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Conserved domains on  [gi|2514804612|ref|XP_056748682|]
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uncharacterized protein N7537_012341 [Penicillium hordei]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
1-229 6.82e-68

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) 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. All ABC transporters share a common architecture 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: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 211.98  E-value: 6.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQA 80
Cdd:cd18580    52 SVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  81 AVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLKT-----------GFLPDDFQKNAQLVNSS 149
Cdd:cd18580   132 IVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSEtlsglstirafGWQERFIEENLRLLDAS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 150 QRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAVRLHSST--AFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRLK 227
Cdd:cd18580   212 QRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSSIsaGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291

                  ..
gi 2514804612 228 SF 229
Cdd:cd18580   292 EY 293
 
Name Accession Description Interval E-value
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
1-229 6.82e-68

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) 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. All ABC transporters share a common architecture 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: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 211.98  E-value: 6.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQA 80
Cdd:cd18580    52 SVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  81 AVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLKT-----------GFLPDDFQKNAQLVNSS 149
Cdd:cd18580   132 IVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSEtlsglstirafGWQERFIEENLRLLDAS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 150 QRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAVRLHSST--AFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRLK 227
Cdd:cd18580   212 QRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSSIsaGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291

                  ..
gi 2514804612 228 SF 229
Cdd:cd18580   292 EY 293
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
19-265 7.31e-32

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: 123.90  E-value: 7.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   19 AGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAAVMLTSSAYLAISYPLLG 98
Cdd:TIGR00957 1036 ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLG 1115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   99 GFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLKTGFL----------PDDFQKNAQL-VNSSQRPAYLLPMIQEWLNLVL 167
Cdd:TIGR00957 1116 LLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLgvsvirafeeQERFIHQSDLkVDENQKAYYPSIVANRWLAVRL 1195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  168 NMIVMVIAVVMTSLAV--RLHSSTAFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRLKSFNESVTPEDREYEDIIP 245
Cdd:TIGR00957 1196 ECVGNCIVLFAALFAVisRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP 1275
                          250       260
                   ....*....|....*....|
gi 2514804612  246 GEEWPQHGTVELKGVSAKYK 265
Cdd:TIGR00957 1276 PSGWPPRGRVEFRNYCLRYR 1295
PLN03232 PLN03232
ABC transporter C family member; Provisional
2-265 1.28e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 67.69  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612    2 IALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAA 81
Cdd:PLN03232   964 VAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFA 1043
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   82 VMLT-SSAYLAISYPLLGGFlFLVQRFYMRTSRQLRLLDLETKSPLYFHLKTGF----------LPDDFQK-NAQLVNSS 149
Cdd:PLN03232  1044 LIGTvSTISLWAIMPLLILF-YAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALnglssiraykAYDRMAKiNGKSMDNN 1122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  150 QRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAV----RLHSSTAFA---GASLYSLMSFGDTLSGTVIFYTKLETSISA 222
Cdd:PLN03232  1123 IRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVlrngNAENQAGFAstmGLLLSYTLNITTLLSGVLRQASKAENSLNS 1202
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2514804612  223 ISRLKSFNESVTPEDREYEDIIPGEEWPQHGTVELKGVSAKYK 265
Cdd:PLN03232  1203 VERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYR 1245
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
1-130 2.82e-09

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: 56.50  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQA 80
Cdd:pfam00664  54 QFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGI 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2514804612  81 AVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL 130
Cdd:pfam00664 134 IVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVA 183
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-264 1.71e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 48.62  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLG-------TTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCV 73
Cdd:COG1132    67 LLGLALLRallsylqRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  74 FQSIGQAAVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL--------------KTGFLPDDF 139
Cdd:COG1132   147 VTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLqeslsgirvvkafgREERELERF 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 140 QKNAQLVNSSQRPAYllpMIQEWLNLVLNMIVMVIAVVMTSLAVRLHSSTAFAGASLYSLMSFGDTLSGTVI----FYTK 215
Cdd:COG1132   227 REANEELRRANLRAA---RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRqlanVLNQ 303
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2514804612 216 LETSISAISRLKSFnESVTPEDREYEDIIPGEewPQHGTVELKGVSAKY 264
Cdd:COG1132   304 LQRALASAERIFEL-LDEPPEIPDPPGAVPLP--PVRGEIEFENVSFSY 349
 
Name Accession Description Interval E-value
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
1-229 6.82e-68

