratase; Provisional
311-491 5.31e-20

enoyl-CoA hydratase; Provisional


Pssm-ID: 180472  Cd Length: 272  Bit Score: 90.15  E-value: 5.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDF-------IYFIRRLTDDRKRESTKMAEAIRNFvNTFIQ 382
Cdd:PRK06210  28 NAWTPVMEAEVYAAMDRAEADPAvRVIVLTGAGRGFCAGADMgelqtidPSDGRRDTDVRPFVGNRRPDYQTRY-HFLTA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 383 FKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACG 462
Cdd:PRK06210 107 LRKPVIAAINGACAGIGLTHALMCDVRFAADGAKFTTAFARRGLIAEHGISWILPRLVGHANALDLLLSARTFYAEEALR 186
                        170       180       190
                 ....*....|....*....|....*....|
gi 221307494 463 KGLVSQVFWPGTFTQEVMVRIKELA-SCNP 491
Cdd:PRK06210 187 LGLVNRVVPPDELMERTLAYAEDLArNVSP 216
PLN02664 PLN02664
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
285-511 5.96e-20

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


Pssm-ID: 178269 [Multi-domain]  Cd Length: 275  Bit Score: 89.96  E-value: 5.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 285 YRYRDIVVRKQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAAD-DSKLVLLSAVGSVFCCGLDFIYF----IRRLT 359
Cdd:PLN02664   4 YKTLEIIQKSPNSSVFHLNLNRPSQRNALSLDFFTEFPKALSSLDQNpNVSVIILSGAGDHFCSGIDLKTLnsisEQSSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 360 DDRKRESTKMAEAIRNF---VNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMF 436
Cdd:PLN02664  84 GDRGRSGERLRRKIKFLqdaITAIEQCRKPVIAAIHGACIGGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTLQRL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221307494 437 PKIMGGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKE-LASCNPVVLEESKALVRCNMKMELEQ 511
Cdd:PLN02664 164 PSIVGYGNAMELALTGRRFSGSEAKELGLVSRVFGSKEDLDEGVRLIAEgIAAKSPLAVTGTKAVLLRSRELSVEQ 239
PRK06023 PRK06023
crotonase/enoyl-CoA hydratase family protein;
311-502 1.55e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 168351  Cd Length: 251  Bit Score: 88.31  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRLTDDrkresTKMAEAIRNFVNTFIQFKKPIIV 389
Cdd:PRK06023  28 NAITRAMYATMAKALKAADADDAiRAHVFLGTEGCFSAGNDMQDFLAAAMGG-----TSFGSEILDFLIALAEAEKPIVS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 390 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQV 469
Cdd:PRK06023 103 GVDGLAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALVPEAGSSLLAPRLMGHQRAFALLALGEGFSAEAAQEAGLIWKI 182
                        170       180       190
                 ....*....|....*....|....*....|...
gi 221307494 470 FWPGTFTQEVMVRIKELASCNPVVLEESKALVR 502
Cdd:PRK06023 183 VDEEAVEAETLKAAEELAAKPPQALQIARDLMR 215
PRK09674 PRK09674
enoyl-CoA hydratase-isomerase; Provisional
289-544 1.65e-19

enoyl-CoA hydratase-isomerase; Provisional


Pssm-ID: 182026 [Multi-domain]  Cd Length: 255  Bit Score: 88.28  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 289 DIVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRR-----LTDDR 362
Cdd:PRK09674   3 ELLVSRQQRVLLLTLN-RPEARNALNNALLTQLVNELEAAATDTSiGVCVITGNARFFAAGADLNEMAEKdlaatLNDPR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 363 KRESTKMAeairnfvntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGG 442
Cdd:PRK09674  82 PQLWQRLQ-----------AFNKPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGGTQRLIRSVGK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 443 ASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQ--ANERECEVL 520
Cdd:PRK09674 151 SLASQMVLTGESITAQQAQQAGLVSEVFPPELTLERALQLASKIARHSPLALRAAKQALRQSQEVDLQAglAQERQLFTL 230
                        250       260
                 ....*....|....*....|....
gi 221307494 521 kkIWGSAQGMDSMLKYLQRKIDEF 544
Cdd:PRK09674 231 --LAATEDRHEGISAFLEKRTPDF 252
PRK07468 PRK07468
crotonase/enoyl-CoA hydratase family protein;
311-502 1.98e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180987 [Multi-domain]  Cd Length: 262  Bit Score: 88.19  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRLTDD---RKRESTKMAEAIRNfVNTFiqfKKP 386
Cdd:PRK07468  27 NALSARMIAELTTAARRLAADAAvRVVVLTGAGKSFCAGGDLGWMRAQMTADratRIEEARRLAMMLKA-LNDL---PKP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 387 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKiMGGASANEMLLSGRKLTAQEACGKGLV 466
Cdd:PRK07468 103 LIGRIQGQAFGGGVGLISVCDVAIAVSGARFGLTETRLGLIPATISPYVVAR-MGEANARRVFMSARLFDAEEAVRLGLL 181
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221307494 467 SQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVR 502
Cdd:PRK07468 182 SRVVPAERLDAAVEAEVTPYLSCAPGAVAAAKALVR 217
PRK09245 PRK09245
crotonase/enoyl-CoA hydratase family protein;
289-510 4.47e-19

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181723  Cd Length: 266  Bit Score: 87.33  E-value: 4.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 289 DIVVRKQDGFTHILLSTKSSENNSLN-PEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRES 366
Cdd:PRK09245   3 DFLLVERDGHIVTLTMNRPETRNALSdNDAVDALVAACAAINADRSvRAVILTGAGTAFSSGGN----VKDMRARVGAFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 367 TKMAEA-------IRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSP-DGCSTVMfPK 438
Cdd:PRK09245  79 GSPADIrqgyrhgIQRIPLALYNLEVPVIAAVNGPAIGAGCDLACMCDIRIASETARFAESFVKLGLIPgDGGAWLL-PR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221307494 439 IMGGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELE 510
Cdd:PRK09245 158 IIGMARAAEMAFTGDAIDAATALEWGLVSRVVPADQLLPAARALAERIAANPPHALRLTKRLLREGQHASLD 229
PRK08140 PRK08140
enoyl-CoA hydratase; Provisional
311-469 2.05e-18

enoyl-CoA hydratase; Provisional


Pssm-ID: 236163  Cd Length: 262  Bit Score: 84.97  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDSKLVLLSAVGSVFCCGLDfiyfirrLTDdrkRESTKMAEA------IRNFVNTFIQ-- 382
Cdd:PRK08140  26 NSFTREMHRELREALDQVEDDGARALLLTGAGRGFCAGQD-------LAD---RDVTPGGAMpdlgesIETFYNPLVRrl 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 383 --FKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEA 460
Cdd:PRK08140  96 raLPLPVIAAVNGVAAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLPRLVGMARALGLALLGEKLSAEQA 175

                 ....*....
gi 221307494 461 CGKGLVSQV 469
Cdd:PRK08140 176 EQWGLIWRV 184
PRK07799 PRK07799
crotonase/enoyl-CoA hydratase family protein;
294-519 4.59e-18

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181122 [Multi-domain]  Cd Length: 263  Bit Score: 84.00  E-value: 4.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 294 KQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKMAEA 372
Cdd:PRK07799  10 EQRGHTLIVTMNRPEARNALSTEMLRIMVDAWDRVDNDPDiRSCILTGAGGAFCAGMDLKAATKKPPGDSFKDGSYDPSR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 373 IRNFVNTFiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSG 452
Cdd:PRK07799  90 IDALLKGR-RLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLFPMGGSAVRLVRQIPYTVACDLLLTG 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307494 453 RKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEV 519
Cdd:PRK07799 169 RHITAAEAKEIGLIGHVVPDGQALDKALELAELINANGPLAVQAILRTIRETEGMHENEAFKIDTKI 235
PRK08139 PRK08139
enoyl-CoA hydratase; Validated
311-520 1.27e-17

enoyl-CoA hydratase; Validated


Pssm-ID: 181249  Cd Length: 266  Bit Score: 83.07  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRES--------TKMAEAIRnfvntfi 381
Cdd:PRK08139  33 NALSEAMLAALQAALDAIAADPSvRVVVLAAAGKAFCAGHD----LKEMRAARGLAYfralfarcSRVMQAIV------- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 382 QFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSpdgCSTVMFP--KIMGGASANEMLLSGRKLTAQE 459
Cdd:PRK08139 102 ALPQPVIARVHGIATAAGCQLVASCDLAVAADTARFAVPGVNIGLF---CSTPMVAlsRNVPRKQAMEMLLTGEFIDAAT 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221307494 460 ACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVL 520
Cdd:PRK08139 179 AREWGLVNRVVPADALDAAVARLAAVIAAKSPAAVRIGKEAFYRQAEMPLADAYAYAGDVM 239
PRK05870 PRK05870
enoyl-CoA hydratase; Provisional
311-540 1.60e-17

enoyl-CoA hydratase; Provisional


Pssm-ID: 180298  Cd Length: 249  Bit Score: 82.08  E-value: 1.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAAD-DSKLVLLSAVGSVFCCGLDfiyfirrLTDDRKRESTKMAEAIRNFVNTFI---QFKKP 386
Cdd:PRK05870  25 NAVTAEMSAQLRAAVAAAEADpDVHALVVTGAGKAFCAGAD-------LTALGAAPGRPAEDGLRRIYDGFLavaSCPLP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 387 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLV 466
Cdd:PRK05870  98 TIAAVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLGLHPGGGATWMLQRAVGPQVARAALLFGMRFDAEAAVRHGLA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 467 SQVfwpgtfTQEVMVRIKEL----ASCNPVVLEESKALVRCNMKME-LEQANEREcevlkkIWGSAQGMDS-----MLKY 536
Cdd:PRK05870 178 LMV------ADDPVAAALELaagpAAAPRELVLATKASMRATASLAqHAAAVEFE------LGPQAASVQSpefaaRLAA 245

