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Conserved domains on  [gi|1063737144|ref|NP_001318769|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 519-616 5.77e-47

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


:

Pssm-ID: 464360  Cd Length: 92  Bit Score: 160.98  E-value: 5.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 519 CRQIACKKCGNLHAWFLTKKSKSTARWCQDCKEFHQAKDGDGWVEQASQHVLFglfqkvdmpRAYVCADSKIYEASQWYI 598
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLW---------RYYACMDGKVYDITEWAI 71

                          90       100
                  ....*....|....*....|.
gi 1063737144 599 CQG---MRCPANTHKPSFHVN 616
Cdd:pfam14901  72 CQGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 408-472 5.84e-21

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


:

Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 86.76  E-value: 5.84e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:pfam00226   1 DYYEILGVSP--DASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
5TM-5TMR_LYT super family cl28761
5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors ...
 216-300 8.82e-05

5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors of the LytS-YhcK type).


The actual alignment was detected with superfamily member pfam07694:

Pssm-ID: 429599  Cd Length: 170  Bit Score: 43.71  E-value: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 216 IRGFDSFIRMGTASFFSIMWCGL-FSAFSMFGM-------------TKFILISVATvlvaLFIGFVVGSVTLAISGLVLL 281
Cdd:pfam07694   1 IPLFRRLLSKRRLRLKDKVLLGLiFGLFSILGTytgieiepgaianTRAVGIVLAG----LLGGPIVGLIAGLIAGLHRY 76

                          90       100
                  ....*....|....*....|....
gi 1063737144 282 WLYG--SFW---TTLLFLFFGGLA 300
Cdd:pfam07694  77 FLGGftALAcgiSTILAGLIAGLL 100
ABC2_membrane super family cl21474
ABC-2 type transporter;
179-349 5.68e-04

ABC-2 type transporter;


The actual alignment was detected with superfamily member pfam01061:

Pssm-ID: 473876 [Multi-domain]  Cd Length: 204  Bit Score: 41.88  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 179 RDLVLTKMRQVFPVVfrwlmhfgsIILLLSLVWLDcAIRGFDSFIRMGtASFFSIMWCGLFSAFSM-------------- 244
Cdd:pfam01061  11 RDPSLGLWRLIQPIL---------MALIFGTLFGN-LGNQQGGLNRPG-LLFFSILFNAFSALSGIspvfekergvlyre 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 245 --FGMTKFILISVATVLVALFIGFVVGSVTLAISGLV--LLWLYGSFWTTLLFLFFGGLAFMMkherVALFIITVYSVYS 320
Cdd:pfam01061  80 laSPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMvgLPPSAGRFFLFLLVLLLTALAASS----LGLFISALAPSFE 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063737144 321 ALSYVGWLGLLLAFNL--AFISTDALIYFFK 349
Cdd:pfam01061 156 DASQLGPLVLLPLLLLsgFFIPIDSMPVWWQ 186
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 519-616 5.77e-47

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 160.98  E-value: 5.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 519 CRQIACKKCGNLHAWFLTKKSKSTARWCQDCKEFHQAKDGDGWVEQASQHVLFglfqkvdmpRAYVCADSKIYEASQWYI 598
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLW---------RYYACMDGKVYDITEWAI 71

                          90       100
                  ....*....|....*....|.
gi 1063737144 599 CQG---MRCPANTHKPSFHVN 616
Cdd:pfam14901  72 CQGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 408-472 5.84e-21

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 86.76  E-value: 5.84e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:pfam00226   1 DYYEILGVSP--DASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 408-464 2.96e-17

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 76.04  E-value: 2.96e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLD 464
Cdd:cd06257     1 DYYDILGVPP--DASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 408-481 1.10e-16

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 77.05  E-value: 1.10e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYDDELKREELL 481
Cdd:COG0484     1 DYYEILGVSR--DASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELL 72
DnaJ smart00271
DnaJ molecular chaperone homology domain;
407-467 1.52e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.19  E-value: 1.52e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063737144  407 PDHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGN-ERAAEAFKKLQNAYEVLLDSVK 467
Cdd:smart00271   1 TDYYEILGVPR--DASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 408-472 9.77e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 73.25  E-value: 9.77e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK10767    5 DYYEVLGVSR--NASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 408-472 2.18e-11

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 66.08  E-value: 2.18e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNmGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:TIGR02349   1 DYYEILGVSK--DASEEEIKKAYRKLAKKYHPDRN-KDKEAEEKFKEINEAYEVLSDPEKRAQYD 62
5TM-5TMR_LYT pfam07694
5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors ...
 216-300 8.82e-05

5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors of the LytS-YhcK type).


