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Conserved domains on  [gi|27894378|ref|NP_444507|]
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chloride intracellular channel protein 6 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
O-ClC super family cl31033
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ...
 453-686 9.53e-147

intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A.12) Proteins of the O-ClC family are voltage-sensitive chloride channels found in intracellular membranes but not the plasma membranes of animal cells. They are found in human nuclear membranes, and the bovine protein targets to the microsomes, but not the plasma membrane, when expressed in Xenopus laevis oocytes. These proteins are thought to function in the regulation of the membrane potential and in transepithelial ion absorption and secretion in the kidney. [Transport and binding proteins, Anions]


The actual alignment was detected with superfamily member TIGR00862:

Pssm-ID: 129941 [Multi-domain]  Cd Length: 236  Bit Score: 426.20  E-value: 9.53e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   453 ITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 532
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   533 LAPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKF 612
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27894378   613 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRMK 686
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 2-420 8.61e-11

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 65.39  E-value: 8.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    2 AEAAEPEGVAPGPQGPPEVPAPlaeRPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHG 81
Cdd:PRK07764 389 GGAGAPAAAAPSAAAAAPAAAP---APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   82 ETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEA----QREPEDSAAPERQEEAEQRPEVPEGSASGEAG 157
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAatlrERWPEILAAVPKRSRKTWAILLPEATVLGVRG 545

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  158 DSVD---AEGPLGDNIEAEGPAGDSVEA-EGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAE 233
Cdd:PRK07764 546 DTLVlgfSTGGLARRFASPGNAEVLVTAlAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPA 625

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  234 GPAGDSVDAEGRVGDSVEA-GDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAiE 312
Cdd:PRK07764 626 APAPAGAAAAPAEASAAPApGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP-A 704

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  313 VAAGESAGRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEEE 392
Cdd:PRK07764 705 PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784

                        410       420
                 ....*....|....*....|....*...
gi 27894378  393 SPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PRK07764 785 MAEDDAPSMDDEDRRDAEEVAMELLEEE 812
 
Name Accession Description Interval E-value
O-ClC TIGR00862
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ...
 453-686 9.53e-147

intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A.12) Proteins of the O-ClC family are voltage-sensitive chloride channels found in intracellular membranes but not the plasma membranes of animal cells. They are found in human nuclear membranes, and the bovine protein targets to the microsomes, but not the plasma membrane, when expressed in Xenopus laevis oocytes. These proteins are thought to function in the regulation of the membrane potential and in transepithelial ion absorption and secretion in the kidney. [Transport and binding proteins, Anions]


Pssm-ID: 129941 [Multi-domain]  Cd Length: 236  Bit Score: 426.20  E-value: 9.53e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   453 ITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 532
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   533 LAPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKF 612
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27894378   613 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRMK 686
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
 545-684 4.49e-106

C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 6 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC6 is expressed predominantly in the stomach, pituitary, and brain. It interacts with D2-like dopamine receptors directly and through scaffolding proteins. CLIC6 may be involved in the regulation of secretion, possibly through chloride ion transport regulation.


Pssm-ID: 198334  Cd Length: 140  Bit Score: 318.12  E-value: 4.49e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 624
Cdd:cd10301   1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKR 684
Cdd:cd10301  81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 466-667 9.96e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 104.30  E-value: 9.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  466 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLAPpryPKLGTQh 545
Cdd:PLN02817  70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPD---PPLATP- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  546 PESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSPLPdeidaystedvtvsgrkFLDGDELTLADCNL 625
Cdd:PLN02817 146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 27894378  626 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 667
Cdd:PLN02817 207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 469-532 3.04e-11

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 59.18  E-value: 3.04e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27894378   469 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 532
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 2-420 8.61e-11

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 65.39  E-value: 8.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    2 AEAAEPEGVAPGPQGPPEVPAPlaeRPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHG 81
Cdd:PRK07764 389 GGAGAPAAAAPSAAAAAPAAAP---APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   82 ETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEA----QREPEDSAAPERQEEAEQRPEVPEGSASGEAG 157
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAatlrERWPEILAAVPKRSRKTWAILLPEATVLGVRG 545

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  158 DSVD---AEGPLGDNIEAEGPAGDSVEA-EGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAE 233
Cdd:PRK07764 546 DTLVlgfSTGGLARRFASPGNAEVLVTAlAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPA 625

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  234 GPAGDSVDAEGRVGDSVEA-GDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAiE 312
Cdd:PRK07764 626 APAPAGAAAAPAEASAAPApGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP-A 704

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  313 VAAGESAGRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEEE 392
Cdd:PRK07764 705 PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784

                        410       420
                 ....*....|....*....|....*...
gi 27894378  393 SPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PRK07764 785 MAEDDAPSMDDEDRRDAEEVAMELLEEE 812
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 25-273 3.35e-10

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 63.48  E-value: 3.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     25 AERPGEPGAAGGEAEGPEGSEGAEEAprgaaavkEAGGGGPDRGpEAEARGTRGAHGETEAE-EGAPEGAEVPQGGEETS 103
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENGEESGGEA--------EQEGETETKG-ENESEGEIPAERKGEQEgEGEIEAKEADHKGETEA 712

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    104 GAQQVEGASPGRGAQGEPRGEAQrepedsaapERQEEAEQrpevpEGSASGEAGDSVDAEgplGDNIEAEGPAGDSVEAE 183
Cdd:TIGR00927  713 EEVEHEGETEAEGTEDEGEIETG---------EEGEEVED-----EGEGEAEGKHEVETE---GDRKETEHEGETEAEGK 775

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    184 grvGDSVDAEGPAGDSVDAEGPLGDNIQAEG----PAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAG-DPAGD 258
Cdd:TIGR00927  776 ---EDEDEGEIQAGEDGEMKGDEGAEGKVEHegetEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKqDEKGV 852

