|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
186-830 |
7.73e-109 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 346.00 E-value: 7.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 186 SSLKDLFNILKKERKYLGFAMFCLIASSLGQMIFPMCISKIINMYGGKEEslkylTNEIYKTVLLIIGI----STFSFFR 261
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD-----LSALLLLLLLLLGLallrALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 262 IYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIH-LSFGIRNFISALIGGICALHISP 340
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 341 RnLFQSFLLPVSGCLLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKH 420
Cdd:COG1132 162 R-LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 421 SLVKSGNHFLFFSIISLFLLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKVLQIIKL 500
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 501 PDNNFhnywNKTSIDFLKSNNFSITFHNVSFSYDNTKDninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTI 580
Cdd:COG1132 321 PPEIP----DPPGAVPLPPVRGEIEFENVSFSYPGDRP--------------VLKDISLTIPPGETVALVGPSGSGKSTL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 581 LNLLTKKNDLNaSGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLMYpykayeemlkeqirlieqnqGafin 660
Cdd:COG1132 383 VNLLLRFYDPT-SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRY--------------------G---- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 661 minnentKKEKNDDDntintydseqdinkndmkntyeiytfllkelqkVQEEIKnnlssdkmkniynDLHIDEFLKNHFN 740
Cdd:COG1132 438 -------RPDATDEE---------------------------------VEEAAK-------------AAQAHEFIEALPD 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 741 -YDNMnVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDY 819
Cdd:COG1132 465 gYDTV-VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543
|
650
....*....|.
gi 124805679 820 IGVIEEGQIIQ 830
Cdd:COG1132 544 ILVLDDGRIVE 554
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
186-840 |
1.90e-80 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 274.02 E-value: 1.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 186 SSLKDLFNILKKERKYLGFAMFCLIASSLGQMIFPMCISKIINmyggkeeslKYLTNEIYKT-VLLIIGI-------STF 257
Cdd:COG2274 142 FGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVID---------RVLPNQDLSTlWVLAIGLllallfeGLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 258 SFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLsNDIEISSKFLIHLSF-GIRNFISALIGGICAL 336
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLtALLDLLFVLIFLIVLF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 337 HISPRnLFqsfLLPVSGCLLIGTTYAKFVKKISVLKQEKLSSCIDFAS---EKIHNISNVRLLNGESYEKKEFINYLEDV 413
Cdd:COG2274 292 FYSPP-LA---LVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLAKY 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 414 YKIGKKHSLVKSGNHFLFFSIISLFLLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSK 493
Cdd:COG2274 368 LNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALER 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 494 VLQIIKLPDNNFHNYwNKTSIDFLKSnnfSITFHNVSFSYDNTKDNInaninnernkkfaLKNVSFFLPHNKSVAIVGKS 573
Cdd:COG2274 448 LDDILDLPPEREEGR-SKLSLPRLKG---DIELENVSFRYPGDSPPV-------------LDNISLTIKPGERVAIVGRS 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 574 GSGKTTILNLLTKkndLNA--SGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENlmypykayeemlkeqIRLi 651
Cdd:COG2274 511 GSGKSTLLKLLLG---LYEptSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIREN---------------ITL- 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 652 eqnqgafinminnentkkekNDDDntintydseqdinkndmkntyeiytfllkelqkvqeeiknnLSSDKMKNIYNDLHI 731
Cdd:COG2274 572 --------------------GDPD-----------------------------------------ATDEEIIEAARLAGL 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 732 DEFLKNHFN-YDnMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHR 810
Cdd:COG2274 591 HDFIEALPMgYD-TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHR 669
|
650 660 670
....*....|....*....|....*....|
gi 124805679 811 LDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:COG2274 670 LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
188-841 |
9.70e-70 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 244.63 E-value: 9.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 188 LKDLFNILKKERKYLGFAMFCLIASSLGQMIFPMCISKIINMYGGKEeSLKYLTNEIYKTVLLIIGISTFSFFRIYFIET 267
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDK-GPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 268 SIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFL-IHLSFGIRNFISALIGGICALHISPRNLFQS 346
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLsLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 347 FL-LPVSgcLLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKS 425
Cdd:TIGR00958 308 LInLPLV--FLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 426 GNhFLFFSIISLFLLHLI-YYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKVLQII----KL 500
