ABC transporter B family member 4, putative [Plasmodium falciparum 3D7]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| SunT super family | cl34455 | ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
978-1354 | 7.76e-34 | ||||||
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]; The actual alignment was detected with superfamily member COG2274: Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 140.35 E-value: 7.76e-34
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| ABC_6TM_exporters super family | cl38913 | Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
173-483 | 3.91e-33 | ||||||
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. The actual alignment was detected with superfamily member cd18572: Pssm-ID: 365789 [Multi-domain] Cd Length: 289 Bit Score: 130.36 E-value: 3.91e-33
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| Name | Accession | Description | Interval | E-value | ||||||
| SunT | COG2274 | ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
978-1354 | 7.76e-34 | ||||||
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]; Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 140.35 E-value: 7.76e-34
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| ABC_6TM_TAP | cd18572 | Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
173-483 | 3.91e-33 | ||||||
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation. Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 130.36 E-value: 3.91e-33
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| ABC_MTABC3_MDL1_MDL2 | cd03249 | ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1235-1354 | 1.30e-29 | ||||||
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another. Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 118.41 E-value: 1.30e-29
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| MdlB | COG1132 | ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
156-488 | 7.40e-28 | ||||||
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.65 E-value: 7.40e-28
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| ABC_membrane | pfam00664 | ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
173-460 | 3.31e-24 | ||||||
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions. Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 103.88 E-value: 3.31e-24
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| 3a01208 | TIGR00958 | Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
141-433 | 1.92e-20 | ||||||
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 1.92e-20
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| 3a01208 | TIGR00958 | Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1236-1353 | 2.79e-19 | ||||||
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.02 E-value: 2.79e-19
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| PRK11176 | PRK11176 | lipid A ABC transporter ATP-binding protein/permease MsbA; |
1235-1354 | 4.11e-18 | ||||||
lipid A ABC transporter ATP-binding protein/permease MsbA; Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 4.11e-18
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| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1266-1294 | 4.21e-09 | ||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 56.50 E-value: 4.21e-09
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| PRK11176 | PRK11176 | lipid A ABC transporter ATP-binding protein/permease MsbA; |
240-456 | 6.06e-08 | ||||||
lipid A ABC transporter ATP-binding protein/permease MsbA; Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 6.06e-08
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| GguA | NF040905 | sugar ABC transporter ATP-binding protein; |
1269-1343 | 4.49e-04 | ||||||
sugar ABC transporter ATP-binding protein; Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 4.49e-04
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| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1228-1312 | 1.80e-03 | ||||||
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment. Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 1.80e-03
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| Name | Accession | Description | Interval | E-value | |||||||
| SunT | COG2274 | ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
978-1354 | 7.76e-34 | |||||||
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]; Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 140.35 E-value: 7.76e-34
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| ABC_6TM_TAP | cd18572 | Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
173-483 | 3.91e-33 | |||||||
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation. Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 130.36 E-value: 3.91e-33
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| MdlB | COG1132 | ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1236-1345 | 5.00e-32 | |||||||
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 133.37 E-value: 5.00e-32
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| ABC_MTABC3_MDL1_MDL2 | cd03249 | ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1235-1354 | 1.30e-29 | |||||||
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another. Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 118.41 E-value: 1.30e-29
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| ABCC_MRP_Like | cd03228 | ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1265-1340 | 1.39e-29 | |||||||
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 115.94 E-value: 1.39e-29
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| ABC_6TM_TAP_ABCB8_10_like | cd18557 | Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
236-483 | 5.89e-29 | |||||||
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 118.05 E-value: 5.89e-29
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| MdlB | COG1132 | ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
156-488 | 7.40e-28 | |||||||
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.65 E-value: 7.40e-28
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| ABC_6TM_bac_exporter_ABCB8_10_like | cd18576 | Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
240-483 | 1.41e-26 | |||||||
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 111.42 E-value: 1.41e-26
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| ABCC_ATM1_transporter | cd03253 | ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1236-1358 | 1.57e-25 | |||||||
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 106.55 E-value: 1.57e-25
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| ABC_6TM_exporters | cd07346 | Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
170-433 | 7.61e-25 | |||||||
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 106.10 E-value: 7.61e-25
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| ABC_membrane | pfam00664 | ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
173-460 | 3.31e-24 | |||||||
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions. Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 103.88 E-value: 3.31e-24
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| ABCC_MsbA | cd03251 | ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1235-1358 | 4.55e-24 | |||||||
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 102.31 E-value: 4.55e-24
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| ABCC_MRP_domain2 | cd03244 | ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1236-1345 | 4.57e-23 | |||||||
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate. Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 99.11 E-value: 4.57e-23
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| ABCC_Glucan_exporter_like | cd03254 | ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
980-1354 | 8.90e-23 | |||||||
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.45 E-value: 8.90e-23
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| ABC_6TM_AtABCB27_like | cd18780 | Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
236-412 | 1.95e-22 | |||||||
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 99.25 E-value: 1.95e-22
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| CydD | COG4988 | ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1236-1353 | 2.75e-22 | |||||||
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 102.91 E-value: 2.75e-22
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| ABC_6TM_LmrA_like | cd18551 | Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
170-431 | 4.16e-22 | |||||||
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 98.27 E-value: 4.16e-22
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| ABC_6TM_ABCB10_like | cd18573 | Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
240-411 | 8.15e-22 | |||||||
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 97.58 E-value: 8.15e-22
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| ABC_6TM_ABCB9_like | cd18784 | Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
227-431 | 1.65e-20 | |||||||
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 1.65e-20
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| 3a01208 | TIGR00958 | Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
141-433 | 1.92e-20 | |||||||
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 1.92e-20
