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Conserved domains on  [gi|221042226|dbj|BAH12790|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MRP_assoc_pro super family cl33195
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 1-255 1.16e-68

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]


The actual alignment was detected with superfamily member TIGR00957:

Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 229.83  E-value: 1.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226     1 MSFAVFLIHTKRKKGVQSSGVLFGYWLLCFV---LPATNAAQQASGAGFQSDPVRHLSTYLCLSLVVAQFVLSCLADQPP 77
Cdd:TIGR00957  111 MLLATFLIQLERRKGVQSSGIMLTFWLVALVcalAILRSKILLALKEDAIVDPFRDTTFYIYFALVLSQLVLSCFSDKSP 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226    78 FFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARGHNKAIA 157
Cdd:TIGR00957  191 LFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAV 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226   158 F------KRKGGSGMEAPETEPFL--RQEGSQWRP-LLKAIWQVFHSTFLLGTLSLVISDVFRFTVPKLLSLFLEFIGDP 228
Cdd:TIGR00957  271 YgkkdpsKPKGSSQLDANEEVEALivKSPHKPRKPsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDP 350

                          250       260
                   ....*....|....*....|....*..
gi 221042226   229 KPPAWKGYLLAVLMFLSACLQTLFEQQ 255
Cdd:TIGR00957  351 MAPDWQGYFYTGLLFVCACLQTLILHQ 377
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 1-255 1.16e-68

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: 229.83  E-value: 1.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226     1 MSFAVFLIHTKRKKGVQSSGVLFGYWLLCFV---LPATNAAQQASGAGFQSDPVRHLSTYLCLSLVVAQFVLSCLADQPP 77
Cdd:TIGR00957  111 MLLATFLIQLERRKGVQSSGIMLTFWLVALVcalAILRSKILLALKEDAIVDPFRDTTFYIYFALVLSQLVLSCFSDKSP 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226    78 FFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARGHNKAIA 157
Cdd:TIGR00957  191 LFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAV 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226   158 F------KRKGGSGMEAPETEPFL--RQEGSQWRP-LLKAIWQVFHSTFLLGTLSLVISDVFRFTVPKLLSLFLEFIGDP 228
Cdd:TIGR00957  271 YgkkdpsKPKGSSQLDANEEVEALivKSPHKPRKPsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDP 350

                          250       260
                   ....*....|....*....|....*..
gi 221042226   229 KPPAWKGYLLAVLMFLSACLQTLFEQQ 255
Cdd:TIGR00957  351 MAPDWQGYFYTGLLFVCACLQTLILHQ 377
ABC_6TM_MRP1_2_3_6_D1_like cd18595
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ...
 199-263 6.81e-18

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, 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: 350039 [Multi-domain]  Cd Length: 290  Bit Score: 80.98  E-value: 6.81e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221042226 199 LGTLSLVISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVL 263
Cdd:cd18595    1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRL 65
PLN03232 PLN03232
ABC transporter C family member; Provisional
 83-260 2.30e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 72.70  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226   83 PQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRnrsaarghnkaiafkrkg 162
Cdd:PLN03232  221 RGGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTE------------------ 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226  163 gsgmEAPETEPFlrqegsqwrpLLKAIWQVFHSTFLLGTLSLVISDVFRFTVPKLLSLFLEFI--GDpkpPAWKGYLLAV 240
Cdd:PLN03232  283 ----ESRRPKPW----------LLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMqeGD---PAWVGYVYAF 345

                         170       180
                  ....*....|....*....|...
gi 221042226  241 LMFLSACLQTLFEQ---QNMYRL 260
Cdd:PLN03232  346 LIFFGVTFGVLCESqyfQNVGRV 368
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 1-255 1.16e-68

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: 229.83  E-value: 1.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226     1 MSFAVFLIHTKRKKGVQSSGVLFGYWLLCFV---LPATNAAQQASGAGFQSDPVRHLSTYLCLSLVVAQFVLSCLADQPP 77
Cdd:TIGR00957  111 MLLATFLIQLERRKGVQSSGIMLTFWLVALVcalAILRSKILLALKEDAIVDPFRDTTFYIYFALVLSQLVLSCFSDKSP 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226    78 FFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARGHNKAIA 157
Cdd:TIGR00957  191 LFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAV 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226   158 F------KRKGGSGMEAPETEPFL--RQEGSQWRP-LLKAIWQVFHSTFLLGTLSLVISDVFRFTVPKLLSLFLEFIGDP 228
Cdd:TIGR00957  271 YgkkdpsKPKGSSQLDANEEVEALivKSPHKPRKPsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDP 350

