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Conserved domains on  [gi|1939402019|ref|NP_788267|]
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chloride intracellular channel protein 6 [Rattus norvegicus]

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. ...
380-613 1.58e-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: 1.58e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 380 ITLFVKAGSDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 459
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 460 LVPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKF 539
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402019 540 LDGDELTLADCNLLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKRMK 613
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
51-318 2.49e-11

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: 66.94  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   51 GEGAEAMASGKEEGGcgqdgeigEVQAQDPRPGPGTETPGTSGAPGEA--EAAECDSEGALIPQGAEEAPSAQQVQGTSS 128
Cdd:TIGR00927  633 GDVAEAEHTGERTGE--------EGERPTEAEGENGEESGGEAEQEGEteTKGENESEGEIPAERKGEQEGEGEIEAKEA 704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  129 GLDAQGEAPEVPEDARREPE---DPKASEAGEEAE-SGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQ 204
Cdd:TIGR00927  705 DHKGETEAEEVEHEGETEAEgteDEGEIETGEEGEeVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ 784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  205 GGGESSPQPQDEAIEIAAAEV-----GGHEPGELAGASAADAKGEGET----LRKDGFEEAAPEEARVDSGENG-FEEAA 274
Cdd:TIGR00927  785 AGEDGEMKGDEGAEGKVEHEGeteagEKDEHEGQSETQADDTEVKDETgeqeLNAENQGEAKQDEKGVDGGGGSdGGDSE 864
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1939402019  275 PEEARVDSGENRDQGRLQEETGEEEARPESGLKGPceEAIQEKA 318
Cdd:TIGR00927  865 EEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWP--ETRQKQA 906
 
Name Accession Description Interval E-value
O-ClC TIGR00862
intracellular chloride channel protein; The Organellar Chloride Channel (O-ClC) Family (TC 1.A. ...
380-613 1.58e-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: 1.58e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 380 ITLFVKAGSDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 459
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 460 LVPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKF 539
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402019 540 LDGDELTLADCNLLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKRMK 613
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
472-611 1.51e-101

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: 304.25  E-value: 1.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKFLDGDELTLADCN 551
Cdd:cd10301     1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKR 611
Cdd:cd10301    81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
393-594 1.02e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 106.62  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 393 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLvpPRyPKLGTQh 472
Cdd:PLN02817   70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKY--PD-PPLATP- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 473 PESNSAGNDVFAKFSAFIKNtkKDANDIYEKNLLRALKKLDSYLNSPLPdeidaystedvtvsqrkFLDGDELTLADCNL 552
Cdd:PLN02817  146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1939402019 553 LPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNT 594
Cdd:PLN02817  207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
51-318 2.49e-11

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 66.94  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   51 GEGAEAMASGKEEGGcgqdgeigEVQAQDPRPGPGTETPGTSGAPGEA--EAAECDSEGALIPQGAEEAPSAQQVQGTSS 128
Cdd:TIGR00927  633 GDVAEAEHTGERTGE--------EGERPTEAEGENGEESGGEAEQEGEteTKGENESEGEIPAERKGEQEGEGEIEAKEA 704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  129 GLDAQGEAPEVPEDARREPE---DPKASEAGEEAE-SGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQ 204
Cdd:TIGR00927  705 DHKGETEAEEVEHEGETEAEgteDEGEIETGEEGEeVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ 784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  205 GGGESSPQPQDEAIEIAAAEV-----GGHEPGELAGASAADAKGEGET----LRKDGFEEAAPEEARVDSGENG-FEEAA 274
Cdd:TIGR00927  785 AGEDGEMKGDEGAEGKVEHEGeteagEKDEHEGQSETQADDTEVKDETgeqeLNAENQGEAKQDEKGVDGGGGSdGGDSE 864
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1939402019  275 PEEARVDSGENRDQGRLQEETGEEEARPESGLKGPceEAIQEKA 318
Cdd:TIGR00927  865 EEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWP--ETRQKQA 906
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
396-459 2.70e-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: 2.70e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939402019 396 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 459
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
66-287 2.90e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  66 CGQDGEIGEVQAQDPRPGPGTETPGTSGAPGEAEAAECDSEGAliPQGAEEAPSAQQVQGTSSGLDAQGEAPEVPEDARR 145
Cdd:PRK07764  586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPA--PAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 146 EPEDPKASEAGEEAESGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQGGGESSPQPQ---DEAIEIAA 222
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSpaaDDPVPLPP 743
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939402019 223 AEVGGHEPGELAGASAADAKGEGETLRKDGFEEAAPEEArvdsgengfEEAAPEEARVDSGENRD 287
Cdd:PRK07764  744 EPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE---------EEMAEDDAPSMDDEDRR 799
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
395-600 5.14e-05