                 ....
gi 221307494 537 LQRK 540
Cdd:PRK05870 246 AQRR 249
PRK07659 PRK07659
enoyl-CoA hydratase; Provisional
290-486 2.04e-17

enoyl-CoA hydratase; Provisional


Pssm-ID: 236073 [Multi-domain]  Cd Length: 260  Bit Score: 82.00  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAADDSKLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRESTKM 369
Cdd:PRK07659   8 VVVKYEGRVATIMLN-RPEALNALDEPMLKELLQALKEVAESSAHIVVLRGNGRGFSAGGD----IKMMLSSNDESKFDG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 370 A-EAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEM 448
Cdd:PRK07659  83 VmNTISEIVVTLYTMPKLTISAIHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGLIPDGGGHFFLQKRVGENKAKQI 162
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 221307494 449 LLSGRKLTAQEACGKGLVSQVFwPGTFTQEVMVRIKEL 486
Cdd:PRK07659 163 IWEGKKLSATEALDLGLIDEVI-GGDFQTAAKQKISEW 199
PLN02600 PLN02600
enoyl-CoA hydratase
311-517 3.63e-17

enoyl-CoA hydratase


Pssm-ID: 178210 [Multi-domain]  Cd Length: 251  Bit Score: 81.39  E-value: 3.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDSKLVLL--SAVGSVFCCGLDfiyfirrLTDDRKRESTKMAEAIRNFVNTFIQFKK--- 385
Cdd:PLN02600  17 NAIGKEMLRGLRSAFEKIQADASARVVMlrSSVPGVFCAGAD-------LKERRKMSPSEVQKFVNSLRSTFSSLEAlsi 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 386 PIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGL 465
Cdd:PLN02600  90 PTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVGRSRAKELIFTGRRIGAREAASMGL 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494 466 VSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQAN--EREC 517
Cdd:PLN02600 170 VNYCVPAGEAYEKALELAQEINQKGPLAIKMAKKAINEGSEVDMASGLeiEEEC 223
PRK06495 PRK06495
enoyl-CoA hydratase/isomerase family protein;
311-499 4.18e-17

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 168580 [Multi-domain]  Cd Length: 257  Bit Score: 81.28  E-value: 4.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSAL-STAAADDSKLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRESTKMAEA--IRNFVNTFIQFKKPI 387
Cdd:PRK06495  25 NALSRELRDELIAVFdEISERPDVRVVVLTGAGKVFCAGAD----LKGRPDVIKGPGDLRAHNrrTRECFHAIRECAKPV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 388 IVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSpDGCSTVMfpKIMGGASANEMLLSGRKLTAQEACGKGLVS 467
Cdd:PRK06495 101 IAAVNGPALGAGLGLVASCDIIVASENAVFGLPEIDVGLA-GGGKHAM--RLFGHSLTRRMMLTGYRVPAAELYRRGVIE 177
                        170       180       190
                 ....*....|....*....|....*....|..
gi 221307494 468 QVFWPGTFTQEVMVRIKELASCNPVVLEESKA 499
Cdd:PRK06495 178 ACLPPEELMPEAMEIAREIASKSPLATRLAKD 209
PRK07827 PRK07827
enoyl-CoA hydratase family protein;
296-540 5.11e-17

enoyl-CoA hydratase family protein;


Pssm-ID: 236109 [Multi-domain]  Cd Length: 260  Bit Score: 80.88  E-value: 5.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 296 DGFTHILLStkSSEN-NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDF------IYFIRRLTDDRKREst 367
Cdd:PRK07827  14 GGVATLTLD--SPHNrNALSARLVAQLHDGLRAAAADPAvRAVVLTHTGGTFCAGADLseagggGGDPYDAAVARARE-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 368 kMAEAIRNFVntfiQFKKPIIVAVNG--PAIGLGasILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKiMGGASA 445
Cdd:PRK07827  90 -MTALLRAIV----ELPKPVIAAIDGhvRAGGFG--LVGACDIVVAGPESTFALTEARIGVAPAIISLTLLPR-LSPRAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 446 NEMLLSGRKLTAQEACGKGLVSQVFwpGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWG 525
Cdd:PRK07827 162 ARYYLTGEKFGAAEAARIGLVTAAA--DDVDAAVAALLADLRRGSPQGLAESKALTTAAVLAGFDRDAEELTEESARLFV 239
                        250
                 ....*....|....*
gi 221307494 526 SAQGMDSMLKYLQRK 540
Cdd:PRK07827 240 SDEAREGMTAFLQKR 254
PRK03580 PRK03580
crotonobetainyl-CoA hydratase;
385-512 6.46e-17

crotonobetainyl-CoA hydratase;


Pssm-ID: 179599 [Multi-domain]  Cd Length: 261  Bit Score: 80.89  E-value: 6.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 385 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKG 464
Cdd:PRK03580  95 KPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRLPPAIANEMVMTGRRMDAEEALRWG 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494 465 LVSQVFwPGtftQEVMVRIKELA----SCNPVVLEESKALVRCNMKMELEQA 512
Cdd:PRK03580 175 IVNRVV-PQ---AELMDRARELAqqlvNSAPLAIAALKEIYRETSEMPVEEA 222
PRK07658 PRK07658
enoyl-CoA hydratase; Provisional
311-529 1.09e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 181070 [Multi-domain]  Cd Length: 257  Bit Score: 80.06  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTD-DRKRESTKMAEAIRNFVNTFIQFKKPII 388
Cdd:PRK07658  23 NALSSQVLHELSELLDQVEKDDNvRVVVIHGEGRFFSAGAD----IKEFTSvTEAEQATELAQLGQVTFERVEKFSKPVI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 389 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQ 468
Cdd:PRK07658  99 AAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGFAGTQRLPRYVGKAKALEMMLTSEPITGAEALKWGLVNG 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221307494 469 VFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQG 529
Cdd:PRK07658 179 VFPEETLLDDAKKLAKKIAGKSPATTRAVLELLQTTKSSSYYEGVKREAKIFGEVFTSEDA 239
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
6-57 1.48e-16

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: 73.47  E-value: 1.48e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   6 LYEVERIVDKrKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNR 57
Cdd:cd18633    1 VFEVEKILDM-KTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
PRK06190 PRK06190
enoyl-CoA hydratase; Provisional
311-502 2.19e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 235733  Cd Length: 258  Bit Score: 79.25  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRESTKMAEaiRNFVNTFIQFKKPIIV 389
Cdd:PRK06190  26 NALSAALRRALFAALAEADADDDvDVVVLTGADPAFCAGLD----LKELGGDGSAYGAQDAL--PNPSPAWPAMRKPVIG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 390 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQV 469
Cdd:PRK06190 100 AINGAAVTGGLELALACDILIASERARFADTHARVGILPGWGLSVRLPQKVGIGRARRMSLTGDFLDAADALRAGLVTEV 179
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 221307494 470 fwpgTFTQEVMVRIKELA----SCNPVVLEESKALVR 502
Cdd:PRK06190 180 ----VPHDELLPRARRLAasiaGNNPAAVRALKASYD 212
PRK06494 PRK06494
enoyl-CoA hydratase; Provisional
311-512 4.60e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 180591 [Multi-domain]  Cd Length: 259  Bit Score: 78.16  E-value: 4.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDSKLV-LLSAVGS-VFCCGLDFIYFIRRltDDRKRESTKMAEAIRNFvntfiQFKKPII 388
Cdd:PRK06494  26 NALHLDAHFELEEVFDDFAADPEQWVaIVTGAGDkAFSAGNDLKEQAAG--GKRGWPESGFGGLTSRF-----DLDKPII 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 389 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQ 468
Cdd:PRK06494  99 AAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGLKRAMGMILTGRRVTAREGLELGFVNE 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 221307494 469 VFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQA 512
Cdd:PRK06494 179 VVPAGELLAAAERWADDILACSPLSIRASKQAVYRGLEVSLEEA 222
PRK05995 PRK05995
enoyl-CoA hydratase; Provisional
311-512 9.55e-16

enoyl-CoA hydratase; Provisional


Pssm-ID: 235664 [Multi-domain]  Cd Length: 262  Bit Score: 77.27  E-value: 9.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIR--RLTDDRKR-ESTKMAEAIRnfvnTFIQFKKP 386
Cdd:PRK05995  26 NAFNETVIAELTAAFRALDADDSvRAVVLAGAGKAFCAGADLNWMKKmaGYSDDENRaDARRLADMLR----AIYRCPKP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 387 IIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPdgcSTVMfPK---IMGGASANEMLLSGRKLTAQEACGK 463
Cdd:PRK05995 102 VIARVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLGLIP---ATIS-PYvirAMGERAARRYFLTAERFDAAEALRL 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494 464 GLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQA 512
Cdd:PRK05995 178 GLVHEVVPAEALDAKVDELLAALVANSPQAVRAGKRLVRDVAGRPIDAA 226
PRK08138 PRK08138
enoyl-CoA hydratase; Provisional
311-512 1.47e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 236162 [Multi-domain]  Cd Length: 261  Bit Score: 76.63  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRL-----TDDRKRESTKMAEAIRnfvntfiQFK 384
Cdd:PRK08138  30 NALNMEVRQQLAEHFTELSEDPDiRAIVLTGGEKVFAAGAD----IKEFatagaIEMYLRHTERYWEAIA-------QCP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 385 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKG 464
Cdd:PRK08138  99 KPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGLMPGAGGTQRLVRAVGKFKAMRMALTGCMVPAPEALAIG 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 221307494 465 LVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQA 512
Cdd:PRK08138 179 LVSEVVEDEQTLPRALELAREIARMPPLALAQIKEVVLAGADAPLDAA 226
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-55 1.48e-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: 70.84  E-value: 1.48e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494   7 YEVE-----RIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18968    2 YEVEvilaaRVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
PRK07657 PRK07657
enoyl-CoA hydratase; Provisional
311-510 1.64e-15