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| ABC_NikE_OppD_transporters | cd03257 | ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1248-1345 | 1.67e-19 | |||||||
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF. Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 89.10 E-value: 1.67e-19
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| 3a01208 | TIGR00958 | Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1236-1353 | 2.79e-19 | |||||||
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.02 E-value: 2.79e-19
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| ABCC_MRP_domain1 | cd03250 | ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1229-1340 | 4.59e-19 | |||||||
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate. Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 87.14 E-value: 4.59e-19
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| ABCC_Hemolysin | cd03252 | ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1235-1358 | 8.07e-19 | |||||||
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy. Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 87.16 E-value: 8.07e-19
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| ABC_6TM_Pgp_ABCB1_D1_like | cd18577 | Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
234-431 | 1.80e-18 | |||||||
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells. Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 87.53 E-value: 1.80e-18
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| ABCC_TAP | cd03248 | ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1266-1341 | 1.98e-18 | |||||||
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes. Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 85.99 E-value: 1.98e-18
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| PRK11176 | PRK11176 | lipid A ABC transporter ATP-binding protein/permease MsbA; |
1235-1354 | 4.11e-18 | |||||||
lipid A ABC transporter ATP-binding protein/permease MsbA; Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 4.11e-18
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| ATM1 | COG5265 | ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1236-1345 | 5.53e-18 | |||||||
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.49 E-value: 5.53e-18
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| ABCC_Protease_Secretion | cd03246 | ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1261-1341 | 6.67e-18 | |||||||
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA. Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 82.65 E-value: 6.67e-18
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| ABC_6TM_MsbA_like | cd18552 | Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
170-408 | 7.55e-18 | |||||||
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 85.55 E-value: 7.55e-18
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| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1266-1340 | 9.37e-18 | |||||||
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 81.91 E-value: 9.37e-18
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| ABCC_bacteriocin_exporters | cd03245 | ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1236-1345 | 1.52e-17 | |||||||
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane. Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 83.02 E-value: 1.52e-17
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| PRK13657 | PRK13657 | glucan ABC transporter ATP-binding protein/ permease; |
1236-1352 | 1.89e-17 | |||||||
glucan ABC transporter ATP-binding protein/ permease; Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.71 E-value: 1.89e-17
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| ABC_6TM_TAP2 | cd18590 | Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
237-483 | 2.02e-17 | |||||||
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation. Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 84.31 E-value: 2.02e-17
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| YddA | COG4178 | ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1263-1339 | 1.31e-16 | |||||||
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only]; Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.86 E-value: 1.31e-16
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| ABC_Iron-Siderophores_B12_Hemin | cd03214 | ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1266-1345 | 1.56e-16 | |||||||
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters. Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 79.02 E-value: 1.56e-16
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| PTZ00265 | PTZ00265 | multidrug resistance protein (mdr1); Provisional |
935-1338 | 1.85e-16 | |||||||
multidrug resistance protein (mdr1); Provisional Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 1.85e-16
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| ABCC_NFT1 | cd03369 | ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1266-1345 | 2.05e-16 | |||||||
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate. Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 79.38 E-value: 2.05e-16
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| CydC | COG4987 | ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1236-1354 | 3.43e-16 | |||||||
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 83.66 E-value: 3.43e-16
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| ABC_6TM_TmrA_like | cd18544 | Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
170-433 | 7.22e-16 | |||||||
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 79.74 E-value: 7.22e-16
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| PRK10789 | PRK10789 | SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1236-1352 | 8.20e-16 | |||||||
SmdA family multidrug ABC transporter permease/ATP-binding protein; Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.45 E-value: 8.20e-16
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| ABC_MetN_methionine_transporter | cd03258 | ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1242-1345 | 1.59e-15 | |||||||
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 77.62 E-value: 1.59e-15
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| GsiA | COG1123 | ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1266-1361 | 2.74e-15 | |||||||
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 80.33 E-value: 2.74e-15
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| DppF | COG1124 | ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1266-1362 | 4.84e-15 | |||||||
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]; Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 76.38 E-value: 4.84e-15
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| ABC_MJ0796_LolCDE_FtsE | cd03255 | ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1242-1341 | 8.39e-15 | |||||||
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane. Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 74.83 E-value: 8.39e-15
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| ABCD_peroxisomal_ALDP | cd03223 | ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1263-1325 | 1.36e-14 | |||||||
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic). Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.96 E-value: 1.36e-14
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| ABC_Org_Solvent_Resistant | cd03261 | ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1266-1362 | 1.80e-14 | |||||||
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 74.46 E-value: 1.80e-14
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| ABC_Metallic_Cations | cd03235 | ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1266-1345 | 2.92e-14 | |||||||
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates. Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 73.34 E-value: 2.92e-14
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| ABC_6TM_PCAT1_LagD_like | cd18570 | Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
236-431 | 5.23e-14 | |||||||
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins. Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 74.40 E-value: 5.23e-14
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| ABC_6TM_Pgp_ABCB1_D2_like | cd18578 | Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
160-411 | 5.91e-14 | |||||||
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells. Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 74.41 E-value: 5.91e-14
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| EcfA2 | COG1122 | Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1266-1345 | 8.06e-14 | |||||||
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 72.37 E-value: 8.06e-14
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| MRP_assoc_pro | TIGR00957 | multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1246-1358 | 1.31e-13 | |||||||
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other] Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.14 E-value: 1.31e-13
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| NatA | COG4555 | ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1266-1361 | 1.84e-13 | |||||||
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism]; Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 71.81 E-value: 1.84e-13