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 44.50  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 395 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEklvppRYPK 467
Cdd:COG0625     9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAE-----RYPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 468 ---LGTQHPE-----------SNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLnsplpdeidaystedvt 533
Cdd:COG0625    80 pplLPADPAArarvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL----------------- 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939402019 534 vSQRKFLDGDELTLADCNLLPKLHIIkivakkyRGFEFP-SEMTGIWRYLNNAYARDEFTNTCPADQE 600
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. ...
380-613 1.58e-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: 1.58e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 380 ITLFVKAGSDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEK 459
Cdd:TIGR00862   3 IELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPEDLQNLAPGTHPPFLTYNTEVKTDVNKIEEFLEET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 460 LVPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKF 539
Cdd:TIGR00862  83 LCPPRYPKLSPKHPESNTAGLDIFAKFSAYIKNSNPEANDNLEKGLLKALKKLDDYLNSPLPEEIDEDSAEDEKVSRRKF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402019 540 LDGDELTLADCNLLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKRMK 613
Cdd:TIGR00862 163 LDGDELTLADCNLLPKLHIVKVVAKKYRNFDIPAEFTGVWRYLSNAYAREEFTNTCPDDKEIELAYADVAKRLK 236
GST_C_CLIC6 cd10301
C-terminal, alpha helical domain of Chloride Intracellular Channel 6; Glutathione ...
472-611 1.51e-101

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: 304.25  E-value: 1.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKFLDGDELTLADCN 551
Cdd:cd10301     1 HPESNSAGNDVFAKFSAFIKNPRKDANENLEKNLLKALRKLDNYLNTPLPDEIDAYSTEDITVSDRKFLDGNELTLADCN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKR 611
Cdd:cd10301    81 LLPKLHIIKVVAKKYRNFEFPTEMTGIWRYLNNAYARDEFTNTCPADQEIEYAYSDVAKR 140
GST_C_CLIC4 cd10296
C-terminal, alpha helical domain of Chloride Intracellular Channel 4; Glutathione ...
472-612 4.59e-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: 264.58  E-value: 4.59e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKFLDGDELTLADCN 551
Cdd:cd10296     1 HPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLDGNEMTLADCN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKRM 612
Cdd:cd10296    81 LLPKLHIVKVVAKKYRNFEIPKEMTGIWRYLSNAYSRDEFTNTCPSDKEIEIAYSDVAKRL 141
GST_C_CLIC5 cd10297
C-terminal, alpha helical domain of Chloride Intracellular Channel 5; Glutathione ...
472-612 4.44e-85

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: 261.82  E-value: 4.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKFLDGDELTLADCN 551
Cdd:cd10297     1 HRESNTAGIDIFSKFSAYIKNTKQQANAALEKGLTKALKKLDDYLNTPLPEEIDADSTEEEKVSNRKFLDGDELTLADCN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKRM 612
Cdd:cd10297    81 LLPKLHVVKIVAKKYRNFEIPSDMTGVWRYLKNAYARDEFTNTCAADKEIELAYADVAKRL 141
GST_C_CLIC1 cd10300
C-terminal, alpha helical domain of Chloride Intracellular Channel 1; Glutathione ...
472-610 5.23e-70

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: 5.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKFLDGDELTLADCN 551
Cdd:cd10300     1 NPESNTAGLDVFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDENSAEDEGVSQRKFLDGNELTLADCN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAK 610
Cdd:cd10300    81 LLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK 139
GST_C_CLIC2 cd10298
C-terminal, alpha helical domain of Chloride Intracellular Channel 2; Glutathione ...
472-610 7.57e-70

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: 222.06  E-value: 7.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKkDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKFLDGDELTLADCN 551
Cdd:cd10298     1 YKESFDVGSDIFAKFSAYIKNSP-ENNANQEKALLREFKRLDDYLNTPLPEEIDHDSAENITVSKRKFLDGDRLTLADCN 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAK 610
Cdd:cd10298    80 LLPKLHVIKVAAKKYCDFDIPADFTGVWRYLNNAYEREEFSQTCPADIEIEKAYASVAK 138
GST_C_CLIC cd03198
C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase ...
472-606 2.94e-64

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: 206.69  E-value: 2.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSplpdeidaystedvtvSQRKFLDGDELTLADCN 551
Cdd:cd03198     1 NPEANTAGEDLFAKFSAYIKNKDPAADEALRKALLKELSKLDAYLSS----------------SSRKFLDGDTLTLADCN 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYS 606
Cdd:cd03198    65 LLPKLHHIRVAGKAYKDFDIPDDFTGLWRYLKNAYETDEFTKTCPADQEIILHYK 119
GST_C_CLIC3 cd10299
C-terminal, alpha helical domain of Chloride Intracellular Channel 3; Glutathione ...
472-606 2.42e-60