                          250
                   ....*....|....*
gi 27894378    259 GVEAGVPAGDSVEAE 273
Cdd:TIGR00927  853 DGGGGSDGGDSEEEE 867
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 12-167 2.97e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 40.66  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   12 PGPQGPPEVPAPLAERpGEPGAAGGEAEGPEGSEGAEEAPRGAAAVK-EAGGGGPdRGPEAE--ARGTRGAHGET-EAEE 87
Cdd:NF038329 122 PGPAGPAGPAGEQGPR-GDRGETGPAGPAGPPGPQGERGEKGPAGPQgEAGPQGP-AGKDGEagAKGPAGEKGPQgPRGE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   88 GAPEGAEVPQG-----GEETSGAQQVEGASPGRGAQGePRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSVDA 162
Cdd:NF038329 200 TGPAGEQGPAGpagpdGEAGPAGEDGPAGPAGDGQQG-PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278


                 ....*.
gi 27894378  163 E-GPLG 167
Cdd:NF038329 279 ErGPVG 284
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
468-673 4.00e-03

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 39.11  E-value: 4.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 468 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEKLAPPR-YP 539
Cdd:COG0625   9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAERYPEPPlLP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 540 KLGTQHPE--------SNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLnsplpdeidaystedvtvSGRK 611
Cdd:COG0625  85 ADPAARARvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL------------------AGGP 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27894378 612 FLDGDELTLADCNLLPKLHIIkivakkyRDFEFP-SEMTGIWRYLNNAYARDEFTNTCPADQE 673
Cdd:COG0625 147 YLAGDRFSIADIALAPVLRRL-------DRLGLDlADYPNLAAWLARLAARPAFQRALAAAEP 202
 
Name Accession Description Interval E-value
O-ClC TIGR00862
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ...
 453-686 9.53e-147

intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A.12) Proteins of the O-ClC family are voltage-sensitive chloride channels found in intracellular membranes but not the plasma membranes of animal cells. They are found in human nuclear membranes, and the bovine protein targets to the microsomes, but not the plasma membrane, when expressed in Xenopus laevis oocytes. These proteins are thought to function in the regulation of the membrane potential and in transepithelial ion absorption and secretion in the kidney. [Transport and binding proteins, Anions]


Pssm-ID: 129941 [Multi-domain]  Cd Length: 236  Bit Score: 426.20  E-value: 9.53e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   453 ITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 532
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   533 LAPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKF 612
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27894378   613 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRMK 686
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
 545-684 4.49e-106

C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 6 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC6 is expressed predominantly in the stomach, pituitary, and brain. It interacts with D2-like dopamine receptors directly and through scaffolding proteins. CLIC6 may be involved in the regulation of secretion, possibly through chloride ion transport regulation.


Pssm-ID: 198334  Cd Length: 140  Bit Score: 318.12  E-value: 4.49e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 624
Cdd:cd10301   1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKR 684
Cdd:cd10301  81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
GST_C_CLIC4 cd10296
C-terminal, alpha helical domain of Chloride Intracellular Channel 4; Glutathione ...
 545-685 9.68e-87

C-terminal, alpha helical domain of Chloride Intracellular Channel 4; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 4 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC4, also known as p64H1, is expressed ubiquitously and its localization varies depending on the nature of the cells and tissues, from the plasma membrane to subcellular compartments including the nucleus, mitochondria, ER, and the trans-Golgi network, among others. In response to cellular stress such as DNA damage and senescence, cytoplasmic CLIC4 translocates to the nucleus, where it acts on the TGF-beta pathway. Studies on knockout mice suggest that CLIC4 also plays an important role in angiogenesis, specifically in network formation, capillary sprouting, and lumen formation. CLIC4 has been found to induce apoptosis in several cell types and to retard the growth of grafted tumors in vivo.


Pssm-ID: 198329  Cd Length: 141  Bit Score: 268.04  E-value: 9.68e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 624
Cdd:cd10296   1 HPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLDGNEMTLADCN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRM 685
Cdd:cd10296  81 LLPKLHIVKVVAKKYRNFEIPKEMTGIWRYLSNAYSRDEFTNTCPSDKEIEIAYSDVAKRL 141
GST_C_CLIC5 cd10297
C-terminal, alpha helical domain of Chloride Intracellular Channel 5; Glutathione ...
 545-685 4.39e-86

C-terminal, alpha helical domain of Chloride Intracellular Channel 5; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 5 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC5 exists in two alternatively-spliced isoforms, CLIC5A or CLIC5B (also called p64). It is expressed at high levels in hair cell stereocilia and is associated with the actin cytoskeleton and ezrin. A recessive mutation in the CLIC5 gene in mice led to the lack of coordination and deafness, due to a defect in the basal region of the hair bundle causing stereocilia to degrade. CLIC5 is therefore essential for normal inner ear function. CLIC5 is also highly expressed in podocytes where it is colocalized with the ezrin/radixin/moesin (ERM) complex. It is essential for foot process integrity, and for podocyte morphology and function.


Pssm-ID: 198330  Cd Length: 141  Bit Score: 266.44  E-value: 4.39e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 624
Cdd:cd10297   1 HRESNTAGIDIFSKFSAYIKNTKQQANAALEKGLTKALKKLDDYLNTPLPEEIDADSTEEEKVSNRKFLDGDELTLADCN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRM 685
Cdd:cd10297  81 LLPKLHVVKIVAKKYRNFEIPSDMTGVWRYLKNAYARDEFTNTCAADKEIELAYADVAKRL 141
GST_C_CLIC2 cd10298
C-terminal, alpha helical domain of Chloride Intracellular Channel 2; Glutathione ...
 545-683 1.17e-71

C-terminal, alpha helical domain of Chloride Intracellular Channel 2; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 2 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC2 contains an intramolecular disulfide bond and exists as a monomer regardless of redox conditions, in contrast to CLIC1 which forms a dimer under oxidizing conditions. It is expressed in most tissues except the brain, and is highly expressed in the lung, spleen, and in cardiac and skeletal muscles. CLIC2 interacts with ryanodine receptors (cardiac RyR2 and skeletal RyR1) and modulates their activity, suggesting that CLIC2 may function in the regulation of calcium release and signaling in cardiac and skeletal muscles.


