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Conserved domains on  [gi|27369633|ref|NP_766057|]
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chloride intracellular channel protein 6 [Mus musculus]

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. ...
363-596 1.03e-146

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: 423.12  E-value: 1.03e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   363 ITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 442
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   443 LVPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKF 522
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369633   523 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAKRMK 596
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
51-338 2.08e-10

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


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 63.86  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633     51 GAGVEARASGKEEGGCGQDEGTGGAQaQDPRTGPEAETPGASGAPGEAEAaerdpEGAIP-QGAEEAPSAQQVQGMSSGL 129
Cdd:TIGR00927  633 GDVAEAEHTGERTGEEGERPTEAEGE-NGEESGGEAEQEGETETKGENES-----EGEIPaERKGEQEGEGEIEAKEADH 706
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    130 DSQGEAPEVPGDSRREPEdptaseaGEEAESGQEAQGGGALglqinpevqglAGDNMDTEAPAGGPLGSESEPQGGGESS 209
Cdd:TIGR00927  707 KGETEAEEVEHEGETEAE-------GTEDEGEIETGEEGEE-----------VEDEGEGEAEGKHEVETEGDRKETEHEG 768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    210 PQPQDEAIEIVTTEIGGNESGELAGASAADAAGEGETLGKDGSEEAASEDARVDAHENGDQGklqeETGEEEARPEPElk 289
Cdd:TIGR00927  769 ETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKD----ETGEQELNAENQ-- 842
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 27369633    290 gpCEGAIQEKPPDGSLDGEEAKSTEHEEESQAELSNHLAEEPSVQGGEE 338
Cdd:TIGR00927  843 --GEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEE 889
 
Name Accession Description Interval E-value
O-ClC TIGR00862
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ...
363-596 1.03e-146

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: 423.12  E-value: 1.03e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   363 ITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 442
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   443 LVPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKF 522
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369633   523 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAKRMK 596
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
455-594 1.99e-100

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: 301.17  E-value: 1.99e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKFLDGDELTLADCN 534
Cdd:cd10301   1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAKR 594
Cdd:cd10301  81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
376-577 3.14e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 105.46  E-value: 3.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633  376 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLvpPRyPKLGTQh 455
Cdd:PLN02817  70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKY--PD-PPLATP- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633  456 PESNSAGNDVFAKFSAFIKNtkKDANEIYEKNLLRALKKLDSYLNSPLPdeidadssedvtvsqrkFLDGDELTLADCNL 535
Cdd:PLN02817 146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 27369633  536 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 577
Cdd:PLN02817 207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
379-442 2.63e-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: 2.63e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369633   379 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 442
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
51-338 2.08e-10

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 63.86  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633     51 GAGVEARASGKEEGGCGQDEGTGGAQaQDPRTGPEAETPGASGAPGEAEAaerdpEGAIP-QGAEEAPSAQQVQGMSSGL 129
Cdd:TIGR00927  633 GDVAEAEHTGERTGEEGERPTEAEGE-NGEESGGEAEQEGETETKGENES-----EGEIPaERKGEQEGEGEIEAKEADH 706
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    130 DSQGEAPEVPGDSRREPEdptaseaGEEAESGQEAQGGGALglqinpevqglAGDNMDTEAPAGGPLGSESEPQGGGESS 209
Cdd:TIGR00927  707 KGETEAEEVEHEGETEAE-------GTEDEGEIETGEEGEE-----------VEDEGEGEAEGKHEVETEGDRKETEHEG 768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    210 PQPQDEAIEIVTTEIGGNESGELAGASAADAAGEGETLGKDGSEEAASEDARVDAHENGDQGklqeETGEEEARPEPElk 289
Cdd:TIGR00927  769 ETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKD----ETGEQELNAENQ-- 842
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 27369633    290 gpCEGAIQEKPPDGSLDGEEAKSTEHEEESQAELSNHLAEEPSVQGGEE 338
Cdd:TIGR00927  843 --GEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEE 889
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-226 2.62e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    2 AEATEPKevAPGSQGQPEGATIEGPGEPGAADLEGREASEEAAEAPRDLGAGVEARASGKEEGGcgqdEGTGGAQAQDPR 81
Cdd:PRK07764 610 EEAARPA--APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA----KAGGAAPAAPPP 683
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   82 TGPEAETPGASGAPGEAEAAERDPEGAIPQGAEEAPSAQQVQgmssglDSQGEAPEVPGDSRREPEDPTASEAGEEAESG 161
Cdd:PRK07764 684 APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA------QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQ 757
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27369633  162 QEAQGGGAlglqinPEVQGLAGDNMDTEAPAGGPLgSESEPQGGGESSPQPQDEAIEIVTTEIGG 226
Cdd:PRK07764 758 PPPPPAPA------PAAAPAAAPPPSPPSEEEEMA-EDDAPSMDDEDRRDAEEVAMELLEEELGA 815
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
378-583 5.50e-05