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: 196.92  E-value: 2.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 472 HPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAysTEDVTVSQRKFLDGDELTLADCN 551
Cdd:cd10299     1 YKESNTAGNDVFHKFSAFIKNPVPAQDDALQKKLLRALLKLDSYLLTPLPHELAQ--NPHLSESQRRFLDGDALTLADCN 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1939402019 552 LLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYS 606
Cdd:cd10299    79 LLPKLHIVKVVCKHYRQFEIPAELKGVTRYLDSASQEKEFKYTCPNSAEILLAYR 133
GST_N_CLIC cd03061
GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, ...
377-465 4.61e-54

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


Pssm-ID: 239359  Cd Length: 91  Bit Score: 178.72  E-value: 4.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 377 EHDITLFVKAGSDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFL 456
Cdd:cd03061     3 EPEIELFVKASSDGESIGNCPFCQRLFMVLWLKGVVFNVTTVDMKRKPEDLKDLAPGTQPPFLLYNGEVKTDNNKIEEFL 82

                  ....*....
gi 1939402019 457 EEKLVPPRY 465
Cdd:cd03061    83 EETLCPPKY 91
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
393-594 1.02e-25

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 106.62  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 393 IGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLvpPRyPKLGTQh 472
Cdd:PLN02817   70 LGDCPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKY--PD-PPLATP- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 473 PESNSAGNDVFAKFSAFIKNtkKDANDIYEKNLLRALKKLDSYLNSPLPdeidaystedvtvsqrkFLDGDELTLADCNL 552
Cdd:PLN02817  146 PEKASVGSKIFSTFIGFLKS--KDPGDGTEQALLDELTSFDDYIKENGP-----------------FINGEKISAADLSL 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1939402019 553 LPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNT 594
Cdd:PLN02817  207 GPKLYHLEIALGHYKNWSVPDSLPFVKSYMKNIFSMESFVKT 248
PLN02378 PLN02378
glutathione S-transferase DHAR1
391-594 7.10e-19

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 85.53  E-value: 7.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 391 ESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKlvpprYPKLGT 470
Cdd:PLN02378   15 DHLGDCPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEK-----YPDPPL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 471 QHP-ESNSAGNDVFAKFSAFIKNtkKDANDIYEKNLLRALKKLDSYLNSplpdeidaystedvtvSQRKFLDGDELTLAD 549
Cdd:PLN02378   90 KTPaEFASVGSNIFGTFGTFLKS--KDSNDGSEHALLVELEALENHLKS----------------HDGPFIAGERVSAVD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1939402019 550 CNLLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNT 594
Cdd:PLN02378  152 LSLAPKLYHLQVALGHFKSWSVPESFPHVHNYMKTLFSLDSFEKT 196
GST_C_DHAR cd03201
C-terminal, alpha helical domain of Dehydroascorbate Reductase; Glutathione S-transferase (GST) ...
473-601 4.76e-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: 4.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 473 PESNSAGNDVFAKFSAFIKNtkKDANDIYEKNLLRALKKLDSYLNSPLPdeidaystedvtvsqrkFLDGDELTLADCNL 552
Cdd:cd03201     5 PEFASVGSKIFSTFVTFLKS--KDANDGSEQALLDELTALDEHLKTNGP-----------------FIAGEKITAVDLSL 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1939402019 553 LPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEI 601
Cdd:cd03201    66 APKLYHLRVALGHYKGWSVPESLTAVHKYMELLFSRESFKKTKAPDEMI 114
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
51-318 2.49e-11