Pssm-ID: 198331  Cd Length: 138  Bit Score: 228.61  E-value: 1.17e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKkDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 624
Cdd:cd10298   1 YKESFDVGSDIFAKFSAYIKNSP-ENNANQEKALLREFKRLDDYLNTPLPEEIDHDSAENITVSKRKFLDGDRLTLADCN 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAK 683
Cdd:cd10298  80 LLPKLHVIKVAAKKYCDFDIPADFTGVWRYLNNAYEREEFSQTCPADIEIEKAYASVAK 138
GST_C_CLIC1 cd10300
C-terminal, alpha helical domain of Chloride Intracellular Channel 1; Glutathione ...
 545-683 3.08e-69

C-terminal, alpha helical domain of Chloride Intracellular Channel 1; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 1 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Soluble CLIC1 is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity. CLIC1 is widely expressed in many tissues and its subcellular localization is dependent on cell type and cell cycle phase. It acts as a sensor of cell oxidation and appears to have a role in diseases that involve oxidative stress including tumorigenic and neurodegenerative diseases.


Pssm-ID: 198333  Cd Length: 139  Bit Score: 222.12  E-value: 3.08e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 624
Cdd:cd10300   1 NPESNTAGLDVFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDENSAEDEGVSQRKFLDGNELTLADCN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAK 683
Cdd:cd10300  81 LLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK 139
GST_C_CLIC cd03198
C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase ...
 545-679 2.95e-66

C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLICs (CLIC1-6 in vertebrates), p64, parchorin, and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. Biochemical studies of the Caenorhabditis elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. CLICs display structural plasticity, with CLIC1 adopting two soluble conformations. The structure of soluble human CLIC1 reveals that it is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved.


Pssm-ID: 198307  Cd Length: 119  Bit Score: 213.62  E-value: 2.95e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSplpdeidaystedvtvSGRKFLDGDELTLADCN 624
Cdd:cd03198   1 NPEANTAGEDLFAKFSAYIKNKDPAADEALRKALLKELSKLDAYLSS----------------SSRKFLDGDTLTLADCN 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYS 679
Cdd:cd03198  65 LLPKLHHIRVAGKAYKDFDIPDDFTGLWRYLKNAYETDEFTKTCPADQEIILHYK 119
GST_C_CLIC3 cd10299
C-terminal, alpha helical domain of Chloride Intracellular Channel 3; Glutathione ...
 545-679 2.81e-57

C-terminal, alpha helical domain of Chloride Intracellular Channel 3; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 3 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. CLIC3 is highly expressed in placental tissues, and may play a role in fetal development.


Pssm-ID: 198332  Cd Length: 133  Bit Score: 190.37  E-value: 2.81e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 545 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAysTEDVTVSGRKFLDGDELTLADCN 624
Cdd:cd10299   1 YKESNTAGNDVFHKFSAFIKNPVPAQDDALQKKLLRALLKLDSYLLTPLPHELAQ--NPHLSESQRRFLDGDALTLADCN 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27894378 625 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYS 679
Cdd:cd10299  79 LLPKLHIVKVVCKHYRQFEIPAELKGVTRYLDSASQEKEFKYTCPNSAEILLAYR 133
GST_N_CLIC cd03061
GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, ...
 450-538 3.00e-54

GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, parchorin and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division and apoptosis. They can exist in both water-soluble and membrane-bound states, and are found in various vesicles and membranes. Biochemical studies of the C. elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. The structure of soluble human CLIC1 reveals that it is monomeric and it adopts a fold similar to GSTs, containing an N-terminal domain with a TRX fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved.


Pssm-ID: 239359  Cd Length: 91  Bit Score: 180.65  E-value: 3.00e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 450 EHDITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFL 529
Cdd:cd03061   3 EPEIELFVKASSDGESIGNCPFCQRLFMVLWLKGVVFNVTTVDMKRKPEDLKDLAPGTQPPFLLYNGEVKTDNNKIEEFL 82


                ....*....
gi 27894378 530 EEKLAPPRY 538
Cdd:cd03061  83 EETLCPPKY 91
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 466-667 9.96e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 104.30  E-value: 9.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  466 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLAPpryPKLGTQh 545
Cdd:PLN02817  70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPD---PPLATP- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  546 PESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSPLPdeidaystedvtvsgrkFLDGDELTLADCNL 625
Cdd:PLN02817 146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 27894378  626 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 667
Cdd:PLN02817 207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
PLN02378 PLN02378
glutathione S-transferase DHAR1
 464-667 9.48e-19

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 85.53  E-value: 9.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  464 ESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKlapprYPKLGT 543
Cdd:PLN02378  15 DHLGDCPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEK-----YPDPPL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  544 QHP-ESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSplpdeidaystedvtvSGRKFLDGDELTLAD 622
Cdd:PLN02378  90 KTPaEFASVGSNIFGTFGTFLKS--KDSNDGSEHALLVELEALENHLKS----------------HDGPFIAGERVSAVD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 27894378  623 CNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 667
Cdd:PLN02378 152 LSLAPKLYHLQVALGHFKSWSVPESFPHVHNYMKTLFSLDSFEKT 196
GST_C_DHAR cd03201
C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) ...
 546-674 5.30e-17

C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) C-terminal domain family, Dehydroascorbate Reductase (DHAR) subfamily; composed of plant-specific DHARs, which are monomeric enzymes catalyzing the reduction of DHA into ascorbic acid (AsA) using glutathione as the reductant. DHAR allows plants to recycle oxidized AsA before it is lost. AsA serves as a cofactor of violaxanthin de-epoxidase in the xanthophyll cycle and as an antioxidant in the detoxification of reactive oxygen species. Because AsA is the major reductant in plants, DHAR serves to regulate their redox state. It has been suggested that a significant portion of DHAR activity is plastidic, acting to reduce the large amounts of ascorbate oxidized during hydrogen peroxide scavenging by ascorbate peroxidase. DHAR contains a conserved cysteine in its active site and in addition to its reductase activity, shows thiol transferase activity similar to glutaredoxins.