enoyl-CoA hydratase; Provisional


Pssm-ID: 181069 [Multi-domain]  Cd Length: 260  Bit Score: 76.70  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAAD-DSKLVLLSAVG-SVFCCGLDfIYFIRRLTDDRKRESTKMaeaIRNFVNTFIQFKKPII 388
Cdd:PRK07657  26 NALSLALLEELQNILTQINEEaNVRVVILTGAGeKAFCAGAD-LKERAGMNEEQVRHAVSL---IRTTMEMVEQLPQPVI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 389 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQ 468
Cdd:PRK07657 102 AAINGIALGGGLELALACDFRIAAESASLGLTETTLAIIPGAGGTQRLPRLIGVGRAKELIYTGRRISAQEAKEIGLVEF 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 221307494 469 VFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELE 510
Cdd:PRK07657 182 VVPAHLLEEKAIEIAEKIASNGPIAVRQAKEAISNGIQVDLH 223
PLN02888 PLN02888
enoyl-CoA hydratase
290-518 9.88e-15

enoyl-CoA hydratase


Pssm-ID: 215480  Cd Length: 265  Bit Score: 74.40  E-value: 9.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLSTKSSENnSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTk 368
Cdd:PLN02888  12 LVPKSRNGIATITINRPKALN-ALTRPMMVELAAAFKRLDEDDSvKVIILTGSGRAFCSGVDLTAAEEVFKGDVKDVET- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 maeairnfvNTFIQF---KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASA 445
Cdd:PLN02888  90 ---------DPVAQMercRKPIIGAINGFAITAGFEIALACDILVASRGAKFIDTHAKFGIFPSWGLSQKLSRIIGANRA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307494 446 NEMLLSGRKLTAQEACGKGLVSQVFWPGtftqEVMVRIKELA----SCNPVVLEESKALVRCNMKMELEQANERECE 518
Cdd:PLN02888 161 REVSLTAMPLTAETAERWGLVNHVVEES----ELLKKAREVAeaiiKNNQGMVLRYKSVINDGLKLDLGHALQLEKE 233
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
7-55 4.03e-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: 66.95  E-value: 4.03e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494   7 YEVERIVDKR----KNKKGKTEYL-VRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18635    2 FEVEKLVGICygdpKKTGERGLYFkVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
7-55 4.78e-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: 66.31  E-value: 4.78e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHDF 55
Cdd:cd18631    2 YVVEKVLDRRV-VKGKVEYLLKWKGYPDEDNTWEPEENL-DCPDLIAEF 48
PRK06072 PRK06072
enoyl-CoA hydratase; Provisional
290-466 7.22e-14

enoyl-CoA hydratase; Provisional


Pssm-ID: 168377 [Multi-domain]  Cd Length: 248  Bit Score: 71.35  E-value: 7.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAAD-DSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTK 368
Cdd:PRK06072   2 IKVESREGYAIVTMS-RPDKLNALNLEMRNEFISKLKQINADpKIRVVIVTGEGRAFCVGADLSEFAPDFAIDLRETFYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 MAEAIRNFvntfiqfKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKiMGGASANEM 448
Cdd:PRK06072  81 IIREIRFS-------DKIYISAINGVTAGACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYFLLK-LTGQRFYEI 152
                        170
                 ....*....|....*...
gi 221307494 449 LLSGRKLTAQEACGKGLV 466
Cdd:PRK06072 153 LVLGGEFTAEEAERWGLL 170
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
4-57 8.47e-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: 65.80  E-value: 8.47e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494   4 EELYEVERIVDKRKNKKGkTEYLVRWKGYDSEDDTWEPeQHLVNCEEYIHDFNR 57
Cdd:cd18978    1 DESYEVEKIINHRGEKNR-RKYLVKWKGYDDTDNSWVT-QEDFNDKDMIDEYEN 52
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
6-57 1.32e-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: 65.16  E-value: 1.32e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNR 57
Cdd:cd18636    1 VYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
PRK05980 PRK05980
crotonase/enoyl-CoA hydratase family protein;
289-469 2.71e-13

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180335 [Multi-domain]  Cd Length: 260  Bit Score: 70.17  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 289 DIVVRKQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGS-VFCCGLDFIYFIRRLTDDRKres 366
Cdd:PRK05980   3 DTVLIEIRDGIALLTLNRPEKLNALNYALIDRLLARLDAIEVDESvRAVILTGAGDrAFSAGADIHEFSASVAAGAD--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 367 tkmaEAIRNFV-------NTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKI 439
Cdd:PRK05980  80 ----VALRDFVrrgqamtARLEAFPKPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPTFGGTQRLPRL 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 221307494 440 MGGASANEMLLSGRKLTAQEACGKGLVSQV 469
Cdd:PRK05980 156 AGRKRALELLLTGDAFSAERALEIGLVNAV 185
PRK05862 PRK05862
enoyl-CoA hydratase; Provisional
311-494 2.81e-13

enoyl-CoA hydratase; Provisional


Pssm-ID: 180295 [Multi-domain]  Cd Length: 257  Bit Score: 70.07  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRESTKmAEAIRNFvNTFIQFKKPIIV 389
Cdd:PRK05862  26 NALNDALMDELGAALAAFDADEGiGAIVITGSEKAFAAGAD----IKEMADLSFMDVYK-GDYITNW-EKVARIRKPVIA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 390 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQV 469
Cdd:PRK05862 100 AVAGYALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGMGGSQRLTRAVGKAKAMDLCLTGRMMDAAEAERAGLVSRV 179
                        170       180
                 ....*....|....*....|....*.
gi 221307494 470 FWPGTFTQEVMVRIKELASCN-PVVL 494
Cdd:PRK05862 180 VPADKLLDEALAAATTIASFSlPAVM 205
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
7-57 5.09e-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: 63.43  E-value: 5.09e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   7 YEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHL-VNCEEYIHDFNR 57
Cdd:cd18638    2 FEVEKIV-KKKTVKGGTEYFVKWKGYSAKENTWETEDNLeKSYKEMIDEFEK 52
PRK05864 PRK05864
enoyl-CoA hydratase; Provisional
311-467 1.49e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 168278 [Multi-domain]  Cd Length: 276  Bit Score: 67.94  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDF-----IYFIRRLTddRKRESTKMAEAIRNFVNTFIQFK 384
Cdd:PRK05864  32 NSMAFDVMVPLKEALAEVSYDNSvRVVVLTGAGRGFSSGADHksagvVPHVEGLT--RPTYALRSMELLDDVILALRRLH 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 385 KPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFG--QSPDGCStVMFPKIMGGASANEMLLSGRKLTAQEACG 462
Cdd:PRK05864 110 QPVIAAVNGPAIGGGLCLALAADIRVASSSAYFRAAGINNGltASELGLS-YLLPRAIGSSRAFEIMLTGRDVDAEEAER 188

                 ....*
gi 221307494 463 KGLVS 467
Cdd:PRK05864 189 IGLVS 193
PRK07260 PRK07260
enoyl-CoA hydratase; Provisional
311-469 1.89e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 180910 [Multi-domain]  Cd Length: 255  Bit Score: 67.46  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKMAEAIRNFVNTFIQFKKPIIV 389
Cdd:PRK07260  24 NGFNIPMCQEILEALRLAEEDPSvRFLLINANGKVFSVGGDLVEMKRAVDEDDVQSLVKIAELVNEISFAIKQLPKPVIM 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 390 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQV 469
Cdd:PRK07260 104 CVDGAVAGAAANMAVAADFCIASTKTKFIQAFVGVGLAPDAGGLFLLTRAIGLNRATHLAMTGEALTAEKALEYGFVYRV 183
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
7-57 2.72e-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: 61.34  E-value: 2.72e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNR 57
Cdd:cd18974    1 WEVEEIVDEKM-IDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
PRK06142 PRK06142
crotonase/enoyl-CoA hydratase family protein;
287-502 3.64e-12