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| ABC_Class3 | cd03229 | ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1266-1340 | 2.09e-13 | |||||||
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 69.91 E-value: 2.09e-13
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| PRK11174 | PRK11174 | cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1266-1345 | 2.46e-13 | |||||||
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 2.46e-13
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| ABC_Carb_Solutes_like | cd03259 | ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1266-1345 | 2.99e-13 | |||||||
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 70.24 E-value: 2.99e-13
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| ABC_6TM_Tm288_like | cd18547 | Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
170-398 | 3.07e-13 | |||||||
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 72.05 E-value: 3.07e-13
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| PLN03130 | PLN03130 | ABC transporter C family member; Provisional |
1267-1360 | 3.31e-13 | |||||||
ABC transporter C family member; Provisional Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 3.31e-13
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| ABC_DR_subfamily_A | cd03230 | ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1266-1341 | 3.50e-13 | |||||||
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 68.96 E-value: 3.50e-13
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| ABC_PstB_phosphate_transporter | cd03260 | ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1266-1350 | 3.69e-13 | |||||||
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD). Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 70.29 E-value: 3.69e-13
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| PLN03232 | PLN03232 | ABC transporter C family member; Provisional |
1266-1360 | 3.95e-13 | |||||||
ABC transporter C family member; Provisional Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.63 E-value: 3.95e-13
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| ABCC_cytochrome_bd | cd03247 | ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1240-1345 | 4.62e-13 | |||||||
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism. Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 68.88 E-value: 4.62e-13
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| MlaF | COG1127 | ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1266-1362 | 5.72e-13 | |||||||
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 70.01 E-value: 5.72e-13
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| CcmA | COG1131 | ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1266-1345 | 6.38e-13 | |||||||
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 69.71 E-value: 6.38e-13
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| PRK10790 | PRK10790 | SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1244-1358 | 9.20e-13 | |||||||
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 9.20e-13
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| ABC_6TM_bac_exporter_ABCB8_10_like | cd18575 | Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
216-402 | 1.05e-12 | |||||||
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 70.21 E-value: 1.05e-12
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| ABC_6TM_YknU_like | cd18542 | Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
170-433 | 1.06e-12 | |||||||
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 70.15 E-value: 1.06e-12
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| LolD | COG1136 | ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1244-1343 | 1.41e-12 | |||||||
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.53 E-value: 1.41e-12
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| ZnuC | COG1121 | ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1266-1345 | 1.45e-12 | |||||||
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 68.96 E-value: 1.45e-12
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| ABC_cobalt_CbiO_domain1 | cd03225 | First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1266-1340 | 1.54e-12 | |||||||
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems. Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 68.26 E-value: 1.54e-12
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| ABC_Pro_Gly_Betaine | cd03294 | ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1238-1362 | 2.61e-12 | |||||||
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 68.82 E-value: 2.61e-12
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| FepC | COG1120 | ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1266-1345 | 2.64e-12 | |||||||
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism]; Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 68.53 E-value: 2.64e-12
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| ABC_6TM_exporter_like | cd18563 | Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
236-431 | 3.28e-12 | |||||||
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 69.08 E-value: 3.28e-12
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| ABCC_CFTR2 | cd03289 | ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1235-1356 | 4.08e-12 | |||||||
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2. Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 68.34 E-value: 4.08e-12
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| bacteriocin_ABC | TIGR01193 | ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1236-1363 | 4.44e-12 | |||||||
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other] Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 70.92 E-value: 4.44e-12
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| AbcC | COG1135 | ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1236-1345 | 5.36e-12 | |||||||
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.95 E-value: 5.36e-12
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| ABC_ModC_molybdenum_transporter | cd03297 | ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1238-1345 | 6.13e-12 | |||||||
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 66.55 E-value: 6.13e-12
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| ABC_ModC_like | cd03299 | ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1231-1362 | 8.97e-12 | |||||||
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 66.59 E-value: 8.97e-12
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| SapF | COG4167 | ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1253-1361 | 1.02e-11 | |||||||
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 66.78 E-value: 1.02e-11
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| CysA | COG1118 | ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1266-1345 | 1.12e-11 | |||||||
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.86 E-value: 1.12e-11
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| YejF | COG4172 | ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1248-1358 | 1.16e-11 | |||||||
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.94 E-value: 1.16e-11
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| ArpD | COG4618 | ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1266-1352 | 1.33e-11 | |||||||
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 69.01 E-value: 1.33e-11
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| ABC_6TM_Pgp_ABCB1 | cd18558 | Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
233-467 | 1.50e-11 | |||||||
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells. Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 67.30 E-value: 1.50e-11
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| ABCG_EPDR | cd03213 | Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1266-1345 | 1.55e-11 | |||||||
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus. Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 64.88 E-value: 1.55e-11
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| PRK11160 | PRK11160 | cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1266-1355 | 1.75e-11 | |||||||
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.70 E-value: 1.75e-11
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| metN | PRK11153 | DL-methionine transporter ATP-binding subunit; Provisional |
1266-1345 | 2.10e-11 | |||||||
DL-methionine transporter ATP-binding subunit; Provisional Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.13 E-value: 2.10e-11
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| SapD | COG4170 | ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1230-1353 | 2.30e-11 | |||||||
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.85 E-value: 2.30e-11
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| MRP_assoc_pro | TIGR00957 | multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1266-1365 | 2.79e-11 | |||||||
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other] Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 2.79e-11
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| CFTR_protein | TIGR01271 | cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1235-1355 | 5.99e-11 | |||||||
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions] Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.63 E-value: 5.99e-11