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 44.50  E-value: 5.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 378 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEklvppRYPK 450
Cdd:COG0625   9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAE-----RYPE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 451 ---LGTQHPE-----------SNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLnsplpdeidadssedvt 516
Cdd:COG0625  80 pplLPADPAArarvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL----------------- 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27369633 517 vSQRKFLDGDELTLADCNLLPKLHIIkivakkyRDFEFP-SEMTGIWRYLNNAYARDEFTNTCPADRE 583
Cdd:COG0625 143 -AGGPYLAGDRFSIADIALAPVLRRL-------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. ...
363-596 1.03e-146

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: 423.12  E-value: 1.03e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   363 ITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 442
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   443 LVPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKF 522
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369633   523 LDGDELTLADCNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAKRMK 596
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
455-594 1.99e-100

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: 301.17  E-value: 1.99e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKFLDGDELTLADCN 534
Cdd:cd10301   1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAKR 594
Cdd:cd10301  81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
GST_C_CLIC5 cd10297
C-terminal, alpha helical domain of Chloride Intracellular Channel 5; Glutathione ...
455-595 1.87e-87

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: 267.60  E-value: 1.87e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKFLDGDELTLADCN 534
Cdd:cd10297   1 HRESNTAGIDIFSKFSAYIKNTKQQANAALEKGLTKALKKLDDYLNTPLPEEIDADSTEEEKVSNRKFLDGDELTLADCN 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAKRM 595
Cdd:cd10297  81 LLPKLHVVKIVAKKYRNFEIPSDMTGVWRYLKNAYARDEFTNTCAADKEIELAYADVAKRL 141
GST_C_CLIC4 cd10296
C-terminal, alpha helical domain of Chloride Intracellular Channel 4; Glutathione ...
455-595 5.02e-87

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


Pssm-ID: 198329  Cd Length: 141  Bit Score: 266.50  E-value: 5.02e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKFLDGDELTLADCN 534
Cdd:cd10296   1 HPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLDGNEMTLADCN 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAKRM 595
Cdd:cd10296  81 LLPKLHIVKVVAKKYRNFEIPKEMTGIWRYLSNAYSRDEFTNTCPSDKEIEIAYSDVAKRL 141
GST_C_CLIC2 cd10298
C-terminal, alpha helical domain of Chloride Intracellular Channel 2; Glutathione ...
455-593 4.06e-72

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: 227.84  E-value: 4.06e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKkDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKFLDGDELTLADCN 534
Cdd:cd10298   1 YKESFDVGSDIFAKFSAYIKNSP-ENNANQEKALLREFKRLDDYLNTPLPEEIDHDSAENITVSKRKFLDGDRLTLADCN 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAK 593
Cdd:cd10298  80 LLPKLHVIKVAAKKYCDFDIPADFTGVWRYLNNAYEREEFSQTCPADIEIEKAYASVAK 138
GST_C_CLIC1 cd10300
C-terminal, alpha helical domain of Chloride Intracellular Channel 1; Glutathione ...
455-593 2.49e-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: 220.58  E-value: 2.49e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSSEDVTVSQRKFLDGDELTLADCN 534
Cdd:cd10300   1 NPESNTAGLDVFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDENSAEDEGVSQRKFLDGNELTLADCN 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYSDAAK 593
Cdd:cd10300  81 LLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK 139
GST_C_CLIC cd03198
C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase ...
455-589 9.17e-65