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 66.94  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   51 GEGAEAMASGKEEGGcgqdgeigEVQAQDPRPGPGTETPGTSGAPGEA--EAAECDSEGALIPQGAEEAPSAQQVQGTSS 128
Cdd:TIGR00927  633 GDVAEAEHTGERTGE--------EGERPTEAEGENGEESGGEAEQEGEteTKGENESEGEIPAERKGEQEGEGEIEAKEA 704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  129 GLDAQGEAPEVPEDARREPE---DPKASEAGEEAE-SGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQ 204
Cdd:TIGR00927  705 DHKGETEAEEVEHEGETEAEgteDEGEIETGEEGEeVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ 784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  205 GGGESSPQPQDEAIEIAAAEV-----GGHEPGELAGASAADAKGEGET----LRKDGFEEAAPEEARVDSGENG-FEEAA 274
Cdd:TIGR00927  785 AGEDGEMKGDEGAEGKVEHEGeteagEKDEHEGQSETQADDTEVKDETgeqeLNAENQGEAKQDEKGVDGGGGSdGGDSE 864
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1939402019  275 PEEARVDSGENRDQGRLQEETGEEEARPESGLKGPceEAIQEKA 318
Cdd:TIGR00927  865 EEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWP--ETRQKQA 906
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
396-459 2.70e-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: 2.70e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939402019 396 CPFSQRLFMILWLKGVIFNVTTVDL--KRKPADLQNLAPGTNPPFMTF-DGEVKTDVNKIEEFLEEK 459
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
131-355 1.75e-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: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  131 DAQGEAPEVPEDARREPEDPKASEAGEEAE--SGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQG--SEGEPQGG 206
Cdd:TIGR00927  639 EHTGERTGEEGERPTEAEGENGEESGGEAEqeGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGetEAEEVEHE 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  207 GESSPQPQDEAIEIAAA----EVGGHEPGELAGASAADAKGEGETLRKDGFEEAAPE----EARVDSGENG--------- 269
Cdd:TIGR00927  719 GETEAEGTEDEGEIETGeegeEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKededEGEIQAGEDGemkgdegae 798
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  270 --------FEEAAPEEARVDSGENRDQGRLQEETGEEEARPESglkgPCEEAIQEKAPDGSLDGEEAKSTGHEESQVELS 341
Cdd:TIGR00927  799 gkvehegeTEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN----QGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEE 874
                          250
                   ....*....|....
gi 1939402019  342 NHLAEETSAQGGEE 355
Cdd:TIGR00927  875 EEEEEEEEEEEEEE 888
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
395-457 7.54e-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: 7.54e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402019 395 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPA-DLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLE 457
Cdd:cd00570     8 GSPRSLRVRLALEEKGLPYELVPVDLGEGEQeEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
165-377 1.88e-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: 54.23  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  165 ALGGSAPESQINPEVQGPVGDN-----MDTEAPAGEPQGSEGEPQGGGEsspqpqdeaiEIAAAEVGGHEPGELAGasaa 239
Cdd:TIGR00927  626 ALGDLSKGDVAEAEHTGERTGEegerpTEAEGENGEESGGEAEQEGETE----------TKGENESEGEIPAERKG---- 691
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  240 DAKGEGETLRKDGFEEAAPEEARVDSGENGFEEAAPEEARVDSGENRDQGRlQEETGEEEARPESGLKGPCEEAIQEKAP 319
Cdd:TIGR00927  692 EQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVE-DEGEGEAEGKHEVETEGDRKETEHEGET 770
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1939402019  320 DGSLDGEEAKSTGHEESQVELSNHLAEETSAQGGEELGRvNGRRENGPASEEGDLGQE 377
Cdd:TIGR00927  771 EAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEA-GEKDEHEGQSETQADDTE 827
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
231-395 4.17e-07

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 53.46  E-value: 4.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  231 GELAGASAADAKGEGEtlRKDGfEEAAPEEARVDSGENGFEEAAPEEARVDSGENRDQGRLQ-----EETGEEEARPESG 305
Cdd:TIGR00927  628 GDLSKGDVAEAEHTGE--RTGE-EGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPaerkgEQEGEGEIEAKEA 704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  306 -LKGPCEEAIQEKAPDGSLDGEEAKSTGHEESQVELSNHlAEETSAQGGEELGRVNGRRENGPASEEGDLGQEHDITLFV 384
Cdd:TIGR00927  705 dHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVED-EGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEI 783
                          170
                   ....*....|.
gi 1939402019  385 KAGSDGESIGN 395
Cdd:TIGR00927  784 QAGEDGEMKGD 794
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
138-379 3.14e-06

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 50.38  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  138 EVPEDARREPEDpKASEAGEEAESGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQGGGESSPQPQDEA 217
Cdd:TIGR00927  629 DLSKGDVAEAEH-TGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHK 707
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  218 IEIAAAEVGGHEPGELAGASA---ADAKGEGETLRKDGFEEA-APEEARVDSGENGFEEAAPEEARVDSGENRDQ----- 288
Cdd:TIGR00927  708 GETEAEEVEHEGETEAEGTEDegeIETGEEGEEVEDEGEGEAeGKHEVETEGDRKETEHEGETEAEGKEDEDEGEiqage 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  289 -GRLQEETGEEEARPESGLKGPCEEAIQEKAPDGSLDGEEAKS-TGHEESQVELSNHLAE-ETSAQGGEELGRVNGRREN 365
Cdd:TIGR00927  788 dGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDeTGEQELNAENQGEAKQdEKGVDGGGGSDGGDSEEEE 867
                          250
                   ....*....|....
gi 1939402019  366 GPASEEGDLGQEHD 379
Cdd:TIGR00927  868 EEEEEEEEEEEEEE 881
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
2-219 7.44e-06