Cdd:TIGR00958 386 GY-LWTTSVLGMLIQVLVlYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdrkpNI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 501 PDNNFHNYwnktsiDFLKSNnfsITFHNVSFSYDNtkdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTI 580
Cdd:TIGR00958 465 PLTGTLAP------LNLEGL---IEFQDVSFSYPN------------RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 581 LNLLTKKNDLNAsGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLMYPYKAYEemlKEQIRlieqnqgafin 660
Cdd:TIGR00958 524 AALLQNLYQPTG-GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP---DEEIM----------- 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 661 minneNTKKEKNDDDNTINtydseqdinkndMKNTYeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfn 740
Cdd:TIGR00958 589 -----AAAKAANAHDFIME------------FPNGY-------------------------------------------- 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 741 ydNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAliKYMKDKTTIIFTHRLDLLNYVDYI 820
Cdd:TIGR00958 608 --DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQI 683
|
650 660
....*....|....*....|.
gi 124805679 821 GVIEEGQIIQFDKRQSVLQKP 841
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
205-494 |
2.55e-61 |
|
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: 209.34 E-value: 2.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINmYGGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFFEKV 284
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLID-TIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 285 LNQDVHFFNKQKTGELINRLSNDIE-ISSKFLIHLSFGIRNFIsALIGGICAL-HISPRnLFQSFLLPVSGCLLIGTTYA 362
Cdd:cd18557 80 LRQEIAFFDKHKTGELTSRLSSDTSvLQSAVTDNLSQLLRNIL-QVIGGLIILfILSWK-LTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 363 KFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSgnhfLFFSIISLF---- 438
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANA----LFQGITSLLiyls 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 439 LLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18557 234 LLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
205-494 |
2.29e-60 |
|
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: 206.98 E-value: 2.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYLTNEIYKTVLLIIGI----STFSFFRIYFIETSIEKITRRLRTHF 280
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVfvvgAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 281 FEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIH-LSFGIRNFISALIGGICALHISPRNLFQSFLL--PVSgclLI 357
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQnLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVvpPIA---VG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 358 GTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSgnhfLFFSIISL 437
Cdd:cd18573 158 AVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASG----LFFGSTGF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124805679 438 F----LLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18573 234 SgnlsLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
188-840 |
3.26e-60 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 214.95 E-value: 3.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 188 LKDLFNILKKERKYLGFAMFCLIASSLGQMIFPMCISKIINmYGGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIET 267
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMID-HGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 268 SIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIE-ISSKFLIHLSFGIRNFISaLIGGICALHISPRNLFQS 346
Cdd:TIGR02204 85 LGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTlLQSVIGSSLSMALRNALM-CIGGLIMMFITSPKLTSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 347 FLLPVSGCLLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKK----HSL 422
Cdd:TIGR02204 164 VLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQrirtRAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 423 VKSGNHFLFFSIISLFLlhliYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKVLQI----- 497
Cdd:TIGR02204 244 LTAIVIVLVFGAIVGVL----WVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELlqaep 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 498 -IKLPdnnfhnywnKTSIDFLKSNNFSITFHNVSFSYDntkdninaninnERNKKFALKNVSFFLPHNKSVAIVGKSGSG 576
Cdd:TIGR02204 320 dIKAP---------AHPKTLPVPLRGEIEFEQVNFAYP------------ARPDQPALDGLNLTVRPGETVALVGPSGAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 577 KTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLMY--PyKAYEEMLKEQIRLIEQN 654
Cdd:TIGR02204 379 KSTLFQLLLRFYD-PQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYgrP-DATDEEVEAAARAAHAH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 655 QgaFINMINNentkkekndddntinTYDSEqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhidef 734
Cdd:TIGR02204 457 E--FISALPE---------------GYDTY-------------------------------------------------- 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 735 lknhfnydnmnVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLL 814
Cdd:TIGR02204 470 -----------LGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
650 660
....*....|....*....|....*.
