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Conserved domains on  [gi|447048927|ref|WP_001126183|]
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MULTISPECIES: metal ABC transporter substrate-binding protein [Bacillus]

Protein Classification

metal ABC transporter substrate-binding protein( domain architecture ID 10099078)

metal ABC transporter substrate-binding protein functions as the initial receptor for the active uptake of metals such as Zn2+ and Mn2+

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 32-316 5.97e-139

Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence).


:

Pssm-ID: 238499 [Multi-domain]  Cd Length: 282  Bit Score: 394.35  E-value: 5.97e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  32 DGKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFAEKMEKTLQKENVK 111
Cdd:cd01017    1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 112 IVNASKGIELRTSTEEEHHDHgdgHKEDEHHHDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTD 191
Cdd:cd01017   81 VVEASKGIKLLKAGGAEHDHD---HSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 192 LDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVASV 271
Cdd:cd01017  158 LDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAET 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 447048927 272 IQKETGTKILRLNHLATISEDDAKNNKDYFTLMEENVNTLKEATN 316
Cdd:cd01017  238 LAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
 
Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 32-316 5.97e-139

Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238499 [Multi-domain]  Cd Length: 282  Bit Score: 394.35  E-value: 5.97e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  32 DGKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFAEKMEKTLQKENVK 111
Cdd:cd01017    1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 112 IVNASKGIELRTSTEEEHHDHgdgHKEDEHHHDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTD 191
Cdd:cd01017   81 VVEASKGIKLLKAGGAEHDHD---HSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 192 LDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVASV 271
Cdd:cd01017  158 LDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAET 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 447048927 272 IQKETGTKILRLNHLATISEDDAKNNKDYFTLMEENVNTLKEATN 316
Cdd:cd01017  238 LAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-307 5.46e-113

ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and metabolism];


Pssm-ID: 440566 [Multi-domain]  Cd Length: 286  Bit Score: 328.36  E-value: 5.46e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927   1 MPKRLtiLSFLLIFTLIFTGCSNTkegNAKKDGKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQ 80
Cdd:COG0803    1 MKRLL--LALLLLAALLLAGCSAA---ASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  81 VAKADLFVYNGAELEPFAEKMEKTLQKENVKIVNASKGIELRTstEEEHHDHGDGhkedehhhdkDPHIWLDPTLAMKQA 160
Cdd:COG0803   76 LAKADLVVYNGLGLEGWLDKLLEAAGNPGVPVVDASEGIDLLE--LEEGHDHGEP----------DPHVWLDPKNAKKVA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 161 EKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQ 240
Cdd:COG0803  144 ENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSP 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447048927 241 KQLADITKTVKEHNLKYILFETFSTPKVASVIQKETGTKILRLNHLATISEDdaknNKDYFTLMEEN 307
Cdd:COG0803  224 ADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGGP----GDTYLDMMRHN 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 37-314 7.66e-110

Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins such as TroA that interacts with an ATP-binding cassette transport system in Treponema pallidum. ZnuA is part of the bacterial zinc-uptake complex ZnuABC, whose components are the following families, ZinT, pfam09223, pfam00950, pfam00005, all of which are regulated by the transcription-regulator family FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), a high-affinity zinc-uptake protein. In Gram-negative bacteria the ZnuABC transporter system ensures an adequate import of zinc in Zn2+-poor environments, such as those encountered by pathogens within the infected host.


Pssm-ID: 460151 [Multi-domain]  Cd Length: 269  Bit Score: 319.88  E-value: 7.66e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927   37 VYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFAEKMEKTLqkENVKIVNAS 116
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEAL--PNKKVVDAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  117 KGIELrtsteeeHHDHGDGHKEDEHHHDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQF 196
Cdd:pfam01297  79 EGVEL-------LDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  197 KAAVANAKTKD--ILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVASVIQK 274
Cdd:pfam01297 152 KEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAK 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 447048927  275 ETGTKILRLnhLATISEDDAKNNKDYFTLMEENVNTLKEA 314
Cdd:pfam01297 232 ETGVKVLGP--LYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
1-316 1.39e-77

