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Conserved domains on  [gi|32563627|ref|NP_492564|]
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protein-disulfide reductase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 556-661 5.18e-37

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02964:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 132  Bit Score: 134.66  E-value: 5.18e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQV---DKNFEILFISSDRSEQEMNYYLqSSHGDWFHLPF-DSPISKHL-Q 630
Cdd:cd02964  15 LEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLkeeGKNFEIVFVSRDRSEESFNEYF-SEMPPWLAVPFeDEELRELLeK 93

                        90       100       110
                ....*....|....*....|....*....|.
gi 32563627 631 QFNTKnAIPTLIIIKPNGTVITVDGRDQVSS 661
Cdd:cd02964  94 QFKVE-GIPTLVVLKPDGDVVTTNARDEVEE 123
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 457-522 6.22e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


:

Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.69  E-value: 6.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   457 AEESERVRKLKEEEKRK----RVLEEEMEMKRKNEEAKIKLEAEMREKAEqAEIKRREEKSRALKKLQKE 522
Cdd:TIGR02794 135 KAEAEAERKAKEEAAKQaeeeAKAKAAAEAKKKAEEAKKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKA 203
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 556-661 5.18e-37

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 134.66  E-value: 5.18e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQV---DKNFEILFISSDRSEQEMNYYLqSSHGDWFHLPF-DSPISKHL-Q 630
Cdd:cd02964  15 LEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLkeeGKNFEIVFVSRDRSEESFNEYF-SEMPPWLAVPFeDEELRELLeK 93

                        90       100       110
                ....*....|....*....|....*....|.
gi 32563627 631 QFNTKnAIPTLIIIKPNGTVITVDGRDQVSS 661
Cdd:cd02964  94 QFKVE-GIPTLVVLKPDGDVVTTNARDEVEE 123
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 558-650 3.42e-29

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 111.25  E-value: 3.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   558 GKVIGLYYSGYWCQPSRDFTPILAQFYSQV--DKNFEILFISSDRSEQEMNYYLQSSHGDWFHLPFDSPISKHLQQFNTK 635
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkkKKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYGV 80

                          90
                  ....*....|....*
gi 32563627   636 NAIPTLIIIKPNGTV 650
Cdd:pfam13905  81 NAIPTLVLLDPNGEV 95
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 556-651 4.50e-10

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 58.16  E-value: 4.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQVdKNFEILFISSDRSEQEMNYYLQsSHGDWFHLPFDsPISKHLQQFNTk 635
Cdd:COG0526  26 LKGKPVLVNFWATWCPPCRAEMPVLKELAEEY-GGVVFVGVDVDENPEAVKAFLK-ELGLPYPVLLD-PDGELAKAYGV- 101

                        90
                ....*....|....*.
gi 32563627 636 NAIPTLIIIKPNGTVI 651
Cdd:COG0526 102 RGIPTTVLIDKDGKIV 117
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 457-522 6.22e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.69  E-value: 6.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   457 AEESERVRKLKEEEKRK----RVLEEEMEMKRKNEEAKIKLEAEMREKAEqAEIKRREEKSRALKKLQKE 522
Cdd:TIGR02794 135 KAEAEAERKAKEEAAKQaeeeAKAKAAAEAKKKAEEAKKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKA 203
PTZ00121 PTZ00121
MAEBL; Provisional
 457-530 8.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 8.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563627   457 AEESERVRKLKEEEKRK--RVLEEEMEMKRKNEEAKIKLEAEMReKAEqaEIKRREEKSRALKKLQKEETNKMEQM 530
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKaeELKKAEEENKIKAEEAKKEAEEDKK-KAE--EAKKDEEEKKKIAHLKKEEEKKAEEI 1773
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 456-529 1.05e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.02  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563627   456 KAEESERVRKLKEEEKRKRvleeEMEMKRKNEEAKIKLEAEMREKAEQAeiKRREEKSRALKKLQKEETNKMEQ 529
Cdd:pfam05672  26 QREREEQERLEKEEEERLR----KEELRRRAEEERARREEEARRLEEER--RREEEERQRKAEEEAEEREQREQ 93
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
556-653 1.22e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 40.37  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627  556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQV-DKNFEILFISSDRSEQEMNYYLQSshgdwFHLPFDSPISKHLQQFNT 634
Cdd:PRK03147  59 LKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYkEKGVEIIAVNVDETELAVKNFVNR-----YGLTFPVAIDKGRQVIDA 133

                         90       100
                 ....*....|....*....|.
gi 32563627  635 KNA--IPTLIIIKPNGTVITV 653
Cdd:PRK03147 134 YGVgpLPTTFLIDKDGKVVKV 154
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 457-529 4.27e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 4.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563627 457 AEESERVRKLKEEEKRKrvLEEEME-MKRKNEEAKIKLEAEMREKAEQaeikRREEKSRALKKLQKEETNKMEQ 529
Cdd:cd16269 207 AEAAEQERKLLEEQQRE--LEQKLEdQERSYEEHLRQLKEKMEEEREN----LLKEQERALESKLKEQEALLEE 274
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
455-529 5.86e-03