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| ABC_NrtD_SsuB_transporters | cd03293 | ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1242-1298 | 8.01e-11 | |||||||
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 63.26 E-value: 8.01e-11
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| GsiA | COG1123 | ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1235-1353 | 8.71e-11 | |||||||
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 66.08 E-value: 8.71e-11
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| ECF_ATPase_1 | TIGR04520 | energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1266-1345 | 9.61e-11 | |||||||
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate] Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 63.99 E-value: 9.61e-11
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| ABC_putative_ATPase | cd03269 | ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1266-1345 | 1.00e-10 | |||||||
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 62.68 E-value: 1.00e-10
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| YhaQ | COG4152 | ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1262-1345 | 1.03e-10 | |||||||
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.36 E-value: 1.03e-10
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| ThiQ | COG3840 | ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1265-1362 | 1.27e-10 | |||||||
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 1.27e-10
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| ABC_6TM_ABCB8_like | cd18574 | Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
174-410 | 1.51e-10 | |||||||
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter. Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 63.72 E-value: 1.51e-10
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| PTZ00265 | PTZ00265 | multidrug resistance protein (mdr1); Provisional |
1235-1360 | 1.55e-10 | |||||||
multidrug resistance protein (mdr1); Provisional Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.55e-10
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| cbiO | PRK13640 | energy-coupling factor transporter ATPase; |
1266-1353 | 2.29e-10 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 2.29e-10
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| cbiO | PRK13635 | energy-coupling factor ABC transporter ATP-binding protein; |
1266-1345 | 2.78e-10 | |||||||
energy-coupling factor ABC transporter ATP-binding protein; Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 2.78e-10
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| ABC_Carb_Monos_I | cd03216 | First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1266-1342 | 4.01e-10 | |||||||
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter. Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 59.75 E-value: 4.01e-10
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| potA | PRK09452 | spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1266-1341 | 5.43e-10 | |||||||
spermidine/putrescine ABC transporter ATP-binding protein PotA; Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 5.43e-10
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| PotA | COG3842 | ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1266-1345 | 7.74e-10 | |||||||
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.42 E-value: 7.74e-10
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| ABC_6TM_T1SS_like | cd18555 | Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
236-433 | 9.72e-10 | |||||||
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides. Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 61.37 E-value: 9.72e-10
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| ABC_MalK_N | cd03301 | The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1230-1341 | 1.11e-09 | |||||||
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed. Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 59.96 E-value: 1.11e-09
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| DppD | COG0444 | ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1248-1353 | 1.71e-09 | |||||||
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]; Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 60.84 E-value: 1.71e-09
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| FtsE | COG2884 | Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1246-1347 | 2.33e-09 | |||||||
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.91 E-value: 2.33e-09
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| cbiO | PRK13650 | energy-coupling factor transporter ATPase; |
1266-1341 | 2.42e-09 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.13 E-value: 2.42e-09
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| ABCC_SUR2 | cd03288 | ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1266-1358 | 2.55e-09 | |||||||
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity. Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 59.54 E-value: 2.55e-09
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| ABC_PotA_N | cd03300 | ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1230-1345 | 2.86e-09 | |||||||
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 59.17 E-value: 2.86e-09
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| PLN03232 | PLN03232 | ABC transporter C family member; Provisional |
1266-1364 | 3.16e-09 | |||||||
ABC transporter C family member; Provisional Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 3.16e-09
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| ABC_CysA_sulfate_importer | cd03296 | ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1213-1362 | 3.60e-09 | |||||||
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 58.89 E-value: 3.60e-09
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| ABC_OpuCA_Osmoprotection | cd03295 | ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1266-1362 | 3.74e-09 | |||||||
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 58.85 E-value: 3.74e-09
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| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1266-1294 | 4.21e-09 | |||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 56.50 E-value: 4.21e-09
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| TauB | COG1116 | ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1266-1298 | 4.32e-09 | |||||||
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 58.95 E-value: 4.32e-09
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| ABC_PhnC_transporter | cd03256 | ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1266-1342 | 4.47e-09 | |||||||
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 58.73 E-value: 4.47e-09
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| PLN03130 | PLN03130 | ABC transporter C family member; Provisional |
1266-1353 | 5.40e-09 | |||||||
ABC transporter C family member; Provisional Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 5.40e-09
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| PRK15134 | PRK15134 | microcin C ABC transporter ATP-binding protein YejF; Provisional |
1253-1345 | 6.79e-09 | |||||||
microcin C ABC transporter ATP-binding protein YejF; Provisional Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 6.79e-09
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| CydD | TIGR02857 | thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1236-1336 | 7.02e-09 | |||||||
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 59.99 E-value: 7.02e-09
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| PRK10851 | PRK10851 | sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1235-1298 | 7.34e-09 | |||||||
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.33 E-value: 7.34e-09
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| PRK10070 | PRK10070 | proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1244-1362 | 7.93e-09 | |||||||
proline/glycine betaine ABC transporter ATP-binding protein ProV; Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.28 E-value: 7.93e-09
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| MalK | COG3839 | ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1266-1299 | 9.36e-09 | |||||||
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 58.93 E-value: 9.36e-09
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| PRK14258 | PRK14258 | phosphate ABC transporter ATP-binding protein; Provisional |
1266-1359 | 1.40e-08 | |||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 1.40e-08
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| ABC_subfamily_A | cd03263 | ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1266-1342 | 1.41e-08 | |||||||
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages. Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 56.74 E-value: 1.41e-08
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| PRK14267 | PRK14267 | phosphate ABC transporter ATP-binding protein; Provisional |
1248-1362 | 1.67e-08 | |||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 1.67e-08
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| ABCC_SUR1_N | cd03290 | ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1266-1339 | 1.90e-08 | |||||||
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity. Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.19 E-value: 1.90e-08