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: 207.85  E-value: 9.17e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSplpdeidadssedvtvSQRKFLDGDELTLADCN 534
Cdd:cd03198   1 NPEANTAGEDLFAKFSAYIKNKDPAADEALRKALLKELSKLDAYLSS----------------SSRKFLDGDTLTLADCN 64
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYS 589
Cdd:cd03198  65 LLPKLHHIRVAGKAYKDFDIPDDFTGLWRYLKNAYETDEFTKTCPADQEIILHYK 119
GST_C_CLIC3 cd10299
C-terminal, alpha helical domain of Chloride Intracellular Channel 3; Glutathione ...
455-589 1.07e-59

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: 194.99  E-value: 1.07e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 455 HPESNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLNSPLPDEIDADSseDVTVSQRKFLDGDELTLADCN 534
Cdd:cd10299   1 YKESNTAGNDVFHKFSAFIKNPVPAQDDALQKKLLRALLKLDSYLLTPLPHELAQNP--HLSESQRRFLDGDALTLADCN 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27369633 535 LLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREIEHAYS 589
Cdd:cd10299  79 LLPKLHIVKVVCKHYRQFEIPAELKGVTRYLDSASQEKEFKYTCPNSAEILLAYR 133
GST_N_CLIC cd03061
GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, ...
360-448 4.74e-53

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: 176.02  E-value: 4.74e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 360 EHDITLFVKAGYDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFL 439
Cdd:cd03061   3 EPEIELFVKASSDGESIGNCPFCQRLFMVLWLKGVVFNVTTVDMKRKPEDLKDLAPGTQPPFLLYNGEVKTDNNKIEEFL 82

                ....*....
gi 27369633 440 EEKLVPPRY 448
Cdd:cd03061  83 EETLCPPKY 91
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
376-577 3.14e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 105.46  E-value: 3.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633  376 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLvpPRyPKLGTQh 455
Cdd:PLN02817  70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKY--PD-PPLATP- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633  456 PESNSAGNDVFAKFSAFIKNtkKDANEIYEKNLLRALKKLDSYLNSPLPdeidadssedvtvsqrkFLDGDELTLADCNL 535
Cdd:PLN02817 146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 27369633  536 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 577
Cdd:PLN02817 207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
PLN02378 PLN02378
glutathione S-transferase DHAR1
374-577 2.81e-18

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 83.61  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633  374 ESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKlvpprYPKLGT 453
Cdd:PLN02378  15 DHLGDCPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEK-----YPDPPL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633  454 QHP-ESNSAGNDVFAKFSAFIKNtkKDANEIYEKNLLRALKKLDSYLNSplpdeidadssedvtvSQRKFLDGDELTLAD 532
Cdd:PLN02378  90 KTPaEFASVGSNIFGTFGTFLKS--KDSNDGSEHALLVELEALENHLKS----------------HDGPFIAGERVSAVD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 27369633  533 CNLLPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNT 577
Cdd:PLN02378 152 LSLAPKLYHLQVALGHFKSWSVPESFPHVHNYMKTLFSLDSFEKT 196
GST_C_DHAR cd03201
C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) ...
456-584 6.28e-16

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: 74.38  E-value: 6.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 456 PESNSAGNDVFAKFSAFIKNtkKDANEIYEKNLLRALKKLDSYLNSPLPdeidadssedvtvsqrkFLDGDELTLADCNL 535
Cdd:cd03201   5 PEFASVGSKIFSTFVTFLKS--KDANDGSEQALLDELTALDEHLKTNGP-----------------FIAGEKITAVDLSL 65
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 27369633 536 LPKLHIIKIVAKKYRDFEFPSEMTGIWRYLNNAYARDEFTNTCPADREI 584
Cdd:cd03201  66 APKLYHLRVALGHYKGWSVPESLTAVHKYMELLFSRESFKKTKAPDEMI 114
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
379-442 2.63e-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: 2.63e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369633   379 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 442
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
51-338 2.08e-10