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 39.74  E-value: 5.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 455 RKAEESERVRKLKEE-EKRKRVLEEEMEM---KRKNEEAKIKLEA-----EMREKAEQA--EIKRREEKSRALKKLQKEE 523
Cdd:COG1193 529 ELEEEREEAERLREElEKLREELEEKLEEleeEKEEILEKAREEAeeilrEARKEAEELirELREAQAEEEELKEARKKL 608


                ....*.
gi 32563627 524 TNKMEQ 529
Cdd:COG1193 609 EELKQE 614
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 556-661 5.18e-37

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 134.66  E-value: 5.18e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQV---DKNFEILFISSDRSEQEMNYYLqSSHGDWFHLPF-DSPISKHL-Q 630
Cdd:cd02964  15 LEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLkeeGKNFEIVFVSRDRSEESFNEYF-SEMPPWLAVPFeDEELRELLeK 93

                        90       100       110
                ....*....|....*....|....*....|.
gi 32563627 631 QFNTKnAIPTLIIIKPNGTVITVDGRDQVSS 661
Cdd:cd02964  94 QFKVE-GIPTLVVLKPDGDVVTTNARDEVEE 123
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 558-650 3.42e-29

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 111.25  E-value: 3.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   558 GKVIGLYYSGYWCQPSRDFTPILAQFYSQV--DKNFEILFISSDRSEQEMNYYLQSSHGDWFHLPFDSPISKHLQQFNTK 635
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkkKKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYGV 80

                          90
                  ....*....|....*
gi 32563627   636 NAIPTLIIIKPNGTV 650
Cdd:pfam13905  81 NAIPTLVLLDPNGEV 95
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 556-660 7.50e-29

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 111.61  E-value: 7.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQV---DKNFEILFISSDRSEQEMNYYLqsSHGDWFHLPF-DSPISKHL-Q 630
Cdd:cd03009  16 LEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLkesGKNFEIVFISWDRDEESFNDYF--SKMPWLAVPFsDRERRSRLnR 93

                        90       100       110
                ....*....|....*....|....*....|
gi 32563627 631 QFNTKnAIPTLIIIKPNGTVITVDGRDQVS 660
Cdd:cd03009  94 TFKIE-GIPTLIILDADGEVVTTDARELVL 122
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 554-661 3.77e-12

Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity.


Pssm-ID: 239306  Cd Length: 146  Bit Score: 64.45  E-value: 3.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 554 RMLDGKVIGLYYSGYWCQPSRDFTPILAQFYSQVDKNFEI--------LFISSDRSEQEMNYYLQSSHGDWFHLPFDSPI 625
Cdd:cd03008  21 ARLENRVLLLFFGAVVSPQCQLFAPKLKDFFVRLTDEFYVdrsaqlalVYVSMDQSEQQQESFLKDMPKKWLFLPFEDEF 100

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 32563627 626 SKHLQ-QFNTKNaIPTLIIIKPNGTVITVDGRDQVSS 661
Cdd:cd03008 101 RRELEaQFSVEE-LPTVVVLKPDGDVLAANAVDEILR 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 556-651 4.50e-10

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 58.16  E-value: 4.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQVdKNFEILFISSDRSEQEMNYYLQsSHGDWFHLPFDsPISKHLQQFNTk 635
Cdd:COG0526  26 LKGKPVLVNFWATWCPPCRAEMPVLKELAEEY-GGVVFVGVDVDENPEAVKAFLK-ELGLPYPVLLD-PDGELAKAYGV- 101

                        90
                ....*....|....*.
gi 32563627 636 NAIPTLIIIKPNGTVI 651
Cdd:COG0526 102 RGIPTTVLIDKDGKIV 117
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 556-653 2.63e-06

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 46.85  E-value: 2.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQ-VDKNFEILFISSDRS-EQEMNYYLQsSHGDWFHLPFDsPISKHLQQFN 633
Cdd:cd02966  17 LKGKVVLVNFWASWCPPCRAEMPELEALAKEyKDDGVEVVGVNVDDDdPAAVKAFLK-KYGITFPVLLD-PDGELAKAYG 94