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235714  Cd Length: 272  Bit Score: 66.92  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 287 YRDIVVRKQDGFTHILLsTKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFI----YFIRRLTDD 361
Cdd:PRK06142   5 YESFTVELADHVAQVTL-NRPGKGNAMNPAFWSELPEIFRWLDADPEvRAVVLSGSGKHFSYGIDLPamagVFGQLGKDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 362 RKRESTKMAEAIRNF---VNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPK 438
Cdd:PRK06142  84 LARPRTDLRREILRLqaaINAVADCRKPVIAAVQGWCIGGGVDLISACDMRYASADAKFSVREVDLGMVADVGSLQRLPR 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221307494 439 IMGGASANEMLLSGRKLTAQEACGKGLVSQVFW-PGTFTQEVMVRIKELASCNPVVLEESKALVR 502
Cdd:PRK06142 164 IIGDGHLRELALTGRDIDAAEAEKIGLVNRVYDdADALLAAAHATAREIAAKSPLAVRGTKEVLD 228
PRK06143 PRK06143
enoyl-CoA hydratase; Provisional
311-540 3.77e-12

enoyl-CoA hydratase; Provisional


Pssm-ID: 180423  Cd Length: 256  Bit Score: 66.60  E-value: 3.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGS-VFCCGLDfIY------------FIRRLTDdrkrestkMAEAIRnf 376
Cdd:PRK06143  29 NILGTPVILALTQALRWLAADPDvRVLVLRGAGEkAFIGGAD-IKematldqasaeaFISRLRD--------LCDAVR-- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 377 vntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGqSPDGCSTVMFPKIMGGASANEMLLSGRKLT 456
Cdd:PRK06143  98 -----HFPVPVIARIPGWCLGGGLELAAACDLRIAAHDAQFGMPEVRVG-IPSVIHAALLPRLIGWARTRWLLLTGETID 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 457 AQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQGMDSMLKY 536
Cdd:PRK06143 172 AAQALAWGLVDRVVPLAELDAAVERLAASLAGCGPQALRQQKRLLREWEDMPLDVAIDDSVAEFGAAFLTGEPQRHMAAF 251

                 ....
gi 221307494 537 LQRK 540
Cdd:PRK06143 252 LNRK 255
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
7-55 4.21e-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: 61.05  E-value: 4.21e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221307494   7 YEVERIVDKRKNKKGKTE--YLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18980    4 YEVEAILDHKVDRRYRDPnfYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
7-55 4.22e-12

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


Pssm-ID: 349297  Cd Length: 50  Bit Score: 61.11  E-value: 4.22e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHDF 55
Cdd:cd18650    2 YVVEKVLDRRV-VKGKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEF 48
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
7-58 4.74e-12

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


Pssm-ID: 349282  Cd Length: 55  Bit Score: 60.98  E-value: 4.74e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221307494   7 YEVERIVD-KRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRR 58
Cdd:cd18632    2 YEVEKIVDeKTDRNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRK 54
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
7-55 4.95e-12

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


Pssm-ID: 349329  Cd Length: 50  Bit Score: 60.72  E-value: 4.95e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18973    1 YVVEAILDNKR-RKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKY 48
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
7-55 5.07e-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: 60.82  E-value: 5.07e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHDF 55
Cdd:cd18653    2 YAVEKICDRRV-RKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
PRK07327 PRK07327
enoyl-CoA hydratase/isomerase family protein;
286-467 6.42e-12

enoyl-CoA hydratase/isomerase family protein;


Pssm-ID: 235991  Cd Length: 268  Bit Score: 66.20  E-value: 6.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 286 RYRDIVVRKQDGftHILLSTKSSEN--NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFiYFIRRLTDDR 362
Cdd:PRK07327   9 DYPALRFDRPPP--GVLEIVLNGPGalNAADARMHRELADIWRDVDRDPDvRVVLIRGEGKAFSAGGDL-ALVEEMADDF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 363 KRESTKMAEAiRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGG 442
Cdd:PRK07327  86 EVRARVWREA-RDLVYNVINCDKPIVSAIHGPAVGAGLVAALLADISIAAKDARIIDGHTRLGVAAGDHAAIVWPLLCGM 164
                        170       180
                 ....*....|....*....|....*
gi 221307494 443 ASANEMLLSGRKLTAQEACGKGLVS 467
Cdd:PRK07327 165 AKAKYYLLLCEPVSGEEAERIGLVS 189
PRK08252 PRK08252
crotonase/enoyl-CoA hydratase family protein;
311-540 6.88e-12

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181325 [Multi-domain]  Cd Length: 254  Bit Score: 65.78  E-value: 6.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDSKLV-LLSAVGSVFCCGLDFIYFIRRltddrKRESTkmaeAIRNFVN-TFIQFKKPII 388
Cdd:PRK08252  25 NAVNAAVAQGLAAALDELDADPDLSVgILTGAGGTFCAGMDLKAFARG-----ERPSI----PGRGFGGlTERPPRKPLI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 389 VAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQ 468
Cdd:PRK08252  96 AAVEGYALAGGFELALACDLIVAARDAKFGLPEVKRGLVAAGGGLLRLPRRIPYHIAMELALTGDMLTAERAHELGLVNR 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221307494 469 VFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQGMDSMLKYLQRK 540
Cdd:PRK08252 176 LTEPGQALDAALELAERIAANGPLAVAASKRIVVESGDWSEDEMFARQRELIAPVFTSADAKEGATAFAEKR 247
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
4-58 8.72e-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: 60.17  E-value: 8.72e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 221307494   4 EELYEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHDFNRR 58
Cdd:cd18644    1 DLVYAAEKILKKRV-RKGKVEYLVKWKGWSNKHNTWEPEENILD-RRLIEIFERT 53
PRK08150 PRK08150
crotonase/enoyl-CoA hydratase family protein;
311-474 1.40e-11

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181254  Cd Length: 255  Bit Score: 64.65  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALsTAAADDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKMAEAIRNfvntfIQFKK-PIIV 389
Cdd:PRK08150  24 NALNDGLIAALRAAF-ARLPEGVRAVVLHGEGDHFCAGLDLSELRERDAGEGMHHSRRWHRVFDK-----IQYGRvPVIA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 390 AVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQV 469
Cdd:PRK08150  98 ALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGIFVGGGGSVRVPRLIGVARMTDMMLTGRVYDAQEGERLGLAQYL 177

                 ....*
gi 221307494 470 FWPGT 474
Cdd:PRK08150 178 VPAGE 182
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
7-49 1.82e-11

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


Pssm-ID: 349326  Cd Length: 49  Bit Score: 58.99  E-value: 1.82e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 221307494   7 YEVERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCE 49
Cdd:cd18970    1 FFVERILDERRRGRGW-QYLVRWLGYGPSDDSWLPRRELEECE 42
PRK06127 PRK06127
enoyl-CoA hydratase; Provisional
290-502 2.03e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 235705  Cd Length: 269  Bit Score: 64.73  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGS-VFCCGLDFIYFIRRLTDDRKreST 367
Cdd:PRK06127  13 LLAEKTGGLGRITFN-NPARHNAMSLDMWEALPQALAAAEDDDAiRVVVLTGAGEkAFVSGADISQFEESRSDAEA--VA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 368 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFG--QSPDG----CSTVmfpkimG 441
Cdd:PRK06127  90 AYEQAVEAAQAALADYAKPTIACIRGYCIGGGMGIALACDIRIAAEDSRFGIPAARLGlgYGYDGvknlVDLV------G 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221307494 442 GASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVR 502
Cdd:PRK06127 164 PSAAKDLFYTARRFDAAEALRIGLVHRVTAADDLETALADYAATIAGNAPLTLRAAKRAIA 224
PRK08290 PRK08290
enoyl-CoA hydratase; Provisional
310-470 2.69e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 236220 [Multi-domain]  Cd Length: 288  Bit Score: 64.60  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 310 NNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRESTK-------------------- 368
Cdd:PRK08290  25 RNAQNRQMLYELDAAFRRAEADDAvRVIVLAGAGKHFSAGHD----LGSGTPGRDRDPGPdqhptlwwdgatkpgveqry 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 ---------MAEAIRNFvntfiqfKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQspdgCSTVMF--P 437
Cdd:PRK08290 101 arewevylgMCRRWRDL-------PKPTIAQVQGACIAGGLMLAWVCDLIVASDDAFFSDPVVRMGI----PGVEYFahP 169
                        170       180       190
                 ....*....|....*....|....*....|...
gi 221307494 438 KIMGGASANEMLLSGRKLTAQEACGKGLVSQVF 470
Cdd:PRK08290 170 WELGPRKAKELLFTGDRLTADEAHRLGMVNRVV 202
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
6-57 3.35e-11

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


Pssm-ID: 349316  Cd Length: 51  Bit Score: 58.34  E-value: 3.35e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   6 LYEVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHDFNR 57
Cdd:cd18960    1 VFVVERILDKRLGRNGGEEFLIKWQGFPESDSSWEPRENL-QCDEMLEEFEK 51
PRK07110 PRK07110
polyketide biosynthesis enoyl-CoA hydratase; Validated
311-487 4.07e-11

polyketide biosynthesis enoyl-CoA hydratase; Validated


Pssm-ID: 235936  Cd Length: 249  Bit Score: 63.45  E-value: 4.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCG------LDFIYFIRRLTDDrkrestkmaeairNFVNTFIQF 383
Cdd:PRK07110  27 NAFSDELCDQLHEAFDTIAQDPRyKVVILTGYPNYFATGgtqeglLSLQTGKGTFTEA-------------NLYSLALNC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 384 KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGK 463
Cdd:PRK07110  94 PIPVIAAMQGHAIGGGLVLGLYADIVVLSRESVYTANFMKYGFTPGMGATAILPEKLGLALGQEMLLTARYYRGAELKKR 173
                        170       180
                 ....*....|....*....|....
gi 221307494 464 GlvsqVFWPGTFTQEVMVRIKELA 487
Cdd:PRK07110 174 G----VPFPVLPRAEVLEKALELA 193
PRK05674 PRK05674
gamma-carboxygeranoyl-CoA hydratase; Validated
297-540 4.19e-11

gamma-carboxygeranoyl-CoA hydratase; Validated


Pssm-ID: 168168  Cd Length: 265  Bit Score: 63.67  E-value: 4.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 297 GFTHILLStKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDFIY--------FIRRLTDDRkrest 367
Cdd:PRK05674  15 GFATLWLS-RADKNNAFNAQMIRELILALDQVQSDASlRFLLLRGRGRHFSAGADLAWmqqsadldYNTNLDDAR----- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 368 KMAEAIRNFVntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPdgcsTVMFP---KIMGGAS 444
Cdd:PRK05674  89 ELAELMYNLY----RLKIPTLAVVQGAAFGGALGLISCCDMAIGADDAQFCLSEVRIGLAP----AVISPfvvKAIGERA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 445 ANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECE-VLKKI 523
Cdd:PRK05674 161 ARRYALTAERFDGRRARELGLLAESYPAAELEAQVEAWIANLLLNSPQALRASKDLLREVGDGELSPALRRYCEnAIARI 240
                        250
                 ....*....|....*..
gi 221307494 524 WGSAQGMDSMLKYLQRK 540
Cdd:PRK05674 241 RVSAEGQEGLRAFLEKR 257
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-45 5.40e-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: 5.40e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKNKkGKTEYLVRWKGYDSEDDTWEPEQHL 45
Cdd:cd18966    1 YEVERILAERRDD-GGKRYLVKWEGYPLEEATWEPEENI 38
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
7-55 5.95e-11

