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Conserved domains on  [gi|948549898|ref|NP_001303938|]
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chloride intracellular channel protein 6 isoform 1 [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. ...
471-704 9.46e-144

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: 419.27  E-value: 9.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  471 IKKYLRAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 550
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  551 LAPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKF 630
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948549898  631 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRMK 704
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
9-382 4.84e-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: 66.16  E-value: 4.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   9 GVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAvkeaggggPDRGPEAEARGTRGAHGETEAEEG 88
Cdd:PRK07764 391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPA--------PAPPSPAGNAPAGGAPSPPPAAAP 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  89 APEGAEVPQGGEETSGAQQVEGASPGRGAQgeprgeAQREPEDSAAPERQEEAEQR----PEV----------------P 148
Cdd:PRK07764 463 SAQPAPAPAAAPEPTAAPAPAPPAAPAPAA------APAAPAAPAAPAGADDAATLrerwPEIlaavpkrsrktwaillP 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 149 EGSASGEAGDSVD---AEGPLGDN---------------------------IEAEGPAGDSVEAEGRVGDSVDAEGPAGD 198
Cdd:PRK07764 537 EATVLGVRGDTLVlgfSTGGLARRfaspgnaevlvtalaeelggdwqveavVGPAPGAAGGEGPPAPASSGPPEEAARPA 616
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 199 SVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEGPAGD 278
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGA 696
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 279 SMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWDAAEEAEVPGvKGSEEAAPGDARADAGEDR 358
Cdd:PRK07764 697 APAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA-QPPPPPAPAPAAAPAAAPP 775
                        410       420
                 ....*....|....*....|....
gi 948549898 359 VGDGPQQEPGEDEERRERSPEGPR 382
Cdd:PRK07764 776 PSPPSEEEEMAEDDAPSMDDEDRR 799
 
Name Accession Description Interval E-value
O-ClC TIGR00862
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ...
471-704 9.46e-144

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: 419.27  E-value: 9.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  471 IKKYLRAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 550
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  551 LAPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKF 630
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948549898  631 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRMK 704
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
563-702 7.12e-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: 7.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 642
Cdd:cd10301    1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKR 702
Cdd:cd10301   81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
484-685 8.32e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 104.30  E-value: 8.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 484 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLAPpryPKLGTQh 563
Cdd:PLN02817  70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPD---PPLATP- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 564 PESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSPLPdeidaystedvtvsgrkFLDGDELTLADCNL 643
Cdd:PLN02817 146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 948549898 644 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 685
Cdd:PLN02817 207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
487-550 3.12e-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: 3.12e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948549898  487 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 550
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
9-382 4.84e-11

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 66.16  E-value: 4.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   9 GVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAvkeaggggPDRGPEAEARGTRGAHGETEAEEG 88
Cdd:PRK07764 391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPA--------PAPPSPAGNAPAGGAPSPPPAAAP 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  89 APEGAEVPQGGEETSGAQQVEGASPGRGAQgeprgeAQREPEDSAAPERQEEAEQR----PEV----------------P 148
Cdd:PRK07764 463 SAQPAPAPAAAPEPTAAPAPAPPAAPAPAA------APAAPAAPAAPAGADDAATLrerwPEIlaavpkrsrktwaillP 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 149 EGSASGEAGDSVD---AEGPLGDN---------------------------IEAEGPAGDSVEAEGRVGDSVDAEGPAGD 198
Cdd:PRK07764 537 EATVLGVRGDTLVlgfSTGGLARRfaspgnaevlvtalaeelggdwqveavVGPAPGAAGGEGPPAPASSGPPEEAARPA 616
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 199 SVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEGPAGD 278
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGA 696
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 279 SMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWDAAEEAEVPGvKGSEEAAPGDARADAGEDR 358
Cdd:PRK07764 697 APAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA-QPPPPPAPAPAAAPAAAPP 775
                        410       420
                 ....*....|....*....|....
gi 948549898 359 VGDGPQQEPGEDEERRERSPEGPR 382
Cdd:PRK07764 776 PSPPSEEEEMAEDDAPSMDDEDRR 799
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
25-273 2.16e-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: 64.25  E-value: 2.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    25 AERPGEPGAAGGEAEGPEGSEGAEEAprgaaavkEAGGGGPDRGpEAEARGTRGAHGETEAE-EGAPEGAEVPQGGEETS 103
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENGEESGGEA--------EQEGETETKG-ENESEGEIPAERKGEQEgEGEIEAKEADHKGETEA 712
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   104 GAQQVEGASPGRGAQGEPRGEAQrepedsaapERQEEAEQrpevpEGSASGEAGDSVDAEgplGDNIEAEGPAGDSVEAE 183
Cdd:TIGR00927  713 EEVEHEGETEAEGTEDEGEIETG---------EEGEEVED-----EGEGEAEGKHEVETE---GDRKETEHEGETEAEGK 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   184 grvGDSVDAEGPAGDSVDAEGPLGDNIQAEG----PAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAG-DPAGD 258
Cdd:TIGR00927  776 ---EDEDEGEIQAGEDGEMKGDEGAEGKVEHegetEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKqDEKGV 852
                          250
                   ....*....|....*
gi 948549898   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 1.54e-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: 41.43  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  12 PGPQGPPEVPAPLAERpGEPGAAGGEAEGPEGSEGAEEAPRGAAAVK-EAGGGGPdRGPEAE--ARGTRGAHGET-EAEE 87
Cdd:NF038329 122 PGPAGPAGPAGEQGPR-GDRGETGPAGPAGPPGPQGERGEKGPAGPQgEAGPQGP-AGKDGEagAKGPAGEKGPQgPRGE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  88 GAPEGAEVPQG-----GEETSGAQQVEGASPGRGAQGePRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSVDA 162
Cdd:NF038329 200 TGPAGEQGPAGpagpdGEAGPAGEDGPAGPAGDGQQG-PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                 ....*.
gi 948549898 163 E-GPLG 167
Cdd:NF038329 279 ErGPVG 284
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
486-691 3.60e-03