gi 124805679 815 NYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
524-827 |
9.16e-51 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 175.65 E-value: 9.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPI 603
Cdd:cd03228 1 IEFKNVSFSYPG-------------RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-SGEILIDGVDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLmypykayeemlkeqirlieqnqgafinminnentkkekndddntintyds 683
Cdd:cd03228 67 RDLDLESLRKNIAYVPQDPFLFSGTIRENI-------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 684 eqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYL 763
Cdd:cd03228 97 ---------------------------------------------------------------------LSGGQRQRIAI 107
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 764 AQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQ 827
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
524-830 |
1.61e-49 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 174.65 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNInaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPI 603
Cdd:cd03249 1 IEFKNVSFRYPSRPDVP------------ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT-SGEILLDGVDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLMY-PYKAYEEMLKEQIRLieqnqgafinminnentkkekndddntintyd 682
Cdd:cd03249 68 RDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYgKPDATDEEVEEAAKK-------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 683 seqdinkndmkntYEIYTFLLKELQKvqeeiknnlssdkmkniyndlhideflknhfnYDNMnVGVNGTSLSGGQKQRIY 762
Cdd:cd03249 116 -------------ANIHDFIMSLPDG--------------------------------YDTL-VGERGSQLSGGQKQRIA 149
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 763 LAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
237-830 |
2.26e-48 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 181.07 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 237 LKYLTNE---------IYKTVLLIIGISTF----SFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINR 303
Cdd:TIGR02203 37 LKPLLDDgfggrdrsvLWWVPLVVIGLAVLrgicSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 304 LSNDIEISSKFLIH-LSFGIRNFISALIGGICALHISPR-NLFQSFLLPVSGclLIGTTYAKFVKKISVLKQEKLSSCID 381
Cdd:TIGR02203 117 ITFDSEQVASAATDaFIVLVRETLTVIGLFIVLLYYSWQlTLIVVVMLPVLS--ILMRRVSKRLRRISKEIQNSMGQVTT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 382 FASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLFFSIISLFLLHLIYYGNYLIAHKFINTGDLF 461
Cdd:TIGR02203 195 VAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 462 SLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKVLQIIKLPDNNfhnywnKTSIDFLKSNNFSITFHNVSFSYDNTkdnin 541
Cdd:TIGR02203 275 AFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK------DTGTRAIERARGDVEFRNVTFRYPGR----- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 542 aninnERNkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKINSAVLRSIVGVITQD 621
Cdd:TIGR02203 344 -----DRP---ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD-SGQILLDGHDLADYTLASLRRQVALVSQD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 622 PFLFNLTVRENLmyPYKAYEEMLKEQIRlieqnqgafinminnentkkekndddntintyDSEQDINKNDMKNtyeiytf 701
Cdd:TIGR02203 415 VVLFNDTIANNI--AYGRTEQADRAEIE--------------------------------RALAAAYAQDFVD------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 llkelqkvqeeiknnlssdkmkNIYNDLHideflknhfnydnMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:TIGR02203 454 ----------------------KLPLGLD-------------TPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 124805679 782 SLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
519-840 |
1.16e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 178.80 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 519 SNNFSITFHNVSFSYDNTKdninaninnernkkFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICV 598
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGR--------------PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-PYSGSILI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 GNVPINKINSAVLRSIVGVITQDPFLFNLTVRENlmypykayeemlkeqIRLieQNQGAfinminnentkkekndddnti 678
Cdd:COG4988 397 NGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREN---------------LRL--GRPDA--------------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 679 ntydSEQDinkndmkntyeiytfLLKELQKVqeeiknnlssdkmkniyndlHIDEFLKNHFN-YDnMNVGVNGTSLSGGQ 757
Cdd:COG4988 439 ----SDEE---------------LEAALEAA--------------------GLDEFVAALPDgLD-TPLGEGGRGLSGGQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 758 KQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSV 837
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558
|
...
