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Conserved domains on  [gi|59896633|gb|AAX11685|]
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ATP-binding cassette sub-family B member 5 variant [Mus musculus]

Protein Classification

6TM ABC transporter family protein( domain architecture ID 1001189)

6TM ABC transporter family protein is a subunit of six transmembrane (6TM) 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ABC_6TM_exporters super family cl38913
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 1-134 1.03e-43

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 cd18578:

Pssm-ID: 365789 [Multi-domain]  Cd Length: 317  Bit Score: 145.29  E-value: 1.03e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   1 MSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEE 80
Cdd:cd18578 142 LVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEE 221

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 59896633  81 TLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGMFM 134
Cdd:cd18578 222 ALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFI 275
 
Name Accession Description Interval E-value
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 1-134 1.03e-43

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: 145.29  E-value: 1.03e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   1 MSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEE 80
Cdd:cd18578 142 LVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEE 221

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 59896633  81 TLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGMFM 134
Cdd:cd18578 222 ALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFI 275
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 5-127 1.53e-20

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: 83.85  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633     5 ILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQT 84
Cdd:pfam00664 133 IIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEE 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 59896633    85 QHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:pfam00664 213 ALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGEL 255
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
3-127 3.02e-08

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 50.55  E-value: 3.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   3 LSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETL 82
Cdd:COG1132 151 GALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREAN 230

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 59896633  83 QTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:COG1132 231 EELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL 275
 
Name Accession Description Interval E-value
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 1-134 1.03e-43

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: 145.29  E-value: 1.03e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   1 MSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEE 80
Cdd:cd18578 142 LVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEE 221

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 59896633  81 TLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGMFM 134
Cdd:cd18578 222 ALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFI 275
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
 5-127 8.73e-35

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: 122.39  E-value: 8.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   5 ILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQT 84
Cdd:cd18558 151 FIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEI 230

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 59896633  85 QHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18558 231 AKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEY 273
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 4-129 1.46e-25

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: 97.55  E-value: 1.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   4 SILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd18577 138 GFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE 217

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMP 129
Cdd:cd18577 218 KARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISP 263
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 5-127 1.53e-20

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: 83.85  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633     5 ILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQT 84
Cdd:pfam00664 133 IIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEE 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 59896633    85 QHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:pfam00664 213 ALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGEL 255
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 4-127 1.60e-15

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: 70.67  E-value: 1.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   4 SILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd18557 127 GLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALD 206

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18557 207 RSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 4-127 2.15e-09

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: 53.71  E-value: 2.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   4 SILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd07346 130 ALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANR 209

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd07346 210 DLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSL 253
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 4-127 2.07e-08

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: 50.98  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   4 SILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd18573 132 GIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVD 211

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18573 212 EVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGEL 255
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
3-127 3.02e-08

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 50.55  E-value: 3.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   3 LSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETL 82
Cdd:COG1132 151 GALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREAN 230

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 59896633  83 QTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:COG1132 231 EELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL 275
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 2-127 4.45e-08

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: 49.94  E-value: 4.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   2 SLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEET 81
Cdd:cd18780 131 IGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEK 210

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 59896633  82 LQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18780 211 INESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGEL 256
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 4-127 2.52e-07

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: 47.86  E-value: 2.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   4 SILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd18576 127 GVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALE 206

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18576 207 RVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGEL 250
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 4-130 6.78e-07

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: 46.77  E-value: 6.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   4 SILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd18572 127 GLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALD 206

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPE 130
Cdd:cd18572 207 KALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAG 253
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
 6-127 3.52e-06

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: 44.64  E-value: 3.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   6 LISFIYG--WEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd18590 127 MLGFMLSlsWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALE 206

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18590 207 RTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 4-127 5.89e-04

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: 38.06  E-value: 5.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   4 SILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQ 83
Cdd:cd18784 127 VIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLK 206

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 59896633  84 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18784 207 DTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 3-127 1.62e-03

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: 37.04  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633   3 LSILISFIY----GWEMTLLILSFAPVLAVTGMIQTAAMagfanrdKQALKRA-GKIA--TEAVEN----IRTVVSLTRE 71
Cdd:cd18549 128 ITIIGSFIIlltiNVPLTLIVFALLPLMIIFTIYFNKKM-------KKAFRRVrEKIGeiNAQLEDslsgIRVVKAFANE 200

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 59896633  72 rAFEQMYEETLQTQHRNALKRAH-ITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 127
Cdd:cd18549 201 -EYEIEKFDEGNDRFLESKKKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEI 256
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 13-129 2.89e-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: 36.34  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633  13 WEMTLLILSFAPVLAVtgmiqtaAMAGFANRDKQAL----KRAGKIAT---EAVENIRTVVSLTRERAFEQMYEETLQTQ 85
Cdd:cd18564 154 WQLALIALAVAPLLLL-------AARRFSRRIKEASreqrRREGALASvaqESLSAIRVVQAFGREEHEERRFARENRKS 226

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 59896633  86 HRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMP 129
Cdd:cd18564 227 LRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTP 270
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 13-103 5.56e-03

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: 35.52  E-value: 5.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59896633  13 WEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKR 92
Cdd:cd18589 136 PKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKE 215

                        90
                ....*....|.
gi 59896633  93 AhitgCCYAVS 103
Cdd:cd18589 216 A----AAYAVS 222
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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