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 39.49  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 486 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEKLAPPR-YP 557
Cdd:COG0625    9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAERYPEPPlLP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 558 KLGTQHPE--------SNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLnsplpdeidaystedvtvSGRK 629
Cdd:COG0625   85 ADPAARARvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL------------------AGGP 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948549898 630 FLDGDELTLADCNLLPKLHIIkivakkyRDFEFP-SEMTGIWRYLNNAYARDEFTNTCPADQE 691
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. ...
471-704 9.46e-144

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: 419.27  E-value: 9.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  471 IKKYLRAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 550
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  551 LAPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKF 630
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948549898  631 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRMK 704
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
563-702 7.12e-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: 7.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 642
Cdd:cd10301    1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKR 702
Cdd:cd10301   81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
GST_C_CLIC4 cd10296
C-terminal, alpha helical domain of Chloride Intracellular Channel 4; Glutathione ...
563-703 1.44e-86

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: 1.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 642
Cdd:cd10296    1 HPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLDGNEMTLADCN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRM 703
Cdd:cd10296   81 LLPKLHIVKVVAKKYRNFEIPKEMTGIWRYLSNAYSRDEFTNTCPSDKEIEIAYSDVAKRL 141
GST_C_CLIC5 cd10297
C-terminal, alpha helical domain of Chloride Intracellular Channel 5; Glutathione ...
563-703 5.73e-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: 5.73e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 642
Cdd:cd10297    1 HRESNTAGIDIFSKFSAYIKNTKQQANAALEKGLTKALKKLDDYLNTPLPEEIDADSTEEEKVSNRKFLDGDELTLADCN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAKRM 703
Cdd:cd10297   81 LLPKLHVVKIVAKKYRNFEIPSDMTGVWRYLKNAYARDEFTNTCAADKEIELAYADVAKRL 141
GST_C_CLIC2 cd10298
C-terminal, alpha helical domain of Chloride Intracellular Channel 2; Glutathione ...
563-701 1.44e-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: 1.44e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKkDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 642
Cdd:cd10298    1 YKESFDVGSDIFAKFSAYIKNSP-ENNANQEKALLREFKRLDDYLNTPLPEEIDHDSAENITVSKRKFLDGDRLTLADCN 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAK 701
Cdd:cd10298   80 LLPKLHVIKVAAKKYCDFDIPADFTGVWRYLNNAYEREEFSQTCPADIEIEKAYASVAK 138
GST_C_CLIC1 cd10300
C-terminal, alpha helical domain of Chloride Intracellular Channel 1; Glutathione ...
563-701 3.32e-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: 222.51  E-value: 3.32e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAYSTEDVTVSGRKFLDGDELTLADCN 642
Cdd:cd10300    1 NPESNTAGLDVFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDENSAEDEGVSQRKFLDGNELTLADCN 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDVAK 701
Cdd:cd10300   81 LLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK 139
GST_C_CLIC cd03198
C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase ...
563-697 3.98e-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: 3.98e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSplpdeidaystedvtvSGRKFLDGDELTLADCN 642
Cdd:cd03198    1 NPEANTAGEDLFAKFSAYIKNKDPAADEALRKALLKELSKLDAYLSS----------------SSRKFLDGDTLTLADCN 64
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYS 697
Cdd:cd03198   65 LLPKLHHIRVAGKAYKDFDIPDDFTGLWRYLKNAYETDEFTKTCPADQEIILHYK 119
GST_C_CLIC3 cd10299
C-terminal, alpha helical domain of Chloride Intracellular Channel 3; Glutathione ...
563-697 3.58e-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: 3.58e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 563 HPESNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLNSPLPDEIDAysTEDVTVSGRKFLDGDELTLADCN 642
Cdd:cd10299    1 YKESNTAGNDVFHKFSAFIKNPVPAQDDALQKKLLRALLKLDSYLLTPLPHELAQ--NPHLSESQRRFLDGDALTLADCN 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 948549898 643 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYS 697
Cdd:cd10299   79 LLPKLHIVKVVCKHYRQFEIPAELKGVTRYLDSASQEKEFKYTCPNSAEILLAYR 133
GST_N_CLIC cd03061
GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, ...
471-556 4.50e-51

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: 172.17  E-value: 4.50e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 471 IKKYLRAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 550
Cdd:cd03061    6 IELFVKASSDGESIGNCPFCQRLFMVLWLKGVVFNVTTVDMKRKPEDLKDLAPGTQPPFLLYNGEVKTDNNKIEEFLEET 85

                 ....*.
gi 948549898 551 LAPPRY 556
Cdd:cd03061   86 LCPPKY 91
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
484-685 8.32e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 104.30  E-value: 8.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 484 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLAPpryPKLGTQh 563
Cdd:PLN02817  70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPD---PPLATP- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 564 PESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSPLPdeidaystedvtvsgrkFLDGDELTLADCNL 643
Cdd:PLN02817 146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 948549898 644 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 685
Cdd:PLN02817 207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
PLN02378 PLN02378
glutathione S-transferase DHAR1
482-685 7.64e-19