gi 124805679 838 LQK 840
Cdd:COG4988 559 LAK 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
524-840 |
2.09e-47 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 168.56 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnernKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPI 603
Cdd:cd03254 3 IEFENVNFSYDE--------------KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-PQKGQILIDGIDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENlmypykayeemlkeqirlieqnqgafINMINNENTKKEkndddntintyds 683
Cdd:cd03254 68 RDISRKSLRSMIGVVLQDTFLFSGTIMEN--------------------------IRLGRPNATDEE------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 684 eqdinkndmkntyeiytfllkelqkVQEEIKnnlssdkmkniynDLHIDEFLKNHFNYDNMNVGVNGTSLSGGQKQRIYL 763
Cdd:cd03254 109 -------------------------VIEAAK-------------EAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAI 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 764 AQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
524-830 |
4.69e-46 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 164.71 E-value: 4.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNInaninnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPI 603
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV-------------LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV-DSGRILIDGHDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLMYpykAYEEMLKEQIRLIEQNQGA--FInminnentkkeknddDNTINTY 681
Cdd:cd03251 67 RDYTLASLRRQIGLVSQDVFLFNDTVAENIAY---GRPGATREEVEEAARAANAheFI---------------MELPEGY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 682 DSeqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmNVGVNGTSLSGGQKQRI 761
Cdd:cd03251 129 DT-------------------------------------------------------------VIGERGVKLSGGQRQRI 147
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 762 YLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
271-841 |
1.49e-45 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 172.64 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 271 KITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHLsfgIRNFISALIGGICALhisprnLFQSFLLP 350
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRV---LLPLLVALLVILAAV------AFLAFFSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 351 VSGCLLIGT--------------TYAKFVKKISVLKQEKLSSCIDFasekIHNISNVRLLNG-ESYEKKefINYLEDVY- 414
Cdd:COG4987 156 ALALVLALGlllaglllpllaarLGRRAGRRLAAARAALRARLTDL----LQGAAELAAYGAlDRALAR--LDAAEARLa 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 415 KIGKKHSLVKSGNHFLFFSIISLFLLHLIYYGNYLIAHKFINTGDL--FSLIMYSLFcgSGIQGMMHAIGDIQKCLGSCS 492
Cdd:COG4987 230 AAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLalLVLAALALF--EALAPLPAAAQHLGRVRAAAR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 493 KVLQIIKLPDNNFHNYWNKTSidflkSNNFSITFHNVSFSYDNTKDNinaninnernkkfALKNVSFFLPHNKSVAIVGK 572
Cdd:COG4987 308 RLNELLDAPPAVTEPAEPAPA-----PGGPSLELEDVSFRYPGAGRP-------------VLDGLSLTLPPGERVAIVGP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 573 SGSGKTTILNLLTKknDLNA-SGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLmypykayeemlkeqiRLI 651
Cdd:COG4987 370 SGSGKSTLLALLLR--FLDPqSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENL---------------RLA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 652 eqNQGAfinminnentkkekNDDDntintydseqdinkndmkntyeiytfLLKELQKVQeeiknnlssdkmkniyndlhI 731
Cdd:COG4987 433 --RPDA--------------TDEE--------------------------LWAALERVG--------------------L 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 732 DEFLKNHFN-YDNMnVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHR 810
Cdd:COG4987 451 GDWLAALPDgLDTW-LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
570 580 590
....*....|....*....|....*....|.
