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Conserved domains on  [gi|2232488575|gb|UPQ63624|]
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Cu++ transporting ATPase alpha polypepdtide, partial [Scarturus elater elater]

Protein Classification

heavy metal-associated domain-containing protein( domain architecture ID 10086127)

heavy metal-associated domain-containing protein such as heavy metal-associated isoprenylated plant proteins and Saccharomyces cerevisiae copper transport protein ATX1, which shuttles copper to the transport ATPase CCC2 and protects against oxygen toxicity

Gene Ontology:  GO:0046872
PubMed:  12594858|10404590|8091505|9437429

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 69-126 9.42e-16

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


:

Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 68.79  E-value: 9.42e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2232488575  69 TFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNAsSATPETLRKAIES 126
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 169-219 5.19e-14

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


:

Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 64.16  E-value: 5.19e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2232488575 169 VINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPlLTSPET 219
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEE 50
copA super family cl32553
copper-exporting P-type ATPase CopA;
10-125 9.94e-09

copper-exporting P-type ATPase CopA;


The actual alignment was detected with superfamily member PRK10671:

Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 54.75  E-value: 9.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488575  10 TAEEIKNQIEAVGFQA---FIKKQPkyLKLGAIDVERLKNTPVKSPEGSHKRSPSctndltTTFIVDGMHCKSCVSNIEN 86
Cdd:PRK10671   48 SAEALIETIKQAGYDAsvsHPKAKP--LTESSIPSEALTAASEELPAATADDDDS------QQLLLSGMSCASCVSRVQN 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2232488575  87 ALSTLQYVSHIAVSLENRSAIVkynASSATPETLRKAIE 125
Cdd:PRK10671  120 ALQSVPGVTQARVNLAERTALV---MGSASPQDLVQAVE 155
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 69-126 9.42e-16

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 68.79  E-value: 9.42e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2232488575  69 TFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNAsSATPETLRKAIES 126
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-127 3.58e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 67.62  E-value: 3.58e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2232488575  67 TTTFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSATPETLRKAIESV 127
Cdd:COG2608     3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA pfam00403
Heavy-metal-associated domain;
69-126 1.35e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 65.72  E-value: 1.35e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2232488575  69 TFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSATPETLRKAIES 126
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 169-219 5.19e-14

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 64.16  E-value: 5.19e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2232488575 169 VINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPlLTSPET 219
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEE 50
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
165-219 5.23e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 64.54  E-value: 5.23e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2232488575 165 TQETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPLLTSPET 219
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLED 55
HMA pfam00403
Heavy-metal-associated domain;
169-219 2.73e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 56.86  E-value: 2.73e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2232488575 169 VINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPLLTSPET 219
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEK 51
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 167-212 5.88e-11

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 56.33  E-value: 5.88e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2232488575 167 ETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDP 212
Cdd:NF033795    1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDE 46
copA PRK10671
copper-exporting P-type ATPase CopA;
10-125 9.94e-09

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 54.75  E-value: 9.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488575  10 TAEEIKNQIEAVGFQA---FIKKQPkyLKLGAIDVERLKNTPVKSPEGSHKRSPSctndltTTFIVDGMHCKSCVSNIEN 86
Cdd:PRK10671   48 SAEALIETIKQAGYDAsvsHPKAKP--LTESSIPSEALTAASEELPAATADDDDS------QQLLLSGMSCASCVSRVQN 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2232488575  87 ALSTLQYVSHIAVSLENRSAIVkynASSATPETLRKAIE 125
Cdd:PRK10671  120 ALQSVPGVTQARVNLAERTALV---MGSASPQDLVQAVE 155
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-125 3.69e-08

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 48.69  E-value: 3.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2232488575  69 TFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSATPETLRKAIE 125
Cdd:TIGR00003   3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
PRK13748 PRK13748
putative mercuric reductase; Provisional
 167-212 2.53e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.54  E-value: 2.53e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2232488575 167 ETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDP 212
Cdd:PRK13748    1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV 46
PLN02957 PLN02957
copper, zinc superoxide dismutase
 65-126 1.05e-05

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 44.74  E-value: 1.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2232488575  65 DLTTTFIVDgMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVkynASSATPETLRKAIES 126
Cdd:PLN02957    5 ELLTEFMVD-MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRV---LGSSPVKAMTAALEQ 62
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 170-211 2.48e-04

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 38.29  E-value: 2.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2232488575 170 INISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYD 211
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFD 45
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 164-212 8.57e-03

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 34.23  E-value: 8.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2232488575 164 LTQETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDP 212
Cdd:NF041115    2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDP 50
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 69-126 9.42e-16