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 85.53  E-value: 7.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 482 ESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKlapprYPKLGT 561
Cdd:PLN02378  15 DHLGDCPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEK-----YPDPPL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 562 QHP-ESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSplpdeidaystedvtvSGRKFLDGDELTLAD 640
Cdd:PLN02378  90 KTPaEFASVGSNIFGTFGTFLKS--KDSNDGSEHALLVELEALENHLKS----------------HDGPFIAGERVSAVD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 948549898 641 CNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 685
Cdd:PLN02378 152 LSLAPKLYHLQVALGHFKSWSVPESFPHVHNYMKTLFSLDSFEKT 196
GST_C_DHAR cd03201
C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) ...
564-692 5.14e-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: 5.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 564 PESNSAGNDVFAKFSAFIKNtkKDANEIHEKNLLKALRKLDNYLNSPLPdeidaystedvtvsgrkFLDGDELTLADCNL 643
Cdd:cd03201    5 PEFASVGSKIFSTFVTFLKS--KDANDGSEQALLDELTALDEHLKTNGP-----------------FIAGEKITAVDLSL 65
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 948549898 644 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEI 692
Cdd:cd03201   66 APKLYHLRVALGHYKGWSVPESLTAVHKYMELLFSRESFKKTKAPDEMI 114
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
487-550 3.12e-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: 3.12e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948549898  487 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 550
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
9-382 4.84e-11

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 66.16  E-value: 4.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   9 GVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAvkeaggggPDRGPEAEARGTRGAHGETEAEEG 88
Cdd:PRK07764 391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPA--------PAPPSPAGNAPAGGAPSPPPAAAP 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  89 APEGAEVPQGGEETSGAQQVEGASPGRGAQgeprgeAQREPEDSAAPERQEEAEQR----PEV----------------P 148
Cdd:PRK07764 463 SAQPAPAPAAAPEPTAAPAPAPPAAPAPAA------APAAPAAPAAPAGADDAATLrerwPEIlaavpkrsrktwaillP 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 149 EGSASGEAGDSVD---AEGPLGDN---------------------------IEAEGPAGDSVEAEGRVGDSVDAEGPAGD 198
Cdd:PRK07764 537 EATVLGVRGDTLVlgfSTGGLARRfaspgnaevlvtalaeelggdwqveavVGPAPGAAGGEGPPAPASSGPPEEAARPA 616
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 199 SVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEGPAGD 278
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGA 696
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 279 SMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWDAAEEAEVPGvKGSEEAAPGDARADAGEDR 358
Cdd:PRK07764 697 APAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA-QPPPPPAPAPAAAPAAAPP 775
                        410       420
                 ....*....|....*....|....
gi 948549898 359 VGDGPQQEPGEDEERRERSPEGPR 382
Cdd:PRK07764 776 PSPPSEEEEMAEDDAPSMDDEDRR 799
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-420 5.10e-11

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 66.16  E-value: 5.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   2 AEAAEPEGVAPGPQGPPEVPAPlaeRPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHG 81
Cdd:PRK07764 389 GGAGAPAAAAPSAAAAAPAAAP---APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  82 ETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEA----QREPEDSAAPERQEEAEQRPEVPEGSASGEAG 157
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAatlrERWPEILAAVPKRSRKTWAILLPEATVLGVRG 545
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 158 DSVD---AEGPLGDNIEAEGPAGDSVEA-EGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAE 233
Cdd:PRK07764 546 DTLVlgfSTGGLARRFASPGNAEVLVTAlAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPA 625
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 234 GPAGDSVDAEGRVGDSVEA-GDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAiE 312
Cdd:PRK07764 626 APAPAGAAAAPAEASAAPApGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP-A 704
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 313 VAAGESAGRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEEE 392
Cdd:PRK07764 705 PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784
                        410       420
                 ....*....|....*....|....*...
gi 948549898 393 SPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PRK07764 785 MAEDDAPSMDDEDRRDAEEVAMELLEEE 812
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
11-441 1.25e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 65.01  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  11 APGPQGPPEVPAPLAERPGEPGAAGGEAEGPegsegAEEAPRGAAAVKEAGGGGPDRGPEAEARgTRGAHGETEAEEGAP 90
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRLGVAGGAGAP-----AAAAPSAAAAAPAAAPAPAAAAPAAAAA-PAPAAAPQPAPAPAP 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  91 EGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAE--QRPEVPEGSASGEAGDSVDAEGPLGD 168
Cdd:PRK07764 438 APAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPApaAAPAAPAAPAAPAGADDAATLRERWP 517
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 169 NI-EAEGPAGDSVEAEgrVGDSVDAEGPAGDSVD---AEGPLGDNIQAEGPAGDSVDA-----------EGRVGDSVDAE 233
Cdd:PRK07764 518 EIlAAVPKRSRKTWAI--LLPEATVLGVRGDTLVlgfSTGGLARRFASPGNAEVLVTAlaeelggdwqvEAVVGPAPGAA 595
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 234 GPAGDSVDAEGRVGDSVE--AGDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAI 311
Cdd:PRK07764 596 GGEGPPAPASSGPPEEAArpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGG 675
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 312 EVAAGESAGRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEE 391
Cdd:PRK07764 676 AAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP 755
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 948549898 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 2.16e-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: 64.25  E-value: 2.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    25 AERPGEPGAAGGEAEGPEGSEGAEEAprgaaavkEAGGGGPDRGpEAEARGTRGAHGETEAE-EGAPEGAEVPQGGEETS 103
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENGEESGGEA--------EQEGETETKG-ENESEGEIPAERKGEQEgEGEIEAKEADHKGETEA 712
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   104 GAQQVEGASPGRGAQGEPRGEAQrepedsaapERQEEAEQrpevpEGSASGEAGDSVDAEgplGDNIEAEGPAGDSVEAE 183
Cdd:TIGR00927  713 EEVEHEGETEAEGTEDEGEIETG---------EEGEEVED-----EGEGEAEGKHEVETE---GDRKETEHEGETEAEGK 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   184 grvGDSVDAEGPAGDSVDAEGPLGDNIQAEG----PAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAG-DPAGD 258
Cdd:TIGR00927  776 ---EDEDEGEIQAGEDGEMKGDEGAEGKVEHegetEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKqDEKGV 852
                          250
                   ....*....|....*
gi 948549898   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 1.86e-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: 61.16  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898     5 AEPEgvAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEG-AEEAPRGAAavkEAGGGGPDRGpEAEARGTRGAH-GE 82
Cdd:TIGR00927  636 AEAE--HTGERTGEEGERPTEAEGENGEESGGEAEQEGETETkGENESEGEI---PAERKGEQEG-EGEIEAKEADHkGE 709
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    83 TEAEEGAPEGAEVPQGGE-ETSGAQQVEGASPGRGAQGEPRGEAQREPE-DSAAPERQEEAEQRPEVPEGSASGEAGDSV 160
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEdEGEIETGEEGEEVEDEGEGEAEGKHEVETEgDRKETEHEGETEAEGKEDEDEGEIQAGEDG 789
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   161 DAEGPLGD--NIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDS-VDAEGrvgdsvdaEGPAG 237
Cdd:TIGR00927  790 EMKGDEGAegKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKgVDGGG--------GSDGG 861