                        90       100
                ....*....|....*....|
gi 32563627 634 tKNAIPTLIIIKPNGTVITV 653
Cdd:cd02966  95 -VRGLPTTFLIDRDGRIRAR 113
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 457-522 6.22e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.69  E-value: 6.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   457 AEESERVRKLKEEEKRK----RVLEEEMEMKRKNEEAKIKLEAEMREKAEqAEIKRREEKSRALKKLQKE 522
Cdd:TIGR02794 135 KAEAEAERKAKEEAAKQaeeeAKAKAAAEAKKKAEEAKKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKA 203
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
556-651 6.43e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 43.32  E-value: 6.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQV-DKNFEILFISSDrSEQEMNYYLQSsHGDWFHLPFDsPISKHLQQFNT 634
Cdd:COG1225  19 LRGKPVVLYFYATWCPGCTAELPELRDLYEEFkDKGVEVLGVSSD-SDEAHKKFAEK-YGLPFPLLSD-PDGEVAKAYGV 95

                        90
                ....*....|....*..
gi 32563627 635 KnAIPTLIIIKPNGTVI 651
Cdd:COG1225  96 R-GTPTTFLIDPDGKIR 111
PTZ00121 PTZ00121
MAEBL; Provisional
 457-530 8.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 8.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563627   457 AEESERVRKLKEEEKRK--RVLEEEMEMKRKNEEAKIKLEAEMReKAEqaEIKRREEKSRALKKLQKEETNKMEQM 530
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKaeELKKAEEENKIKAEEAKKEAEEDKK-KAE--EAKKDEEEKKKIAHLKKEEEKKAEEI 1773
PTZ00121 PTZ00121
MAEBL; Provisional
 457-530 1.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563627   457 AEESERVRKlkEEEKRKrvleeEMEMKRKNEEAKiKLEAEMREKAEQAEiKRREEKSRA--LKKLQKEETNKMEQM 530
Cdd:PTZ00121 1655 AEEENKIKA--AEEAKK-----AEEDKKKAEEAK-KAEEDEKKAAEALK-KEAEEAKKAeeLKKKEAEEKKKAEEL 1721
PTZ00121 PTZ00121
MAEBL; Provisional
 457-530 1.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   457 AEESERVR----KLKEEEKRK--RVLEEEMEMKRKNEEAKiKLEAEMREKAEQAEIKRREEKSRALK-KLQKEETNKMEQ 529
Cdd:PTZ00121 1683 AEEDEKKAaealKKEAEEAKKaeELKKKEAEEKKKAEELK-KAEEENKIKAEEAKKEAEEDKKKAEEaKKDEEEKKKIAH 1761


                  .
gi 32563627   530 M 530
Cdd:PTZ00121 1762 L 1762
PTZ00121 PTZ00121
MAEBL; Provisional
 457-530 5.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   457 AEESERVRKLKEEEKRKRVLEEEMEMKRKNEEAKI-----------KLEAEMREKAEQAEIK----RREEKSR----ALK 517
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyeeekKMKAEEAKKAEEAKIKaeelKKAEEEKkkveQLK 1639

                          90
                  ....*....|...
gi 32563627   518 KLQKEETNKMEQM 530
Cdd:PTZ00121 1640 KKEAEEKKKAEEL 1652
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 456-529 1.05e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.02  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563627   456 KAEESERVRKLKEEEKRKRvleeEMEMKRKNEEAKIKLEAEMREKAEQAeiKRREEKSRALKKLQKEETNKMEQ 529
Cdd:pfam05672  26 QREREEQERLEKEEEERLR----KEELRRRAEEERARREEEARRLEEER--RREEEERQRKAEEEAEEREQREQ 93
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
556-653 1.22e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 40.37  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627  556 LDGKVIGLYYSGYWCQPSRDFTPILAQFYSQV-DKNFEILFISSDRSEQEMNYYLQSshgdwFHLPFDSPISKHLQQFNT 634
Cdd:PRK03147  59 LKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYkEKGVEIIAVNVDETELAVKNFVNR-----YGLTFPVAIDKGRQVIDA 133

                         90       100
                 ....*....|....*....|.
gi 32563627  635 KNA--IPTLIIIKPNGTVITV 653
Cdd:PRK03147 134 YGVgpLPTTFLIDKDGKVVKV 154
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 459-530 1.71e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 1.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32563627   459 ESERVRKLKEEEKRkrvleeEMEMKRKNEEAKIKLEAEM-REKAEQAEIKRRE-EKSRALKKLQKEETNK-MEQM 530
Cdd:pfam17380 297 EQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMdRQAAIYAEQERMAmERERELERIRQEERKReLERI 365
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 461-526 1.86e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 41.09  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32563627  461 ERVRKLKEEEKRKRVLEEEMEMKR-KNEEAKIKL-EAEMREKAEQAEIKRREEKSRALKKLQKEETNK 526
Cdd:PTZ00436 140 EHIHKVKNEKKKERQLAEQLAAKRlKDEQHRHKArKQELRKREKDRERARREDAAAAAAAKQKAAAKK 207
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 558-650 2.32e-03