gi 124805679 811 LDLLNYVDYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
248-830 |
3.89e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 162.88 E-value: 3.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 248 VLLII--GIStfSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEI----SSKFLIHLsfg 321
Cdd:PRK11176 72 IGLMIlrGIT--SFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQvassSSGALITV--- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 322 IRNfiSALIGGICALHISprNLFQ-SFLL----PVSGcLLIGTTYAKFvKKISVLKQEKLSSCIDFASEKIHNISNVRLL 396
Cdd:PRK11176 147 VRE--GASIIGLFIMMFY--YSWQlSLILiviaPIVS-IAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLIF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 397 NGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLFFSIISLFLLHLIYYGNyliahkfintgdlFSLIMYSLFCG----- 471
Cdd:PRK11176 221 GGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAAS-------------FPSVMDTLTAGtitvv 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 472 -SGIQGMMHAI-------GDIQKCLGSCSKVLQIIKLP---DNNfhnywnKTSIDFLKSNnfsITFHNVSFSYDnTKDNI 540
Cdd:PRK11176 288 fSSMIALMRPLksltnvnAQFQRGMAACQTLFAILDLEqekDEG------KRVIERAKGD---IEFRNVTFTYP-GKEVP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 541 naninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKINSAVLRSIVGVITQ 620
Cdd:PRK11176 358 ------------ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-EGEILLDGHDLRDYTLASLRNQVALVSQ 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 621 DPFLFNLTVRENLMYPYKayeemlkeqirlieqnqgafinminnentkkekndddntiNTYDSEQDINKNDMKNTYEiyt 700
Cdd:PRK11176 425 NVHLFNDTIANNIAYART----------------------------------------EQYSREQIEEAARMAYAMD--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 701 FLlkelqkvqeeiknnlssDKMKNiyndlhideflknhfNYDNMnVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPT 780
Cdd:PRK11176 462 FI-----------------NKMDN---------------GLDTV-IGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 124805679 781 SSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
205-494 |
6.57e-42 |
|
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: 155.10 E-value: 6.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIIN-----MYGGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIETSIEKITRRLRTH 279
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDavtnhSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 280 FFEKVLNQDVHFFNKQKTGELINRLSNDIE-ISSKFLIHLSFGIRNFISALIGGICALHISPRnlFQSFLLPVSGCLLIG 358
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQvLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWK--LTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 359 TT-YAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSG-NHFLFFsIIS 436
Cdd:cd18780 159 AViYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGfNGFMGA-AAQ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 437 LFLLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18780 238 LAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
202-494 |
1.55e-40 |
|
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: 151.47 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIIN---MYGGKEESLKYLTNEIYKTVL--LIIGISTF--SFFRIYFIETSIEKITR 274
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDaftDFGSGESSPDEFLDDVNKYALyfVYLGIGSFvlSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 275 RLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIE-----ISSKflihLSFGIRNFISALIGGICALHISPR-NLFQSFL 348
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNliqdgIGEK----LGLLIQSLSTFIAGFIIAFIYSWKlTLVLLAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 349 LPVsgCLLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNH 428
Cdd:cd18577 157 LPL--IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 429 -FLFFSIISLFLLhLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18577 235 gLLFFIIFAMYAL-AFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
523-832 |
2.83e-40 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 148.03 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYdntkdninaninnERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVP 602
Cdd:cd03244 2 DIEFKNVSLRY-------------RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-SSGSILIDGVD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPFLFNLTVRENLMyPYKAYEEmlkeqirlieqnqgafinminnentkkekndddntintyd 682
Cdd:cd03244 68 ISKIGLHDLRSRISIIPQDPVLFSGTIRSNLD-PFGEYSD---------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 683 seqdinkndmkntyeiytfllkelqkvqEEIKNNLSsdkmkniynDLHIDEFLKNHFNYDNMNVGVNGTSLSGGQKQRIY 762
Cdd:cd03244 107 ----------------------------EELWQALE---------RVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLC 149
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124805679 763 LAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLD-LLNYvDYIGVIEEGQIIQFD 832
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDtIIDS-DRILVLDKGRVVEFD 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