                   ....*.
gi 948549898   238 DSVDAE 243
Cdd:TIGR00927  862 DSEEEE 867
PRK12678 PRK12678
transcription termination factor Rho; Provisional
9-204 5.39e-08

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 56.07  E-value: 5.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   9 GVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEG 88
Cdd:PRK12678  61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  89 AP----EGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEvPEGSASGEAGDSVDAEG 164
Cdd:PRK12678 141 AArkagEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD-RDRRDRREQGDRREERG 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 948549898 165 plgdNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSVDAEG 204
Cdd:PRK12678 220 ----RRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDG 255
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1-409 7.59e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 7.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    1 MAEAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAH 80
Cdd:PHA03307   13 AAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   81 GETEAEEGAPEGAEVPQGGEETSGaqqvEGASPGRGAQGEPRGEAQREPEDSAAPErqEEAEQRPEVPEGSASGEAGDSV 160
Cdd:PHA03307   93 STLAPASPAREGSPTPPGPSSPDP----PPPTPPPASPPPSPAPDLSEMLRPVGSP--GPPPAASPPAAGASPAAVASDA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  161 DAEGPLGDNIEAegpAGDSVEAEGRVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSV 240
Cdd:PHA03307  167 ASSRQAALPLSS---PEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  241 DAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEGPAGDSMDAEGPAG-RARRVSGEPQQSGDGSLSPQAEAIEVAAGESA 319
Cdd:PHA03307  244 SSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSpRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  320 GRSPGELAWDAAEEAEV--PGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRE-RSPEGPREEEAAGGEEESPDS 396
Cdd:PHA03307  324 SSSSSTSSSSESSRGAAvsPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASaGRPTRRRARAAVAGRARRRDA 403
                         410
                  ....*....|...
gi 948549898  397 SPHGEASRGAAEP 409
Cdd:PHA03307  404 TGRFPAGRPRPSP 416
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
486-548 8.70e-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: 8.70e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948549898 486 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPA-DLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLE 548
Cdd:cd00570    8 GSPRSLRVRLALEEKGLPYELVPVDLGEGEQeEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
PRK12678 PRK12678
transcription termination factor Rho; Provisional
55-259 2.71e-07