Pssm-ID: 429599  Cd Length: 170  Bit Score: 43.71  E-value: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 216 IRGFDSFIRMGTASFFSIMWCGL-FSAFSMFGM-------------TKFILISVATvlvaLFIGFVVGSVTLAISGLVLL 281
Cdd:pfam07694   1 IPLFRRLLSKRRLRLKDKVLLGLiFGLFSILGTytgieiepgaianTRAVGIVLAG----LLGGPIVGLIAGLIAGLHRY 76

                          90       100
                  ....*....|....*....|....
gi 1063737144 282 WLYG--SFW---TTLLFLFFGGLA 300
Cdd:pfam07694  77 FLGGftALAcgiSTILAGLIAGLL 100
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
189-303 2.21e-04

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 44.09  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 189 VFPVVFRWLM-HFG-----------SIILLLSLVWLDCAIRGFDSFIRMGTASFFSImWCGLFSAFSMFGMTKF-ILISV 255
Cdd:COG2271   149 LAPPLLGWLLaAFGwraaflilglpGLLLALLRFWLLALAYFLVYFALYGFLTWLPT-YLVEVRGLSLAQAGLLlSLPFL 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 256 ATVLVALFIGF------------VVGSVTLAISGLVLLWLYGSFWTTLLFLFFGGLAFMM 303
Cdd:COG2271   228 AGIVGSLLGGWlsdrlgrrrklvLAIGLLLAALALLLLALLPSPALAIALLFLAGFGLGG 287
MFS_MefA_like cd06173
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
 197-333 2.96e-04

Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters; This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340863 [Multi-domain]  Cd Length: 383  Bit Score: 43.76  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 197 LMHFGSIILLLSLVWLDCAIRG------FDSFIRMGT------ASFFSIMWCGLFSAFSMFGMTKFILI----------S 254
Cdd:cd06173   166 LSFLLSALLLLFIRRPPPAAPGesssllLRDLREGLRylrrspLLRLLLLALALFALLGGALTVLLPLLakevlgggaaG 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 255 VATVLVALFIGFVVGSVTLAI-------------------SGLVLLWLYGSFWTTLLFLFFGGLAFMmkhervaLFIIT- 314
Cdd:cd06173   246 YGLLLAAFGVGALLGALLLGRlskrrrrgrllligalllgLALLVLGLSPSLWLLLAALFLLGLAGG-------LFNVPl 318

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063737144 315 ---------------VYSVYSALSYVGW-LGLLLA 333
Cdd:cd06173   319 ntllqlrvpdelrgrVFSVYNALNSGAMpLGALLA 353
ABC2_membrane pfam01061
ABC-2 type transporter;
179-349 5.68e-04

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 41.88  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 179 RDLVLTKMRQVFPVVfrwlmhfgsIILLLSLVWLDcAIRGFDSFIRMGtASFFSIMWCGLFSAFSM-------------- 244
Cdd:pfam01061  11 RDPSLGLWRLIQPIL---------MALIFGTLFGN-LGNQQGGLNRPG-LLFFSILFNAFSALSGIspvfekergvlyre 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 245 --FGMTKFILISVATVLVALFIGFVVGSVTLAISGLV--LLWLYGSFWTTLLFLFFGGLAFMMkherVALFIITVYSVYS 320
Cdd:pfam01061  80 laSPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMvgLPPSAGRFFLFLLVLLLTALAASS----LGLFISALAPSFE 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063737144 321 ALSYVGWLGLLLAFNL--AFISTDALIYFFK 349
Cdd:pfam01061 156 DASQLGPLVLLPLLLLsgFFIPIDSMPVWWQ 186
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 519-616 5.77e-47

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 160.98  E-value: 5.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 519 CRQIACKKCGNLHAWFLTKKSKSTARWCQDCKEFHQAKDGDGWVEQASQHVLFglfqkvdmpRAYVCADSKIYEASQWYI 598
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLW---------RYYACMDGKVYDITEWAI 71

                          90       100
                  ....*....|....*....|.
gi 1063737144 599 CQG---MRCPANTHKPSFHVN 616
Cdd:pfam14901  72 CQGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 408-472 5.84e-21

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 86.76  E-value: 5.84e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:pfam00226   1 DYYEILGVSP--DASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 408-464 2.96e-17

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 76.04  E-value: 2.96e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLD 464
Cdd:cd06257     1 DYYDILGVPP--DASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 408-481 1.10e-16

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 77.05  E-value: 1.10e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYDDELKREELL 481
Cdd:COG0484     1 DYYEILGVSR--DASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELL 72
DnaJ smart00271
DnaJ molecular chaperone homology domain;
407-467 1.52e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.19  E-value: 1.52e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063737144  407 PDHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGN-ERAAEAFKKLQNAYEVLLDSVK 467
Cdd:smart00271   1 TDYYEILGVPR--DASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 408-472 9.77e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 73.25  E-value: 9.77e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK10767    5 DYYEVLGVSR--NASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 408-472 1.39e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 66.76  E-value: 1.39e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14281    4 DYYEVLGVSRSADKDE--IKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14289 PRK14289
molecular chaperone DnaJ;
408-472 1.78e-11

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 66.39  E-value: 1.78e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14289    6 DYYEVLGVSKTATVDE--IKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYD 68
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 408-469 1.79e-11