Pssm-ID: 198310  Cd Length: 121  Bit Score: 77.46  E-value: 5.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 546 PESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSPLPdeidaystedvtvsgrkFLDGDELTLADCNL 625
Cdd:cd03201   5 PEFASVGSKIFSTFVTFLKS--KDANDGSEQALLDELTALDEHLKTNGP-----------------FIAGEKITAVDLSL 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 27894378 626 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEI 674
Cdd:cd03201  66 APKLYHLRVALGHYKGWSVPESLTAVHKYMELLFSRESFKKTKAPDEMI 114
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 469-532 3.04e-11

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 59.18  E-value: 3.04e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27894378   469 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 532
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 2-420 8.61e-11

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 65.39  E-value: 8.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    2 AEAAEPEGVAPGPQGPPEVPAPlaeRPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHG 81
Cdd:PRK07764 389 GGAGAPAAAAPSAAAAAPAAAP---APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   82 ETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEA----QREPEDSAAPERQEEAEQRPEVPEGSASGEAG 157
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAatlrERWPEILAAVPKRSRKTWAILLPEATVLGVRG 545

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  158 DSVD---AEGPLGDNIEAEGPAGDSVEA-EGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAE 233
Cdd:PRK07764 546 DTLVlgfSTGGLARRFASPGNAEVLVTAlAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPA 625

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  234 GPAGDSVDAEGRVGDSVEA-GDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAiE 312
Cdd:PRK07764 626 APAPAGAAAAPAEASAAPApGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP-A 704

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  313 VAAGESAGRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEEE 392
Cdd:PRK07764 705 PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784

                        410       420
                 ....*....|....*....|....*...
gi 27894378  393 SPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PRK07764 785 MAEDDAPSMDDEDRRDAEEVAMELLEEE 812
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 11-441 2.65e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 63.85  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   11 APGPQGPPEVPAPLAERPGEPGAAGGEAEGPegsegAEEAPRGAAAVKEAGGGGPDRGPEAEARgTRGAHGETEAEEGAP 90
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRLGVAGGAGAP-----AAAAPSAAAAAPAAAPAPAAAAPAAAAA-PAPAAAPQPAPAPAP 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   91 EGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAE--QRPEVPEGSASGEAGDSVDAEGPLGD 168
Cdd:PRK07764 438 APAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPApaAAPAAPAAPAAPAGADDAATLRERWP 517

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  169 NI-EAEGPAGDSVEAEgrVGDSVDAEGPAGDSVD---AEGPLGDNIQAEGPAGDSVDA-----------EGRVGDSVDAE 233
Cdd:PRK07764 518 EIlAAVPKRSRKTWAI--LLPEATVLGVRGDTLVlgfSTGGLARRFASPGNAEVLVTAlaeelggdwqvEAVVGPAPGAA 595

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  234 GPAGDSVDAEGRVGDSVE--AGDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAI 311
Cdd:PRK07764 596 GGEGPPAPASSGPPEEAArpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGG 675

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  312 EVAAGESAGRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEE 391
Cdd:PRK07764 676 AAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP 755

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 27894378  392 ESPDSSPHGEAsRGAAEPEAQLSNHLAEEGPAEGSGEAARVNGRREDGEA 441
Cdd:PRK07764 756 AQPPPPPAPAP-AAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEV 804
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 25-273 3.35e-10

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 63.48  E-value: 3.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     25 AERPGEPGAAGGEAEGPEGSEGAEEAprgaaavkEAGGGGPDRGpEAEARGTRGAHGETEAE-EGAPEGAEVPQGGEETS 103
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENGEESGGEA--------EQEGETETKG-ENESEGEIPAERKGEQEgEGEIEAKEADHKGETEA 712

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    104 GAQQVEGASPGRGAQGEPRGEAQrepedsaapERQEEAEQrpevpEGSASGEAGDSVDAEgplGDNIEAEGPAGDSVEAE 183
Cdd:TIGR00927  713 EEVEHEGETEAEGTEDEGEIETG---------EEGEEVED-----EGEGEAEGKHEVETE---GDRKETEHEGETEAEGK 775

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    184 grvGDSVDAEGPAGDSVDAEGPLGDNIQAEG----PAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAG-DPAGD 258
Cdd:TIGR00927  776 ---EDEDEGEIQAGEDGEMKGDEGAEGKVEHegetEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKqDEKGV 852

                          250
                   ....*....|....*
gi 27894378    259 GVEAGVPAGDSVEAE 273
Cdd:TIGR00927  853 DGGGGSDGGDSEEEE 867
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 5-243 2.76e-09

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.78  E-value: 2.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378      5 AEPEgvAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEG-AEEAPRGAAavkEAGGGGPDRGpEAEARGTRGAH-GE 82
Cdd:TIGR00927  636 AEAE--HTGERTGEEGERPTEAEGENGEESGGEAEQEGETETkGENESEGEI---PAERKGEQEG-EGEIEAKEADHkGE 709

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     83 TEAEEGAPEGAEVPQGGE-ETSGAQQVEGASPGRGAQGEPRGEAQREPE-DSAAPERQEEAEQRPEVPEGSASGEAGDSV 160
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEdEGEIETGEEGEEVEDEGEGEAEGKHEVETEgDRKETEHEGETEAEGKEDEDEGEIQAGEDG 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    161 DAEGPLGDNIEAEGpagdsvEAEGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDA-EGRVGDSVDAEGPAGDS 239
Cdd:TIGR00927  790 EMKGDEGAEGKVEH------EGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAkQDEKGVDGGGGSDGGDS 863


                   ....
gi 27894378    240 VDAE 243
Cdd:TIGR00927  864 EEEE 867
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 9-204 6.72e-08

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 55.68  E-value: 6.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    9 GVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEG 88
Cdd:PRK12678  61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   89 AP----EGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEvPEGSASGEAGDSVDAEG 164
Cdd:PRK12678 141 AArkagEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD-RDRRDRREQGDRREERG 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 27894378  165 plgdNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSVDAEG 204
Cdd:PRK12678 220 ----RRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDG 255
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 468-530 8.47e-08