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 49.22  E-value: 7.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019    2 AEATEPKEVSSGSQGQPEGaviEGPGEPGAADLEGREASEGAAEAPRDLGEGAEAMASGKEEGG---CGQDGEiGEVQAQ 78
Cdd:TIGR00927  677 GENESEGEIPAERKGEQEG---EGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEgeeVEDEGE-GEAEGK 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   79 DPRPGPGTETPGTSGAPGEAEAAECDSEGALipqGAEEAPSAQQVQGTSSGLDAQGEAPEVPEDARREPEDPKASEAGEE 158
Cdd:TIGR00927  753 HEVETEGDRKETEHEGETEAEGKEDEDEGEI---QAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVK 829
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939402019  159 AESGqealggsapESQINPEVQGpvgdnmdtEAPAGEpQGSEGEPQGGGESSPQPQDEAIE 219
Cdd:TIGR00927  830 DETG---------EQELNAENQG--------EAKQDE-KGVDGGGGSDGGDSEEEEEEEEE 872
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
396-457 2.51e-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: 2.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939402019 396 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVktdvnkIEEFLE 457
Cdd:cd03060     9 CPYAMRARMALLLAGITVELREVELKNKPAEMLAASPkGTVPVLVLGNGTV------IEESLD 65
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
66-287 2.90e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  66 CGQDGEIGEVQAQDPRPGPGTETPGTSGAPGEAEAAECDSEGAliPQGAEEAPSAQQVQGTSSGLDAQGEAPEVPEDARR 145
Cdd:PRK07764  586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPA--PAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 146 EPEDPKASEAGEEAESGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQGGGESSPQPQ---DEAIEIAA 222
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSpaaDDPVPLPP 743
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939402019 223 AEVGGHEPGELAGASAADAKGEGETLRKDGFEEAAPEEArvdsgengfEEAAPEEARVDSGENRD 287
Cdd:PRK07764  744 EPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE---------EEMAEDDAPSMDDEDRR 799
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
74-260 4.30e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 46.63  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  74 EVQAQDPRPGPGTE-------TPGTSGAPGEAEAAE--CDSEGALIPQGAEEAPSAQQVQGTSsgldaqgEAPEVPEDAR 144
Cdd:PRK08691  388 ETAAKKPQPRPEAEtaqtpvqTASAAAMPSEGKTAGpvSNQENNDVPPWEDAPDEAQTAAGTA-------QTSAKSIQTA 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 145 REPEDPKASEAGEEAESGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQGGGESSPQPQDEAiEIAAAE 224
Cdd:PRK08691  461 SEAETPPENQVSKNKAADNETDAPLSEVPSENPIQATPNDEAVETETFAHEAPAEPFYGYGFPDNDCPPEDGA-EIPPPD 539
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1939402019 225 VGGHEPGELAGAsAADAKGEGETLRKDGFEEAAPEE 260
Cdd:PRK08691  540 WEHAAPADTAGG-GADEEAEAGGIGGNNTPSAPPPE 574
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
395-600 5.14e-05

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 44.50  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 395 NCPFSQRLFMILWLKGVIFNVTTVDLKR---KPADLQNLapgtNP----PFMTFDGEVKTDVNKIEEFLEEklvppRYPK 467
Cdd:COG0625     9 PSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLAL----NPlgkvPVLVDDGLVLTESLAILEYLAE-----RYPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 468 ---LGTQHPE-----------SNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLnsplpdeidaystedvt 533
Cdd:COG0625    80 pplLPADPAArarvrqwlawaDGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL----------------- 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939402019 534 vSQRKFLDGDELTLADCNLLPKLHIIkivakkyRGFEFP-SEMTGIWRYLNNAYARDEFTNTCPADQE 600
Cdd:COG0625   143 -AGGPYLAGDRFSIADIALAPVLRRL-------DRLGLDlADYPNLAAWLARLAARPAFQRALAAAEP 202
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
87-246 1.71e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 44.58  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  87 ETPGTSGAPGEAEAAECDSEGALIPQGAEEAP----SAQQVQGTSSGLDAQGEAPEVPEDARREPEDPKASEAGEEAESG 162
Cdd:PRK13108  293 DEALEREPAELAAAAVASAASAVGPVGPGEPNqpddVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 163 QEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEG-EPQGGGESSPQPQDEAIEIAAAEVGGHEPGELAGASAADA 241
Cdd:PRK13108  373 REQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDEtEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQDD 452

                  ....*
gi 1939402019 242 KGEGE 246
Cdd:PRK13108  453 FSSRR 457
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
449-572 2.60e-04