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 63.86  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633     51 GAGVEARASGKEEGGCGQDEGTGGAQaQDPRTGPEAETPGASGAPGEAEAaerdpEGAIP-QGAEEAPSAQQVQGMSSGL 129
Cdd:TIGR00927  633 GDVAEAEHTGERTGEEGERPTEAEGE-NGEESGGEAEQEGETETKGENES-----EGEIPaERKGEQEGEGEIEAKEADH 706
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    130 DSQGEAPEVPGDSRREPEdptaseaGEEAESGQEAQGGGALglqinpevqglAGDNMDTEAPAGGPLGSESEPQGGGESS 209
Cdd:TIGR00927  707 KGETEAEEVEHEGETEAE-------GTEDEGEIETGEEGEE-----------VEDEGEGEAEGKHEVETEGDRKETEHEG 768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    210 PQPQDEAIEIVTTEIGGNESGELAGASAADAAGEGETLGKDGSEEAASEDARVDAHENGDQGklqeETGEEEARPEPElk 289
Cdd:TIGR00927  769 ETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKD----ETGEQELNAENQ-- 842
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 27369633    290 gpCEGAIQEKPPDGSLDGEEAKSTEHEEESQAELSNHLAEEPSVQGGEE 338
Cdd:TIGR00927  843 --GEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEE 889
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
9-324 1.59e-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: 1.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633      9 EVAPGSQGQPEgATIEGPGEPGAADLEGREASEEAAEAPRDLGAGVEARASGKEEG-----GCGQDEGTGGAQAQdprtg 83
Cdd:TIGR00927  629 DLSKGDVAEAE-HTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGeipaeRKGEQEGEGEIEAK----- 702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633     84 pEAETPGASGAPGEAEAAERDPEGAIPQGAEEAPSAQQVQGMSSGLDSQG-EAPEVPGDsrrepEDPTASEAGEEAEsGQ 162
Cdd:TIGR00927  703 -EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGkHEVETEGD-----RKETEHEGETEAE-GK 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    163 EAQGGGALGLQINPEVQGLAGDNMDTEapAGGPLGSESEPQGGGESSPQPQDEAIEivtteiggNESGElagasaadaag 242
Cdd:TIGR00927  776 EDEDEGEIQAGEDGEMKGDEGAEGKVE--HEGETEAGEKDEHEGQSETQADDTEVK--------DETGE----------- 834
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    243 egETLGKDGSEEAASEDARVDAHENGDQGKLQEETGEEEARPEPElkgpcegaiqekppdgsldGEEAKSTEHEEESQAE 322
Cdd:TIGR00927  835 --QELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEE-------------------EEEEEEEEEEEENEEP 893