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 49.49  E-value: 8.47e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27894378 468 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPA-DLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLE 530
Cdd:cd00570   8 GSPRSLRVRLALEEKGLPYELVPVDLGEGEQeEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1-409 1.20e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.18  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     1 MAEAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAH 80
Cdd:PHA03307   13 AAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    81 GETEAEEGAPEGAEVPQGGEETSGaqqvEGASPGRGAQGEPRGEAQREPEDSAAPErqEEAEQRPEVPEGSASGEAGDSV 160
Cdd:PHA03307   93 STLAPASPAREGSPTPPGPSSPDP----PPPTPPPASPPPSPAPDLSEMLRPVGSP--GPPPAASPPAAGASPAAVASDA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   161 DAEGPLGDNIEAegpAGDSVEAEGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSV 240
Cdd:PHA03307  167 ASSRQAALPLSS---PEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   241 DAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAG-RARRVSGEPQQSGDGSLSPQAEAIEVAAGESA 319
Cdd:PHA03307  244 SSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSpRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   320 GRSPGELAWDAAEEAEV--PGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRE-RSPEGPREEEAAGGEEESPDS 396
Cdd:PHA03307  324 SSSSSTSSSSESSRGAAvsPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASaGRPTRRRARAAVAGRARRRDA 403

                         410
                  ....*....|...
gi 27894378   397 SPHGEASRGAAEP 409
Cdd:PHA03307  404 TGRFPAGRPRPSP 416
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 55-259 3.41e-07

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 53.75  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   55 AAVKEAGGGG----PDRGPEAEARGTRGAHGETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPE 130
Cdd:PRK12678  53 AAIKEARGGGaaaaAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  131 DSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSvDAEGPLGDNI 210
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQ 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 27894378  211 QAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDG 259
Cdd:PRK12678 212 GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGG 260
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 52-328 4.12e-07

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 53.46  E-value: 4.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     52 RGAAAVKEAGGGGPDRGPEAEARGTR-GAHGETEAEEGAPEG------AEVPQGGEETSGAQQvEGASPGRGaQGEPRGE 124
Cdd:TIGR00927  619 RPVAKVMALGDLSKGDVAEAEHTGERtGEEGERPTEAEGENGeesggeAEQEGETETKGENES-EGEIPAER-KGEQEGE 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    125 AQREPE------DSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNiEAEGPAGDSVEAEGRVGDSVDAEGPAGD 198
Cdd:TIGR00927  697 GEIEAKeadhkgETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEG-EAEGKHEVETEGDRKETEHEGETEAEGK 775

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    199 SVDAEGplgdNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAegpAGD 278
Cdd:TIGR00927  776 EDEDEG----EIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEA---KQD 848

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 27894378    279 SMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAW 328
Cdd:TIGR00927  849 EKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEW 898
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1-198 2.14e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.14  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    1 MAEAAEPEGVAPGPQGPPEVPAPlaerPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGtrgah 80
Cdd:PRK07764 607 GPPEEAARPAAPAAPAAPAAPAP----AGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA----- 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   81 geTEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSV 160
Cdd:PRK07764 678 --PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP 755

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 27894378  161 DAEGPLGDNIEAEGPAGDS--VEAEGRVGDSVDAEGPAGD 198
Cdd:PRK07764 756 AQPPPPPAPAPAAAPAAAPppSPPSEEEEMAEDDAPSMDD 795
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
3-179 3.70e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 50.23  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    3 EAAEPEGVAPGPQGPPE----VPAPLAERPGEPGAAGGEAEGP-EGSEGAEEAPRGAAAVKEAGGGGPDRGPE---AEAR 74
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARvagaVPAPGARAAAAVGASAVPAVTAvTGAAGAALAPKAAAAAAATRAEAPPAAPAppaTADR 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   75 GTRGAHGETEAEEGAPEGAEVPQGGEEtSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPErQEEAEQRPEVPEGSASG 154
Cdd:PRK07003 439 GDDAADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEPAPRAAAP-SAATPAAVPDARAPAAA 516

                        170       180
                 ....*....|....*....|....*
gi 27894378  155 EAGDSVDAEGPLGDNIEAEGPAGDS 179
Cdd:PRK07003 517 SREDAPAAAAPPAPEARPPTPAAAA 541
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1-409 4.51e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     1 MAEAAEPEGVAPGPQGPPEVPAPLAERPGEPGA-AGGEAEGPEGSEGAEEAPRGAaavkEAGGGGPDRGPE-AEARGTRG 78
Cdd:PHA03307   67 PPTGPPPGPGTEAPANESRSTPTWSLSTLAPASpAREGSPTPPGPSSPDPPPPTP----PPASPPPSPAPDlSEMLRPVG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    79 AHGETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGD 158
Cdd:PHA03307  143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   159 SvdaegplgdnieaegpagDSVEAEGRVGDSVDAEGPAGDSVDAEGPLGDNiqaEGPAGDSVDAEGRVGDSVDAEGPAGD 238
Cdd:PHA03307  223 A------------------PGRSAADDAGASSSDSSSSESSGCGWGPENEC---PLPRPAPITLPTRIWEASGWNGPSSR 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   239 SVDAEGRVGDSVEAGDPA---GDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAA 315
Cdd:PHA03307  282 PGPASSSSSPRERSPSPSpssPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   316 GESAGRSPgelawDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEdeerRERSPEGPREEEAAGGEEESPD 395
Cdd:PHA03307  362 PSSPRKRP-----RPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAG----RPRPSPLDAGAASGAFYARYPL 432

                         410
                  ....*....|....
gi 27894378   396 SSPHGEASRGAAEP 409
Cdd:PHA03307  433 LTPSGEPWPGSPPP 446
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 232-444 2.69e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 47.59  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  232 AEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAgDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAI 311
Cdd:PRK12678  73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPA-ARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQ 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  312 EVAAGESAGRSPGELAwDAAEEAEVPGVKGSEEAAPGDARADaGEDRVGDGPQQEPGEDEERRERSPEGPReeEAAGGEE 391
Cdd:PRK12678 152 PATEARADAAERTEEE-ERDERRRRGDREDRQAEAERGERGR-REERGRDGDDRDRRDRREQGDRREERGR--RDGGDRR 227

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 27894378  392 ESPDSSPHGEASRGAAEPEAQLSNHLAEEGPAEGSGEAARVNGRREDGEASEP 444
Cdd:PRK12678 228 GRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGG 280
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 469-530 2.82e-05