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 59.63  E-value: 1.79e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQK 469
Cdd:COG5407     1 DPYEVLGVAK--TASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRA 60
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 408-472 2.18e-11

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 66.08  E-value: 2.18e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNmGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:TIGR02349   1 DYYEILGVSK--DASEEEIKKAYRKLAKKYHPDRN-KDKEAEEKFKEINEAYEVLSDPEKRAQYD 62
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 408-472 4.11e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 65.17  E-value: 4.11e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14294    5 DYYEILGVTR--DASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14297 PRK14297
molecular chaperone DnaJ;
408-472 5.29e-11

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 64.80  E-value: 5.29e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14297    5 DYYEVLGLEKGASDDE--IKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYD 67
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 408-472 7.35e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 64.38  E-value: 7.35e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14301    5 DYYEVLGVSR--DASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14279 PRK14279
molecular chaperone DnaJ;
408-477 8.35e-11

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 64.37  E-value: 8.35e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYdDELKR 477
Cdd:PRK14279   10 DFYKELGVSSDASAEE--IKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEY-DETRR 76
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
407-477 9.56e-11

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 58.58  E-value: 9.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063737144 407 PDHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGN-ERAAEAFKKLQNAYEVLLDSVKQKSYDDELKR 477
Cdd:COG2214     5 KDHYAVLGVPP--DASLEEIRQAYRRLAKLLHPDRGGELkALAEELFQRLNEAYEVLSDPERRAEYDRELGQ 74
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 408-472 9.96e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 64.09  E-value: 9.96e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14284    2 DYYTILGVSKTASPEE--IKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 408-472 1.01e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 63.86  E-value: 1.01e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14285    4 DYYEILGLSKGASKDE--IKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 408-472 1.23e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 64.05  E-value: 1.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14277    6 DYYEILGVDR--NATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 409-472 3.72e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 62.31  E-value: 3.72e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737144 409 HYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14286    6 YYDILGVSKSANDEE--IKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14295 PRK14295
molecular chaperone DnaJ;
408-473 4.28e-10

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 62.17  E-value: 4.28e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYDD 473
Cdd:PRK14295   10 DYYKVLGVPK--DATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDE 73
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 408-472 2.07e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 60.07  E-value: 2.07e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNmGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14278    4 DYYGLLGVSR--NASDAEIKRAYRKLARELHPDVN-PDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 408-472 8.11e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 58.30  E-value: 8.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNmGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14283    6 DYYEVLGVDR--NADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYD 67
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 408-472 1.96e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 56.82  E-value: 1.96e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMgNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14292    3 DYYELLGVSR--TASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14280 PRK14280
molecular chaperone DnaJ;
408-472 3.03e-08

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 56.27  E-value: 3.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMgNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14280    5 DYYEVLGVSKSASKDE--IKKAYRKLSKKYHPDINK-EEGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 408-472 3.47e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 56.01  E-value: 3.47e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNmGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14298    6 DYYEILGLSKDASVED--IKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 408-472 2.18e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 53.55  E-value: 2.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMgNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14276    5 EYYDRLGVSK--DASQDEIKKAYRKLSKKYHPDINK-EPGAEEKYKEVQEAYETLSDPQKRAAYD 66
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 387-472 3.31e-07

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 53.11  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 387 TSGTDSELTSEDeiARLLNCPDHYSALGLARYG-NVDMAYLKREYRKKAMLVHPDKNM--GNERAAEAFKKLQNAYEVLL 463
Cdd:COG5269    25 GRNVLNLYTRED--FKNWKKVDLYALLGLSKYRtKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLG 102


                  ....*....
gi 1063737144 464 DSVKQKSYD 472
Cdd:COG5269   103 DRKLRLQYD 111
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 408-472 3.73e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 52.85  E-value: 3.73e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMgNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14291    4 DYYEILGVSR--NATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14293 PRK14293
molecular chaperone DnaJ;
408-472 5.13e-07

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 52.30  E-value: 5.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPD--KNMGNEraaEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14293    4 DYYEILGVSR--DADKDELKRAYRRLARKYHPDvnKEPGAE---DRFKEINRAYEVLSDPETRARYD 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 408-473 5.96e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 52.24  E-value: 5.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNERAAE-AFKKLQNAYEVLLDSVKQKSYDD 473
Cdd:PRK14290    4 DYYKILGVDR--NASQEDIKKAFRELAKKWHPDLHPGNKAEAEeKFKEISEAYEVLSDPQKRRQYDQ 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
407-464 9.22e-07

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 46.71  E-value: 9.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063737144 407 PDHYSALGLARygNVDMAYLKREYRKKAMLVHPDK----------NMGNERAAEafkkLQNAYEVLLD 464
Cdd:COG1076     4 DDAFELLGLPP--DADDAELKRAYRKLQREHHPDRlaaglpeeeqRLALQKAAA----INEAYETLKD 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 375-473 2.58e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 50.20  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 375 GFPGDRGPGVASTSGTDSeltsedeiaRLLNCPDHYSALGLARygNVDMAYLKREYRKKAMLVHPDKNmGNEraaEAFKK 454
Cdd:PTZ00037    5 GFPFDGMPGGGFDGGRRK---------REVDNEKLYEVLNLSK--DCTTSEIKKAYRKLAIKHHPDKG-GDP---EKFKE 69