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 53.75  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  55 AAVKEAGGGG----PDRGPEAEARGTRGAHGETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPE 130
Cdd:PRK12678  53 AAIKEARGGGaaaaAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 131 DSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSvDAEGPLGDNI 210
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQ 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 948549898 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 3.20e-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: 53.85  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    52 RGAAAVKEAGGGGPDRGPEAEARGTR-GAHGETEAEEGAPEG------AEVPQGGEETSGAQQvEGASPGRGaQGEPRGE 124
Cdd:TIGR00927  619 RPVAKVMALGDLSKGDVAEAEHTGERtGEEGERPTEAEGENGeesggeAEQEGETETKGENES-EGEIPAER-KGEQEGE 696
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   125 AQREPE------DSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNiEAEGPAGDSVEAEGRVGDSVDAEGPAGD 198
Cdd:TIGR00927  697 GEIEAKeadhkgETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEG-EAEGKHEVETEGDRKETEHEGETEAEGK 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   199 SVDAEGplgdNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAegpAGD 278
Cdd:TIGR00927  776 EDEDEG----EIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEA---KQD 848
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 948549898   279 SMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAW 328
Cdd:TIGR00927  849 EKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEW 898
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1-198 1.45e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.53  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   1 MAEAAEPEGVAPGPQGPPEVPAPlaerPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGtrgah 80
Cdd:PRK07764 607 GPPEEAARPAAPAAPAAPAAPAP----AGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA----- 677
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  81 geTEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSV 160
Cdd:PRK07764 678 --PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP 755
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 948549898 161 DAEGPLGDNIEAEGPAGDS--VEAEGRVGDSVDAEGPAGD 198
Cdd:PRK07764 756 AQPPPPPAPAPAAAPAAAPppSPPSEEEEMAEDDAPSMDD 795
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
3-179 2.64e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 51.00  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   3 EAAEPEGVAPGPQGPPE----VPAPLAERPGEPGAAGGEAEGP-EGSEGAEEAPRGAAAVKEAGGGGPDRGPE---AEAR 74
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARvagaVPAPGARAAAAVGASAVPAVTAvTGAAGAALAPKAAAAAAATRAEAPPAAPAppaTADR 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  75 GTRGAHGETEAEEGAPEGAEVPQGGEEtSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPErQEEAEQRPEVPEGSASG 154
Cdd:PRK07003 439 GDDAADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEPAPRAAAP-SAATPAAVPDARAPAAA 516
                        170       180
                 ....*....|....*....|....*
gi 948549898 155 EAGDSVDAEGPLGDNIEAEGPAGDS 179
Cdd:PRK07003 517 SREDAPAAAAPPAPEARPPTPAAAA 541
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1-409 2.64e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    1 MAEAAEPEGVAPGPQGPPEVPAPLAERPGEPGA-AGGEAEGPEGSEGAEEAPRGAaavkEAGGGGPDRGPE-AEARGTRG 78
Cdd:PHA03307   67 PPTGPPPGPGTEAPANESRSTPTWSLSTLAPASpAREGSPTPPGPSSPDPPPPTP----PPASPPPSPAPDlSEMLRPVG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   79 AHGETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGD 158
Cdd:PHA03307  143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  159 SvdaegplgdnieaegpagDSVEAEGRVGDSVDAEGPAGDSVDAEGPLGDNiqaEGPAGDSVDAEGRVGDSVDAEGPAGD 238
Cdd:PHA03307  223 A------------------PGRSAADDAGASSSDSSSSESSGCGWGPENEC---PLPRPAPITLPTRIWEASGWNGPSSR 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  239 SVDAEGRVGDSVEAGDPA---GDGVEAGVPAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAA 315
Cdd:PHA03307  282 PGPASSSSSPRERSPSPSpssPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  316 GESAGRSPgelawDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEdeerRERSPEGPREEEAAGGEEESPD 395
Cdd:PHA03307  362 PSSPRKRP-----RPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAG----RPRPSPLDAGAASGAFYARYPL 432
                         410
                  ....*....|....
gi 948549898  396 SSPHGEASRGAAEP 409
Cdd:PHA03307  433 LTPSGEPWPGSPPP 446
PHA03169 PHA03169
hypothetical protein; Provisional
3-202 1.07e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.43  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   3 EAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAG-GEAEGPEGSEGAEEAPRGAAavKEAGGGGPDRGPEAEARGTRGAHG 81
Cdd:PHA03169  31 EQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEqGHRQTESDTETAEESRHGEK--EERGQGGPSGSGSESVGSPTPSPS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  82 ETEAEEGapEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREpEDSAAPERQEEAEQRPEVPEGSASGEAGDSVD 161
Cdd:PHA03169 109 GSAEELA--SGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE-SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 948549898 162 ----AEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSVDA 202
Cdd:PHA03169 186 epdsPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
PHA03169 PHA03169
hypothetical protein; Provisional
2-182 1.75e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   2 AEAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGG--------EAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEA 73
Cdd:PHA03169  41 ARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETaeesrhgeKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSP 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  74 RGTRGAHGETEAEEGAPEGAEvPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPE--DSAAPERQEEAEQRPEVPEGS 151
Cdd:PHA03169 121 ENTSGSSPESPASHSPPPSPP-SHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEepEPPTSEPEPDSPGPPQSETPT 199
                        170       180       190
                 ....*....|....*....|....*....|.
gi 948549898 152 ASGEAGDSVDAEGPLGDNIEAEGPAGDSVEA 182
Cdd:PHA03169 200 SSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
PRK12678 PRK12678
transcription termination factor Rho; Provisional
232-444 2.67e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 47.59  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 232 AEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAgDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAI 311
Cdd:PRK12678  73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPA-ARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQ 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 312 EVAAGESAGRSPGELAwDAAEEAEVPGVKGSEEAAPGDARADaGEDRVGDGPQQEPGEDEERRERSPEGPReeEAAGGEE 391
Cdd:PRK12678 152 PATEARADAAERTEEE-ERDERRRRGDREDRQAEAERGERGR-REERGRDGDDRDRRDRREQGDRREERGR--RDGGDRR 227
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 948549898 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 ...
487-548 2.90e-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: 2.90e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948549898 487 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVktdvnkIEEFLE 548
Cdd:cd03060    9 CPYAMRARMALLLAGITVELREVELKNKPAEMLAASPkGTVPVLVLGNGTV------IEESLD 65
PHA03169 PHA03169
hypothetical protein; Provisional
26-222 3.86e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.50  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  26 ERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEagggGPDRGPEAEARGTRGAHGETEAE-EGAPEGAEVPQGGEET-- 102
Cdd:PHA03169  31 EQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQ----GHRQTESDTETAEESRHGEKEERgQGGPSGSGSESVGSPTps 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 103 -SGAQQV--EGASPGRGAQGEPRGEAQREPeDSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNIEAEGPAGDS 179
Cdd:PHA03169 107 pSGSAEElaSGLSPENTSGSSPESPASHSP-PPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 948549898 180 VEAEGRVGDSVDAE--GPAGDSVDAEGPLGDNIQAEGPAGDSVDA 222
Cdd:PHA03169 186 EPDSPGPPQSETPTssPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-193 4.42e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   2 AEAAEPEGVAPGPQGPPEVPAPLAERPGEPGAA---GGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRG 78
Cdd:PRK07764 631 GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdggDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP 710
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  79 AHGeteAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGD 158
Cdd:PRK07764 711 AGQ---ADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE 787
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 948549898 159 SVDAEGPLGDNIEAEGPAGDSVEAE--GRVGDSVDAE 193
Cdd:PRK07764 788 DDAPSMDDEDRRDAEEVAMELLEEElgAKKIEEFAAD 824
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
2-153 4.66e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.77  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   2 AEAAEPEGVAPGPQGPPEVPAplaeRPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHG 81
Cdd:PRK07003 407 GAALAPKAAAAAAATRAEAPP----AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPAS 482
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948549898  82 ETEAEegAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPErqEEAEQRPEVPEGSAS 153
Cdd:PRK07003 483 DAPPD--AAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPP--TPAAAAPAARAGGAA 550
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
25-184 4.91e-05

