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Conserved domains on  [gi|1771599299|ref|WP_152873240|]
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zinc ABC transporter substrate-binding protein AdcA [Streptococcus dysgalactiae]

Protein Classification

zinc ABC transporter substrate-binding protein AdcA( domain architecture ID 10099085)

zinc ABC transporter substrate-binding protein AdcA functions as the initial receptor in the ATP-driven transport of zinc and/or manganese

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

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 ...
 29-320 1.33e-132

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: 385.88  E-value: 1.33e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  29 EDKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDVKKSLKSKKVT 108
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 109 IVKGTGNMLLVAGAGHDHHHEdadkkhehnkHSEEGHNHAFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAAT 188
Cdd:cd01017    81 VVEASKGIKLLKAGGAEHDHD----------HSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 189 YIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENA 268
Cdd:cd01017   151 YAKKLEALDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1771599299 269 SNKVAKTLAKEAGVKTAVLSPLEGLTEKEMKAGEDYFTVMRKNLETLRLTTD 320
Cdd:cd01017   231 SSKIAETLAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
 332-515 1.66e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


:

Pssm-ID: 430470  Cd Length: 181  Bit Score: 335.75  E-value: 1.66e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 332 TTKTVYNGYFKDKDVKDRKLSDWSGNWQSVYPYLQDGTLDQVWDYKAKKsKGKMTAAEYKDYYTTGYKTDVEQIKIngKK 411
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKE-KGDKTAEEYKAYYTKGYKTDVDRIVI--DG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 412 KTMTFVRNGEKKTFTYTYAGKEILTYPKGNRGVRFMFEAKEADAGEFKYVQFSDHAIAPEKAEHFHLYWGGDSQEKLHKE 491
Cdd:pfam09223  78 DTITFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEE 157

                         170       180
                  ....*....|....*....|....
gi 1771599299 492 LEHWPTYYGSDLSGREIAQEINAH 515
Cdd:pfam09223 158 MDNWPTYYPSSLSGEEIVQEMLAH 181
 
Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 29-320 1.33e-132

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: 385.88  E-value: 1.33e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  29 EDKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDVKKSLKSKKVT 108
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 109 IVKGTGNMLLVAGAGHDHHHEdadkkhehnkHSEEGHNHAFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAAT 188
Cdd:cd01017    81 VVEASKGIKLLKAGGAEHDHD----------HSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 189 YIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENA 268
Cdd:cd01017   151 YAKKLEALDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1771599299 269 SNKVAKTLAKEAGVKTAVLSPLEGLTEKEMKAGEDYFTVMRKNLETLRLTTD 320
Cdd:cd01017   231 SSKIAETLAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
 332-515 1.66e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


Pssm-ID: 430470  Cd Length: 181  Bit Score: 335.75  E-value: 1.66e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 332 TTKTVYNGYFKDKDVKDRKLSDWSGNWQSVYPYLQDGTLDQVWDYKAKKsKGKMTAAEYKDYYTTGYKTDVEQIKIngKK 411
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKE-KGDKTAEEYKAYYTKGYKTDVDRIVI--DG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 412 KTMTFVRNGEKKTFTYTYAGKEILTYPKGNRGVRFMFEAKEADAGEFKYVQFSDHAIAPEKAEHFHLYWGGDSQEKLHKE 491
Cdd:pfam09223  78 DTITFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEE 157

                         170       180
                  ....*....|....*....|....
gi 1771599299 492 LEHWPTYYGSDLSGREIAQEINAH 515
Cdd:pfam09223 158 MDNWPTYYPSSLSGEEIVQEMLAH 181
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
328-515 5.59e-106

Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];


Pssm-ID: 442667  Cd Length: 191  Bit Score: 314.54  E-value: 5.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 328 PEEDTTKTVYNGYFKDKDVKDRKLSDWSGNWQSVYPYLQDGTLDQVWDYKAKKSKGkMTAAEYKDYYTTGYKTDVEQIKI 407
Cdd:COG3443     8 PHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKDGD-KTAEEYKAYYTKGYATDVDRIVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 408 NGKkkTMTFVRNGEKKTFTYTYAGKEILTYPKGNRGVRFMFEAKEADAGEFKYVQFSDHAIAPEKAEHFHLYWgGDSQEK 487
Cdd:COG3443    87 EGN--TVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYW-GNDQEA 163