                          250       260
                   ....*....|....*....|....*..
gi 221042226   229 KPPAWKGYLLAVLMFLSACLQTLFEQQ 255
Cdd:TIGR00957  351 MAPDWQGYFYTGLLFVCACLQTLILHQ 377
ABC_6TM_MRP1_2_3_6_D1_like cd18595
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ...
 199-263 6.81e-18

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, 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: 350039 [Multi-domain]  Cd Length: 290  Bit Score: 80.98  E-value: 6.81e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221042226 199 LGTLSLVISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVL 263
Cdd:cd18595    1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRL 65
PLN03232 PLN03232
ABC transporter C family member; Provisional
 83-260 2.30e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 72.70  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226   83 PQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRnrsaarghnkaiafkrkg 162
Cdd:PLN03232  221 RGGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTE------------------ 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226  163 gsgmEAPETEPFlrqegsqwrpLLKAIWQVFHSTFLLGTLSLVISDVFRFTVPKLLSLFLEFI--GDpkpPAWKGYLLAV 240
Cdd:PLN03232  283 ----ESRRPKPW----------LLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMqeGD---PAWVGYVYAF 345

                         170       180
                  ....*....|....*....|...
gi 221042226  241 LMFLSACLQTLFEQ---QNMYRL 260
Cdd:PLN03232  346 LIFFGVTFGVLCESqyfQNVGRV 368
PLN03130 PLN03130
ABC transporter C family member; Provisional
 57-255 2.32e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 66.69  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226   57 YLCLSLVVAQFVLSCLA-----------DQPPFFPEDPQQS---------NPCPETGAAFPSKATFWWVSGLVWRGYRRP 116
Cdd:PLN03130  175 YLYISEVAAQVLFGILLlvyfpnldpypGYTPIGSESVDDYeyeelpggeQICPERHANIFSRIFFGWMTPLMQLGYKRP 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226  117 LRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARghnkaiafkrkggsgmeapetepflrqegsQWrpLLKAIWQVFHST 196
Cdd:PLN03130  255 LTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPK------------------------------PW--LLRALNNSLGGR 302

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221042226  197 FLLGTLSLVISDVFRFTVPKLLSLFLEFI--GDpkpPAWKGYLLAVLMFLSACLQTLFEQQ 255
Cdd:PLN03130  303 FWLGGFFKIGNDLSQFVGPLLLNLLLESMqnGE---PAWIGYIYAFSIFVGVVLGVLCEAQ 360
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
 199-263 3.17e-09

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 56.34  E-value: 3.17e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221042226 199 LGTLSLVISDVFRFTVPKLLSLFLEFIGD-PKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVL 263
Cdd:cd18579    1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRL 66
ABC_6TM_MRP7_D1_like cd18598
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ...
 198-262 3.31e-07

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) 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: 350042 [Multi-domain]  Cd Length: 288  Bit Score: 50.24  E-value: 3.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042226 198 LLGTLSLvISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFE-----QQNMYRLKV 262
Cdd:cd18598    1 PLGLLKL-LADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSshynfQMNKVSLKV 69
ABC_6TM_YOR1_D1_like cd18597
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ...
 199-259 1.25e-06

Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350041 [Multi-domain]  Cd Length: 293  Bit Score: 48.60  E-value: 1.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221042226 199 LGTLSLVISDVFRFTVPKLLSLFLEFI-----GDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYR 259
Cdd:cd18597    1 LAGLLKLLADVLQVLSPLLLKYLINFVedaylGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYR 66
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 90-160 1.38e-06

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: 49.14  E-value: 1.38e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221042226    90 PETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARGHNKAI-AFKR 160
Cdd:TIGR01271    5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKLLnALRR 76
ABC_6TM_VMR1_D1_like cd18596
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
 198-258 3.05e-04

Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350040 [Multi-domain]  Cd Length: 309  Bit Score: 41.33  E-value: 3.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221042226 198 LLGTLSLVISdVFRFTVPKLLSLFLEFIGDPKPPA-WKGYLLAVLMFLSACLQTLFEQQNMY 258
Cdd:cd18596    1 LQALLAVLSS-VLSFAPPFFLNRLLRYLEDPGEDAtVRPWVWVLLLFLGPLLSSLLDQQYLW 61
PTZ00243 PTZ00243
ABC transporter; Provisional
 183-250 3.30e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 38.61  E-value: 3.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221042226  183 RPLLKAIWQVFHSTFLLgtlsLVISDVFRFTVPKLLSLFLEFIGDPkPPAW-KGYLLAVLMFLSACLQT 250
Cdd:PTZ00243  236 RTLFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDAD-NATWgRGLGLVLTLFLTQLIQS 299
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
 212-258 3.61e-03

Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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.


Pssm-ID: 350003 [Multi-domain]  Cd Length: 290  Bit Score: 37.96  E-value: 3.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 221042226 212 FTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMY 258
Cdd:cd18559   14 FSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSM 60
 
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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