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. Like Omega enzymes, proteins in this subfamily contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 42.35  E-value: 2.82e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27894378 469 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVktdvnkIEEFLE 530
Cdd:cd03060   9 CPYAMRARMALLLAGITVELREVELKNKPAEMLAASPkGTVPVLVLGNGTV------IEESLD 65
PHA03169 PHA03169
hypothetical protein; Provisional
 3-202 2.85e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.89  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    3 EAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGgpdRGPEAEARGTRGAHGE 82
Cdd:PHA03169  31 EQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGG---PSGSGSESVGSPTPSP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   83 TEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREpEDSAAPERQEEAEQRPEVPEGSASGEAGDSVD- 161
Cdd:PHA03169 108 SGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE-SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPe 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 27894378  162 ---AEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSVDA 202
Cdd:PHA03169 187 pdsPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
PHA03169 PHA03169
hypothetical protein; Provisional
 2-182 4.33e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.50  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    2 AEAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGG--------EAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEA 73
Cdd:PHA03169  41 ARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETaeesrhgeKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   74 RGTRGAHGETEAEEGAPEGAEvPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPE--DSAAPERQEEAEQRPEVPEGS 151
Cdd:PHA03169 121 ENTSGSSPESPASHSPPPSPP-SHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEepEPPTSEPEPDSPGPPQSETPT 199

                        170       180       190
                 ....*....|....*....|....*....|.
gi 27894378  152 ASGEAGDSVDAEGPLGDNIEAEGPAGDSVEA 182
Cdd:PHA03169 200 SSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
2-153 6.01e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.38  E-value: 6.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    2 AEAAEPEGVAPGPQGPPEVPAplaeRPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHG 81
Cdd:PRK07003 407 GAALAPKAAAAAAATRAEAPP----AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPAS 482

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27894378   82 ETEAEegAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPErqEEAEQRPEVPEGSAS 153
Cdd:PRK07003 483 DAPPD--AAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPP--TPAAAAPAARAGGAA 550
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 2-193 6.55e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    2 AEAAEPEGVAPGPQGPPEVPAPLAERPGEPGAA---GGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRG 78
Cdd:PRK07764 631 GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdggDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP 710

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   79 AHGeteAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGD 158
Cdd:PRK07764 711 AGQ---ADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE 787

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 27894378  159 SVDAEGPLGDNIEAEGPAGDSVEAE--GRVGDSVDAE 193
Cdd:PRK07764 788 DDAPSMDDEDRRDAEEVAMELLEEElgAKKIEEFAAD 824
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 522-645 6.55e-05

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 42.49  E-value: 6.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 522 VNKIEEFLEEKLAPPRYPKLGTQhpesnsagndvfakfsAFIKNTKKDANEIHEKNLLKALRKLDNYLnsplpdeidays 601
Cdd:cd00299   1 VRALEDWADATLAPPLVRLLYLE----------------KVPLPKDEAAVEAAREELPALLAALEQLL------------ 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 27894378 602 tedvtvSGRKFLDGDELTLADCNLLPKLHIIKIVAKKYRDFE-FP 645
Cdd:cd00299  53 ------AGRPYLAGDQFSLADVALAPVLARLEALGPYYDLLDeYP 91
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 25-184 7.07e-05

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 45.74  E-value: 7.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   25 AERPGEPGAAGGEAEGPEGSEGAeeaprgAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEGApegAEVPQGGEETSG 104
Cdd:PRK13108 292 VDEALEREPAELAAAAVASAASA------VGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVV---QVADRDGESTPA 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  105 AQQVEGASPGRGAQGEPRGEAQREPEDSA---APERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDN-IEAEGPAGDSV 180
Cdd:PRK13108 363 VEETSEADIEREQPGDLAGQAPAAHQVDAeaaSAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDeLAVAGPGDDPA 442


                 ....
gi 27894378  181 EAEG 184
Cdd:PRK13108 443 EPDG 446
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 302-468 8.42e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 46.14  E-value: 8.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    302 GSLSPQAEAIEVAAGEsagRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGP 381
Cdd:TIGR00927  628 GDLSKGDVAEAEHTGE---RTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA 704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    382 REEEAAGGEEESPDSSPHGEASRGAAEPEAQLSNHLAE---EGPAEGSGEAARVNGRREDGEASEPRALGQEHDITLFVK 458
Cdd:TIGR00927  705 DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEdegEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ 784

                          170
                   ....*....|
gi 27894378    459 AGYDGESIGN 468
Cdd:TIGR00927  785 AGEDGEMKGD 794
PHA03169 PHA03169
hypothetical protein; Provisional
 26-222 1.15e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   26 ERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEagggGPDRGPEAEARGTRGAHGETEAE-EGAPEGAEVPQGGEET-- 102
Cdd:PHA03169  31 EQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQ----GHRQTESDTETAEESRHGEKEERgQGGPSGSGSESVGSPTps 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  103 -SGAQQV--EGASPGRGAQGEPRGEAQREPeDSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNIEAEGPAGDS 179
Cdd:PHA03169 107 pSGSAEElaSGLSPENTSGSSPESPASHSP-PPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 27894378  180 VEAEGRVGDSVDAE--GPAGDSVDAEGPLGDNIQAEGPAGDSVDA 222
Cdd:PHA03169 186 EPDSPGPPQSETPTssPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
PHA03169 PHA03169
hypothetical protein; Provisional
 185-409 1.88e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.58  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  185 RVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDpAGDGVEAGV 264
Cdd:PHA03169  26 HGGTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGS-GSESVGSPT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  265 PAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWDAAEEAEVPGVKGSEE 344
Cdd:PHA03169 105 PSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSE 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27894378  345 AAPGDARADAGEDRVGDGPQQEPGeDEERRERSPEGPREEEAAGGEEESPDSSPHGEASRGAAEP 409
Cdd:PHA03169 185 PEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 177-447 2.24e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.60  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    177 GDSVEAEGRvGDSVDAEGPAgdSVDAEGPLGDniQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPA 256
Cdd:TIGR00927  633 GDVAEAEHT-GERTGEEGER--PTEAEGENGE--ESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHK 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    257 GDGVEAGVPAGDSVEAEGPA--------------GDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRS 322
Cdd:TIGR00927  708 GETEAEEVEHEGETEAEGTEdegeietgeegeevEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGE 787