                         170       180
                  ....*....|....*....|....*...
gi 1771599299 488 LHKELEHWPTYYGSDLSGREIAQEINAH 515
Cdd:COG3443   164 LLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 34-316 1.58e-100

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: 303.32  E-value: 1.58e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  34 VVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDvkkslkskkvtIVKGT 113
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDK-----------LLEAL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 114 GNMLLV-AGAGHDHHHedadkkHEHNKHSEEGHNHAFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYIEK 192
Cdd:pfam01297  70 PNKKVVdASEGVELLD------EEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 193 LKELDKDYTAALSDA--KQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENASN 270
Cdd:pfam01297 144 LDALDAEIKEQLASIpeKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSP 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1771599299 271 KVAKTLAKEAGVKtaVLSPLEGLTEKEMKAGEDYFTVMRKNLETLR 316
Cdd:pfam01297 224 KLAETVAKETGVK--VLGPLYTDSLGEPGGGATYLDLMRHNLDTLA 267
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-311 2.36e-99

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: 301.01  E-value: 2.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299   1 MKKKILLMMSLISVFFAWQLTQAKQvlAEDKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQD 80
Cdd:COG0803     1 MKRLLLALLLLAALLLAGCSAAASS--AAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  81 ADAFVYMDDNMETWISDVKKSLKSKKVTIVKGTGNMLLVAGAGHDHHHEdadkkhehnkhseeghnhaFDPHVWLSPYRS 160
Cdd:COG0803    79 ADLVVYNGLGLEGWLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGE-------------------PDPHVWLDPKNA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 161 ITVVENIRDSLSKAYPEKAENFKANAATYIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISINGVTPDA 240
Cdd:COG0803   140 KKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGS 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771599299 241 EPSAKRIATLSKYVKKYGIKYIYFEENASNKVAKTLAKEAGVKTAVLSPLEGLTEkemkAGEDYFTVMRKN 311
Cdd:COG0803   220 EPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGG----PGDTYLDMMRHN 286
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
 338-515 2.52e-64

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 208.09  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 338 NGYFKDKDVKDRKLSDWSGNWQSVYPYLQDGTLDQVWDYKAKKSKGKmTAAEYKDYYTTGYKTDVEQIKIngKKKTMTFV 417
Cdd:PRK10306   42 NGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQKKAKKDKTK-TFEEIKAYYRKGYATDVEMIGI--ENGIVEFH 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 418 RNGEKKTFTYTYAGKEILTYPKGNRGVRFMFEAKEADAGEFKYVQFSDHAIAPEKAEHFHLYWGGDSQEKLHKELEHWPT 497
Cdd:PRK10306  119 RGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPKYVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPT 198

                         170
                  ....*....|....*...
gi 1771599299 498 YYGSDLSGREIAQEINAH 515
Cdd:PRK10306  199 YYPYQLSSEEVVDEMLHH 216
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
1-290 1.45e-33

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 129.36  E-value: 1.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299   1 MKKKILLMMSLISVFFAWQLTQAKqvlaedkVKVVTTFYPVyeftkGVIGN---DG--DVSMLMKAGTEPHDF--EPStk 73
Cdd:PRK09545    1 LHKKTLLFAALLAALLGGATQAAN-------AAVVTSIKPL-----GFIASaiaDGvtETEVLLPDGASPHDYslRPS-- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  74 DIKKIQDADAFVYMDDNMETWISDVKKSLKSKKV-TIVKGTG-NMLLVAGAGHDHHHEDADkkHEHNKHSEEGHNHA-FD 150
Cdd:PRK09545   67 DVKRLQSADLVVWVGPEMEAFLEKPVSKLPENKQvTIAQLPDvKPLLMKGAHDDHHDDDHD--HAGHEKSDEDHHHGeYN 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 151 PHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQ 230
Cdd:PRK09545  145 MHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTP 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 231 ISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENASNKVAKTLAKEAGVKTAVLSPL 290
Cdd:PRK09545  225 LGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPL 284
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 145-316 2.06e-18

anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ABC transporter permease subunits as identified by pfam00950, but additionally contain the Actinobacterial insert domain described by TIGR03769. Some homologs (lacking the insert) have been described as transporters of manganese or of chelated iron. Members of this family typically are found along with an ATP-binding cassette protein, a permease, and an LPXTG-anchored protein with two or three copies of the TIGR03769 insert that occurs just once in this protein family. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163484 [Multi-domain]  Cd Length: 479  Bit Score: 88.00  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 145 HNHA-FDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYIEKLKELDKDYTAALSD--AKQKSFVTQHAAFGY 221
Cdd:TIGR03772 304 HVHGeIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATipPSRRHLITTHDAYSY 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 222 MALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEEN--ASNKVAKTLAKEAGVKtavLSPLEGLT-EKEM 298
Cdd:TIGR03772 384 LGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNlaARSTTLNEIADELGVR---VCAIYGDTfDDDV 460

                         170
                  ....*....|....*...
gi 1771599299 299 KageDYFTVMRKNLETLR 316
Cdd:TIGR03772 461 T---NYVDLMRFNADSLA 475
 
Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 29-320 1.33e-132

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: 385.88  E-value: 1.33e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  29 EDKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDVKKSLKSKKVT 108
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 109 IVKGTGNMLLVAGAGHDHHHEdadkkhehnkHSEEGHNHAFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAAT 188
Cdd:cd01017    81 VVEASKGIKLLKAGGAEHDHD----------HSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 189 YIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENA 268
Cdd:cd01017   151 YAKKLEALDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1771599299 269 SNKVAKTLAKEAGVKTAVLSPLEGLTEKEMKAGEDYFTVMRKNLETLRLTTD 320
Cdd:cd01017   231 SSKIAETLAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
 332-515 1.66e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


Pssm-ID: 430470  Cd Length: 181  Bit Score: 335.75  E-value: 1.66e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 332 TTKTVYNGYFKDKDVKDRKLSDWSGNWQSVYPYLQDGTLDQVWDYKAKKsKGKMTAAEYKDYYTTGYKTDVEQIKIngKK 411
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKE-KGDKTAEEYKAYYTKGYKTDVDRIVI--DG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 412 KTMTFVRNGEKKTFTYTYAGKEILTYPKGNRGVRFMFEAKEADAGEFKYVQFSDHAIAPEKAEHFHLYWGGDSQEKLHKE 491
Cdd:pfam09223  78 DTITFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEE 157

                         170       180
                  ....*....|....*....|....
gi 1771599299 492 LEHWPTYYGSDLSGREIAQEINAH 515
Cdd:pfam09223 158 MDNWPTYYPSSLSGEEIVQEMLAH 181
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
328-515 5.59e-106

Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];


Pssm-ID: 442667  Cd Length: 191  Bit Score: 314.54  E-value: 5.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 328 PEEDTTKTVYNGYFKDKDVKDRKLSDWSGNWQSVYPYLQDGTLDQVWDYKAKKSKGkMTAAEYKDYYTTGYKTDVEQIKI 407
Cdd:COG3443     8 PHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKDGD-KTAEEYKAYYTKGYATDVDRIVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 408 NGKkkTMTFVRNGEKKTFTYTYAGKEILTYPKGNRGVRFMFEAKEADAGEFKYVQFSDHAIAPEKAEHFHLYWgGDSQEK 487
Cdd:COG3443    87 EGN--TVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYW-GNDQEA 163

                         170       180
                  ....*....|....*....|....*...
gi 1771599299 488 LHKELEHWPTYYGSDLSGREIAQEINAH 515
Cdd:COG3443   164 LLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 34-316 1.58e-100

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: 303.32  E-value: 1.58e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  34 VVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDvkkslkskkvtIVKGT 113
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDK-----------LLEAL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 114 GNMLLV-AGAGHDHHHedadkkHEHNKHSEEGHNHAFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYIEK 192
Cdd:pfam01297  70 PNKKVVdASEGVELLD------EEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 193 LKELDKDYTAALSDA--KQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENASN 270
Cdd:pfam01297 144 LDALDAEIKEQLASIpeKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSP 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1771599299 271 KVAKTLAKEAGVKtaVLSPLEGLTEKEMKAGEDYFTVMRKNLETLR 316
Cdd:pfam01297 224 KLAETVAKETGVK--VLGPLYTDSLGEPGGGATYLDLMRHNLDTLA 267
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-311 2.36e-99