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 245.84  E-value: 1.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927   1 MPKRLTILSFLLIFTLIFTGCSNTKEGNAKKDgKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQ 80
Cdd:NF033605   1 MKKSLYILSLVIALAIVLAACGKGDSKNKDND-KIKINTTVFPLKSFAEQIGGKHVEVESIYPAGTDLHSYEPTQKDILN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  81 VAKADLFVYNGAELEPFAEKMEKTLQKENVKI-----VNASKGIELRTSTEEEHHDHGDGHKEDEHHHDK--DPHIWLDP 153
Cdd:NF033605  80 ASKADLFVYTGDDLDPVAKKVASTIKKDDKKLsledkLDKSTLLTDQHEHGEEHEHEEEGHEHEHHHHHGgyDPHVWLDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 154 TLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGIS 233
Cdd:NF033605 160 KFDQTFAKEIKDELVKKDPKHKDEYEKNYKKLNKDLKGIDKDMKDITKDKQGNAVFISHESLGYLADRYGFVQKGVQNMN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 234 ASDePSQKQLADITKTVKEHNLKYILFETFSTPKVASVIQKETGTKILRLNHLATISEDDAKNNK-DYFTLMEENVNTLK 312
Cdd:NF033605 240 AED-PSQKELTEIVKEINDSGAKYILYEDNVSNKVTDTIRKETDAKPLKFYNMESLNKEQQKDKDlTYQSLMKENIKNID 318


                 ....
gi 447048927 313 EATN 316
Cdd:NF033605 319 KALN 322
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
15-288 1.17e-38

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 138.60  E-value: 1.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  15 TLIFTGCSNTKEGNAKKDGKLTVYTTIFPLADFAKKIGgDYVT-VEAIYPPGADSH--TFEPSQKQTVQvaKADLFVYNG 91
Cdd:PRK09545   5 TLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIA-DGVTeTEVLLPDGASPHdySLRPSDVKRLQ--SADLVVWVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  92 AELEPFaekMEKTLQK----ENVKI--VNASKGIELRTSTEEEH---HDHGDGHKEDEHHH--DKDPHIWLDPTLAMKQA 160
Cdd:PRK09545  82 PEMEAF---LEKPVSKlpenKQVTIaqLPDVKPLLMKGAHDDHHdddHDHAGHEKSDEDHHhgEYNMHIWLSPEIARATA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 161 EKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQ 240
Cdd:PRK09545 159 VAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGA 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 447048927 241 KQLADITKTVKEHNLKYILFETFSTPKVASVIQKETGTKILRLNHLAT 288
Cdd:PRK09545 239 QRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGT 286
 
Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 32-316 5.97e-139

Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238499 [Multi-domain]  Cd Length: 282  Bit Score: 394.35  E-value: 5.97e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  32 DGKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFAEKMEKTLQKENVK 111
Cdd:cd01017    1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 112 IVNASKGIELRTSTEEEHHDHgdgHKEDEHHHDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTD 191
Cdd:cd01017   81 VVEASKGIKLLKAGGAEHDHD---HSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 192 LDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVASV 271
Cdd:cd01017  158 LDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAET 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 447048927 272 IQKETGTKILRLNHLATISEDDAKNNKDYFTLMEENVNTLKEATN 316
Cdd:cd01017  238 LAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-307 5.46e-113

ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and metabolism];


Pssm-ID: 440566 [Multi-domain]  Cd Length: 286  Bit Score: 328.36  E-value: 5.46e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927   1 MPKRLtiLSFLLIFTLIFTGCSNTkegNAKKDGKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQ 80
Cdd:COG0803    1 MKRLL--LALLLLAALLLAGCSAA---ASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  81 VAKADLFVYNGAELEPFAEKMEKTLQKENVKIVNASKGIELRTstEEEHHDHGDGhkedehhhdkDPHIWLDPTLAMKQA 160
Cdd:COG0803   76 LAKADLVVYNGLGLEGWLDKLLEAAGNPGVPVVDASEGIDLLE--LEEGHDHGEP----------DPHVWLDPKNAKKVA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 161 EKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQ 240
Cdd:COG0803  144 ENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSP 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447048927 241 KQLADITKTVKEHNLKYILFETFSTPKVASVIQKETGTKILRLNHLATISEDdaknNKDYFTLMEEN 307
Cdd:COG0803  224 ADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGGP----GDTYLDMMRHN 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 37-314 7.66e-110

Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins such as TroA that interacts with an ATP-binding cassette transport system in Treponema pallidum. ZnuA is part of the bacterial zinc-uptake complex ZnuABC, whose components are the following families, ZinT, pfam09223, pfam00950, pfam00005, all of which are regulated by the transcription-regulator family FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), a high-affinity zinc-uptake protein. In Gram-negative bacteria the ZnuABC transporter system ensures an adequate import of zinc in Zn2+-poor environments, such as those encountered by pathogens within the infected host.