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: 40.56  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 449 VNKIEEFLEEKLVPPRYPKLGTQhpesnsagndvfakfsAFIKNTKKDANDIYEKNLLRALKKLDSYLnsplpdeidays 528
Cdd:cd00299     1 VRALEDWADATLAPPLVRLLYLE----------------KVPLPKDEAAVEAAREELPALLAALEQLL------------ 52
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1939402019 529 tedvtvSQRKFLDGDELTLADCNLLPKLHIIKIVAKKYRGFE-FP 572
Cdd:cd00299    53 ------AGRPYLAGDQFSLADVALAPVLARLEALGPYYDLLDeYP 91
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
395-459 2.73e-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: 2.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939402019 395 NCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDgEVKTDVNKIEEFLEEK 459
Cdd:cd03059     8 DDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPyGTVPTLVDRD-LVLYESRIIMEYLDER 72
PRK12678 PRK12678
transcription termination factor Rho; Provisional
163-373 3.00e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 163 QEALGGSAPESQinpevqgpvgdnmDTEAPAGEPQGSEGEPQGGGESSPQPQDEAIEIAAAEVGGHEPGELAGASAADAK 242
Cdd:PRK12678   56 KEARGGGAAAAA-------------ATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAP 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 243 GEGETLRKDGFEEAAPEEARVDSGENGFEEAAPEEARVDSGENRDQGRLQEETGEEEARPESGLKGPCEEAIQEKAPDGS 322
Cdd:PRK12678  123 EAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1939402019 323 LDGEEAKSTGHEESqvelsnhlaEETSAQGGEELGRVNGRRENGPASEEGD 373
Cdd:PRK12678  203 RDRRDRREQGDRRE---------ERGRRDGGDRRGRRRRRDRRDARGDDNR 244
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-179 3.39e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   2 AEATEPKevSSGSQGQPEGAVIEGPGEPGAADLEGREASEGAAEAPRDLGEGAEAMASGKEEGGCGQDGEIGEVQAQDPR 81
Cdd:PRK07764  610 EEAARPA--APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP 687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  82 PGPGTETPGTSGAPGEAEAAECDSEGALIPQGAEEAPSAQQVQGTSSGlDAQGEAPEVPEDARREPEDPKASEAGEEAES 161
Cdd:PRK07764  688 AAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA-DDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766
                         170
                  ....*....|....*...
gi 1939402019 162 GQEALGGSAPESQINPEV 179
Cdd:PRK07764  767 AAAPAAAPPPSPPSEEEE 784
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
4-238 6.06e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   4 ATEPKEVSSGSQGQPEGAVIEG----PGEPGAADLEGREASEGAAEAPRDlGEGAEAMASGKEEGGCGQDGEIGEVQAQD 79
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEeaarPAAPAAPAAPAAPAPAGAAAAPAE-ASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  80 PRPGPGTETPGTSGAPGEAEAAecdsegaliPQGAEEAPSAQQvqgtssglDAQGEAPEVPEDARREPEDPKASEAGEEA 159
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAA---------PAAPAGAAPAQP--------APAPAATPPAGQADDPAAQPPQAAQGASA 730
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 160 ESGQEALGGSAPESqinPEVQGPVGDNMDTEAPAGEPQGSEGEPQGGGESSPQPQDEAIEIAAAEVG--GHEPGELAGAS 237
Cdd:PRK07764  731 PSPAADDPVPLPPE---PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDdeDRRDAEEVAME 807

                  .
gi 1939402019 238 A 238
Cdd:PRK07764  808 L 808
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
6-201 6.31e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 42.66  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   6 EPKEVSSGSQGQPEGAVIEGPGEPGAADlegrEASEGAAEAPRDLGEgaeamASGKEEGGCGQDGEIGEVQAQD-PRPGP 84
Cdd:PRK13108  280 EAPGALRGSEYVVDEALEREPAELAAAA----VASAASAVGPVGPGE-----PNQPDDVAEAVKAEVAEVTDEVaAESVV 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  85 GTETPGTSGAPGEAEAAECDSEGALIPQGAEEAPSAQQVqgtssglDAQGEAPEVPEDARREPEDPKASEAgEEAESgqe 164
Cdd:PRK13108  351 QVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQV-------DAEAASAAPEEPAALASEAHDETEP-EVPEK--- 419
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1939402019 165 alggSAPESqinpevqGPVGDNMDTEA-PAGEPQGSEG 201
Cdd:PRK13108  420 ----AAPIP-------DPAKPDELAVAgPGDDPAEPDG 446
PHA03169 PHA03169
hypothetical protein; Provisional
108-343 7.62e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 108 ALIPQGAEEAPSAQQVQGTSSGLDAQGEAPEVPEDARREPEDPKASEAGEEAESGQEALGGSAPESQinpevqgpvgdnm 187
Cdd:PHA03169   43 AAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSG------------- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 188 dteapAGEPQGSEGEPQGGGESSPQ--PQDEAIEIAAAEVGGHEPGELAGASAADAKGEGETLRKDGFEEAAPeearvds 265
Cdd:PHA03169  110 -----SAEELASGLSPENTSGSSPEspASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEE------- 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939402019 266 GENGFEEAAPEEARVDSGENRDQGRLQEETGEEEARPESglkgpcEEAIQEKAPDGSLDGE-EAKSTGHEESQVELSNH 343
Cdd:PHA03169  178 PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQS------PTPQQAPSPNTQQAVEhEDEPTEPEREGPPFPGH 250
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
502-582 9.47e-04