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: 301.01  E-value: 2.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299   1 MKKKILLMMSLISVFFAWQLTQAKQvlAEDKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQD 80
Cdd:COG0803     1 MKRLLLALLLLAALLLAGCSAAASS--AAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  81 ADAFVYMDDNMETWISDVKKSLKSKKVTIVKGTGNMLLVAGAGHDHHHEdadkkhehnkhseeghnhaFDPHVWLSPYRS 160
Cdd:COG0803    79 ADLVVYNGLGLEGWLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGE-------------------PDPHVWLDPKNA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 161 ITVVENIRDSLSKAYPEKAENFKANAATYIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISINGVTPDA 240
Cdd:COG0803   140 KKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGS 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771599299 241 EPSAKRIATLSKYVKKYGIKYIYFEENASNKVAKTLAKEAGVKTAVLSPLEGLTEkemkAGEDYFTVMRKN 311
Cdd:COG0803   220 EPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGG----PGDTYLDMMRHN 286
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
 30-315 5.54e-66

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: 214.93  E-value: 5.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  30 DKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDVKKSLKSKKV-T 108
Cdd:cd01019     2 AEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVlT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 109 IVKGTGnmllVAGAGHDHHHEDADKKHEHNKHSEEGHNH-AFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAA 187
Cdd:cd01019    82 LAKLID----LKTLEDGASHGDHEHDHEHAHGEHDGHEEgGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 188 TYIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEEN 267
Cdd:cd01019   158 AFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQ 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1771599299 268 ASNKVAKTLAKEAGVKTAVLSPLEGLTEkemKAGEDYFTVMRKNLETL 315
Cdd:cd01019   238 FHPKIAETLAEGTGAKVGELDPLGGLIE---LGKNSYVNFLRNLADSL 282
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
 338-515 2.52e-64

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 208.09  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 338 NGYFKDKDVKDRKLSDWSGNWQSVYPYLQDGTLDQVWDYKAKKSKGKmTAAEYKDYYTTGYKTDVEQIKIngKKKTMTFV 417
Cdd:PRK10306   42 NGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQKKAKKDKTK-TFEEIKAYYRKGYATDVEMIGI--ENGIVEFH 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 418 RNGEKKTFTYTYAGKEILTYPKGNRGVRFMFEAKEADAGEFKYVQFSDHAIAPEKAEHFHLYWGGDSQEKLHKELEHWPT 497
Cdd:PRK10306  119 RGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPKYVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPT 198

                         170
                  ....*....|....*...
gi 1771599299 498 YYGSDLSGREIAQEINAH 515
Cdd:PRK10306  199 YYPYQLSSEEVVDEMLHH 216
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 27-316 1.20e-56

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: 190.57  E-value: 1.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  27 LAEDKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDVKKSLKSKK 106
Cdd:cd01137    13 TAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWLERLVKNAGKDV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 107 VTIVKGTGNMLLVAGAGHDHHHEDadkkhehnkhseeghnhafdPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANA 186
Cdd:cd01137    93 PVVAVSEGIDPIPLEEGHYKGKPD--------------------PHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 187 ATYIEKLKELDKDYTAALSD--AKQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYF 264
Cdd:cd01137   153 AAYKAKLKALDEWAKAKFATipAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFV 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1771599299 265 EENASNKVAKTLAKEAGVKTAVLSPLEGLTEKEmKAGEDYFTVMRKNLETLR 316
Cdd:cd01137   233 ESTVNDRLMKQVAKETGAKIGGQLYTDSLSEKG-GPADTYLDMMEHNLDTIV 283
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 32-316 8.60e-55