                   ..
gi 27369633    323 LS 324
Cdd:TIGR00927  894 LS 895
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
378-440 7.32e-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: 7.32e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369633 378 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPA-DLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLE 440
Cdd:cd00570   8 GSPRSLRVRLALEEKGLPYELVPVDLGEGEQeEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
379-440 2.44e-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: 2.44e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27369633 379 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVktdvnkIEEFLE 440
Cdd:cd03060   9 CPYAMRARMALLLAGITVELREVELKNKPAEMLAASPkGTVPVLVLGNGTV------IEESLD 65
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-226 2.62e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    2 AEATEPKevAPGSQGQPEGATIEGPGEPGAADLEGREASEEAAEAPRDLGAGVEARASGKEEGGcgqdEGTGGAQAQDPR 81
Cdd:PRK07764 610 EEAARPA--APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA----KAGGAAPAAPPP 683
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   82 TGPEAETPGASGAPGEAEAAERDPEGAIPQGAEEAPSAQQVQgmssglDSQGEAPEVPGDSRREPEDPTASEAGEEAESG 161
Cdd:PRK07764 684 APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA------QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQ 757
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27369633  162 QEAQGGGAlglqinPEVQGLAGDNMDTEAPAGGPLgSESEPQGGGESSPQPQDEAIEIVTTEIGG 226
Cdd:PRK07764 758 PPPPPAPA------PAAAPAAAPPPSPPSEEEEMA-EDDAPSMDDEDRRDAEEVAMELLEEELGA 815
PHA03169 PHA03169
hypothetical protein; Provisional
11-216 2.78e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.89  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   11 APGSQGQPEGATIEGPGEPGAADLEGREASEeaaeaprDLGAGVEARASGKEEGGCGQDEGTGGAQAQDPRTGP-EAETP 89
Cdd:PHA03169  41 ARAAKPAPPAPTTSGPQVRAVAEQGHRQTES-------DTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPsGSAEE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   90 GASGAPGEAEAAErDPEGAIPQGAEEAPSAQQVQGMSSGLDSQGEAPEVPGDSRREPEDPTASEAGEEAESGQEAQGGGA 169
Cdd:PHA03169 114 LASGLSPENTSGS-SPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGP 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 27369633  170 lGLQINPEVQGLAGDNMDTEAPAGGPLGSESEPQGGGESSPQPQDEA 216
Cdd:PHA03169 193 -PQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPT 238
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
378-583 5.50e-05

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 44.50  E-value: 5.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 378 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEklvppRYPK 450
Cdd:COG0625   9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAE-----RYPE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 451 ---LGTQHPE-----------SNSAGNDVFAKFSAFIKNTKKDANEIYEKNLLRALKKLDSYLnsplpdeidadssedvt 516
Cdd:COG0625  80 pplLPADPAArarvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL----------------- 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27369633 517 vSQRKFLDGDELTLADCNLLPKLHIIkivakkyRDFEFP-SEMTGIWRYLNNAYARDEFTNTCPADRE 583
Cdd:COG0625 143 -AGGPYLAGDRFSIADIALAPVLRRL-------DRLGLDlADYPNLAAWLARLAARPAFQRALAAAEP 202
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
432-555 5.74e-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: 5.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 432 VNKIEEFLEEKLVPPRYPKLGTQhpesnsagndvfakfsAFIKNTKKDANEIYEKNLLRALKKLDSYLnsplpdeidads 511
Cdd:cd00299   1 VRALEDWADATLAPPLVRLLYLE----------------KVPLPKDEAAVEAAREELPALLAALEQLL------------ 52
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 27369633 512 sedvtvSQRKFLDGDELTLADCNLLPKLHIIKIVAKKYRDFE-FP 555
Cdd:cd00299  53 ------AGRPYLAGDQFSLADVALAPVLARLEALGPYYDLLDeYP 91
PHA03169 PHA03169
hypothetical protein; Provisional
2-166 6.26e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.73  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    2 AEATEPKEVAPGSQGQPEGATIEGPGEPGAADLEGREASEEAAEAPRDLGAGVEARASGKEEGGCGQDEGTgGAQAQDPR 81
Cdd:PHA03169  76 AEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPES 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   82 TGPEAETPGASGAPGEAEAAERDPEGAIPQGAEEAPSAQQVQGMSSGLDSQGEAPEVPGDSRREPEDPTASEAGEEAESG 161
Cdd:PHA03169 155 HNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234