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 38.36  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   558 GKVIGLY-YSGYWCQPSRDFTPILAQFYSQ-VDKNFEILFISSDRSEQEMNYylQSSHGDWFHLPFD--SPISKHLQQFN 633
Cdd:pfam00578  25 GKWVVLFfYPADWTPVCTTELPALADLYEEfKKLGVEVLGVSVDSPESHKAF--AEKYGLPFPLLSDpdGEVARAYGVLN 102

                          90
                  ....*....|....*....
gi 32563627   634 TKN--AIPTLIIIKPNGTV 650
Cdd:pfam00578 103 EEEggALRATFVIDPDGKV 121
PTZ00121 PTZ00121
MAEBL; Provisional
 457-526 3.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563627   457 AEE---SERVRKLKEEEKRKRVLEEEMEMKRKNEEAKIKLEaEMREKAEQA----EIKRREEKSRAlKKLQKEETNK 526
Cdd:PTZ00121 1292 ADEakkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-AAKKKAEEAkkaaEAAKAEAEAAA-DEAEAAEEKA 1366
PTZ00121 PTZ00121
MAEBL; Provisional
 445-530 4.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   445 KKKEEEDEKRRKAEESERVRKLKEEEKRKRVLEEEMEMKRKNEEAKIKLEaEMREKAEQAEiKRREEKSRALKKLQKEET 524
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAK-KAAEAKKKADEAKKAEEA 1521


                  ....*.
gi 32563627   525 NKMEQM 530
Cdd:PTZ00121 1522 KKADEA 1527
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 457-529 4.27e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 4.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563627 457 AEESERVRKLKEEEKRKrvLEEEME-MKRKNEEAKIKLEAEMREKAEQaeikRREEKSRALKKLQKEETNKMEQ 529
Cdd:cd16269 207 AEAAEQERKLLEEQQRE--LEQKLEdQERSYEEHLRQLKEKMEEEREN----LLKEQERALESKLKEQEALLEE 274
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 457-528 4.50e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 39.30  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   457 AEESERVRKLKEEEKRKRVLEE--EMEMKRKN--------------------------------EEAKIKLEAEMREKAE 502
Cdd:pfam13904  74 AQKEEREKEEQEAELRKRLAKEkyQEWLQRKArqqtkkreeshkqkaaesaskslakperkvsqEEAKEVLQEWERKKLE 153

                          90       100
                  ....*....|....*....|....*.
gi 32563627   503 QAEIKRREEKSRALKKLQKEETNKME 528
Cdd:pfam13904 154 QQQRKREEEQREQLKKEEEEQERKQL 179
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
455-529 5.86e-03

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 39.74  E-value: 5.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627 455 RKAEESERVRKLKEE-EKRKRVLEEEMEM---KRKNEEAKIKLEA-----EMREKAEQA--EIKRREEKSRALKKLQKEE 523
Cdd:COG1193 529 ELEEEREEAERLREElEKLREELEEKLEEleeEKEEILEKAREEAeeilrEARKEAEELirELREAQAEEEELKEARKKL 608


                ....*.
gi 32563627 524 TNKMEQ 529
Cdd:COG1193 609 EELKQE 614
PTZ00121 PTZ00121
MAEBL; Provisional
 449-530 7.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563627   449 EEDEKRRKAEESERVRKLKEEEKRKRV--LEEEMEMKRKNEEAKIKLEaEMREKAEqaEIKRREEKSRALKKLQK--EET 524
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKADEAKKKAE-EDKKKAD--ELKKAAAAKKKADEAKKkaEEK 1430


                  ....*.
gi 32563627   525 NKMEQM 530
Cdd:PTZ00121 1431 KKADEA 1436
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 458-530 8.30e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 8.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563627   458 EESERVRKLKEEEKRKRVLEEE-MEMKRKNEEAKIKLEAEMR--EKAEQAEIKRREEKSRALKKLQKEETNKMEQM 530
Cdd:pfam17380 319 EEAEKARQAEMDRQAAIYAEQErMAMERERELERIRQEERKRelERIRQEEIAMEISRMRELERLQMERQQKNERV 394
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 467-532 9.70e-03

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 36.89  E-value: 9.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563627   467 KEEEKRKRVLEEEMEMKRKNEEakiklEAEMREKAEQAEIKRREEKSrALKKLQKEETNKMEQMNN 532
Cdd:pfam04696  41 RLEEKAKQEKEELEERKREERE-----ELFEERRAEQIELRALEEKL-ELKELMETWHENLKALAN 100
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 461-522 9.94e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 9.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563627   461 ERVRKL--KEEEKRKRVLEEEMEMKRKNEEAKIKLEAEMREKAEQAEIKRREEKSRaLKKLQKE 522
Cdd:pfam17380 512 ERKRKLleKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR-LEAMERE 574
 
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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