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| cbiO | PRK13648 | cobalt transporter ATP-binding subunit; Provisional |
1231-1345 | 2.23e-08 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.07 E-value: 2.23e-08
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| CcmA | COG4133 | ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1266-1299 | 2.68e-08 | |||||||
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 55.56 E-value: 2.68e-08
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| ABC_drug_resistance_like | cd03264 | ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1231-1345 | 3.58e-08 | |||||||
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 55.28 E-value: 3.58e-08
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| PRK15079 | PRK15079 | oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1230-1309 | 3.64e-08 | |||||||
oligopeptide ABC transporter ATP-binding protein OppF; Provisional Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.02 E-value: 3.64e-08
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| AppF | COG4608 | ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1266-1353 | 4.38e-08 | |||||||
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.66 E-value: 4.38e-08
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| ssuB | PRK11247 | aliphatic sulfonates transport ATP-binding subunit; Provisional |
1266-1298 | 4.59e-08 | |||||||
aliphatic sulfonates transport ATP-binding subunit; Provisional Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.84 E-value: 4.59e-08
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| PRK14246 | PRK14246 | phosphate ABC transporter ATP-binding protein; Provisional |
1230-1362 | 4.86e-08 | |||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 4.86e-08
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| ABC_NatA_sodium_exporter | cd03266 | ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1266-1345 | 5.44e-08 | |||||||
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein. Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 55.07 E-value: 5.44e-08
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| PRK14247 | PRK14247 | phosphate ABC transporter ATP-binding protein; Provisional |
1266-1362 | 5.52e-08 | |||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 5.52e-08
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| PRK11176 | PRK11176 | lipid A ABC transporter ATP-binding protein/permease MsbA; |
240-456 | 6.06e-08 | |||||||
lipid A ABC transporter ATP-binding protein/permease MsbA; Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 6.06e-08
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| fbpC | PRK11432 | ferric ABC transporter ATP-binding protein; |
1263-1362 | 6.16e-08 | |||||||
ferric ABC transporter ATP-binding protein; Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 6.16e-08
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| nikE | PRK10419 | nickel ABC transporter ATP-binding protein NikE; |
1266-1343 | 7.22e-08 | |||||||
nickel ABC transporter ATP-binding protein NikE; Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 7.22e-08
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| ABC_YhbG | cd03218 | ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1266-1353 | 7.38e-08 | |||||||
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium. Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 54.86 E-value: 7.38e-08
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| PRK10261 | PRK10261 | glutathione transporter ATP-binding protein; Provisional |
1253-1361 | 7.44e-08 | |||||||
glutathione transporter ATP-binding protein; Provisional Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 7.44e-08
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| PTZ00243 | PTZ00243 | ABC transporter; Provisional |
1266-1341 | 7.70e-08 | |||||||
ABC transporter; Provisional Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 7.70e-08
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| PRK13549 | PRK13549 | xylose transporter ATP-binding subunit; Provisional |
1266-1342 | 1.07e-07 | |||||||
xylose transporter ATP-binding subunit; Provisional Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 1.07e-07
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| ABC_HisP_GlnQ | cd03262 | ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1244-1297 | 1.31e-07 | |||||||
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein. Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 53.69 E-value: 1.31e-07
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| PstB | COG1117 | ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1266-1359 | 1.47e-07 | |||||||
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.27 E-value: 1.47e-07
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| ABC_6TM_Sav1866_like | cd18554 | Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
233-396 | 1.52e-07 | |||||||
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 54.73 E-value: 1.52e-07
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| ABCC_CFTR1 | cd03291 | ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1221-1354 | 1.53e-07 | |||||||
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2. Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.48 E-value: 1.53e-07
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| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
980-1063 | 1.62e-07 | |||||||
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 52.25 E-value: 1.62e-07
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| ABC_6TM_TmrB_like | cd18541 | Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
170-433 | 1.75e-07 | |||||||
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 54.34 E-value: 1.75e-07
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| ABC_6TM_HetC_like | cd18568 | Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
236-431 | 1.82e-07 | |||||||
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 54.49 E-value: 1.82e-07
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| ABC_6TM_exporter_like | cd18550 | Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
236-394 | 2.41e-07 | |||||||
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 54.03 E-value: 2.41e-07
|
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| ABC_6TM_TAP1 | cd18589 | Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
238-483 | 2.75e-07 | |||||||
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation. Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 54.01 E-value: 2.75e-07
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| PRK10895 | PRK10895 | lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1266-1361 | 2.80e-07 | |||||||
lipopolysaccharide ABC transporter ATP-binding protein; Provisional Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 2.80e-07
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| PRK15056 | PRK15056 | manganese/iron ABC transporter ATP-binding protein; |
1266-1345 | 2.85e-07 | |||||||
manganese/iron ABC transporter ATP-binding protein; Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.73 E-value: 2.85e-07
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| met_CoM_red_A2 | TIGR03269 | methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1248-1345 | 3.77e-07 | |||||||
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis] Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 54.42 E-value: 3.77e-07
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| PRK13633 | PRK13633 | energy-coupling factor transporter ATPase; |
1265-1345 | 3.85e-07 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 3.85e-07
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| glnQ | PRK09493 | glutamine ABC transporter ATP-binding protein GlnQ; |
1266-1362 | 3.85e-07 | |||||||
glutamine ABC transporter ATP-binding protein GlnQ; Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.79 E-value: 3.85e-07
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| MglA | COG1129 | ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1266-1345 | 4.32e-07 | |||||||
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 4.32e-07
|
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| artP | PRK11124 | arginine transporter ATP-binding subunit; Provisional |
1266-1345 | 4.60e-07 | |||||||
arginine transporter ATP-binding subunit; Provisional Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 4.60e-07
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| ModF | COG1119 | ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1266-1355 | 4.69e-07 | |||||||
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism]; Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 52.78 E-value: 4.69e-07
|
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| ModC | COG4148 | ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1266-1345 | 5.25e-07 | |||||||
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 53.57 E-value: 5.25e-07
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| ABC_FeS_Assembly | cd03217 | ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1257-1345 | 5.53e-07 | |||||||
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet. Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 51.76 E-value: 5.53e-07
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| ABC_6TM_YknV_like | cd18545 | Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