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) 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. All ABC transporters share a common architecture 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: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 211.98  E-value: 6.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQA 80
Cdd:cd18580    52 SVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  81 AVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLKT-----------GFLPDDFQKNAQLVNSS 149
Cdd:cd18580   132 IVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSEtlsglstirafGWQERFIEENLRLLDAS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 150 QRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAVRLHSST--AFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRLK 227
Cdd:cd18580   212 QRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSSIsaGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291

                  ..
gi 2514804612 228 SF 229
Cdd:cd18580   292 EY 293
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
19-265 7.31e-32

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: 123.90  E-value: 7.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   19 AGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAAVMLTSSAYLAISYPLLG 98
Cdd:TIGR00957 1036 ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLG 1115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   99 GFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLKTGFL----------PDDFQKNAQL-VNSSQRPAYLLPMIQEWLNLVL 167
Cdd:TIGR00957 1116 LLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLgvsvirafeeQERFIHQSDLkVDENQKAYYPSIVANRWLAVRL 1195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  168 NMIVMVIAVVMTSLAV--RLHSSTAFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRLKSFNESVTPEDREYEDIIP 245
Cdd:TIGR00957 1196 ECVGNCIVLFAALFAVisRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP 1275
                          250       260
                   ....*....|....*....|
gi 2514804612  246 GEEWPQHGTVELKGVSAKYK 265
Cdd:TIGR00957 1276 PSGWPPRGRVEFRNYCLRYR 1295
ABC_6TM_MRP1_2_3_6_D2_like cd18603
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ...
4-227 5.80e-31

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) 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: 350047 [Multi-domain]  Cd Length: 296  Bit Score: 116.42  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   4 LFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGqaAVM 83
Cdd:cd18603    57 FVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVIS--TLV 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  84 LTSSA---YLAISYPlLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL--------------KTgflpDDF-QKNAQL 145
Cdd:cd18603   135 VISIStpiFLVVIIP-LAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFsetlqgastiraygVQ----ERFiRESDRR 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 146 VNSSQRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAV--RLHSSTAFAGASLYSLMSFGDTLSGTVIFYTKLETSISAI 223
Cdd:cd18603   210 VDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVlsRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSV 289

                  ....
gi 2514804612 224 SRLK 227
Cdd:cd18603   290 ERIK 293
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
2-226 1.40e-26

Six-transmembrane helical domain 2 (TMD2) 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: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 104.48  E-value: 1.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   2 IALFLLGTTLLIVSVkRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAA 81
Cdd:cd18606    50 IFLFLFGLLLAYLGI-RASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  82 VMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLK---TGfLP--------DDF-QKNAQLVNSS 149
Cdd:cd18606   129 LIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSeslSG-LStiraygaqDRFiKKNEKLIDNM 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2514804612 150 QRPAYLLPMIQEWLNLVLNMI--VMVIAVVMTSLAVRLHSSTAFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRL 226
Cdd:cd18606   208 NRAYFLTIANQRWLAIRLDLLgsLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERL 286
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
1-229 1.40e-24

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) 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: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 99.46  E-value: 1.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQA 80
Cdd:cd18604    56 SVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVIL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  81 AVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL--------------KTgflpDDF-QKNAQL 145
Cdd:cd18604   136 IAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFgetlaglvtirafgAE----ERFiEEMLRR 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 146 VNSSQRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAVRLHSSTA-FAGASLYSLMSFGDTLSGTVIFYTKLETSISAIS 224
Cdd:cd18604   212 IDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPGIDAgLAGFSLSFALGFSSAILWLVRSYNELELDMNSVE 291

                  ....*
gi 2514804612 225 RLKSF 229
Cdd:cd18604   292 RIQEY 296
ABC_6TM_SUR1_D2_like cd18602
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ...
2-226 3.18e-20

Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350046 [Multi-domain]  Cd Length: 307  Bit Score: 87.66  E-value: 3.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   2 IALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAA 81
Cdd:cd18602    64 VILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAII 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  82 VMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFH-------LKT--------GFlpddFQKNAQLV 146
Cdd:cd18602   144 VNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHfsetlggLTTirafrqqaRF----TQQMLELI 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 147 NSSQRPAYLLPMIQEWLNLVLNMI--VMVIAVVMTSLAVRLHS--STAFAGASL-YSLMSFGdTLSGTVIFYTKLETSIS 221
Cdd:cd18602   220 DRNNTAFLFLNTANRWLGIRLDYLgaVIVFLAALSSLTAALAGyiSPSLVGLAItYALLVPI-YLNWVVRNLADVEMQMN 298