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 46.51  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  25 AERPGEPGAAGGEAEGPEGSEGAeeaprgAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEGApegAEVPQGGEETSG 104
Cdd:PRK13108 292 VDEALEREPAELAAAAVASAASA------VGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVV---QVADRDGESTPA 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 105 AQQVEGASPGRGAQGEPRGEAQREPEDSA---APERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDN-IEAEGPAGDSV 180
Cdd:PRK13108 363 VEETSEADIEREQPGDLAGQAPAAHQVDAeaaSAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDeLAVAGPGDDPA 442

                 ....
gi 948549898 181 EAEG 184
Cdd:PRK13108 443 EPDG 446
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
540-663 6.80e-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: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 540 VNKIEEFLEEKLAPPRYPKLGTQhpesnsagndvfakfsAFIKNTKKDANEIHEKNLLKALRKLDNYLnsplpdeidays 619
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLE----------------KVPLPKDEAAVEAAREELPALLAALEQLL------------ 52
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 948549898 620 tedvtvSGRKFLDGDELTLADCNLLPKLHIIKIVAKKYRDFE-FP 663
Cdd:cd00299   53 ------AGRPYLAGDQFSLADVALAPVLARLEALGPYYDLLDeYP 91
PHA03169 PHA03169
hypothetical protein; Provisional
185-409 8.82e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 8.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 185 RVGDSVDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDpAGDGVEAGV 264
Cdd:PHA03169  26 HGGTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGS-GSESVGSPT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 265 PAGDSVEAEGPAGDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWDAAEEAEVPGVKGSEE 344
Cdd:PHA03169 105 PSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSE 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948549898 345 AAPGDARADAGEDRVGDGPQQEPGeDEERRERSPEGPREEEAAGGEEESPDSSPHGEASRGAAEP 409
Cdd:PHA03169 185 PEPDSPGPPQSETPTSSPPPQSPP-DEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
177-528 1.20e-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: 45.76  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   177 GDSVEAEGRvGDSVDAEGPAgdSVDAEGPLGDniQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPA 256
Cdd:TIGR00927  633 GDVAEAEHT-GERTGEEGER--PTEAEGENGE--ESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHK 707
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   257 GDGVEAGVPAGDSVEAEGPA--------------GDSMDAEGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRS 322
Cdd:TIGR00927  708 GETEAEEVEHEGETEAEGTEdegeietgeegeevEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGE 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   323 PGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGPREEEAAGGEeespdssphGEA 402
Cdd:TIGR00927  788 DGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGG---------GGS 858
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   403 SRGAAEPEAQLSNHLAEEGPAEGSGEaarvngrREDGEASEPRALG-----QEHDITLFV-----KVKLTALGCSRIAIK 472
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEE-------EEEEENEEPLSLEwpetrQKQAIYLFLlpivfPLWLTVPDVRRQEAR 931
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 948549898   473 KYLRAGYDGESIGNCPFSqrLFMILWLKGVifnVTTVDLKRKPADLQNLAPGTNPP 528
Cdd:TIGR00927  932 KFFVITFLGSIMWIAMFS--YLMVWWAHQV---GETIGISEEIMGLTILAAGTSIP 982
PHA03378 PHA03378
EBNA-3B; Provisional
5-121 1.91e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.06  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   5 AEPEGVAPGPQGPPEVPaPLAERPgePGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAhgETE 84
Cdd:PHA03378 694 MQPPPRAPTPMRPPAAP-PGRAQR--PAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRAR--PPA 768
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 948549898  85 AEEGAPEGAEVPQGGeeTSGAQQVEGA-SPGRGAQGEP 121
Cdd:PHA03378 769 AAPGAPTPQPPPQAP--PAPQQRPRGApTPQPPPQAGP 804
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
115-290 2.14e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 44.20  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 115 RGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGeAGDSVDAEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEG 194
Cdd:PRK13108 286 RGSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQ-PDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 195 PAgDSVDAEGPLGDNIQAEGPAGDSVDAEGRVGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEG 274
Cdd:PRK13108 365 ET-SEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAE 443
                        170
                 ....*....|....*.
gi 948549898 275 PAGDSMDAEGPAGRAR 290
Cdd:PRK13108 444 PDGIRRQDDFSSRRRR 459
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
486-550 3.16e-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: 3.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 948549898 486 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDgEVKTDVNKIEEFLEEK 550
Cdd:cd03059    8 DDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPyGTVPTLVDRD-LVLYESRIIMEYLDER 72
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
487-555 5.76e-04