                          90
                  ....*....|....*....
gi 1063737144 455 LQNAYEVLLDSVKQKSYDD 473
Cdd:PTZ00037   70 ISRAYEVLSDPEKRKIYDE 88
PRK14288 PRK14288
molecular chaperone DnaJ;
409-472 2.95e-06

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 50.07  E-value: 2.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737144 409 HYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14288    5 YYEILEVEKHSNQET--IKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYD 66
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 408-472 1.56e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 47.70  E-value: 1.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGnERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14287    5 DYYEVLGVDRNASVDE--VKKAYRKLARKYHPDVNKA-PDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 392-482 2.24e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.86  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144  392 SELTSEDEIARLLNCPD--HYSALGLARygNVDMAYLKREYRKKAMLVHPDKNMGNErAAEAFKKLQNAYEVLLDSVKQK 469
Cdd:PTZ00341   556 SDVQQDSEAAPTIEIPDtlFYDILGVGV--NADMKEISERYFKLAENYYPPKRSGNE-GFHKFKKINEAYQILGDIDKKK 632

                           90
                   ....*....|....*..
gi 1063737144  470 SYD----DELKREELLN 482
Cdd:PTZ00341   633 MYNkfgyDGIKGVNFIH 649
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 408-472 4.14e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 46.55  E-value: 4.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNvdMAYLKREYRKKAMLVHPDkNMGNERAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14300    4 DYYQILGVSKTAS--QADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
5TM-5TMR_LYT pfam07694
5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors ...
 216-300 8.82e-05

5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors of the LytS-YhcK type).


Pssm-ID: 429599  Cd Length: 170  Bit Score: 43.71  E-value: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 216 IRGFDSFIRMGTASFFSIMWCGL-FSAFSMFGM-------------TKFILISVATvlvaLFIGFVVGSVTLAISGLVLL 281
Cdd:pfam07694   1 IPLFRRLLSKRRLRLKDKVLLGLiFGLFSILGTytgieiepgaianTRAVGIVLAG----LLGGPIVGLIAGLIAGLHRY 76

                          90       100
                  ....*....|....*....|....
gi 1063737144 282 WLYG--SFW---TTLLFLFFGGLA 300
Cdd:pfam07694  77 FLGGftALAcgiSTILAGLIAGLL 100
Yip1 pfam04893
Yip1 domain; The Yip1 integral membrane domain contains four transmembrane alpha helices. The ...
 230-339 1.51e-04

Yip1 domain; The Yip1 integral membrane domain contains four transmembrane alpha helices. The domain is characterized by the motifs DLYGP and GY. The Yip1 protein is a golgi protein involved in vesicular transport that interacts with GTPases.


Pssm-ID: 461468 [Multi-domain]  Cd Length: 173  Bit Score: 42.81  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 230 FFSIMWCGLFSAFSMFGMT-------KFILISVATVLVALFIGFVVGsvtLAISGLVLLWLY------GSFWTTLLFLFF 296
Cdd:pfam04893  26 LILLLLLALLAALALLIGGtqvgwalSLTQLSALAVAIGALIGILLG---LLILAALLYWLGrlfggrGSFKQTLAVAGY 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063737144 297 GGLAFMMkherVALFIITVYSVYSALSYVGWLGLLLAFNLAFI 339
Cdd:pfam04893 103 ALLPLIL----GGLLSGLLPLLWLPLSLVGLLFGIWSLYLLYL 141
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
189-303 2.21e-04

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 44.09  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 189 VFPVVFRWLM-HFG-----------SIILLLSLVWLDCAIRGFDSFIRMGTASFFSImWCGLFSAFSMFGMTKF-ILISV 255
Cdd:COG2271   149 LAPPLLGWLLaAFGwraaflilglpGLLLALLRFWLLALAYFLVYFALYGFLTWLPT-YLVEVRGLSLAQAGLLlSLPFL 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 256 ATVLVALFIGF------------VVGSVTLAISGLVLLWLYGSFWTTLLFLFFGGLAFMM 303
Cdd:COG2271   228 AGIVGSLLGGWlsdrlgrrrklvLAIGLLLAALALLLLALLPSPALAIALLFLAGFGLGG 287
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 196-334 2.60e-04

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 43.46  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 196 WLMHFGSIILLLSLVWL--DCAIRGFDSfirmgtasffsimWCGLFSAFSMFGMTKFILISVATVLVALFIGFVvgsvTL 273
Cdd:COG1807    84 FAARLPSALLGLLTVLLvyLLARRLFGR-------------RAALLAALLLLTSPLLLLFGRLATPDALLLLFW----TL 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 274 AISGLVLLWLYGSFWTTLLFLFFGGLAFMMKHeRVALFI----ITVYSVY-----SALSYVGWLGLLLAF 334
Cdd:COG1807   147 ALYALLRALERRRLRWLLLAGLALGLGFLTKG-PVALLLpglaLLLYLLLtrrwrRLRRLRLLLGLLLAL 215
PRK10266 PRK10266
curved DNA-binding protein;
408-490 2.65e-04