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


Pssm-ID: 349298  Cd Length: 50  Bit Score: 57.69  E-value: 5.95e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHDF 55
Cdd:cd18651    2 YVVEKVLDRRV-VKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEF 48
PRK06144 PRK06144
enoyl-CoA hydratase; Provisional
289-534 6.43e-11

enoyl-CoA hydratase; Provisional


Pssm-ID: 180424 [Multi-domain]  Cd Length: 262  Bit Score: 63.09  E-value: 6.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 289 DIVVRKQDGFTHILLSTKSSENnSLNPEVMREVQSALSTAAADDS--KLVLLSAVGSVFCCGLDFIYFiRRLTDDRkrES 366
Cdd:PRK06144   9 ELLLEVRGGIARITFNRPAARN-AMTWAMYEGLAEICEAIAADPSirAVVLRGAGDKAFVAGTDIAQF-RAFSTAE--DA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 367 TKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYT-TFGQ--SPDGCSTVMfpKIMGGA 443
Cdd:PRK06144  85 VAYERRIDRVLGALEQLRVPTIAAIAGACVGGGAAIAAACDLRIATPSARFGFPIArTLGNclSMSNLARLV--ALLGAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 444 SANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRcnmkmELEQANERECE-VLKK 522
Cdd:PRK06144 163 RVKDMLFTARLLEAEEALAAGLVNEVVEDAALDARADALAELLAAHAPLTLRATKEALR-----RLRREGLPDGDdLIRM 237
                        250
                 ....*....|....*
gi 221307494 523 IWGSA---QGMDSML 534
Cdd:PRK06144 238 CYMSEdfrEGVEAFL 252
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-55 8.21e-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: 57.34  E-value: 8.21e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   7 YEVERIVDKR---KNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18964    1 FFVERIIGRRpsaRDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDF 52
PRK06563 PRK06563
crotonase/enoyl-CoA hydratase family protein;
291-534 1.77e-10

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 180625 [Multi-domain]  Cd Length: 255  Bit Score: 61.52  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 291 VVRKQDGftHILLST--KSSENNSLNPEVMREVQSALSTAAADDSKLV-LLSAVGSVFCCGLDFIYFIRRLTDDRKRESt 367
Cdd:PRK06563   1 VSRERRG--HVLLIGldRPAKRNAFDSAMLDDLALALGEYEADDELRVaVLFAHGEHFTAGLDLADVAPKLAAGGFPFP- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 368 kmAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKawfqtpyTTFGQ-------SPDGCSTVMFPKIM 440
Cdd:PRK06563  78 --EGGIDPWGTVGRRLSKPLVVAVQGYCLTLGIELMLAADIVVAADN-------TRFAQlevqrgiLPFGGATLRFPQAA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 441 GGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVL 520
Cdd:PRK06563 149 GWGNAMRYLLTGDEFDAQEALRLGLVQEVVPPGEQLERAIELAERIARAAPLGVQATLASARAAVREGEAAAAAQLPPEL 228
                        250
                 ....*....|....*..
gi 221307494 521 KKIWGS---AQGMDSML 534
Cdd:PRK06563 229 RPLFTSedaKEGVQAFL 245
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
7-55 1.93e-10

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: 56.15  E-value: 1.93e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 221307494   7 YEVERIVDKRKNKKGKT-EYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18640    1 EPVEKIVAKRFNPRKKTwEYLVKWENRSHHENTWEPMANLERCKYLLQMF 50
PRK08258 PRK08258
enoyl-CoA hydratase family protein;
330-516 2.39e-10

enoyl-CoA hydratase family protein;


Pssm-ID: 181329  Cd Length: 277  Bit Score: 61.52  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 330 ADDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRES---TKMA----EAIRNFvntfiqfKKPIIVAVNGPAIGLGASI 402
Cdd:PRK08258  59 ADDVKAVVLTGAGGNFCSGGDVHEIIGPLTKMDMPELlafTRMTgdlvKAMRAC-------PQPIIAAVDGVCAGAGAIL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 403 LPLCDVVWANEKAWFQTPYTTFGQSpdGC---STVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEV 479
Cdd:PRK08258 132 AMASDLRLGTPSAKTAFLFTRVGLA--GAdmgACALLPRIIGQGRASELLYTGRSMSAEEGERWGFFNRLVEPEELLAEA 209
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 221307494 480 MVRIKELASCNPVVLEESKALVRCNMKMELEQANERE 516
Cdd:PRK08258 210 QALARRLAAGPTFAHGMTKTMLHQEWDMGLEEAIEAE 246
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
7-47 4.02e-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: 55.09  E-value: 4.02e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18627    1 FAAECILKKRI-RKGKVEYLVKWKGWSQKYNTWEPEENILD 40
PRK09120 PRK09120
p-hydroxycinnamoyl CoA hydratase/lyase; Validated
311-512 4.07e-10

p-hydroxycinnamoyl CoA hydratase/lyase; Validated


Pssm-ID: 236383  Cd Length: 275  Bit Score: 60.79  E-value: 4.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALST-AAADDSKLVLLSAVGSVFCCGLDFI-YFirRLTDDR--------KRESTKMAEAIRnfvntf 380
Cdd:PRK09120  30 NAMSPTLNREMIDVLDAlEFDDDAGVLVLTGAGDAWSAGMDLKeYF--RETDAQpeilqeriRREAYGWWRRLR------ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 381 iQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEA 460
Cdd:PRK09120 102 -WYQKPTIAMVNGWCFGGGFSPLVACDLAIAADEAQFGLSEINWGIPPGGGVSKAMADTVGHRDALYYIMTGETFTGRKA 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 221307494 461 CGKGLVSQVFwPgtfTQEVMVRIKELASC----NPVVLEESKALVRCNMKMELEQA 512
Cdd:PRK09120 181 AEMGLVNESV-P---LAQLRARTRELAAKllekNPVVLRAAKDGFKRVRELTWDQA 232
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
7-55 5.11e-10

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: 55.01  E-value: 5.11e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHDF 55
Cdd:cd18652    2 FVVEKVLDRRV-VNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
7-55 5.99e-10

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: 54.83  E-value: 5.99e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18972    1 YEVEAIVGHKPKKKPR-QFLVSWLGYDSSHNEWKQKEELENARELLQDY 48
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
290-472 9.17e-10

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: 61.39  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  290 IVVRKQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAADDS--KLVLLSAVGSVFCCGLDfIYFIRrlTDDRKREST 367
Cdd:TIGR02441  15 RHYEVKGDVAVVKIDSPNSKVNTLSKELFAEFKEVMNELWTNEAikSAVLISGKPGSFVAGAD-IQMIA--ACKTAQEVT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  368 KMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWA--NEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASA 445
Cdd:TIGR02441  92 QLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIAtkDRKTLLGLPEVMLGLLPGAGGTQRLPKLTGVPAA 171
                         170       180
                  ....*....|....*....|....*..
gi 221307494  446 NEMLLSGRKLTAQEACGKGLVSQVFWP 472
Cdd:TIGR02441 172 LDMMLTGKKIRADRAKKMGIVDQLVDP 198
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
4-55 1.23e-09

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: 54.07  E-value: 1.23e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494   4 EELYEVERIVDKRKN--KKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18969    1 EEEYEIEEILDVKKGgfEDGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEY 54
PLN02921 PLN02921
naphthoate synthase
282-499 1.50e-09

naphthoate synthase


Pssm-ID: 178509 [Multi-domain]  Cd Length: 327  Bit Score: 59.42  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 282 ESAYRYRDIVVRKQ--DGFTHILLStKSSENNSLNPEVMREVQSALStAAADDSK---LVLLSAVGSVFCCGLDfiYFIR 356
Cdd:PLN02921  59 GSGKEFTDIIYEKAvgEGIAKITIN-RPERRNAFRPRTVKELQRAFN-DARDDSSvgvIILTGKGTKAFCSGGD--QAVR 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 357 rlTDDRKRESTKMAEAirNFVNTFIQFK---KPIIVAVNGPAIGlGASILPL-CDVVWANEKAWFQTPYTTFGQSPDGCS 432
Cdd:PLN02921 135 --GKDGYVGPDDAGRL--NVLDLQIQIRrlpKPVIAMVAGYAVG-GGHILHMvCDLTIAADNAVFGQTGPKVGSFDAGYG 209
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307494 433 TVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKA 499
Cdd:PLN02921 210 SSIMARLVGQKKAREMWFLARFYTASEALKMGLVNTVVPLDELEGETVKWCREILRNSPTAIRVLKS 276
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
8-43 1.59e-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: 1.59e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 221307494   8 EVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQ 43
Cdd:cd18659    4 IVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEE 39
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
7-55 1.76e-09