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 39.13  E-value: 5.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948549898  487 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLAPPR 555
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
25-149 1.39e-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: 42.29  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    25 AERPGEPGAAGGEAEGPEGS-EGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEGAPEGAEVPQGGEETS 103
Cdd:TIGR00927  759 GDRKETEHEGETEAEGKEDEdEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELN 838
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 948549898   104 GAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPE 149
Cdd:TIGR00927  839 AENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEE 884
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
12-167 1.54e-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: 41.43  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  12 PGPQGPPEVPAPLAERpGEPGAAGGEAEGPEGSEGAEEAPRGAAAVK-EAGGGGPdRGPEAE--ARGTRGAHGET-EAEE 87
Cdd:NF038329 122 PGPAGPAGPAGEQGPR-GDRGETGPAGPAGPPGPQGERGEKGPAGPQgEAGPQGP-AGKDGEagAKGPAGEKGPQgPRGE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  88 GAPEGAEVPQG-----GEETSGAQQVEGASPGRGAQGePRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSVDA 162
Cdd:NF038329 200 TGPAGEQGPAGpagpdGEAGPAGEDGPAGPAGDGQQG-PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                 ....*.
gi 948549898 163 E-GPLG 167
Cdd:NF038329 279 ErGPVG 284
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
111-436 1.61e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  111 ASPGRGAQGEPRGEAQREPE-DSAAPERQEEAEQRPEVPEGSASGEAGDSvDAEGPLGDNIEAEGPAGDSVEAEGRVGDS 189
Cdd:PHA03307   62 CDRFEPPTGPPPGPGTEAPAnESRSTPTWSLSTLAPASPAREGSPTPPGP-SSPDPPPPTPPPASPPPSPAPDLSEMLRP 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  190 VDAEGPAGDSVDAEGPLGDNIQAEGPAGDSVDAegRVGDSVDAEGPAGDSVDAEgrVGDSVEAGDPAGDGVEAGVPAGDS 269
Cdd:PHA03307  141 VGSPGPPPAASPPAAGASPAAVASDAASSRQAA--LPLSSPEETARAPSSPPAE--PPPSTPPAAASPRPPRRSSPISAS 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  270 VEAEGPAGDSMDAeGPAGRARRVSGEPQQSGDGSLSPQAEAIEVAAGESAGRSPGELAWDAAEEAEVPgvKGSEEAAPGD 349
Cdd:PHA03307  217 ASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPG--PASSSSSPRE 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  350 ARADAGEDRVGDGP---------QQEPGEDEERRERSPEGPREEEAAGGEEESPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PHA03307  294 RSPSPSPSSPGSGPapssprassSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSR 373
                         330
                  ....*....|....*.
gi 948549898  421 GPAEGSGEAARVNGRR 436
Cdd:PHA03307  374 APSSPAASAGRPTRRR 389
PHA03169 PHA03169
hypothetical protein; Provisional
3-155 1.76e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   3 EAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDR-----GPEAEARGTR 77
Cdd:PHA03169  98 ESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQpssflQPSHEDSPEE 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  78 GAHGETEAEEGAPEGAEVPQGGEETSGAQQVEGASP-----GRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSA 152
Cdd:PHA03169 178 PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEpqsptPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTV 257

                 ...
gi 948549898 153 SGE 155
Cdd:PHA03169 258 VGW 260
PHA03169 PHA03169
hypothetical protein; Provisional
54-277 2.94e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  54 AAAVKEAGGGGPDRGPEAEARGTRGaHGETEAEEgapEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSA 133
Cdd:PHA03169  41 ARAAKPAPPAPTTSGPQVRAVAEQG-HRQTESDT---ETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELAS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 134 APERQEEAEQRPEvpegsasGEAGDSVDAEGPLGDNIEAEGPAGDSVEAEGRVGDSVDAEGPAGDSVDAEGPLGDNIQAE 213
Cdd:PHA03169 117 GLSPENTSGSSPE-------SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDS 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948549898 214 GPAGDSVDAegrvGDSVDAEGPAGDSVDAEGRVGDSVEAGDPAGDGVEAGVPAGDSVEAEGPAG 277
Cdd:PHA03169 190 PGPPQSETP----TSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249
motB PRK05996
MotB family protein;
29-157 3.27e-03

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 40.45  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  29 GEPGAA-GGEAEGPEGSEgAEEAP------RGAAAVKEAGGGGPdrgPEAEARGTRGAHGETEAEEGAPEGAEVPQGGEE 101
Cdd:PRK05996 158 GDGGAAqSGPATGADGGE-AYRDPfdpdfwSKQVEVTTAGDLLP---PGQAREQAQGAKSATAAPATVPQAAPLPQAQPK 233
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 948549898 102 TSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSA-SGEAG 157
Cdd:PRK05996 234 KAATEEELIADAKKAATGEPAANAAKAAKPEPMPDDQQKEAEQLQAAIAQAiGGVAG 290
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
486-691 3.60e-03