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 43.66  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 408 DHYSALGLARygNVDMAYLKREYRKKAMLVHPDknMGNERAAEA-FKKLQNAYEVLLDSVKQKSYDDELKREELLNYFRR 486
Cdd:PRK10266    5 DYYAIMGVKP--TDDLKTIKTAYRRLARKYHPD--VSKEPDAEArFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQ 80


                  ....
gi 1063737144 487 FQNS 490
Cdd:PRK10266   81 FQHG 84
MFS_MefA_like cd06173
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
 197-333 2.96e-04

Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters; This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340863 [Multi-domain]  Cd Length: 383  Bit Score: 43.76  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 197 LMHFGSIILLLSLVWLDCAIRG------FDSFIRMGT------ASFFSIMWCGLFSAFSMFGMTKFILI----------S 254
Cdd:cd06173   166 LSFLLSALLLLFIRRPPPAAPGesssllLRDLREGLRylrrspLLRLLLLALALFALLGGALTVLLPLLakevlgggaaG 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 255 VATVLVALFIGFVVGSVTLAI-------------------SGLVLLWLYGSFWTTLLFLFFGGLAFMmkhervaLFIIT- 314
Cdd:cd06173   246 YGLLLAAFGVGALLGALLLGRlskrrrrgrllligalllgLALLVLGLSPSLWLLLAALFLLGLAGG-------LFNVPl 318

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063737144 315 ---------------VYSVYSALSYVGW-LGLLLA 333
Cdd:cd06173   319 ntllqlrvpdelrgrVFSVYNALNSGAMpLGALLA 353
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 408-472 3.38e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 43.40  E-value: 3.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737144 408 DHYSALGLARYGNVDMayLKREYRKKAMLVHPDKNMGNErAAEAFKKLQNAYEVLLDSVKQKSYD 472
Cdd:PRK14296    5 DYYEVLGVSKTASEQE--IRQAYRKLAKQYHPDLNKSPD-AHDKMVEINEAADVLLDKDKRKQYD 66
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
194-340 3.60e-04

Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 43.42  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 194 FRWLMHFGSIILLLSLVWL------------DCAIRGFDSFIR-------MGTASFFSIMWCGLFSAFSMFGMTKF---- 250
Cdd:COG2814   163 WRWVFLVNAVLALLALLLLlrllpesrpaarARLRGSLRELLRrprllllLLLAFLLGFGFFALFTYLPLYLQEVLglsa 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 251 -------ILISVATVLVALFIGF----------VVGSVTLAISGLVLLWLYGSFWTTLLFLFFGGLAFMMkhervalFII 313
Cdd:COG2814   243 saaglllALFGLGGVLGALLAGRladrfgrrrlLLIGLLLLALGLLLLALAGSLWLLLLALFLLGFGFGL-------LFP 315

                         170       180
                  ....*....|....*....|....*..
gi 1063737144 314 TVYSVYSALSYVGWLGLLLAFNLAFIS 340
Cdd:COG2814   316 LLQALVAELAPPEARGRASGLYNSAFF 342
ABC2_membrane pfam01061
ABC-2 type transporter;
179-349 5.68e-04

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 41.88  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 179 RDLVLTKMRQVFPVVfrwlmhfgsIILLLSLVWLDcAIRGFDSFIRMGtASFFSIMWCGLFSAFSM-------------- 244
Cdd:pfam01061  11 RDPSLGLWRLIQPIL---------MALIFGTLFGN-LGNQQGGLNRPG-LLFFSILFNAFSALSGIspvfekergvlyre 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 245 --FGMTKFILISVATVLVALFIGFVVGSVTLAISGLV--LLWLYGSFWTTLLFLFFGGLAFMMkherVALFIITVYSVYS 320
Cdd:pfam01061  80 laSPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMvgLPPSAGRFFLFLLVLLLTALAASS----LGLFISALAPSFE 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063737144 321 ALSYVGWLGLLLAFNL--AFISTDALIYFFK 349
Cdd:pfam01061 156 DASQLGPLVLLPLLLLsgFFIPIDSMPVWWQ 186
PHA02624 PHA02624
large T antigen; Provisional
 391-483 8.37e-04

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 42.66  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 391 DSELTSED--EIARLLNCPDHYsalglarYGNVDMayLKREYRKKAMLVHPDKNmGNEraaEAFKKLQNAYEVLLDSVK- 467
Cdd:PHA02624    2 DKTLSREEskELMDLLGLPMAA-------WGNLPL--MRKAYLRKCKEYHPDKG-GDE---EKMKRLNSLYKKLQEGVKs 68