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


Pssm-ID: 349280  Cd Length: 51  Bit Score: 53.68  E-value: 1.76e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKNKkGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDF 55
Cdd:cd18630    2 YVVEKILGKRFVN-GRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
7-52 1.84e-09

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: 53.64  E-value: 1.84e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 221307494   7 YEVERIVD----KRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLVNCEEYI 52
Cdd:cd18977    4 YEVEKIVGekwkKRKNRRVK-LYKVRFKGYGPEEDEWLTKEELKNAPEIL 52
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
4-58 2.98e-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: 53.14  E-value: 2.98e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 221307494   4 EELYEVERIVDKRkNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHDFNRR 58
Cdd:cd18647    1 EQVFAAECILSKR-LRKGKLEYLVKWRGWSSKHNSWEPEENILD-PRLLLAFQKK 53
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
7-52 5.59e-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: 52.13  E-value: 5.59e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 221307494   7 YEVERIVDKRKNKKGKT-EYLVRWKGYDSEDD-TWEPEQHLVNCEEYI 52
Cdd:cd18637    2 YVVEKILKHRMARKGGGyEYLLKWEGYDDPSDnTWSSEADCAGCKDLI 49
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
7-55 5.65e-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: 52.13  E-value: 5.65e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLvNCEEYIHDF 55
Cdd:cd18639    1 YEVEYLCDYKK-IREQEYYLVKWKGYPDSENTWEPRQNL-KCSRLLKQF 47
PRK05869 PRK05869
enoyl-CoA hydratase; Validated
294-499 7.36e-09

enoyl-CoA hydratase; Validated


Pssm-ID: 235632 [Multi-domain]  Cd Length: 222  Bit Score: 56.39  E-value: 7.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 294 KQDGFTHILLSTKSSenNSLNPEVMREVQSALSTAAA-DDSKLVLLSAVGSVFCCGLDfIYFIRRLTDDrkrESTKMAEA 372
Cdd:PRK05869  14 QDAGLATLLLSRPPT--NALTRQVYREIVAAANELGRrDDVAAVILYGGHEIFSAGDD-MPELRTLSAQ---EADTAARV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 373 IRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSG 452
Cdd:PRK05869  88 RQQAVDAVAAIPKPTVAAITGYALGAGLTLALAADWRVSGDNVKFGATEILAGLAPSGDGMARLTRAAGPSRAKELVFSG 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 221307494 453 RKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKA 499
Cdd:PRK05869 168 RFFDAEEALALGLIDEMVAPDDVYDAAAAWARRFLDGPPHALAAAKA 214
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
4-47 1.04e-08

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


Pssm-ID: 349293  Cd Length: 56  Bit Score: 51.63  E-value: 1.04e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 221307494   4 EELYEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18646    2 EQVFAVESIRKKRV-RKGKVEYLVKWKGWPPKYSTWEPEEHILD 44
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
7-47 1.51e-08

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: 51.01  E-value: 1.51e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 221307494   7 YEVERIVDKRkNKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18975    1 YEVESILNSR-LHRGKLQYLIQWKGYPLEEASWELEDNIKN 40
PRK07509 PRK07509
crotonase/enoyl-CoA hydratase family protein;
290-488 1.59e-08

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181008 [Multi-domain]  Cd Length: 262  Bit Score: 55.66  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLsTKSSENNSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDRKRESTK 368
Cdd:PRK07509   5 VSVTIEDGIADVRL-NRPDKMNALDFAMFEELIATIKRLKKDRGiRAVILSGEGGAFCAGLD----VKSVASSPGNAVKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 369 MAEAIRNFVNTFIQF-------KKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMG 441
Cdd:PRK07509  80 LFKRLPGNANLAQRVslgwrrlPVPVIAALEGVCFGGGLQIALGADIRIAAPDTKLSIMEAKWGLVPDMAGTVSLRGLVR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 221307494 442 GASANEMLLSGRKLTAQEACGKGLVSQVfwpgtfTQEVMVRIKELAS 488
Cdd:PRK07509 160 KDVARELTYTARVFSAEEALELGLVTHV------SDDPLAAALALAR 200
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
9-57 1.96e-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: 1.96e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 221307494   9 VERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQ-HLVNCEEYIHDFNR 57
Cdd:cd18662    6 IHRIINHRVDKDGNTWYLVKWRDLPYDQSTWESEDdDIPDYEKHIQEYWD 55
PRK07112 PRK07112
enoyl-CoA hydratase/isomerase;
287-466 4.31e-08

enoyl-CoA hydratase/isomerase;


Pssm-ID: 235938  Cd Length: 255  Bit Score: 54.30  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 287 YRDIVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAaDDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRES 366
Cdd:PRK07112   3 YQTIRVRQQGDVCFLQLH-RPEAQNTINDRLIAECMDVLDRCE-HAATIVVLEGLPEVFCFGADFSAIAEKPDAGRADLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 367 TkmAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPdGCSTVMFPKIMGGASAN 446
Cdd:PRK07112  81 D--AEPLYDLWHRLATGPYVTIAHVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIP-ACVLPFLIRRIGTQKAH 157
                        170       180
                 ....*....|....*....|
gi 221307494 447 EMLLSGRKLTAQEACGKGLV 466
Cdd:PRK07112 158 YMTLMTQPVTAQQAFSWGLV 177
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
7-49 6.30e-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: 48.93  E-value: 6.30e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 221307494   7 YEVERIVD-KRKNKKGK-TEYLVRWKGYDseDDTWEPEQHLVNCE 49
Cdd:cd18971    1 YEVEEILAaRRRRIRGKgREVLVKWVGYA--EPTWEPLDNLADTA 43
PRK08788 PRK08788
enoyl-CoA hydratase; Validated
314-496 9.15e-08

enoyl-CoA hydratase; Validated


Pssm-ID: 236338  Cd Length: 287  Bit Score: 53.76  E-value: 9.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 314 NPEVMRE-------VQSALSTAAADDSKLVLLSAVGSVFCCGLDFIYFiRRLTDDRKRESTKM-AEAIRNFVNTFIQ-FK 384
Cdd:PRK08788  41 NLELLDDimnlqraIRQRLDDSGLPVDFWVLASDVPGVFNLGGDLALF-AELIRAGDRDALLAyARACVDGVHAFHRgFG 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 385 KPII-VA-VNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGqspdgcstvMFPKiMGGAS----------ANEMLLSG 452
Cdd:PRK08788 120 AGAIsIAlVQGDALGGGFEAALSHHTIIAERGAKMGFPEILFN---------LFPG-MGAYSflarrvgpklAEELILSG 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 453 RKLTAQEACGKGLVSQVFWPGTFTQEV----------------MVRIKELAscNPVVLEE 496
Cdd:PRK08788 190 KLYTAEELHDMGLVDVLVEDGQGEAAVrtfirkskrklngwraMLRARRRV--NPLSLEE 247
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
4-47 1.03e-07

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


Pssm-ID: 349292  Cd Length: 55  Bit Score: 48.51  E-value: 1.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 221307494   4 EELYEVERIvDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18645    1 EHVFAVESI-EKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILD 43
PLN02851 PLN02851
3-hydroxyisobutyryl-CoA hydrolase-like protein
302-499 1.10e-07

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178443 [Multi-domain]  Cd Length: 407  Bit Score: 54.21  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 302 LLSTKSSENNSLNPEVMREVQSALSTAAADDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKMAEAIRNFVNTFI 381
Cdd:PLN02851  56 ILNRPSSLNALTIPMVARLKRLYESWEENPDIGFVLMKGSGRAFCSGADVVSLYHLINEGNVEECKLFFENLYKFVYLQG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 382 QFKKPIIVAVNGPAIGLGASI-LPLCDVVwANEKAWFQTPYTTFGQSPDGCSTVMFPKiMGGASANEMLLSGRKLTAQEA 460
Cdd:PLN02851 136 TYLKPNVAIMDGITMGCGAGIsIPGMFRV-VTDKTVFAHPEVQMGFHPDAGASYYLSR-LPGYLGEYLALTGQKLNGVEM 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 221307494 461 CGKGLVSQVfwpgTFTQEVMV---RIKELASCNPVVLEESKA 499
Cdd:PLN02851 214 IACGLATHY----CLNARLPLieeRLGKLLTDDPAVIEDSLA 251
PRK12478 PRK12478
crotonase/enoyl-CoA hydratase family protein;
311-468 1.56e-07

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 183548  Cd Length: 298  Bit Score: 53.04  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAAD-DSKLVLLSAVGSVFCCGLDF----IYFIRRLTDDRKRESTK---MAEA-----IRNFV 377
Cdd:PRK12478  27 NTIVPPMPDEIEAAIGLAERDqDIKVIVLRGAGRAFSGGYDFgggfQHWGEAMMTDGRWDPGKdfaMVTAretgpTQKFM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 378 NTFiQFKKPIIVAVNGPAIGlGASILPLC-DVVWANEKAWFQTPYTTFGqspdGCS-TVMFPKIMGGASANEMLLSGRKL 455
Cdd:PRK12478 107 AIW-RASKPVIAQVHGWCVG-GASDYALCaDIVIASDDAVIGTPYSRMW----GAYlTGMWLYRLSLAKVKWHSLTGRPL 180
                        170
                 ....*....|...
gi 221307494 456 TAQEACGKGLVSQ 468
Cdd:PRK12478 181 TGVQAAEAELINE 193
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
4-63 4.99e-07