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 38.07  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 502 EKNLLRALKKLDSYLnsplpdeidaystedvtvSQRKFLDGDELTLADCNLLPKLHIIKIVakkYRGFEFPSEMTGIWRY 581
Cdd:pfam13410   6 REQLRAALDALEARL------------------ADGPGLLGDRPTLADIALAPVLARLDAA---YPGLDLREGYPRLRAW 64

                  .
gi 1939402019 582 L 582
Cdd:pfam13410  65 L 65
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
396-464 1.07e-03

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 37.98  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939402019 396 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLVPPR 464
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
PHA03169 PHA03169
hypothetical protein; Provisional
5-235 1.16e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   5 TEPKEVSSGSQGQPEGAVIEGPGEPGAADLEGREASEGAAEAPRDLGEGAEAMASGKEEGGCGQDGEIGEVQAQDPRPGP 84
Cdd:PHA03169   54 SGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPAS 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  85 GTETPGTSGAPGEAEAAEcdsegaliPQGAEEAPSAQQVQGtssgldAQGEAPEVPEDArrEPEDPKASEAGEEAESGQE 164
Cdd:PHA03169  134 HSPPPSPPSHPGPHEPAP--------PESHNPSPNQQPSSF------LQPSHEDSPEEP--EPPTSEPEPDSPGPPQSET 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939402019 165 alGGSAPESQINPEVQGPVGDNMDTEAPAGE-PQGSEGEPQGGGESSPQPQDEAIEIAAAEVGGHEPGELAG 235
Cdd:PHA03169  198 --PTSSPPPQSPPDEPGEPQSPTPQQAPSPNtQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPG 267
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
5-174 1.25e-03

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019    5 TEPKEVSSGSQGQPEGAVIEGPGEPGA----------ADLEGREASEGAAEAPRDLGEGAEAMASGKEEGGC-------- 66
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEDEGEIETGEegeevedegeGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGeiqagedg 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   67 ---GQDGEIGEVQAQDPRPGPGTETPGTSGAPGEAEAAECDSEGA--LIPQGAEEAPSAQQVQGTSSGLDAQGEAPEVPE 141
Cdd:TIGR00927  790 emkGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEqeLNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEE 869
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1939402019  142 DARREPEDPKASEAGEEAESGQEALGGSAPESQ 174
Cdd:TIGR00927  870 EEEEEEEEEEEEEEEEEEEENEEPLSLEWPETR 902
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
78-337 2.40e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   78 QDPRPGPGTETPGTSGAPGEAEAAECDSEGALIPQGAEEAPSAQQVQGT----SSGLDAQGEAPEVPEDARREP------ 147
Cdd:PHA03307    69 TGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPpptpPPASPPPSPAPDLSEMLRPVGspgppp 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  148 --EDPKASEAGEEAESGQEALGGSAPESQINPEVQGPVGdnmdteAPAGEPQGSegEPQGGGESSPQPQDEAIEIAAAE- 224
Cdd:PHA03307   149 aaSPPAAGASPAAVASDAASSRQAALPLSSPEETARAPS------SPPAEPPPS--TPPAAASPRPPRRSSPISASASSp 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  225 --VGGHEPGELAGASAADAKGEGETLRKDGFEEAAPE--EARVDSGENGFEEAAPEEARVDSGENRDQGRLQEETGE-EE 299
Cdd:PHA03307   221 apAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLprPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSpSP 300
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1939402019  300 ARPESGLKGPCEEAIQEKAPDGSLDGEEAKSTGHEESQ 337
Cdd:PHA03307   301 SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRG 338
PHA03169 PHA03169
hypothetical protein; Provisional
2-141 3.06e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019   2 AEATEPKEVSSGSQGQPEGAviEGPGEPGAADLEGREASEGAAEAPRDLGEGAEAMASGKEEGgcgQDGEIGEVQAQDPR 81
Cdd:PHA03169  115 ASGLSPENTSGSSPESPASH--SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSP---EEPEPPTSEPEPDS 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  82 PGPGTETPGTSGAPGEAEAaecDSEGALIPQGAEEAPSAQQVQGTSSGLDAQGEAPEVPE 141
Cdd:PHA03169  190 PGPPQSETPTSSPPPQSPP---DEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPP 246
PTZ00121 PTZ00121
MAEBL; Provisional
114-347 3.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  114 AEEAPSAQQVQGTSSGLDAQgEAPEVPEDARREPEDPKASEA---GEEAESGQEALGGSAPESQINPEVQGPVGDNMDTE 190
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  191 APAGEPQGSEGEPQGGGES--SPQPQDEAIEIAAAEVGGHEPGELAGAS-----AADAKGEGETLRKDGFEEAAPEEARv 263
Cdd:PTZ00121  1359 AEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKAdelkkAAAAKKKADEAKKKAEEKKKADEAK- 1437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  264 dsgENGFEEAAPEEARVDSGENRDQGRLQEETgeEEARPESGLKGPCEEAiqEKAPDGSLDGEEAKSTGHEESQVELSNH 343
Cdd:PTZ00121  1438 ---KKAEEAKKADEAKKKAEEAKKAEEAKKKA--EEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKK 1510