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: 186.19  E-value: 8.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  32 VKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDF--EPStkDIKKIQDADAFVYMDDNMETWISDVKKSLKSKKVTI 109
Cdd:COG4531    10 PRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYalRPS--DARALQDADLVFWVGPDLEPFLEKPLETLAPDAKVV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 110 ----VKGTgNMLLVAGAGHDHHHEDADKKHEHNKHSEEGHNHA---FDPHVWLSPYRSITVVENIRDSLSKAYPEKAENF 182
Cdd:COG4531    88 elleLPGL-TLLPFREGGDFEHHDHHDEHHHHHHHHDDHHDHHhggYDPHLWLSPENAKAWAAAIADALSELDPENAATY 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 183 KANAATYIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQ---ISINgvtPDAEPSAKRIATLSKYVKKYGI 259
Cdd:COG4531   167 QANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNAlgaITLN---PEIQPGAKRLAEIREKLKELGA 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1771599299 260 KYIYFEENASNKVAKTLAKEAGVKTAVLSPLeGLTekeMKAGED-YFTVMRKNLETLR 316
Cdd:COG4531   244 VCVFAEPQFNPALVETVAEGTGVRTGVLDPL-GAD---LEPGPDlYFQLLRQLADSLA 297
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
 30-306 1.67e-52

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: 179.09  E-value: 1.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  30 DKVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNME-TWIsdVKKSLKSKKVT 108
Cdd:cd01018     1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWL--ERFRSNNPKMQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 109 IVKGTGNMLLVAGAGHDHHHEDADKKHEHnkhseeghnHAFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAAT 188
Cdd:cd01018    79 VVNMSKGITLIPMADHHHHHHGEHEHHHH---------GNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 189 YIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISI--NGVtpdaEPSAKRIATLSKYVKKYGIKYIYFEE 266
Cdd:cd01018   150 LLAELDALDSEIRTILSKLKQRAFMVYHPAWGYFARDYGLTQIPIeeEGK----EPSPADLKRLIDLAKEKGVRVVFVQP 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1771599299 267 NASNKVAKTLAKEAGVKTAVLSPLEGLTEKEMKAGEDYFT 306
Cdd:cd01018   226 QFSTKSAEAIAREIGAKVVTIDPLAADWEENLLKVADAFA 265
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
1-290 1.45e-33

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 129.36  E-value: 1.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299   1 MKKKILLMMSLISVFFAWQLTQAKqvlaedkVKVVTTFYPVyeftkGVIGN---DG--DVSMLMKAGTEPHDF--EPStk 73
Cdd:PRK09545    1 LHKKTLLFAALLAALLGGATQAAN-------AAVVTSIKPL-----GFIASaiaDGvtETEVLLPDGASPHDYslRPS-- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  74 DIKKIQDADAFVYMDDNMETWISDVKKSLKSKKV-TIVKGTG-NMLLVAGAGHDHHHEDADkkHEHNKHSEEGHNHA-FD 150
Cdd:PRK09545   67 DVKRLQSADLVVWVGPEMEAFLEKPVSKLPENKQvTIAQLPDvKPLLMKGAHDDHHDDDHD--HAGHEKSDEDHHHGeYN 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 151 PHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQ 230
Cdd:PRK09545  145 MHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTP 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 231 ISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENASNKVAKTLAKEAGVKTAVLSPL 290
Cdd:PRK09545  225 LGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPL 284
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
 31-315 1.96e-31

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: 122.47  E-value: 1.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  31 KVKVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDVKKSLKSKKVTIv 110
Cdd:cd01016     1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSSKSVI- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 111 kgtgnmllvagAGHDHHHEDADKKHEhnkhsEEGHnhaFDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYI 190
Cdd:cd01016    80 -----------ALEDTLDRSQLILDE-----EEGT---YDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 191 EKLKELDKDYTAALSD--AKQKSFVTQHAAFGYMALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEENA 268
Cdd:cd01016   141 EELDSLDAYAKKKIAEipEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSV 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1771599299 269 SNKVAKTL---AKEAGVKTAVLSPLEGLTEKEMKAGED-YFTVMRKNLETL 315
Cdd:cd01016   221 NQKSIEALqdaVKARGHDVQIGGELYSDAMGEEGTSEGtYIGMFKHNVDTI 271
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
 30-315 1.72e-24