                          90
                  ....*....|....*.
gi 1063737144 468 QKSYDDELKREELLNY 483
Cdd:PHA02624   69 ARQSFGTQDSSEIPTY 84
YadH COG0842
ABC-type multidrug transport system, permease component [Defense mechanisms];
225-344 1.19e-03

ABC-type multidrug transport system, permease component [Defense mechanisms];


Pssm-ID: 440604 [Multi-domain]  Cd Length: 200  Bit Score: 40.57  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 225 MGTA-SFFSIMWCGLFSAFSMFGMTKFILIsVATVLVALFIGFVVGSVTLAISGLVL-LWLYG-SFWTTLLFLFFGGLAF 301
Cdd:COG0842    20 MLTAlSIAREREQGTLERLLVTPVSRLEIL-LGKVLAYLLRGLLQALLVLLVALLFFgVPLRGlSLLLLLLVLLLFALAF 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1063737144 302 MMkherVALFIITVYSVYSALSYVGWLGLLLAFNL--AFISTDAL 344
Cdd:COG0842    99 SG----LGLLISTLARSQEQASAISNLVILPLTFLsgAFFPIESL 139
ArsB COG1055
Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];
249-334 1.89e-03

Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];


Pssm-ID: 440675 [Multi-domain]  Cd Length: 415  Bit Score: 41.27  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 249 KFILISVATVLVALFIGFVVGSVT------LAISGLVLLWLYGSF----------WTTLLFlFFGglafmmkhervaLFI 312
Cdd:COG1055   215 RRLLRISLLVLALLLVGFVLHSFLglppalIALLGAAVLLLLARVdvrevlkkvdWSTLLF-FIG------------LFV 281

                          90       100
                  ....*....|....*....|..
gi 1063737144 313 ItVYsvysALSYVGWLGLLLAF 334
Cdd:COG1055   282 V-VG----GLENTGLLDLLAEL 298
ArsB_NhaD_permease cd00625
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
 194-340 1.94e-03

Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, antimonite, sulfate and organic anions across biological membranes in all three kingdoms of life. A typical anion permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump.


Pssm-ID: 238344 [Multi-domain]  Cd Length: 396  Bit Score: 41.08  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 194 FRWLMHFGSIILLLSLVWLdcaIRGFDSFIRMGTASFFSIMwcGLFSAFSMFGMTKFILISVATVLVALFIGFVVGSVT- 272
Cdd:cd00625   157 FLAFMAPPALGLLLLLLGL---LYLLFRKKLLLPDEDKLTV--LAEPLPARPLLKKFLLLALLLLLLFVLLFFFLIPLGl 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 273 ---LAISGLVLLWL--------YGSF-WTTLLFlFFGGLAFM--MKH----ERVALFIITV--YSVYSALSYVGWLGLLL 332
Cdd:cd00625   232 ialLGALLLLLLLVrgldpeevLKSVdWGTLLF-FAGLFVLVgaLEStgllEWLAELLVALvgLPPLAALLLIGLLSALL 310


                  ....*...
gi 1063737144 333 AfnlAFIS 340
Cdd:cd00625   311 S---NFIS 315
7TM-7TMR_HD pfam07698
7TM receptor with intracellular HD hydrolase; These bacterial 7TM receptor proteins have an ...
 194-347 2.31e-03

7TM receptor with intracellular HD hydrolase; These bacterial 7TM receptor proteins have an intracellular pfam01966. This entry corresponds to the 7 helix transmembrane domain. These proteins also contain an N-terminal extracellular domain.


Pssm-ID: 429603 [Multi-domain]  Cd Length: 190  Bit Score: 39.84  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 194 FRWLMHFGSIILLLSLVWLdcAIRGF--DSFIRMGTASFFSIMWCGLFS---AFSMFGMTKFILISVA--TVLVALFIGF 266
Cdd:pfam07698   2 LPLLGLALLVLLLLAVLLL--YLRRFrpELFRRNKDLLLLSLLLLLILLlskLVSLISNSIPYLVPLAagPMLLTILLDS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 267 VVGSVTLAISGLVLLWLYGSFWTTLLFLFFGGL--AFMMKH--ERVALFIItvySVYSALSYVG-WLGLLLAFNLAF--- 338
Cdd:pfam07698  80 RLALVVSVLLALLLGIMFGNNLEVILYALLSGLvgAYSVRRlrSRSDLLRA---GLFVALVNVLlYLALGLISGNNFsle 156


                  ....*....
gi 1063737144 339 ISTDALIYF 347
Cdd:pfam07698 157 ILTDLGLAF 165
NosY COG1277
ABC-type transport system involved in multi-copper enzyme maturation, permease component ...
 249-339 2.51e-03

ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440888 [Multi-domain]  Cd Length: 201  Bit Score: 39.80  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 249 KFiLISVATVLVALFIGFVVGSVTLAISGLVLLWLYGSFWTTLLFLFFGGLAFMMkherVALFiITVYSVYSALSYVGWL 328
Cdd:COG1277    99 KF-LGALLVLLLALLITFLLALLLGLLLFGSPPPDLGAILGFYLGLLLLGLAFLA----IGLF-ISALTRNQIVAAILAI 172