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


Pssm-ID: 349295  Cd Length: 58  Bit Score: 46.97  E-value: 4.99e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNcEEYIHDFNRRHTEKQ 63
Cdd:cd18648    1 ERVFAAESII-KRRIRKGRIEYLVKWKGWAIKYSTWEPEENILD-SRLIAAFEQKERERE 58
PRK08259 PRK08259
crotonase/enoyl-CoA hydratase family protein;
290-488 9.27e-07

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 236205  Cd Length: 254  Bit Score: 50.28  E-value: 9.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 290 IVVRKQDGFTHILLStKSSENNSLNPEVMREVQSALSTAAADDSKLV-LLSAVGSVFCCGLDfiyfIRRLTDDRKRES-- 366
Cdd:PRK08259   5 VRVERNGPVTTVILN-RPEVRNAVDGPTAAALADAFRAFDADDAASVaVLWGAGGTFCAGAD----LKAVGTGRGNRLhp 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 367 --------TKMaeairnfvntfiQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGqSP--DGcSTVMF 436
Cdd:PRK08259  80 sgdgpmgpSRM------------RLSKPVIAAVSGYAVAGGLELALWCDLRVAEEDAVFGVFCRRWG-VPliDG-GTVRL 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494 437 PKIMGGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELAS 488
Cdd:PRK08259 146 PRLIGHSRAMDLILTGRPVDADEALAIGLANRVVPKGQARAAAEELAAELAA 197
PLN02874 PLN02874
3-hydroxyisobutyryl-CoA hydrolase-like protein
311-462 9.30e-07

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 178462 [Multi-domain]  Cd Length: 379  Bit Score: 51.34  E-value: 9.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGSVFCCGLDfiyfIRRLTDDR-KRESTKMAEAIRNFVNTFIQ-FKKPI 387
Cdd:PLN02874  33 NVISLSVVSLLAEFLEQWEKDDSvELIIIKGAGRAFSAGGD----LKMFYDGReSDDSCLEVVYRMYWLCYHIHtYKKTQ 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307494 388 IVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDgCSTVMFPKIMGGASANEMLLSGRKLTAQE--ACG 462
Cdd:PLN02874 109 VALVHGLVMGGGAGLMVPMKFRVVTEKTVFATPEASVGFHTD-CGFSYILSRLPGHLGEYLALTGARLNGKEmvACG 184
PLN02267 PLN02267
enoyl-CoA hydratase/isomerase family protein
301-485 9.90e-07

enoyl-CoA hydratase/isomerase family protein


Pssm-ID: 215151  Cd Length: 239  Bit Score: 50.10  E-value: 9.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 301 ILLSTKSSENNsLNPEVMREVQSALSTAAADDSKLVLL--SAVGSVFCCGLDfIYFIRRLTDDRKReSTKMAEAIRNFVN 378
Cdd:PLN02267  12 ILTLTGDGEHR-LNPTLIDSIRSALRQVKSQATPGSVLitTAEGKFFSNGFD-LAWAQAAGSAPSR-LHLMVAKLRPLVA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 379 TFIQFKKPIIVAVNGPAIGLGAsILPLCD--VVWANEKAWFQTPYTTFGQS-PDGCSTVMFPKIMGGASANEMLLSGRKL 455
Cdd:PLN02267  89 DLISLPMPTIAAVTGHASAAGF-ILALSHdyVLMRKDRGVLYMSEVDIGLPlPDYFMALLRAKIGSPAARRDVLLRAAKL 167
                        170       180       190
                 ....*....|....*....|....*....|
gi 221307494 456 TAQEACGKGLVSQVFWPGTFTQEVMVRIKE 485
Cdd:PLN02267 168 TAEEAVEMGIVDSAHDSAEETVEAAVRLGE 197
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
4-57 1.15e-06

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: 45.64  E-value: 1.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWePEQHLVNCEEYIHDFNR 57
Cdd:cd18962    1 EGHYVVEAIV-NDVLIDGKHMYEVKWEGYPSDHNNW-VAEWDLNDKEILRKYNK 52
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
4-47 1.16e-06

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


Pssm-ID: 349296  Cd Length: 55  Bit Score: 45.87  E-value: 1.16e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 221307494   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVN 47
Cdd:cd18649    2 ERVFAAEALL-KRRIRKGRMEYLVKWKGWSQKYSTWEPEENILD 44
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
7-57 1.65e-06

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


Pssm-ID: 349332  Cd Length: 51  Bit Score: 45.25  E-value: 1.65e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGYDSEDDTWEPEQHLVN-CEEYIHDFNR 57
Cdd:cd18976    1 YIVESLLDRRK-VRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAYDA 51
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-57 2.00e-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: 44.77  E-value: 2.00e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494   7 YEVERIVdKRKNKKGKTEYLVRWKGYDSEDDTWEPEQ---HLVNCEEYIHDFNR 57
Cdd:cd18965    1 YIIEALL-KKRQFNRKLEYLVKWHGLPESENTWEREKdikHVSHWKQLLKDLRA 53
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
7-57 4.03e-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: 44.01  E-value: 4.03e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221307494   7 YEVERIVDKRKnKKGKTEYLVRWKGY-DSEDDTWEPEQHLVNCEEYIHDFNR 57
Cdd:cd18961    1 YEVEKILSHRI-VNGKPLYLVMWVGYpGPVENSEMWEEDLKNCGELLKAYKD 51
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
280-469 1.33e-05

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 47.97  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 280 QTESAYRyrdiVVRKQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAADDS--KLVLLSAVGSVFCCGLDfIYFIRR 357
Cdd:PRK11154   2 EMASAFT----LNVREDNIAVITIDVPGEKMNTLKAEFAEQVRAILKQLREDKElkGVVFISGKPDNFIAGAD-INMLAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 358 LTDdrKRESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCD--VVWANEKAWFQTPYTTFGQSPDGCSTVM 435
Cdd:PRK11154  77 CKT--AQEAEALARQGQQLFAEIEALPIPVVAAIHGACLGGGLELALACHyrVCTDDPKTVLGLPEVQLGLLPGSGGTQR 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 221307494 436 FPKIMGGASANEMLLSGRKLTAQEACGKGLVSQV 469
Cdd:PRK11154 155 LPRLIGVSTALDMILTGKQLRAKQALKLGLVDDV 188
CD_POL_like cd18979
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ...
10-46 1.65e-05

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


Pssm-ID: 349335  Cd Length: 48  Bit Score: 42.09  E-value: 1.65e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 221307494  10 ERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLV 46
Cdd:cd18979    4 EKVLDIRQRDKGNKEFLVQWQGLSVEEATWEPYKDLV 40
CD2_cpSRP43_like cd18629
chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
5-45 2.84e-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: 2.84e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 221307494   5 ELYEVERIVDKRkNKKGKTEYLVRWKgyDSEDDTWEPEQHL 45
Cdd:cd18629    1 EYAEVNEILESR-GKGKDMEYLIEWK--DGGDCEWVKGVHV 38
PRK09076 PRK09076
enoyl-CoA hydratase; Provisional
311-516 2.87e-05

enoyl-CoA hydratase; Provisional


Pssm-ID: 236373 [Multi-domain]  Cd Length: 258  Bit Score: 45.68  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS--KLVLLSAVGSVFCCGLDFIYFirrlTDDRKRESTKMA-------EAIRNFvntfi 381
Cdd:PRK09076  24 NTWTADSLQALKQLVLELNADKDvyALVITGDGEKFFSAGADLNLF----ADGDKAVAREMArrfgeafEALSAF----- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 382 qfKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEAC 461
Cdd:PRK09076  95 --RGVSIAAINGYAMGGGLECALACDIRIAEEQAQMALPEASVGLLPCAGGTQNLPWLVGEGWAKRMILCGERVDAATAL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221307494 462 GKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQA--NERE 516
Cdd:PRK09076 173 RIGLVEEVVEKGEAREAALALAQKVANQSPSAVAACKTLIQAARNGPRAAAlaLERE 229
PRK11423 PRK11423
methylmalonyl-CoA decarboxylase; Provisional
311-487 5.69e-05

methylmalonyl-CoA decarboxylase; Provisional


Pssm-ID: 236908 [Multi-domain]  Cd Length: 261  Bit Score: 45.02  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDSKLVLLSA-VGS-VFCCGLDfiyfIRRLTDDRkRESTKMAEAIRNFVNTFIQFKKPII 388
Cdd:PRK11423  26 NALSKVLIDDLMQALSDLNRPEIRVVILRApSGSkVWSAGHD----IHELPSGG-RDPLSYDDPLRQILRMIQKFPKPVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 389 VAVNGPAIGlGASILPL-CDVVWANEKAWFQ-------TPYTTFGqspdgcsTVMFPKIMGGASANEMLLSGRKLTAQEA 460
Cdd:PRK11423 101 AMVEGSVWG-GAFELIMsCDLIIAASTSTFAmtpanlgVPYNLSG-------ILNFTNDAGFHIVKEMFFTASPITAQRA 172
                        170       180       190
                 ....*....|....*....|....*....|
gi 221307494 461 CGKGLVSQVFWPG---TFTQEVMVRIKELA 487
Cdd:PRK11423 173 LAVGILNHVVEVEeleDFTLQMAHHISEKA 202
PLN02157 PLN02157
3-hydroxyisobutyryl-CoA hydrolase-like protein
335-523 1.58e-04