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: 102.52  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  30 DKVKVVTT--FYPvyEFTKGVIGNDGDV-SMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWISDvkkslkskk 106
Cdd:cd01020     1 GKINVVAStnFWG--SVAEAVGGDHVEVtSIITNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTK--------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 107 vtIVKGTGNMLLVAGAGHDHHHEDADkkhehnkhseeghnhafDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANA 186
Cdd:cd01020    70 --LLADTKDVIVIAADLDGHDDKEGD-----------------NPHLWYDPETMSKVANALADALVKADPDNKKYYQANA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 187 ATYIEKLKELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGL--------NQISINGvtpdAEPSAKRIATLSKYVKKYG 258
Cdd:cd01020   131 KKFVASLKPLAAKIAELSAKYKGAPVAATEPVFDYLLDALGMkertpkgyTATTESE----TEPSPADIAAFQNAIKNRQ 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 259 IKYIYFEENASNKVAKT---LAKEAGVktavlsPLEGLTEkEMKAGEDYFTVMRKNLETL 315
Cdd:cd01020   207 IDALIVNPQQASSATTNitgLAKRSGV------PVVEVTE-TMPNGTTYLTWMLKQVDQL 259
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 145-316 2.06e-18

anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ABC transporter permease subunits as identified by pfam00950, but additionally contain the Actinobacterial insert domain described by TIGR03769. Some homologs (lacking the insert) have been described as transporters of manganese or of chelated iron. Members of this family typically are found along with an ATP-binding cassette protein, a permease, and an LPXTG-anchored protein with two or three copies of the TIGR03769 insert that occurs just once in this protein family. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163484 [Multi-domain]  Cd Length: 479  Bit Score: 88.00  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 145 HNHA-FDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYIEKLKELDKDYTAALSD--AKQKSFVTQHAAFGY 221
Cdd:TIGR03772 304 HVHGeIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATipPSRRHLITTHDAYSY 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 222 MALDYGLNQISINGVTPDAEPSAKRIATLSKYVKKYGIKYIYFEEN--ASNKVAKTLAKEAGVKtavLSPLEGLT-EKEM 298
Cdd:TIGR03772 384 LGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNlaARSTTLNEIADELGVR---VCAIYGDTfDDDV 460

                         170
                  ....*....|....*...
gi 1771599299 299 KageDYFTVMRKNLETLR 316
Cdd:TIGR03772 461 T---NYVDLMRFNADSLA 475
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
 34-245 1.61e-14

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: 72.15  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  34 VVTTFYPVYEFTKGVIGNDGDVSMLMKAGTEPHDFEPSTKDIKKIQDADAFVYMDDNMETWisDVKKSLKSKKVTIVKGT 113
Cdd:cd01145     5 VVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGF--EPKLAELSSNSKVQPGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 114 GNMLlvagaghdhhhEDADKKHEHNKHSEEGHNHAfDPHVWLSPYRSITVVENIRDSLSKAYPEKAENFKANAATYIEKL 193
Cdd:cd01145    83 KILI-----------EDSDTVGMVDRAMGDYHGKG-NPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1771599299 194 KELDKDYTAALSDAKQKSFVTQHAAFGYMALDYGLNQISIngVTPDAEPSAK 245
Cdd:cd01145   151 NKLLREWERQFEGLKGIQVVAYHPSYQYLADWLGIEVVAS--LEPLPELPPT 200
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 33-213 5.60e-04

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: 40.62  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299  33 KVVTTFYPVYEFTKGVIGNDGDVSMLMKAGTE-------------PHDFEPSTKDIKKIQdADAFVYMDDNMETWIsdvk 99
Cdd:cd00636     2 RVVALDPGATELLLALGGDDKPVGVADPSGYPpeakallekvpdvGHGYEPNLEKIAALK-PDLIIANGSGLEAWL---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771599299 100 kslkskkvtivkgtgNMLLVAGAGhdhhhedadkkhehnkhseeghNHAFDPHVWLSPYRSITVVENIRDSLskaypeka 179
Cdd:cd00636    77 ---------------DKLSKIAIP----------------------VVVVDEASELSLENIKESIRLIGKAL-------- 111

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1771599299 180 eNFKANAATYIEKLKELDKDYTAALSDAKQKSFV 213
Cdd:cd00636   112 -GKEENAEELIAELDARLAELRAKLAKIPKKKVS 144
 
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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