                          90
                  ....*....|.
gi 1063737144 329 GLLLAFNLAFI 339
Cdd:COG1277   173 ALWLLLVILLA 183
MFS_MdtG_SLC18_like cd17325
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ...
 204-301 2.60e-03

bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters; This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340883 [Multi-domain]  Cd Length: 375  Bit Score: 40.64  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 204 ILLLSLVWLDCAIRGFDSFIRMGTASFFSIMWCGLFSA-FSMFGMTkFILISVATVLVALFIG-----------FVVGSV 271
Cdd:cd17325   195 LLRDRRLLALFLAIFVLAFAFGALEPFLPLYAAELGGLsPAQIGLL-FGAQGLASALSQPPAGklsdrigrkplILIGLL 273

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063737144 272 TLAIsGLVLLWLYGSFWTTLLFLFFGGLAF 301
Cdd:cd17325   274 LSAV-ALLLLPLATSFWLLLLLLALLGLGL 302
MFS_MelB_like cd17332
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
 215-314 2.63e-03

Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major Facilitator Superfamily; This family is composed of Salmonella enterica Na+/melibiose symporter MelB, Major Facilitator Superfamily domain-containing proteins, MFSD2 and MFSD12, and other sugar transporters. MelB catalyzes the electrogenic symport of galactosides with Na+, Li+ or H+. The MFSD2 subfamily is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. MelB-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340890 [Multi-domain]  Cd Length: 424  Bit Score: 40.67  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 215 AIRGFDSFIRMGTASFFsiMWCGLFSAFSMFGM-TKFILISVAtVLVALFIGFVVGSVTLAISGLVLLWLYGS----FWT 289
Cdd:cd17332   216 ALLKNRPFLILLLAYLL--YFLAFNIVNTVLVYyFKYVLGGRA-ELVLLLLLILSGALLALLPWPPLKKRFGKkkafFIG 292

                          90       100
                  ....*....|....*....|....*
gi 1063737144 290 TLLFLFFGGLAFMMKHERVALFIIT 314
Cdd:cd17332   293 LLLAILGLLLLFFLPPGNLVLILVL 317
MFS_SLC45_SUC cd17313
Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily ...
 186-291 2.65e-03

Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily of transporters; This group includes the solute carrier 45 (SLC45) family as well as plant sucrose transporters (SUCs or SUTs) and similar proteins such as Schizosaccharomyces pombe general alpha-glucoside permease. the SLC45 family is composed of four (A1-A4) vertebrate proteins as well as related insect proteins such as Drosophila sucrose transporter SCRT or Slc45-1. Members of this group transport sucrose and other sugars like maltose into the cell, with the concomitant uptake of protons (symport system). Plant sucrose transporters are crucial to carbon partitioning, playing a key role in phloem loading/unloading. They play a key role in loading and unloading of sucrose into the phloem and as a result, they control sucrose distribution throughout the whole plant and drive the osmotic flow system in the phloem. They also play a role in the exchange of sucrose between beneficial symbionts (mycorrhiza and Rhizobium) as well as pathogens such as nematodes and parasitic fungi. There are nine sucrose transporter genes in Arabidopsis and five in rice. Vertebrate SLC45 family proteins have been implicated in the regulation of glucose homoeostasis in the brain (SLC45A1), with skin and hair pigmentation (SLC45A2), and with prostate cancer and myelination (SLC45A3). Mutations in SLC45A2, also called MATP (membrane-associated transporter protein) or melanoma antigen AIM1, cause oculocutaneous albinism type 4 (OCA4), an autosomal recessive disorder of melanin biosynthesis that results in congenital hypopigmentation of ocular and cutaneous tissues. The SLC45 family and related sugar transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340871 [Multi-domain]  Cd Length: 421  Bit Score: 40.69  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 186 MRQVFPVVFRWLMHFGSIILLLSL-----VW--LDCAIRGFDSFIRMGTAS--FFSIMwCGLFSAFSMFGMTKF-----I 251
Cdd:cd17313   236 LLRLLLVIFFWWIAFFPFELFFTDymgeeVYhgTSAASSHYGAGVRMGAWGllIFSLA-FLIFSLPIGKLGKKIgrkkvY 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063737144 252 LISVATVLVALFIGFVVGSVTLAisgLVLLWLYGSFWTTL 291
Cdd:cd17313   315 LIGLVLFAVGMALMALVHNVTVA---LVLFALGGIGWATI 351
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 229-347 3.09e-03

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.