3-hydroxyisobutyryl-CoA hydrolase-like protein


Pssm-ID: 177817 [Multi-domain]  Cd Length: 401  Bit Score: 44.29  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 335 LVLLSAVGSVFCCGLDFI--YFIR-RLTDDRKREstkMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWA 411
Cdd:PLN02157  84 FVMMKGSGRAFCAGGDIVslYHLRkRGSPDAIRE---FFSSLYSFIYLLGTYLKPHVAILNGVTMGGGTGVSIPGTFRVA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 412 NEKAWFQTPYTTFGQSPDGCSTVMFPKiMGGASANEMLLSGRKLTAQEACGKGLVSQVFWpgtfTQEVMV---RIKELAS 488
Cdd:PLN02157 161 TDRTIFATPETIIGFHPDAGASFNLSH-LPGRLGEYLGLTGLKLSGAEMLACGLATHYIR----SEEIPVmeeQLKKLLT 235
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 221307494 489 CNPVVLEEskALVRCnmkmeLEQANERECEVLKKI 523
Cdd:PLN02157 236 DDPSVVES--CLEKC-----AEVAHPEKTGVIRRI 263
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
8-43 1.65e-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: 39.58  E-value: 1.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 221307494   8 EVERIVDKRK-----NKKGKTEYLVRWKGYDSEDDTWEPEQ 43
Cdd:cd18663    5 EVDRILDVSVstdpnTGEPVTHYLVKWCSLPYEDSTWELEE 45
PRK05617 PRK05617
3-hydroxyisobutyryl-CoA hydrolase; Provisional
311-429 2.54e-04

3-hydroxyisobutyryl-CoA hydrolase; Provisional


Pssm-ID: 235533 [Multi-domain]  Cd Length: 342  Bit Score: 43.27  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGS-VFCCGLDfiyfIRRLTDDRKREStkmAEAIRNF------VNTFI- 381
Cdd:PRK05617  25 NALSLEMIRAIDAALDAWEDDDAvAAVVIEGAGErGFCAGGD----IRALYEAARAGD---PLAADRFfreeyrLNALIa 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221307494 382 QFKKPIIVAVNGPAIG------LGASIlplcDVVwaNEKAWFQTPYTTFGQSPD 429
Cdd:PRK05617  98 RYPKPYIALMDGIVMGggvgisAHGSH----RIV--TERTKMAMPETGIGFFPD 145
PRK06213 PRK06213
crotonase/enoyl-CoA hydratase family protein;
311-407 2.62e-04

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235744  Cd Length: 229  Bit Score: 42.65  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 311 NSLNPEVMREVQSALsTAAADDSKLVLLSAVGSVFCCGLDFIYFirrltddrkresTKMAEAIRNFVN---TFI----QF 383
Cdd:PRK06213  24 NALSPAMIDALNAAL-DQAEDDRAVVVITGQPGIFSGGFDLKVM------------TSGAQAAIALLTagsTLArrllSH 90
                         90       100
                 ....*....|....*....|....
gi 221307494 384 KKPIIVAVNGPAIGLGASILPLCD 407
Cdd:PRK06213  91 PKPVIVACTGHAIAKGAFLLLSAD 114
ECH_2 pfam16113
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
311-432 3.85e-04

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


Pssm-ID: 465024 [Multi-domain]  Cd Length: 331  Bit Score: 42.84  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494  311 NSLNPEVMREVQSALSTAAADDS-KLVLLSAVGS-VFCCGLDfiyfIRRLTDDRKRESTkmaEAIRNF------VNTFI- 381
Cdd:pfam16113  13 NALNLEMVRALLAALKAWEDDPAvKLVVLKGAGErAFCAGGD----VRALYEAAKAGGG---EAGRDFfreeyrLNYLIa 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 221307494  382 QFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPD-GCS 432
Cdd:pfam16113  86 TYPKPYVALMDGIVMGGGVGLSVHGSFRVVTERTRFAMPETAIGLFPDvGGS 137
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
7-57 6.35e-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: 38.00  E-value: 6.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 221307494   7 YEVERIVDKR----KNKKGKTE---YLVRWKGYDseDDTWEPEQHLVNcEEYIHDFNR 57
Cdd:cd18967    1 WEIEAILAHHmsdpRTHPGKPAtmlYLTKWEGFP--DETWEPAESFDD-RKILHDYRR 55
CD_eEF3 cd18626
chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic ...
9-46 2.17e-03

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


Pssm-ID: 349276 [Multi-domain]  Cd Length: 56  Bit Score: 36.43  E-value: 2.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 221307494   9 VERIVDKRKNKKGKtEYLVRWKGYDSEDDTWEPEQHLV 46
Cdd:cd18626    4 IEKIVGRRKLKKSY-EYEVKWKGMSSKDNSWIPREELE 40
PLN02988 PLN02988
3-hydroxyisobutyryl-CoA hydrolase
291-491 2.49e-03

3-hydroxyisobutyryl-CoA hydrolase


Pssm-ID: 178568 [Multi-domain]  Cd Length: 381  Bit Score: 40.47  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 291 VVRKQDGFTHILLSTKSSENNSLNPEVM-REVQSALSTAAADDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKM 369
Cdd:PLN02988  11 VLVEEKSSVRILTLNRPKQLNALSFHMIsRLLQLFLAFEEDPSVKLVILKGHGRAFCAGGDVAAVVRDIEQGNWRLGANF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 370 --AEAIRNFVntFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKiMGGASANE 447
Cdd:PLN02988  91 fsDEYMLNYV--MATYSKAQVSILNGIVMGGGAGVSVHGRFRIATENTVFAMPETALGLFPDVGASYFLSR-LPGFFGEY 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 221307494 448 MLLSGRKLTAQEACGKGLVSQvFWPGTFTQEVMVRIKELASCNP 491
Cdd:PLN02988 168 VGLTGARLDGAEMLACGLATH-FVPSTRLTALEADLCRIGSNDP 210
PRK07938 PRK07938
enoyl-CoA hydratase family protein;
320-499 2.88e-03

enoyl-CoA hydratase family protein;


Pssm-ID: 181174  Cd Length: 249  Bit Score: 39.57  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 320 EVQSALSTAAAD-DSKLVLLSAVGSVFCCGLDfiyfIRRLtdDRKRESTKMAEAIRNFVNTF---IQFKKPIIVAVNGPA 395
Cdd:PRK07938  32 ALADAITAAGADpDTRVVVLRAEGRGFNAGVD----IKEL--QATPGFTALIDANRGCFAAFravYECAVPVIAAVHGFC 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 396 IGLGASILPLCDVVWANEKAWFQTPYTTFGQspdgcstvmfpkiMGGAS----------ANEMLLSGRKLTAQEACGKGL 465
Cdd:PRK07938 106 LGGGIGLVGNADVIVASDDATFGLPEVDRGA-------------LGAAThlqrlvpqhlMRALFFTAATITAAELHHFGS 172
                        170       180       190
                 ....*....|....*....|....*....|....
gi 221307494 466 VSQVFWPGTFTQEVMVRIKELASCNPVVLEESKA 499
Cdd:PRK07938 173 VEEVVPRDQLDEAALEVARKIAAKDTRVIRAAKE 206
PRK08321 PRK08321
1,4-dihydroxy-2-naphthoyl-CoA synthase;
377-469 3.80e-03

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


Pssm-ID: 181386  Cd Length: 302  Bit Score: 39.62  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307494 377 VNTFIQF-KKPIIVAVNGPAIGLGASILPLCDVVWAN-EKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRK 454
Cdd:PRK08321 127 VQRLIRFmPKVVIAVVPGWAAGGGHSLHVVCDLTLASrEHARFKQTDADVGSFDGGYGSAYLARQVGQKFAREIFFLGRT 206
                         90
                 ....*....|....*
gi 221307494 455 LTAQEACGKGLVSQV 469
Cdd:PRK08321 207 YSAEEAHDMGAVNAV 221
CD3_cpSRP43_like cd18628
chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
11-56 4.91e-03

chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; This subgroup includes the chromodomain 3 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain.


Pssm-ID: 349278  Cd Length: 51  Bit Score: 35.43  E-value: 4.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 221307494  11 RIVDKRKnkkgKTEYLVRWkgYDSEDDTWEPEQHLVNceEYIHDFN 56
Cdd:cd18628   13 RVGDDGK----TIEYLVKW--TDMSDATWEPQDNVDS--TLVLLYQ 50
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
9-41 5.29e-03

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


Pssm-ID: 349312  Cd Length: 65  Bit Score: 35.44  E-value: 5.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 221307494   9 VERIVDKRKNK----------KGKTEYLVRWKGYDSEDDTWEP 41
Cdd:cd18665    5 IDIVLDHRLKEgleegelddpKENYEFLIKWTDESHLHNTWET 47
chromodomain cd18963
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
4-45 5.83e-03

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


Pssm-ID: 349319  Cd Length: 57  Bit Score: 35.36  E-value: 5.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 221307494   4 EELYEVERIVdKRKNKKGKTEYLVRWKGYDSEddtwEPEQHL 45
Cdd:cd18963    1 ERVFAAECII-KRRVRKGRIEYLVKWKGWASK----EREREL 37
 
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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