Pssm-ID: 460151 [Multi-domain]  Cd Length: 269  Bit Score: 319.88  E-value: 7.66e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927   37 VYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFAEKMEKTLqkENVKIVNAS 116
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEAL--PNKKVVDAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  117 KGIELrtsteeeHHDHGDGHKEDEHHHDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQF 196
Cdd:pfam01297  79 EGVEL-------LDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  197 KAAVANAKTKD--ILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVASVIQK 274
Cdd:pfam01297 152 KEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAK 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 447048927  275 ETGTKILRLnhLATISEDDAKNNKDYFTLMEENVNTLKEA 314
Cdd:pfam01297 232 ETGVKVLGP--LYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
1-316 1.39e-77

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 245.84  E-value: 1.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927   1 MPKRLTILSFLLIFTLIFTGCSNTKEGNAKKDgKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQ 80
Cdd:NF033605   1 MKKSLYILSLVIALAIVLAACGKGDSKNKDND-KIKINTTVFPLKSFAEQIGGKHVEVESIYPAGTDLHSYEPTQKDILN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  81 VAKADLFVYNGAELEPFAEKMEKTLQKENVKI-----VNASKGIELRTSTEEEHHDHGDGHKEDEHHHDK--DPHIWLDP 153
Cdd:NF033605  80 ASKADLFVYTGDDLDPVAKKVASTIKKDDKKLsledkLDKSTLLTDQHEHGEEHEHEEEGHEHEHHHHHGgyDPHVWLDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 154 TLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGIS 233
Cdd:NF033605 160 KFDQTFAKEIKDELVKKDPKHKDEYEKNYKKLNKDLKGIDKDMKDITKDKQGNAVFISHESLGYLADRYGFVQKGVQNMN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 234 ASDePSQKQLADITKTVKEHNLKYILFETFSTPKVASVIQKETGTKILRLNHLATISEDDAKNNK-DYFTLMEENVNTLK 312
Cdd:NF033605 240 AED-PSQKELTEIVKEINDSGAKYILYEDNVSNKVTDTIRKETDAKPLKFYNMESLNKEQQKDKDlTYQSLMKENIKNID 318


                 ....
gi 447048927 313 EATN 316
Cdd:NF033605 319 KALN 322
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 18-314 1.65e-70

Metal binding protein PsaA. These proteins have been shown to function as initial receptors in ABC transport of Mn2+ and as surface adhesins in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238557 [Multi-domain]  Cd Length: 287  Bit Score: 220.23  E-value: 1.65e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  18 FTGCSNTKEGNAKKDGKLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPF 97
Cdd:cd01137    1 LAACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  98 AEKMEKTLQKeNVKIVNASKGIELRTSteEEHHDHGdghkedehhhDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQE 177
Cdd:cd01137   81 LERLVKNAGK-DVPVVAVSEGIDPIPL--EEGHYKG----------KPDPHAWMSPKNAIIYVKNIAKALSEADPANAET 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 178 FEKNFAALQTKFTDLDDQFKAAVAN--AKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNL 255
Cdd:cd01137  148 YQKNAAAYKAKLKALDEWAKAKFATipAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKV 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 447048927 256 KYILFETFSTPKVASVIQKETGTKILRLNHLATISEDDaKNNKDYFTLMEENVNTLKEA 314
Cdd:cd01137  228 PAVFVESTVNDRLMKQVAKETGAKIGGQLYTDSLSEKG-GPADTYLDMMEHNLDTIVEG 285
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
 34-302 1.14e-66

Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and bind their specific ligands in the cleft between these domains. In addition, many of these proteins possess a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238500 [Multi-domain]  Cd Length: 266  Bit Score: 209.91  E-value: 1.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  34 KLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELE-PFAEKMeKTLQKeNVKI 112
Cdd:cd01018    2 KPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERF-RSNNP-KMQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 113 VNASKGIELRTSTEEEHHDHGdgHKEDEHHHDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTDL 192
Cdd:cd01018   80 VNMSKGITLIPMADHHHHHHG--EHEHHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 193 DDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAgiSASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVASVI 272
Cdd:cd01018  158 DSEIRTILSKLKQRAFMVYHPAWGYFARDYGLTQIPIE--EEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAI 235