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    323 PGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEeespdssphGEA 402
Cdd:TIGR00927  788 DGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGG---------GGS 858

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 27894378    403 SRGAAEPEAQLSNHLAEEGPAEGSGEaarvngrREDGEASEPRAL 447
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEE-------EEEEENEEPLSL 896
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 115-290 2.75e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.81  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  115 RGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGeAGDSVDAEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEG 194
Cdd:PRK13108 286 RGSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQ-PDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  195 PAgDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEG 274
Cdd:PRK13108 365 ET-SEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAE 443

                        170
                 ....*....|....*.
gi 27894378  275 PAGDSMDAEGPAGRAR 290
Cdd:PRK13108 444 PDGIRRQDDFSSRRRR 459
PHA03378 PHA03378
EBNA-3B; Provisional
 5-121 2.75e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    5 AEPEGVAPGPQGPPEVPaPLAERPgePGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAhgETE 84
Cdd:PHA03378 694 MQPPPRAPTPMRPPAAP-PGRAQR--PAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRAR--PPA 768

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 27894378   85 AEEGAPEGAEVPQGGeeTSGAQQVEGA-SPGRGAQGEP 121
Cdd:PHA03378 769 AAPGAPTPQPPPQAP--PAPQQRPRGApTPQPPPQAGP 804
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 468-532 3.07e-04

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 39.62  E-value: 3.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27894378 468 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDgEVKTDVNKIEEFLEEK 532
Cdd:cd03059   8 DDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPyGTVPTLVDRD-LVLYESRIIMEYLDER 72
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
469-537 5.44e-04

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 39.13  E-value: 5.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27894378   469 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLAPPR 537
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 25-149 1.55e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     25 AERPGEPGAAGGEAEGPEGS-EGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEGAPEGAEVPQGGEETS 103
Cdd:TIGR00927  759 GDRKETEHEGETEAEGKEDEdEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELN 838

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 27894378    104 GAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPE 149
Cdd:TIGR00927  839 AENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEE 884
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 267-453 1.75e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    267 GDSVEAEGpAGDSMDAEGPagRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWD-------AAEEAEVPGV 339
Cdd:TIGR00927  633 GDVAEAEH-TGERTGEEGE--RPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEqegegeiEAKEADHKGE 709

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    340 KGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEEESPDSSPHGEASRGAAEPEAQLsnHLAE 419
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEI--QAGE 787

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 27894378    420 EGPAEG-SGEAARVNGRREDGEASEPRALGQEHDI 453
Cdd:TIGR00927  788 DGEMKGdEGAEGKVEHEGETEAGEKDEHEGQSETQ 822
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 111-436 2.62e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   111 ASPGRGAQGEPRGEAQREPE-DSAAPERQEEAEQRPEVPEGSASGEAGDSvDAEGPLGDNIEAEGPAGDSVEAEGRVGDS 189
Cdd:PHA03307   62 CDRFEPPTGPPPGPGTEAPAnESRSTPTWSLSTLAPASPAREGSPTPPGP-SSPDPPPPTPPPASPPPSPAPDLSEMLRP 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   190 VDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAegRVGDSVDAEGPAGDSVDAEgrVGDSVEAGDPAGDGVEAGVPAGDS 269
Cdd:PHA03307  141 VGSPGPPPAASPPAAGASPAAVASDAASSRQAA--LPLSSPEETARAPSSPPAE--PPPSTPPAAASPRPPRRSSPISAS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   270 VEAEGPAGDSMDAeGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWDAAEEAEVPgvKGSEEAAPGD 349
Cdd:PHA03307  217 ASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPG--PASSSSSPRE 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   350 ARADAGEDRVGDGP---------QQEPGEDEERRERSPEGPREEEAAGGEEESPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PHA03307  294 RSPSPSPSSPGSGPapssprassSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSR 373

                         330
                  ....*....|....*.
gi 27894378   421 GPAEGSGEAARVNGRR 436
Cdd:PHA03307  374 APSSPAASAGRPTRRR 389
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 12-167 2.97e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 40.66  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   12 PGPQGPPEVPAPLAERpGEPGAAGGEAEGPEGSEGAEEAPRGAAAVK-EAGGGGPdRGPEAE--ARGTRGAHGET-EAEE 87
Cdd:NF038329 122 PGPAGPAGPAGEQGPR-GDRGETGPAGPAGPPGPQGERGEKGPAGPQgEAGPQGP-AGKDGEagAKGPAGEKGPQgPRGE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   88 GAPEGAEVPQG-----GEETSGAQQVEGASPGRGAQGePRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSVDA 162
Cdd:NF038329 200 TGPAGEQGPAGpagpdGEAGPAGEDGPAGPAGDGQQG-PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278


                 ....*.
gi 27894378  163 E-GPLG 167
Cdd:NF038329 279 ErGPVG 284
PHA03169 PHA03169
hypothetical protein; Provisional
 3-155 3.98e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    3 EAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRG-----PEAEARGTR 77
Cdd:PHA03169  98 ESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPssflqPSHEDSPEE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   78 GAHGETEAEEGAPEGAEVPQGGEETSGAQQVEGASP-----GRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSA 152
Cdd:PHA03169 178 PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEpqsptPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTV 257


                 ...
gi 27894378  153 SGE 155
Cdd:PHA03169 258 VGW 260
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
468-673 4.00e-03