234-407 | 6.42e-07 | |||||||
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 52.86 E-value: 6.42e-07
|
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| CFTR_protein | TIGR01271 | cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1221-1358 | 6.69e-07 | |||||||
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions] Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 6.69e-07
|
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| TauB | COG4525 | ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1266-1298 | 7.69e-07 | |||||||
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.17 E-value: 7.69e-07
|
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| PTZ00243 | PTZ00243 | ABC transporter; Provisional |
1261-1356 | 7.97e-07 | |||||||
ABC transporter; Provisional Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 7.97e-07
|
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| thiQ | PRK10771 | thiamine ABC transporter ATP-binding protein ThiQ; |
1266-1299 | 9.92e-07 | |||||||
thiamine ABC transporter ATP-binding protein ThiQ; Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.51 E-value: 9.92e-07
|
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| YejF | COG4172 | ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1250-1361 | 1.19e-06 | |||||||
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.76 E-value: 1.19e-06
|
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| PhnL | COG4778 | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1267-1300 | 1.26e-06 | |||||||
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism]; Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 50.90 E-value: 1.26e-06
|
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| cbiO | PRK13642 | energy-coupling factor transporter ATPase; |
1266-1350 | 1.31e-06 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 1.31e-06
|
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| LptB | COG1137 | ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1266-1353 | 1.48e-06 | |||||||
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.80 E-value: 1.48e-06
|
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| dppF | PRK11308 | dipeptide transporter ATP-binding subunit; Provisional |
1253-1345 | 1.79e-06 | |||||||
dipeptide transporter ATP-binding subunit; Provisional Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 1.79e-06
|
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| PRK10619 | PRK10619 | histidine ABC transporter ATP-binding protein HisP; |
1266-1362 | 1.92e-06 | |||||||
histidine ABC transporter ATP-binding protein HisP; Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 1.92e-06
|
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| ABC_6TM_PrtD_LapB_HlyB_like | cd18566 | Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
236-431 | 2.02e-06 | |||||||
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion. Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 51.04 E-value: 2.02e-06
|
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| SufC | COG0396 | Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1266-1345 | 2.02e-06 | |||||||
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 50.45 E-value: 2.02e-06
|
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| cbiO | PRK13649 | energy-coupling factor transporter ATPase; |
1266-1345 | 2.13e-06 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.90 E-value: 2.13e-06
|
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| ABC_6TM_MRP5_8_9_D2 | cd18599 | Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
208-400 | 2.19e-06 | |||||||
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0). Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 51.41 E-value: 2.19e-06
|
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| ABC_ThiQ_thiamine_transporter | cd03298 | ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1266-1299 | 2.46e-06 | |||||||
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 49.80 E-value: 2.46e-06
|
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| tauB | PRK11248 | taurine ABC transporter ATP-binding subunit; |
1266-1298 | 2.68e-06 | |||||||
taurine ABC transporter ATP-binding subunit; Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 2.68e-06
|
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| PRK13536 | PRK13536 | nodulation factor ABC transporter ATP-binding protein NodI; |
1266-1351 | 2.82e-06 | |||||||
nodulation factor ABC transporter ATP-binding protein NodI; Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.98 E-value: 2.82e-06
|
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| PRK14271 | PRK14271 | phosphate ABC transporter ATP-binding protein; Provisional |
1266-1353 | 3.04e-06 | |||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.48 E-value: 3.04e-06
|
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| cbiO | PRK13637 | energy-coupling factor transporter ATPase; |
1266-1345 | 3.33e-06 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.43 E-value: 3.33e-06
|
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| ABC_6TM_exporter_like | cd18778 | Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
236-396 | 3.91e-06 | |||||||
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 50.23 E-value: 3.91e-06
|
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| ABC_6TM_PrtD_LapB_HlyB_like | cd18782 | uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
236-392 | 4.61e-06 | |||||||
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion. Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 49.90 E-value: 4.61e-06
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| cbiO | PRK13639 | cobalt transporter ATP-binding subunit; Provisional |
1266-1345 | 5.94e-06 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 5.94e-06
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| PRK15134 | PRK15134 | microcin C ABC transporter ATP-binding protein YejF; Provisional |
1266-1350 | 6.52e-06 | |||||||
microcin C ABC transporter ATP-binding protein YejF; Provisional Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 6.52e-06
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| oppD | PRK09473 | oligopeptide transporter ATP-binding component; Provisional |
1250-1345 | 6.61e-06 | |||||||
oligopeptide transporter ATP-binding component; Provisional Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 6.61e-06
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| PRK13537 | PRK13537 | nodulation factor ABC transporter ATP-binding protein NodI; |
1266-1352 | 6.77e-06 | |||||||
nodulation factor ABC transporter ATP-binding protein NodI; Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.80 E-value: 6.77e-06
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| cbiO | PRK13636 | cobalt transporter ATP-binding subunit; Provisional |
1266-1363 | 6.92e-06 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.46 E-value: 6.92e-06
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| GlnQ | COG1126 | ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1244-1297 | 7.22e-06 | |||||||
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 48.84 E-value: 7.22e-06
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| PRK14239 | PRK14239 | phosphate transporter ATP-binding protein; Provisional |
1266-1353 | 7.49e-06 | |||||||
phosphate transporter ATP-binding protein; Provisional Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.00 E-value: 7.49e-06
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| potG | PRK11607 | putrescine ABC transporter ATP-binding subunit PotG; |
1266-1297 | 7.87e-06 | |||||||
putrescine ABC transporter ATP-binding subunit PotG; Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.83 E-value: 7.87e-06
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| ABC_6TM_Tm287_like | cd18548 | Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
170-433 | 8.67e-06 | |||||||
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 49.32 E-value: 8.67e-06
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| ABC_FtsE | cd03292 | Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1266-1341 | 8.97e-06 | |||||||
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 48.17 E-value: 8.97e-06
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| cbiO | PRK13643 | energy-coupling factor transporter ATPase; |
1266-1352 | 9.10e-06 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.96 E-value: 9.10e-06
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| cbiO | PRK13641 | energy-coupling factor transporter ATPase; |
1266-1363 | 9.41e-06 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 9.41e-06
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| PRK10247 | PRK10247 | putative ABC transporter ATP-binding protein YbbL; Provisional |
1260-1304 | 1.02e-05 | |||||||
putative ABC transporter ATP-binding protein YbbL; Provisional Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.17 E-value: 1.02e-05
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| ABC_Carb_Monos_II | cd03215 | Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1265-1341 | 1.09e-05 | |||||||
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter. Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 47.43 E-value: 1.09e-05