                  ....*
gi 2514804612 222 AISRL 226
Cdd:cd18602   299 SVERV 303
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
18-229 3.65e-20

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: 87.59  E-value: 3.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  18 RAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELP---DALLNtqfCVFQSIGQAAVMLTSSAYLAISY 94
Cdd:cd18605    72 RAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPfilNILLA---QLFGLLGYLVVICYQLPWLLLLL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  95 PLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLK---TGF-------LPDDF-QKNAQLVNSSQRPAYLLPMIQEWL 163
Cdd:cd18605   149 LPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSetlKGLvtirafrKQERFlKEYLEKLENNQRAQLASQAASQWL 228
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2514804612 164 NLVLNMI--VMVIAVVMTSLAVRLHSSTAFAGA---SLYSLMSFGDTLSGTVIFYTKLETSISAISRLKSF 229
Cdd:cd18605   229 SIRLQLLgvLIVTFVALTAVVQHFFGLSIDAGLiglALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
ABC_6TM_MRP5_8_9_D2 cd18599
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ...
1-196 3.48e-19

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: 84.92  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLGTTLLIVSVK---RAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELP---DALLNTQFCVF 74
Cdd:cd18599    68 ILVILLLSLIRGFVFVKvtlRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPftlENFLQNVLLVV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  75 QSIGQAAVMLtssAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL--------------KTgflpDDFQ 140
Cdd:cd18599   148 FSLIIIAIVF---PWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLtatiqglstihafnKE----KEFL 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2514804612 141 KNAQ-LVNSSQRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAVRLHS--STAFAGASL 196
Cdd:cd18599   221 SKFKkLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGsiSPAFAGLAL 279
ABC_6TM_MRP4_D2_like cd18601
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ...
18-132 4.86e-13

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), 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: 350045 [Multi-domain]  Cd Length: 314  Bit Score: 67.73  E-value: 4.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  18 RAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAAVMLTSSAYLAI-SYPL 96
Cdd:cd18601    89 SASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIpVIPL 168
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2514804612  97 LGGFLFLvQRFYMRTSRQLRLLDLETKSPLYFHLKT 132
Cdd:cd18601   169 VILFLFL-RRYYLKTSREVKRIEGTTRSPVFSHLSS 203
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
10-264 1.16e-12

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: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   10 TLLIVSvkragANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAAVMLTSSAY 89
Cdd:TIGR01271  952 TLLTVS-----KRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPY 1026
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   90 LAI-SYPLLGGFLFLvQRFYMRTSRQLRLLDLETKSPLYFHLKTGFlpddfqKNAQLVNSSQRPAYLLPMIQEWLNL--- 165
Cdd:TIGR01271 1027 IFIaAIPVAVIFIML-RAYFLRTSQQLKQLESEARSPIFSHLITSL------KGLWTIRAFGRQSYFETLFHKALNLhta 1099
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  166 --------------VLNMIVMVIAVVMTSLAVRLHS-STAFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRLKSFN 230
Cdd:TIGR01271 1100 nwflylstlrwfqmRIDIIFVFFFIAVTFIAIGTNQdGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFI 1179
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2514804612  231 ESVTPEDREYEDIIPG--------------EEWPQHGTVELKGVSAKY 264
Cdd:TIGR01271 1180 DLPQEEPRPSGGGGKYqlstvlvienphaqKCWPSGGQMDVQGLTAKY 1227
PLN03232 PLN03232
ABC transporter C family member; Provisional
2-265 1.28e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 67.69  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612    2 IALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAA 81
Cdd:PLN03232   964 VAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFA 1043
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   82 VMLT-SSAYLAISYPLLGGFlFLVQRFYMRTSRQLRLLDLETKSPLYFHLKTGF----------LPDDFQK-NAQLVNSS 149
Cdd:PLN03232  1044 LIGTvSTISLWAIMPLLILF-YAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALnglssiraykAYDRMAKiNGKSMDNN 1122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  150 QRPAYLLPMIQEWLNLVLNMIVMVIAVVMTSLAV----RLHSSTAFA---GASLYSLMSFGDTLSGTVIFYTKLETSISA 222
Cdd:PLN03232  1123 IRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVlrngNAENQAGFAstmGLLLSYTLNITTLLSGVLRQASKAENSLNS 1202
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2514804612  223 ISRLKSFNESVTPEDREYEDIIPGEEWPQHGTVELKGVSAKYK 265
Cdd:PLN03232  1203 VERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYR 1245
ABC_6TM_CFTR_D2 cd18600
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ...
11-132 3.48e-10

Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) 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. All ABC transporters share a common architecture 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: 350044 [Multi-domain]  Cd Length: 324  Bit Score: 59.43  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  11 LLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAAVMLTSSAYL 90
Cdd:cd18600    93 PLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYI 172
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2514804612  91 AISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHLKT 132
Cdd:cd18600   173 FLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVT 214
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
1-130 2.82e-09

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: 56.50  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQA 80
Cdd:pfam00664  54 QFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGI 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2514804612  81 AVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL 130
Cdd:pfam00664 134 IVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVA 183
PTZ00243 PTZ00243
ABC transporter; Provisional
15-237 3.65e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 57.10  E-value: 3.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   15 SVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAAVMLTSSAYLAISY 94
Cdd:PTZ00243  1025 AMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVAL 1104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   95 PLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL--------------KTGFLPDDFQKNAQLVNSSqrpAYLLPMIQ 160
Cdd:PTZ00243  1105 VPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLeealqgsatitaygKAHLVMQEALRRLDVVYSC---SYLENVAN 1181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  161 EWLNLVL----NMIVMVIAV--VMTSLAVRLHSSTAFAGASLYSLMSFGDTLSGTVIFYTKLETSISAISRLKSFNESVT 234
Cdd:PTZ00243  1182 RWLGVRVeflsNIVVTVIALigVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVP 1261

                   ...
gi 2514804612  235 PED 237
Cdd:PTZ00243  1262 HED 1264
PLN03130 PLN03130
ABC transporter C family member; Provisional
6-265 3.70e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 57.06  E-value: 3.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612    6 LLGTTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELpdALLNTQFC--VFQSIGQAAVM 83
Cdd:PLN03130   971 LLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV--AVFVNMFLgqIFQLLSTFVLI 1048
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   84 -LTSSAYLAISYPLLGGFlFLVQRFYMRTSRQLRLLDLETKSPLYFH-------LKT-----------GFLPDDFQKNAQ 144
Cdd:PLN03130  1049 gIVSTISLWAIMPLLVLF-YGAYLYYQSTAREVKRLDSITRSPVYAQfgealngLSTiraykaydrmaEINGRSMDNNIR 1127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  145 --LVN-SSQRpayllpmiqeWLNLVLNMIVMVIAVVMTSLAV----RLHSSTAFA---GASLYSLMSFGDTLSGTVIFYT 214
Cdd:PLN03130  1128 ftLVNmSSNR----------WLAIRLETLGGLMIWLTASFAVmqngRAENQAAFAstmGLLLSYALNITSLLTAVLRLAS 1197
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2514804612  215 KLETSISAISRLKSFNESVTPEDREYEDIIPGEEWPQHGTVELKGVSAKYK 265
Cdd:PLN03130  1198 LAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYR 1248
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-264 1.71e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 48.62  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612   1 MIALFLLG-------TTLLIVSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCV 73
Cdd:COG1132    67 LLGLALLRallsylqRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  74 FQSIGQAAVMLTSSAYLAISYPLLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL--------------KTGFLPDDF 139
Cdd:COG1132   147 VTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLqeslsgirvvkafgREERELERF 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612 140 QKNAQLVNSSQRPAYllpMIQEWLNLVLNMIVMVIAVVMTSLAVRLHSSTAFAGASLYSLMSFGDTLSGTVI----FYTK 215
Cdd:COG1132   227 REANEELRRANLRAA---RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRqlanVLNQ 303
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2514804612 216 LETSISAISRLKSFnESVTPEDREYEDIIPGEewPQHGTVELKGVSAKY 264
Cdd:COG1132   304 LQRALASAERIFEL-LDEPPEIPDPPGAVPLP--PVRGEIEFENVSFSY 349
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
14-130 1.85e-04

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: 42.20  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514804612  14 VSVKRAGANLHQSILTTLIQAPLSFFTNTDTGIVTNLFSQDLNLIDTELPDALLNTQFCVFQSIGQAAVMLTSSAYLAIS 93
Cdd:cd18559    64 IGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG 143
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2514804612  94 YPlLGGFLFLVQRFYMRTSRQLRLLDLETKSPLYFHL 130
Cdd:cd18559   144 IP-LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLF 179
 
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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