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 39.11  E-value: 4.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 468 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEKLAPPR-YP 539
Cdd:COG0625   9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAERYPEPPlLP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 540 KLGTQHPE--------SNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLnsplpdeidaystedvtvSGRK 611
Cdd:COG0625  85 ADPAARARvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL------------------AGGP 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27894378 612 FLDGDELTLADCNLLPKLHIIkivakkyRDFEFP-SEMTGIWRYLNNAYARDEFTNTCPADQE 673
Cdd:COG0625 147 YLAGDRFSIADIALAPVLRRL-------DRLGLDlADYPNLAAWLARLAARPAFQRALAAAEP 202
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 3-166 4.24e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.36  E-value: 4.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378      3 EAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGG--GGPDRGPEAEARGTRGAH 80
Cdd:TIGR00927  719 GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEdeGEIQAGEDGEMKGDEGAE 798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378     81 GETEAEEGAPEGAEVpQGGEETSGAQQVEGASPGRGAQ---GEPRGEAQREPE--------DSAAPERQEEAEQRPEVPE 149
Cdd:TIGR00927  799 GKVEHEGETEAGEKD-EHEGQSETQADDTEVKDETGEQelnAENQGEAKQDEKgvdggggsDGGDSEEEEEEEEEEEEEE 877

                          170
                   ....*....|....*..
gi 27894378    150 GSASGEAGDSVDAEGPL 166
Cdd:TIGR00927  878 EEEEEEEEEEEENEEPL 894
motB PRK05996
MotB family protein;
29-157 4.39e-03

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 40.07  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   29 GEPGAA-GGEAEGPEGSEgAEEAP------RGAAAVKEAGGGGPdrgPEAEARGTRGAHGETEAEEGAPEGAEVPQGGEE 101
Cdd:PRK05996 158 GDGGAAqSGPATGADGGE-AYRDPfdpdfwSKQVEVTTAGDLLP---PGQAREQAQGAKSATAAPATVPQAAPLPQAQPK 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 27894378  102 TSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSA-SGEAG 157
Cdd:PRK05996 234 KAATEEELIADAKKAATGEPAANAAKAAKPEPMPDDQQKEAEQLQAAIAQAiGGVAG 290
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2-148 4.86e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 4.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378    2 AEAAEPEGVAPGPQGPP--EVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGA 79
Cdd:PRK12323 413 AAAARAVAAAPARRSPApeALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPA 492

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   80 HGETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGE-AQREPEDSAAPERQEEAEQRPEVP 148
Cdd:PRK12323 493 DDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAfETLAPAPAAAPAPRAAAATEPVVA 562
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
21-199 6.11e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   21 PAPLAerpGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEGAPEGAEVP---- 96
Cdd:PRK07003 360 PAVTG---GGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPpata 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   97 -QGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNIE-AEG 174
Cdd:PRK07003 437 dRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARApAAA 516

                        170       180
                 ....*....|....*....|....*
gi 27894378  175 PAGDSVEAEGRVGDSVDAEGPAGDS 199
Cdd:PRK07003 517 SREDAPAAAAPPAPEARPPTPAAAA 541
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
 576-668 6.39e-03

C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.


Pssm-ID: 198299 [Multi-domain]  Cd Length: 142  Bit Score: 37.55  E-value: 6.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378 576 KNLLKALRKLDNYLnsplpdeidaystedvtvSGRKFLDGDELTLADCNLLPKL--------HIIKIVAKKYRDfeFPSe 647
Cdd:cd03190  40 KELFEALDKLEKRL------------------SKQPYLLGDRLTEADIRLFTTLirfdpvyhQHFKCNLKTIRD--YPN- 98

                        90       100
                ....*....|....*....|.
gi 27894378 648 mtgIWRYLNNAYARDEFTNTC 668
Cdd:cd03190  99 ---LWRYLRRLYQNPGVFETT 116
PHA03378 PHA03378
EBNA-3B; Provisional
 12-141 7.20e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   12 PGPQGP----PEVPAPLAERPgePGAAGGEAEGPEGSEGAEEAPRGAAavkeaGGGGPDRGPEAEARGTRGAHGETEAEE 87
Cdd:PHA03378 676 PSPTGAntmlPIQWAPGTMQP--PPRAPTPMRPPAAPPGRAQRPAAAT-----GRARPPAAAPGRARPPAAAPGRARPPA 748

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 27894378   88 GAPEGAEVPQGGeetSGAQQVEGASPGRGA-QGEPRG--EAQREPEDSAAPERQEEA 141
Cdd:PHA03378 749 AAPGRARPPAAA---PGRARPPAAAPGAPTpQPPPQAppAPQQRPRGAPTPQPPPQA 802
PHA03169 PHA03169
hypothetical protein; Provisional
 54-277 7.44e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 7.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378   54 AAAVKEAGGGGPDRGPEAEARGTRGaHGETEAEEgapEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSA 133
Cdd:PHA03169  41 ARAAKPAPPAPTTSGPQVRAVAEQG-HRQTESDT---ETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELAS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  134 APERQEEAEQRPEvpegsasGEAGDSVDAEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSVDAEGPLGDNIQAE 213
Cdd:PHA03169 117 GLSPENTSGSSPE-------SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDS 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27894378  214 GPAGDSVDAegrvGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEGPAG 277
Cdd:PHA03169 190 PGPPQSETP----TSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 469-530 9.13e-03

GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 239353 [Multi-domain]  Cd Length: 89  Bit Score: 35.79  E-value: 9.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27894378 469 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVKTDVNKIEEFLE 530
Cdd:cd03055  27 CPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPqGKVPALEIDEGKVVYESLIICEYLD 89
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 261-438 9.25e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 39.19  E-value: 9.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  261 EAGVPAGDSVEAEGPAGDSMDAeGPAGrarrvSGEPQQSGDGSLSPQAEAIEVAAGESAgRSPGELAWDAAEEAEVPgvk 340
Cdd:PRK13108 294 EALEREPAELAAAAVASAASAV-GPVG-----PGEPNQPDDVAEAVKAEVAEVTDEVAA-ESVVQVADRDGESTPAV--- 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894378  341 gsEEAAPGDARADAGEDRVGDGPQqEPGEDEERRERSPEGPreeeaAGGEEESPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PRK13108 364 --EETSEADIEREQPGDLAGQAPA-AHQVDAEAASAAPEEP-----AALASEAHDETEPEVPEKAAPIPDPAKPDELAVA 435

                        170       180
                 ....*....|....*....|....
gi 27894378  421 GPA------EGSGEAARVNGRRED 438
Cdd:PRK13108 436 GPGddpaepDGIRRQDDFSSRRRR 459
 
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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