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| PRK11000 | PRK11000 | maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1264-1345 | 1.12e-05 | |||||||
maltose/maltodextrin ABC transporter ATP-binding protein MalK; Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 49.26 E-value: 1.12e-05
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| PRK15112 | PRK15112 | peptide ABC transporter ATP-binding protein SapF; |
1235-1344 | 1.39e-05 | |||||||
peptide ABC transporter ATP-binding protein SapF; Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.25 E-value: 1.39e-05
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| PRK15093 | PRK15093 | peptide ABC transporter ATP-binding protein SapD; |
1247-1351 | 1.42e-05 | |||||||
peptide ABC transporter ATP-binding protein SapD; Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 1.42e-05
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| ABC_cobalt_CbiO_domain2 | cd03226 | Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1266-1342 | 1.47e-05 | |||||||
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems. Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 47.64 E-value: 1.47e-05
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| cbiO | PRK13644 | energy-coupling factor transporter ATPase; |
1255-1345 | 1.49e-05 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.44 E-value: 1.49e-05
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| cbiO | PRK13632 | cobalt transporter ATP-binding subunit; Provisional |
1266-1345 | 1.52e-05 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.45 E-value: 1.52e-05
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| ABC_Mj1267_LivG_branched | cd03219 | ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1266-1345 | 1.86e-05 | |||||||
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 47.43 E-value: 1.86e-05
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| xylG | TIGR02633 | D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1266-1342 | 2.14e-05 | |||||||
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 48.67 E-value: 2.14e-05
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| cbiO | PRK13652 | cobalt transporter ATP-binding subunit; Provisional |
1266-1345 | 2.37e-05 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.88 E-value: 2.37e-05
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| PRK14243 | PRK14243 | phosphate transporter ATP-binding protein; Provisional |
1266-1322 | 2.49e-05 | |||||||
phosphate transporter ATP-binding protein; Provisional Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 2.49e-05
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| ABCG_PDR_domain1 | cd03233 | First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1266-1345 | 2.51e-05 | |||||||
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 46.87 E-value: 2.51e-05
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| PRK11831 | PRK11831 | phospholipid ABC transporter ATP-binding protein MlaF; |
1266-1353 | 2.52e-05 | |||||||
phospholipid ABC transporter ATP-binding protein MlaF; Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 2.52e-05
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| PRK09984 | PRK09984 | phosphonate ABC transporter ATP-binding protein; |
1266-1345 | 2.58e-05 | |||||||
phosphonate ABC transporter ATP-binding protein; Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 2.58e-05
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| PRK10575 | PRK10575 | Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1257-1359 | 4.25e-05 | |||||||
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.70 E-value: 4.25e-05
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| 3a01205 | TIGR00956 | Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1262-1349 | 4.56e-05 | |||||||
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 4.56e-05
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| ABCF_EF-3 | cd03221 | ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1266-1340 | 4.92e-05 | |||||||
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions. Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 44.75 E-value: 4.92e-05
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| PhnK | COG1101 | ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1262-1297 | 4.98e-05 | |||||||
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 46.62 E-value: 4.98e-05
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| ABC_6TM_YwjA_like | cd18549 | Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
268-429 | 6.71e-05 | |||||||
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 46.29 E-value: 6.71e-05
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| cbiO | PRK13638 | energy-coupling factor ABC transporter ATP-binding protein; |
1266-1345 | 7.12e-05 | |||||||
energy-coupling factor ABC transporter ATP-binding protein; Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.15 E-value: 7.12e-05
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| 3a01203 | TIGR00954 | Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1265-1323 | 7.50e-05 | |||||||
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.05 E-value: 7.50e-05
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| ABC_TM1139_LivF_branched | cd03224 | ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1266-1345 | 1.06e-04 | |||||||
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 45.12 E-value: 1.06e-04
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| PRK11160 | PRK11160 | cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
978-1075 | 1.17e-04 | |||||||
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.36 E-value: 1.17e-04
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| PRK13651 | PRK13651 | cobalt transporter ATP-binding subunit; Provisional |
1266-1345 | 1.36e-04 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.46 E-value: 1.36e-04
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| PRK10584 | PRK10584 | putative ABC transporter ATP-binding protein YbbA; Provisional |
1266-1343 | 1.36e-04 | |||||||
putative ABC transporter ATP-binding protein YbbA; Provisional Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.77 E-value: 1.36e-04
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| ABCG_White | cd03234 | White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1266-1311 | 1.36e-04 | |||||||
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners. Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 44.95 E-value: 1.36e-04
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| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
996-1080 | 1.53e-04 | |||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 43.41 E-value: 1.53e-04
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| CydC | TIGR02868 | thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1266-1322 | 1.59e-04 | |||||||
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 45.81 E-value: 1.59e-04
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| PRK11264 | PRK11264 | putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1251-1362 | 2.58e-04 | |||||||
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 44.36 E-value: 2.58e-04
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| LivF | COG0410 | ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1266-1354 | 3.31e-04 | |||||||
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism]; Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 43.82 E-value: 3.31e-04
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| ABC_6TM_CyaB_HlyB_like | cd18588 | Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
236-431 | 3.54e-04 | |||||||
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein). Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 44.03 E-value: 3.54e-04
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| znuC | PRK09544 | high-affinity zinc transporter ATPase; Reviewed |
1266-1327 | 3.65e-04 | |||||||
high-affinity zinc transporter ATPase; Reviewed Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.95 E-value: 3.65e-04
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| modC | PRK11144 | molybdenum ABC transporter ATP-binding protein ModC; |
1266-1345 | 4.28e-04 | |||||||
molybdenum ABC transporter ATP-binding protein ModC; Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 4.28e-04
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| GguA | NF040905 | sugar ABC transporter ATP-binding protein; |
1269-1343 | 4.49e-04 | |||||||
sugar ABC transporter ATP-binding protein; Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 4.49e-04
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| cbiO | PRK13646 | energy-coupling factor transporter ATPase; |
1266-1355 | 4.91e-04 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.61 E-value: 4.91e-04
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| ABC_KpsT_Wzt | cd03220 | ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1264-1345 | 5.34e-04 | |||||||
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2. Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 42.90 E-value: 5.34e-04
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| PRK10908 | PRK10908 | cell division ATP-binding protein FtsE; |
1244-1341 | 5.44e-04 | |||||||
cell division ATP-binding protein FtsE; Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.94 E-value: 5.44e-04