Pssm-ID: 349949 [Multi-domain]  Cd Length: 378  Bit Score: 40.49  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 229 SFFSIMWCGLFSAFSMFG---MTKFILISVATVLVALFIGFVVGSVTLAISGLVL-------LWLYGSFWTTLLFLFFGG 298
Cdd:cd06174   209 LLAIFLVNLAYYSFSTLLplfLLDLGGLSVAVAGLLLSLFGLAGALGSLLLGLLSdrligrkPLLLIGLLLMALGLALLL 288

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063737144 299 LAFmmkherVALFIITVYSVYSALSYVGWLGLLLAFNLAFISTDALIYF 347
Cdd:cd06174   289 LAP------SLLLLLLLLLLLGFGLGGLLPLSFALIAELFPPEIRGTAF 331
MFS_1 pfam07690
Major Facilitator Superfamily;
195-348 4.32e-03

Major Facilitator Superfamily;


Pssm-ID: 429598 [Multi-domain]  Cd Length: 344  Bit Score: 40.09  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 195 RWLMHFGSIILLLSLVWLdcairgfdsfirMGTASFFSIMWC----GLFSAFSMFGMTKFILISVATVLVALFIGFVVGS 270
Cdd:pfam07690  62 RRVLLIGLLLFALGLLLL------------LFASSLWLLLVLrvlqGLGAGALFPAALALIADWFPPEERGRALGLVSAG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 271 VTL--AISGLVLLWLYGSFWTTLLFLFFGGLAFMM-----------------KHERVALFIITVYSVYSALSYVGWLGLL 331
Cdd:pfam07690 130 FGLgaALGPLLGGLLASLFGWRAAFLILAILSLLAavllllprpppeskrpkPAEEARLSLIVAWKALLRDPVLWLLLAL 209

                         170
                  ....*....|....*..
gi 1063737144 332 LAFNLAFISTDALIYFF 348
Cdd:pfam07690 210 LLFGFAFFGLLTYLPLY 226
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 218-333 4.34e-03

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.


Pssm-ID: 349949 [Multi-domain]  Cd Length: 378  Bit Score: 40.10  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 218 GFDSFIRMGTASFFSIMWCGLFSA-FSMFGMTkFILISVATVLVALFIGFVV----------GSVTLAISGLVLLWLYGS 286
Cdd:cd06174     5 FFLTGLARGLISPLLPALLQSFGLsASQLGLL-FALFSLGYALLQPLAGLLAdrfgrrpvllLGLLLFALGALLFAFAPS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063737144 287 FWTTLLFLFFGGLAFMM--------------KHERVALFiitvySVYSALSYVGW-LGLLLA 333
Cdd:cd06174    84 FWLLLLGRFLLGLGSGLidpavlaliadlfpERERGRAL-----GLLQAFGSVGGiLGPLLG 140
DUF3021 pfam11457
Protein of unknown function (DUF3021); This is a bacterial family of uncharacterized proteins.
 249-354 4.36e-03

Protein of unknown function (DUF3021); This is a bacterial family of uncharacterized proteins.


Pssm-ID: 402870  Cd Length: 130  Bit Score: 38.02  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 249 KFILISVAT-----VLVALFIGFVVGSVTLAISGLVLLWLYGSFwttLLFLFFGGLAFMMKHERVALFI------ITVYS 317
Cdd:pfam11457   2 KKIFLGILIgiligVIIGLIISLFYGGGTLYTLTAVLKQFLLSA---LIGLLFALPSLIFESERWSLLKqtlihfLITLA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063737144 318 VYSALSY-VGWLGLLLAFNLAFISTDALIYFF---------KNKINQ 354
Cdd:pfam11457  79 VVLPLAYlNGWFPLNVIGILIYTLIFIAIYLViwlifylyyKKEVKK 125
LtrA pfam06772
Bacterial low temperature requirement A protein (LtrA); This family consists of several ...
 263-362 6.86e-03

Bacterial low temperature requirement A protein (LtrA); This family consists of several bacteria specific low temperature requirement A (LtrA) protein sequences which have been found to be essential for growth at low temperatures in Listeria monocytogenes.


Pssm-ID: 462006  Cd Length: 352  Bit Score: 39.21  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737144 263 FIGFVVGSVTLAISGLVLLWLYGSFWTTLLFL-FFGGLAFMMKH------------ERVALFII-----TVYSVYSALSY 324
Cdd:pfam06772 125 AAGLALSALLWLAGALLPGPARLALWLAALLIeYFVVPLLGRRRtgdtpvhaehlaERYGLFTIialgeSVVAIGAGVAD 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063737144 325 VGWLG-LLLAFNLAFISTDAL--IYF--FKNKINQQSTADRPT 362
Cdd:pfam06772 205 QHWSGpTLLAAVLGFVLTAALwwIYFdvPALAAEHALTSARRG 247
PHA03102 PHA03102
Small T antigen; Reviewed
 399-467 8.29e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 37.34  E-value: 8.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063737144 399 EIARLLncpdhySALGLAR--YGNVDMayLKREYRKKAMLVHPDKNmGNEraaEAFKKLQNAYEVLLDSVK 467
Cdd:PHA03102    3 ESKELM------DLLGLPRsaWGNLPL--MRKAYLRKCLEFHPDKG-GDE---EKMKELNTLYKKFRESVK 61
 
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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