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 68.79  E-value: 9.42e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2232488575  69 TFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNAsSATPETLRKAIES 126
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-127 3.58e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 67.62  E-value: 3.58e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2232488575  67 TTTFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSATPETLRKAIESV 127
Cdd:COG2608     3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA pfam00403
Heavy-metal-associated domain;
69-126 1.35e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 65.72  E-value: 1.35e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2232488575  69 TFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSATPETLRKAIES 126
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 169-219 5.19e-14

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 64.16  E-value: 5.19e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2232488575 169 VINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPlLTSPET 219
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEE 50
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
165-219 5.23e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 64.54  E-value: 5.23e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2232488575 165 TQETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPLLTSPET 219
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLED 55
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
67-139 4.12e-12

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 64.78  E-value: 4.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2232488575  67 TTTFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSATPETLRKAIESVSpgqYKVSIASD 139
Cdd:COG2217     2 RVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAG---YEAEPADA 71
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
166-219 8.92e-12

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 63.62  E-value: 8.92e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2232488575 166 QETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPLLTSPET 219
Cdd:COG2217     1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEE 54
HMA pfam00403
Heavy-metal-associated domain;
169-219 2.73e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 56.86  E-value: 2.73e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2232488575 169 VINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDPLLTSPET 219
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEK 51
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 167-212 5.88e-11

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 56.33  E-value: 5.88e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2232488575 167 ETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDP 212
Cdd:NF033795    1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDE 46
copA PRK10671
copper-exporting P-type ATPase CopA;
10-125 9.94e-09

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 54.75  E-value: 9.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488575  10 TAEEIKNQIEAVGFQA---FIKKQPkyLKLGAIDVERLKNTPVKSPEGSHKRSPSctndltTTFIVDGMHCKSCVSNIEN 86
Cdd:PRK10671   48 SAEALIETIKQAGYDAsvsHPKAKP--LTESSIPSEALTAASEELPAATADDDDS------QQLLLSGMSCASCVSRVQN 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2232488575  87 ALSTLQYVSHIAVSLENRSAIVkynASSATPETLRKAIE 125
Cdd:PRK10671  120 ALQSVPGVTQARVNLAERTALV---MGSASPQDLVQAVE 155
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-125 3.69e-08

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 48.69  E-value: 3.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2232488575  69 TFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSATPETLRKAIE 125
Cdd:TIGR00003   3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
copA PRK10671
copper-exporting P-type ATPase CopA;
67-208 2.35e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 50.51  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488575  67 TTTFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIvkynaSSATPETLrkaIESVSPGQYKvsiASDVESTSNS 146
Cdd:PRK10671    4 TIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVT-----GTASAEAL---IETIKQAGYD---ASVSHPKAKP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2232488575 147 PSSSSLQKVPLNIVSQPLTQETVIN-------ISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTV 208
Cdd:PRK10671   73 LTESSIPSEALTAASEELPAATADDddsqqllLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALV 141
PRK13748 PRK13748
putative mercuric reductase; Provisional
 167-212 2.53e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.54  E-value: 2.53e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2232488575 167 ETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDP 212
Cdd:PRK13748    1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV 46
PLN02957 PLN02957
copper, zinc superoxide dismutase
 65-126 1.05e-05

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 44.74  E-value: 1.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2232488575  65 DLTTTFIVDgMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVkynASSATPETLRKAIES 126
Cdd:PLN02957    5 ELLTEFMVD-MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRV---LGSSPVKAMTAALEQ 62
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 170-211 2.48e-04

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 38.29  E-value: 2.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2232488575 170 INISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYD 211
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFD 45
PRK13748 PRK13748
putative mercuric reductase; Provisional
 68-137 1.13e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 39.36  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488575  68 TTFIVDGMHCKSCVSNIENALSTLQYVSHIAVSLENRSAIVKYNASSAtPETLRKAIESVSpgqYKVSIA 137
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTS-PDALTAAVAGLG---YRATLA 67
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
 165-211 1.99e-03

mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification]


Pssm-ID: 131107 [Multi-domain]  Cd Length: 92  Bit Score: 36.17  E-value: 1.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2232488575 165 TQETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYD 211
Cdd:TIGR02052  22 TQTVTLEVPGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFD 68
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 172-202 3.80e-03

zinc/cadmium/mercury/lead-transporting ATPase; Provisional


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 38.05  E-value: 3.80e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2232488575 172 ISGMTCNSCVQSIEGMISKRPGVKSIRVSLA 202
Cdd:PRK11033   59 VSGMDCPSCARKVENAVRQLAGVNQVQVLFA 89
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 164-212 8.57e-03

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 34.23  E-value: 8.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2232488575 164 LTQETVINISGMTCNSCVQSIEGMISKRPGVKSIRVSLANSTGTVEYDP 212
Cdd:NF041115    2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDP 50
 
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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