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 39.49  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 486 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEKLAPPR-YP 557
Cdd:COG0625    9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAERYPEPPlLP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 558 KLGTQHPE--------SNSAGNDVFAKFSAFIKNTKKDANEIHEKNLLKALRKLDNYLnsplpdeidaystedvtvSGRK 629
Cdd:COG0625   85 ADPAARARvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL------------------AGGP 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948549898 630 FLDGDELTLADCNLLPKLHIIkivakkyRDFEFP-SEMTGIWRYLNNAYARDEFTNTCPADQE 691
Cdd:COG0625  147 YLAGDRFSIADIALAPVLRRL-------DRLGLDlADYPNLAAWLARLAARPAFQRALAAAEP 202
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
3-166 3.63e-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: 40.75  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898     3 EAAEPEGVAPGPQGPPEVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGG--GGPDRGPEAEARGTRGAH 80
Cdd:TIGR00927  719 GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEdeGEIQAGEDGEMKGDEGAE 798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898    81 GETEAEEGAPEGAEVpQGGEETSGAQQVEGASPGRGAQ---GEPRGEAQREPE--------DSAAPERQEEAEQRPEVPE 149
Cdd:TIGR00927  799 GKVEHEGETEAGEKD-EHEGQSETQADDTEVKDETGEQelnAENQGEAKQDEKgvdggggsDGGDSEEEEEEEEEEEEEE 877
                          170
                   ....*....|....*..
gi 948549898   150 GSASGEAGDSVDAEGPL 166
Cdd:TIGR00927  878 EEEEEEEEEEEENEEPL 894
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
302-452 3.95e-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: 40.75  E-value: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   302 GSLSPQAEAIEVAAGEsagRSPGELAWDAAEEAEVPGVKGSEEAAPGDARADAGEDRVGDGPQQEPGEDEERRERSPEGP 381
Cdd:TIGR00927  628 GDLSKGDVAEAEHTGE---RTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA 704
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948549898   382 REEEAAGGEEESPDSSPHGEASRGAAEPEAQLSNHLAE---EGPAEGSGEAARVNGRREDGEASEPRALGQEHD 452
Cdd:TIGR00927  705 DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEdegEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE 778
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2-148 4.38e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898   2 AEAAEPEGVAPGPQGPP--EVPAPLAERPGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGA 79
Cdd:PRK12323 413 AAAARAVAAAPARRSPApeALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPA 492
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  80 HGETEAEEGAPEGAEVPQGGEETSGAQQVEGASPGRGAQGEPRGE-AQREPEDSAAPERQEEAEQRPEVP 148
Cdd:PRK12323 493 DDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAfETLAPAPAAAPAPRAAAATEPVVA 562
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
21-199 4.93e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  21 PAPLAerpGEPGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRGPEAEARGTRGAHGETEAEEGAPEGAEVP---- 96
Cdd:PRK07003 360 PAVTG---GGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPpata 436
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  97 -QGGEETSGAQQVEGASPGRGAQGEPRGEAQREPEDSAAPERQEEAEQRPEVPEGSASGEAGDSVDAEGPLGDNIE-AEG 174
Cdd:PRK07003 437 dRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARApAAA 516
                        170       180
                 ....*....|....*....|....*
gi 948549898 175 PAGDSVEAEGRVGDSVDAEGPAGDS 199
Cdd:PRK07003 517 SREDAPAAAAPPAPEARPPTPAAAA 541
PHA03378 PHA03378
EBNA-3B; Provisional
12-141 4.94e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898  12 PGPQGP----PEVPAPLAERPgePGAAGGEAEGPEGSEGAEEAPRGAAAVKEAGGGGPDRgpeaeARGTRGAHGETEAEE 87
Cdd:PHA03378 676 PSPTGAntmlPIQWAPGTMQP--PPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGR-----ARPPAAAPGRARPPA 748
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 948549898  88 GAPEGAEVPQGGeetSGAQQVEGASPGRGA-QGEPRG--EAQREPEDSAAPERQEEA 141
Cdd:PHA03378 749 AAPGRARPPAAA---PGRARPPAAAPGAPTpQPPPQAppAPQQRPRGAPTPQPPPQA 802
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
261-438 6.26e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 39.58  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 261 EAGVPAGDSVEAEGPAGDSMDAeGPAGrarrvSGEPQQSGDGSLSPQAEAIEVAAGESAgRSPGELAWDAAEEAEVPgvk 340
Cdd:PRK13108 294 EALEREPAELAAAAVASAASAV-GPVG-----PGEPNQPDDVAEAVKAEVAEVTDEVAA-ESVVQVADRDGESTPAV--- 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 341 gsEEAAPGDARADAGEDRVGDGPQqEPGEDEERRERSPEGPreeeaAGGEEESPDSSPHGEASRGAAEPEAQLSNHLAEE 420
Cdd:PRK13108 364 --EETSEADIEREQPGDLAGQAPA-AHQVDAEAASAAPEEP-----AALASEAHDETEPEVPEKAAPIPDPAKPDELAVA 435
                        170       180
                 ....*....|....*....|....
gi 948549898 421 GPA------EGSGEAARVNGRRED 438
Cdd:PRK13108 436 GPGddpaepDGIRRQDDFSSRRRR 459
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
594-686 6.58e-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: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549898 594 KNLLKALRKLDNYLnsplpdeidaystedvtvSGRKFLDGDELTLADCNLLPKL--------HIIKIVAKKYRDfeFPSe 665
Cdd:cd03190   40 KELFEALDKLEKRL------------------SKQPYLLGDRLTEADIRLFTTLirfdpvyhQHFKCNLKTIRD--YPN- 98
                         90       100
                 ....*....|....*....|.
gi 948549898 666 mtgIWRYLNNAYARDEFTNTC 686
Cdd:cd03190   99 ---LWRYLRRLYQNPGVFETT 116
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
487-548 9.38e-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: 9.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948549898 487 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVKTDVNKIEEFLE 548
Cdd:cd03055   27 CPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPqGKVPALEIDEGKVVYESLIICEYLD 89
 
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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