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| ugpC | PRK11650 | sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1266-1298 | 5.50e-04 | |||||||
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.06 E-value: 5.50e-04
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| cbiO | PRK13631 | cobalt transporter ATP-binding subunit; Provisional |
1266-1345 | 6.21e-04 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 43.69 E-value: 6.21e-04
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| met_CoM_red_A2 | TIGR03269 | methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1266-1345 | 6.95e-04 | |||||||
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis] Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 44.02 E-value: 6.95e-04
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| PRK10982 | PRK10982 | galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1266-1342 | 7.23e-04 | |||||||
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 7.23e-04
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| MglA | COG1129 | ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1266-1291 | 8.41e-04 | |||||||
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.47 E-value: 8.41e-04
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| ABC_6TM_CvaB_RaxB_like | cd18567 | Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
235-431 | 9.61e-04 | |||||||
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 42.83 E-value: 9.61e-04
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| COG4559 | COG4559 | ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1266-1352 | 9.85e-04 | |||||||
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 42.41 E-value: 9.85e-04
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| PRK10762 | PRK10762 | D-ribose transporter ATP binding protein; Provisional |
1266-1342 | 1.01e-03 | |||||||
D-ribose transporter ATP binding protein; Provisional Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 1.01e-03
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| NupO | COG3845 | ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1266-1344 | 1.14e-03 | |||||||
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism]; Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.09 E-value: 1.14e-03
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| PRK10535 | PRK10535 | macrolide ABC transporter ATP-binding protein/permease MacB; |
1266-1342 | 1.27e-03 | |||||||
macrolide ABC transporter ATP-binding protein/permease MacB; Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.17 E-value: 1.27e-03
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| ABC_6TM_ATM1_ABCB7 | cd18582 | Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
235-398 | 1.69e-03 | |||||||
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 42.10 E-value: 1.69e-03
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| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1228-1312 | 1.80e-03 | |||||||
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment. Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 1.80e-03
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| YbbA | COG4181 | Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1266-1343 | 1.84e-03 | |||||||
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 41.65 E-value: 1.84e-03
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| Uup | COG0488 | ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1266-1290 | 1.86e-03 | |||||||
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only]; Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 42.36 E-value: 1.86e-03
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| ABC_NatA_like | cd03267 | ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1266-1345 | 1.87e-03 | |||||||
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein. Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 41.55 E-value: 1.87e-03
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| ABC_6TM_exporter_like | cd18564 | Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
235-394 | 1.87e-03 | |||||||
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 42.11 E-value: 1.87e-03
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| PRK13540 | PRK13540 | cytochrome c biogenesis protein CcmA; Provisional |
1265-1332 | 2.13e-03 | |||||||
cytochrome c biogenesis protein CcmA; Provisional Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.09 E-value: 2.13e-03
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| PRK10575 | PRK10575 | Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
970-1062 | 2.30e-03 | |||||||
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 41.31 E-value: 2.30e-03
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| cbiO | PRK13645 | energy-coupling factor transporter ATPase; |
1266-1353 | 2.67e-03 | |||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.53 E-value: 2.67e-03
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| PRK13539 | PRK13539 | cytochrome c biogenesis protein CcmA; Provisional |
1266-1301 | 3.98e-03 | |||||||
cytochrome c biogenesis protein CcmA; Provisional Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 40.24 E-value: 3.98e-03
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| ABC_CcmA_heme_exporter | cd03231 | Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1266-1312 | 3.99e-03 | |||||||
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE. Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 40.17 E-value: 3.99e-03
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| 3a01204 | TIGR00955 | The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1264-1345 | 4.22e-03 | |||||||
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.57 E-value: 4.22e-03
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| ABC_6TM_MRP7_D2_like | cd18605 | Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
209-399 | 4.34e-03 | |||||||
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0). Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 40.98 E-value: 4.34e-03
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| ycf16 | CHL00131 | sulfate ABC transporter protein; Validated |
1260-1361 | 4.89e-03 | |||||||
sulfate ABC transporter protein; Validated Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 4.89e-03
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| lolD | PRK11629 | lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1266-1308 | 4.92e-03 | |||||||
lipoprotein-releasing ABC transporter ATP-binding protein LolD; Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.18 E-value: 4.92e-03
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| dppD | PRK11022 | dipeptide transporter ATP-binding subunit; Provisional |
1266-1345 | 5.00e-03 | |||||||
dipeptide transporter ATP-binding subunit; Provisional Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 5.00e-03
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| PRK10762 | PRK10762 | D-ribose transporter ATP binding protein; Provisional |
1266-1291 | 5.01e-03 | |||||||
D-ribose transporter ATP binding protein; Provisional Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 5.01e-03
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| cbiO | PRK13632 | cobalt transporter ATP-binding subunit; Provisional |
971-1059 | 5.04e-03 | |||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 40.36 E-value: 5.04e-03
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| PRK13538 | PRK13538 | cytochrome c biogenesis heme-transporting ATPase CcmA; |
1266-1299 | 5.11e-03 | |||||||
cytochrome c biogenesis heme-transporting ATPase CcmA; Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 39.79 E-value: 5.11e-03
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| sufC | PRK09580 | cysteine desulfurase ATPase component; Reviewed |
1267-1345 | 5.44e-03 | |||||||
cysteine desulfurase ATPase component; Reviewed Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 5.44e-03
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| ABC_6TM_exporter_like | cd18540 | Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
167-349 | 6.34e-03 | |||||||
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 40.16 E-value: 6.34e-03
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| ccmA | TIGR01189 | heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1266-1299 | 7.19e-03 | |||||||
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other] Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 39.26 E-value: 7.19e-03
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| PLN03211 | PLN03211 | ABC transporter G-25; Provisional |
1266-1327 | 7.72e-03 | |||||||
ABC transporter G-25; Provisional Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 40.63 E-value: 7.72e-03
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| PRK13549 | PRK13549 | xylose transporter ATP-binding subunit; Provisional |
1266-1291 | 9.17e-03 | |||||||
xylose transporter ATP-binding subunit; Provisional Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 9.17e-03
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| PRK15439 | PRK15439 | autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1271-1341 | 9.53e-03 | |||||||
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.03 E-value: 9.53e-03
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