                 ....*
gi 27369633  162 QEAQG 166
Cdd:PHA03169 235 DEPTE 239
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
66-216 9.82e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 9.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   66 CGQDEGTGGAQAQDPRTGPEAETPGASGAPGEAEAAErDPEGAIPQGAEEAPSAQQVQGMSSGLDSQGEAPEVPGDSRRE 145
Cdd:PRK07764 586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPA-APAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369633  146 PEDPTASEAGEEAESGQEAQGGGALGLQINPEVQGLAGDNMDTEAPAGGPLGSESEPQGGGESSPQPQDEA 216
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA 735
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
378-442 2.65e-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: 2.65e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27369633 378 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDgEVKTDVNKIEEFLEEK 442
Cdd:cd03059   8 DDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPyGTVPTLVDRD-LVLYESRIIMEYLDER 72
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2-210 6.06e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633     2 AEATEPKEVAPGSQGQPEGATIEGPGEPGAADLEGREASEEAAEAPRDLGAGVEARASgkEEGGCGQDEGTGGAQAQDPR 81
Cdd:PHA03307   99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAG--ASPAAVASDAASSRQAALPL 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633    82 TGPEAETPgASGAPGEAEAAERDPEGAIPQGAEEAPSAQQVQGMSSGLDSQGEApevpGDSRREPEDPTASEAGEEAESG 161
Cdd:PHA03307  177 SSPEETAR-APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA----DDAGASSSDSSSSESSGCGWGP 251
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 27369633   162 QEAQGGGALGLQINP--EVQGLAGDNMDTEAPAGGPLGSESEPqgGGESSP 210
Cdd:PHA03307  252 ENECPLPRPAPITLPtrIWEASGWNGPSSRPGPASSSSSPRER--SPSPSP 300
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
5-163 6.50e-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: 43.06  E-value: 6.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633      5 TEPKEVAPGSQGQPEGATIEGPGEPGA----ADLEGREASEEAAEAPRDlGAGVEARASGKEEGGCGQDEGTGGAQAqdp 80
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEDEGEIETGEegeeVEDEGEGEAEGKHEVETE-GDRKETEHEGETEAEGKEDEDEGEIQA--- 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633     81 rtGPEAETPGASGAPGEAEAAERDPEGAIPQGAEEAPSAQQVQGMSSGLDSQGEAPEVPGDSRREPEDPTASEAGEEAES 160
Cdd:TIGR00927  786 --GEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDS 863

                   ...
gi 27369633    161 GQE 163
Cdd:TIGR00927  864 EEE 866
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
482-578 8.18e-04

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: 39.86  E-value: 8.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633 482 EIYEK---NLLRALKKLDSYLnsplpdeidadssedvtvSQRKFLDGDELTLADCNLLPKL--------HIIKIVAKKYR 550
Cdd:cd03190  33 EAYDKavkELFEALDKLEKRL------------------SKQPYLLGDRLTEADIRLFTTLirfdpvyhQHFKCNLKTIR 94
                        90       100
                ....*....|....*....|....*...
gi 27369633 551 DfeFPSemtgIWRYLNNAYARDEFTNTC 578
Cdd:cd03190  95 D--YPN----LWRYLRRLYQNPGVFETT 116
PRK12678 PRK12678
transcription termination factor Rho; Provisional
21-168 8.31e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   21 ATIE----GPGEPGAADLEGREASEEAAEAPRDLGAGVEARASGKEEGGCGQDEGTGGAQAQDPRTGPEAETPGASGAPG 96
Cdd:PRK12678  53 AAIKeargGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27369633   97 EAEAAERDPEGAIPQGAEEAPSAQQvqgmSSGLDSQGEAPEVPGDSRREPEDPTASEAGEEAESGQEAQGGG 168
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEAR----ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG 200
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
379-447 1.04e-03

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 37.98  E-value: 1.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27369633   379 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLVPPR 447
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
485-565 1.61e-03

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 37.30  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369633   485 EKNLLRALKKLDSYLnsplpdeidadssedvtvSQRKFLDGDELTLADCNLLPKLHIIKIVakkYRDFEFPSEMTGIWRY 564
Cdd:pfam13410   6 REQLRAALDALEARL------------------ADGPGLLGDRPTLADIALAPVLARLDAA---YPGLDLREGYPRLRAW 64

                  .
gi 27369633   565 L 565
Cdd:pfam13410  65 L 65
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
379-440 7.27e-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: 36.18  E-value: 7.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27369633 379 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVKTDVNKIEEFLE 440
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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