                   ....
gi 1939402019  344 LAEE 347
Cdd:PTZ00121  1511 KADE 1514
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
38-239 5.81e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  38 EASEGAAEAPRDLGEGAEAMASGKEEGGCGQDGEIGEVQAQDPRPGPGTETPGT-SGAPGEAEAAECDSEGALIPQGAEE 116
Cdd:PRK07003  359 EPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkAAAAAAATRAEAPPAAPAPPATADR 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 117 APSAQQVQGTSSGlDAQGEAPEVPEDARREPEDPKASEAGEEAESGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEP 196
Cdd:PRK07003  439 GDDAADGDAPVPA-KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1939402019 197 QGSEGEPQgggeSSPQPQDEAIEIAAAEvgghEPGELAGASAA 239
Cdd:PRK07003  518 REDAPAAA----APPAPEARPPTPAAAA----PAARAGGAAAA 552
PRK12678 PRK12678
transcription termination factor Rho; Provisional
121-327 5.95e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 39.50  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 121 QQVQGTSSGLDAQGEAPEVPEDARREPEDPKASEAGEEAESGQEALGGSAPESQINPEvQGPVGDNMDTEAPAGEPQGSE 200
Cdd:PRK12678   56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAA-AAAEAASAPEAAQARERRERG 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 201 GEPQGGGESSPQPQDEAIEIAAAEVGGHEPGELAGASAADAKGEGETLRKDGFEEAAPEEARVDSGEngfeEAAPEEARV 280
Cdd:PRK12678  135 EAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD----DRDRRDRRE 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1939402019 281 DSGENRDQGRLQEETGEEEARPESGLKGPCEEAIQEKAPDGSLDGEE 327
Cdd:PRK12678  211 QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEG 257
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
396-457 6.28e-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: 6.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939402019 396 CPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAP-GTNPPFMTFDGEVKTDVNKIEEFLE 457
Cdd:cd03055    27 CPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPqGKVPALEIDEGKVVYESLIICEYLD 89
fliD PRK08724
flagellar filament capping protein FliD;
93-301 7.93e-03

flagellar filament capping protein FliD;


Pssm-ID: 236335 [Multi-domain]  Cd Length: 673  Bit Score: 39.08  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019  93 GAPGEAEAAECDSEGALIPQGAEEAPSAQQVQGTSSGLDAQGEAPEVPEDARREPEDPKASEAGEEAESGQEALGGSAPE 172
Cdd:PRK08724  222 QVIAPLTPEEQKVAPELSDEEGNAIPPADQEVAEEIQDAAQIAQQQEATAALAALEEPISAGGATAAAAGQAAIDAAEAK 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402019 173 SQINPEvqgpvgDNMD--TEAPAGEPQGSEGEPqgggesspqpqDEAIEIAAAEVGGHEPGelagasaADAKGEGETLrk 250
Cdd:PRK08724  302 AYLRPE------DRIPgwTETASGTLLDSYPEP-----------EEELDEAAIAKAPDVPG-------WSNTASGTLT-- 355
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1939402019 251 DGFEEAAPEEARVDSgengfeEAAPEEARVDSGENRdqGRLQEETGEEEAR 301
Cdd:PRK08724  356 DSYVTPKEAQAEIEQ------KLAQEKAQLDAAVEK--GELTPEQAKQIAR 398
 
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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