                        250       260       270
                 ....*....|....*....|....*....|
gi 447048927 273 QKETGTKILRLNHLATISEDDAKNNKDYFT 302
Cdd:cd01018  236 AREIGAKVVTIDPLAADWEENLLKVADAFA 265
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
 37-314 1.48e-62

Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in the ABC uptake of Zn2+. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a single helix and bind their specific ligands in the cleft between these domains. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238501 [Multi-domain]  Cd Length: 286  Bit Score: 199.91  E-value: 1.48e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  37 VYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFAEKMEKTLQKenVKIVNAS 116
Cdd:cd01019    6 VLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKK--GKVLTLA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 117 KGIELRT-------STEEEHHDHGDGHKEDEHHHDKDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKF 189
Cdd:cd01019   84 KLIDLKTledgashGDHEHDHEHAHGEHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNARL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 190 TDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVA 269
Cdd:cd01019  164 AELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPKIA 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 447048927 270 SVIQKETGTKILRLNHLATIseDDAKNNkDYFTLMEENVNTLKEA 314
Cdd:cd01019  244 ETLAEGTGAKVGELDPLGGL--IELGKN-SYVNFLRNLADSLASC 285
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 36-313 1.76e-52

ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion transport and metabolism];


Pssm-ID: 443599 [Multi-domain]  Cd Length: 300  Bit Score: 174.25  E-value: 1.76e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  36 TVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTF--EPSQKQTVQvaKADLFVYNGAELEPFaekMEKTLQK--ENVK 111
Cdd:COG4531   11 RVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYalRPSDARALQ--DADLVFWVGPDLEPF---LEKPLETlaPDAK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 112 IVNASK--GIEL---RTSTEEEHHDHGDGHKEDEHHHD---------KDPHIWLDPTLAMKQAEKIKNALVALQPDHKQE 177
Cdd:COG4531   86 VVELLElpGLTLlpfREGGDFEHHDHHDEHHHHHHHHDdhhdhhhggYDPHLWLSPENAKAWAAAIADALSELDPENAAT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 178 FEKNFAALQTKFTDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQiaiAG-ISASDE--PSQKQLADITKTVKEHN 254
Cdd:COG4531  166 YQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNA---LGaITLNPEiqPGAKRLAEIREKLKELG 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 447048927 255 LKYILFETFSTPKVASVIQKETGTKILRLNHLATISEDDAKNnkdYFTLMEENVNTLKE 313
Cdd:COG4531  243 AVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDL---YFQLLRQLADSLAS 298
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
15-288 1.17e-38

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 138.60  E-value: 1.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  15 TLIFTGCSNTKEGNAKKDGKLTVYTTIFPLADFAKKIGgDYVT-VEAIYPPGADSH--TFEPSQKQTVQvaKADLFVYNG 91
Cdd:PRK09545   5 TLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIA-DGVTeTEVLLPDGASPHdySLRPSDVKRLQ--SADLVVWVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  92 AELEPFaekMEKTLQK----ENVKI--VNASKGIELRTSTEEEH---HDHGDGHKEDEHHH--DKDPHIWLDPTLAMKQA 160
Cdd:PRK09545  82 PEMEAF---LEKPVSKlpenKQVTIaqLPDVKPLLMKGAHDDHHdddHDHAGHEKSDEDHHhgEYNMHIWLSPEIARATA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 161 EKIKNALVALQPDHKQEFEKNFAALQTKFTDLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASDEPSQ 240
Cdd:PRK09545 159 VAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGA 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 447048927 241 KQLADITKTVKEHNLKYILFETFSTPKVASVIQKETGTKILRLNHLAT 288
Cdd:PRK09545 239 QRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGT 286
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
 34-314 2.64e-34

Metal binding protein TroA. These proteins have been shown to function as initial receptors in ABC transport of Zn2+ and possibly Fe3+ in many eubacterial species. The TroA proteins belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238498 [Multi-domain]  Cd Length: 276  Bit Score: 126.32  E-value: 2.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  34 KLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEpfaEKMEKTLQKEN--VK 111
Cdd:cd01016    1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLE---GKMSDVLSKLGssKS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 112 IVNASKGIElrtsteeehhDHGDGHKEDEHHHdkDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTD 191
Cdd:cd01016   78 VIALEDTLD----------RSQLILDEEEGTY--DPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDS 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 192 LDDQFKAAVAN-AKTKDILVS-HAAYGYWEQRYGLKQIAIAGISASDEPSQKQLADITKTVKEHNLKYILFETFSTPKVA 269
Cdd:cd01016  146 LDAYAKKKIAEiPEQQRVLVTaHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSI 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 447048927 270 SVIQ---KETGTKILRLNHLATISEDDAKNNKD-YFTLMEENVNTLKEA 314
Cdd:cd01016  226 EALQdavKARGHDVQIGGELYSDAMGEEGTSEGtYIGMFKHNVDTIVEA 274
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
 33-316 4.22e-28

Metal binding protein TroA_b. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238502 [Multi-domain]  Cd Length: 264  Bit Score: 109.45  E-value: 4.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  33 GKLTVYTTIFPLADFAKKIGGDYVTVEAIY-PPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFaekMEKTLQKENVK 111
Cdd:cd01020    1 GKINVVASTNFWGSVAEAVGGDHVEVTSIItNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPW---MTKLLADTKDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 112 IVNASkgielrtsTEEEHHDH-GDghkedehhhdkDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFT 190
Cdd:cd01020   78 IVIAA--------DLDGHDDKeGD-----------NPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLK 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 191 DLDDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAGISASD----EPSQKQLADITKTVKEHNLKYILFETFSTP 266
Cdd:cd01020  139 PLAAKIAELSAKYKGAPVAATEPVFDYLLDALGMKERTPKGYTATTesetEPSPADIAAFQNAIKNRQIDALIVNPQQAS 218

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447048927 267 KVASVIQ---KETGTKILRlnhlatISEdDAKNNKDYFTLMEENVNTLKEATN 316
Cdd:cd01020  219 SATTNITglaKRSGVPVVE------VTE-TMPNGTTYLTWMLKQVDQLEKALQ 264
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
 34-231 6.60e-25

Periplasmic binding protein TroA_c. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238565 [Multi-domain]  Cd Length: 203  Bit Score: 99.50  E-value: 6.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  34 KLTVYTTIFPLADFAKKIGGDYVTVEAIYPPGADSHTFEPSQKQTVQVAKADLFVYNGAELEPFAEKMEKtlQKENVKIV 113
Cdd:cd01145    2 ALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLAE--LSSNSKVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 114 NASKG-IELRTSTEEEHHDHGDGHKEDehhhdkDPHIWLDPTLAMKQAEKIKNALVALQPDHKQEFEKNFAALQTKFTDL 192
Cdd:cd01145   80 PGIKIlIEDSDTVGMVDRAMGDYHGKG------NPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKL 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 447048927 193 DDQFKAAVANAKTKDILVSHAAYGYWEQRYGLKQIAIAG 231
Cdd:cd01145  154 LREWERQFEGLKGIQVVAYHPSYQYLADWLGIEVVASLE 192
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 37-210 7.18e-07

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


Pssm-ID: 238347 [Multi-domain]  Cd Length: 148  Bit Score: 47.94  E-value: 7.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927  37 VYTTIFPLADFAKKIGGDYVTVEAIYPPGADS-------------HTFEPSQKQTVQVaKADLFVYNGAELEPFAEKmek 103
Cdd:cd00636    3 VVALDPGATELLLALGGDDKPVGVADPSGYPPeakallekvpdvgHGYEPNLEKIAAL-KPDLIIANGSGLEAWLDK--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447048927 104 tLQKENVKIVNASKGIElrtsteeehhdhgdghkedehhhdkdphiwLDPTLAMKQAEKIKNALValqpdhkqeFEKNFA 183
Cdd:cd00636   79 -LSKIAIPVVVVDEASE------------------------------LSLENIKESIRLIGKALG---------KEENAE 118

                        170       180
                 ....*....|....*....|....*..
gi 447048927 184 ALQTKFTDLDDQFKAAVANAKTKDILV 210
Cdd:cd00636  119 ELIAELDARLAELRAKLAKIPKKKVSL 145
 
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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