523-829 |
4.44e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 147.35 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTKDNinaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVP 602
Cdd:cd03245 2 RIEFRNVSFSYPNQEIP-------------ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK-PTSGSVLLDGTD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPFLFNLTVRENLM--YPYkAYEEMLKEQIRLIeqnqGafinminnentkkekndddntint 680
Cdd:cd03245 68 IRQLDPADLRRNIGYVPQDVTLFYGTLRDNITlgAPL-ADDERILRAAELA----G------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhIDEFLKNHFNYDNMNVGVNGTSLSGGQKQR 760
Cdd:cd03245 119 --------------------------------------------------VTDFVNKHPNGLDLQIGERGRGLSGGQRQA 148
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQII 829
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
524-830 |
1.26e-39 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 146.61 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnernKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPI 603
Cdd:cd03253 1 IEFENVTFAYDP--------------GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-SGSILIDGQDI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLMYpykayeemlkeqirlieqnqgafinmiNNENTKKEkndddntintyds 683
Cdd:cd03253 66 REVTLDSLRRAIGVVPQDTVLFNDTIGYNIRY---------------------------GRPDATDE------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 684 eqdinkndmkntyEIYtfllkELQKVQeeiknnlssdkmkniyndlHIDEFLKN-HFNYDNMnVGVNGTSLSGGQKQRIY 762
Cdd:cd03253 106 -------------EVI-----EAAKAA-------------------QIHDKIMRfPDGYDTI-VGERGLKLSGGEKQRVA 147
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 763 LAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
205-490 |
3.66e-39 |
|
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: 146.86 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINmyGGKEESLKYLTNEIyktVLLIIGI----STFSFFRIYFIETSIEKITRRLRTHF 280
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLID--AALGGGDTASLNQI---ALLLLGLfllqAVFSFFRIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 281 FEKVLNQDVHFFNKQKTGELINRLSNDIE-ISSKFLIHLSFGIRNFISaLIGGICAL-HISPR-NLFQSFLLPVsgCLLI 357
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTqIQDTLTTTLAEFLRQILT-LIGGVVLLfFISWKlTLLMLATVPV--VVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 358 GTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSgnhfLFFSIISL 437
Cdd:cd18576 153 AVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRA----LFSSFIIF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 438 FL----LHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGS 490
Cdd:cd18576 229 LLfgaiVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGA 285
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
523-840 |
3.19e-38 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 152.71 E-value: 3.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNtkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNAsGEICVGNVP 602
Cdd:TIGR03375 463 EIEFRNVSFAYPG-------------QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTE-GSVLLDGVD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPFLFNLTVRENLMY--PYkAYEEMLKEQIRLIeqnqGafinminnentkkekndddntint 680
Cdd:TIGR03375 529 IRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALgaPY-ADDEEILRAAELA----G------------------------ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhIDEFLKNHFNYDNMNVGVNGTSLSGGQKQR 760
Cdd:TIGR03375 580 --------------------------------------------------VTEFVRRHPDGLDMQIGERGRSLSGGQRQA 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
486-840 |
1.79e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 145.74 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 486 KCLGSCSKVLQIIKL-PDNNFhnywNKTSIdfLKSNNFSITFHNVSFSYDNTKDNinaninnernkkfALKNVSFFLPHN 564
Cdd:PRK11160 306 QVIASARRINEITEQkPEVTF----PTTST--AAADQVSLTLNNVSFTYPDQPQP-------------VLKGLSLQIKAG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 565 KSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLmypykayeeml 644
Cdd:PRK11160 367 EKVALLGRTGCGKSTLLQLLTRAWDPQ-QGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNL----------- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 645 keqirLIeqnqgafinminnenTKKEKNDddntintydsEQdinkndmkntyeiytfLLKELQKVqeEIKNNLSSDKMKN 724
Cdd:PRK11160 435 -----LL---------------AAPNASD----------EA----------------LIEVLQQV--GLEKLLEDDKGLN 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 725 IYndlhideflknhfnydnmnVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTT 804
Cdd:PRK11160 467 AW-------------------LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV 527
|
330 340 350
....*....|....*....|....*....|....*.
gi 124805679 805 IIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:PRK11160 528 LMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
205-494 |
1.92e-36 |
|
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: 139.22 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYLTNEIYktvLLIIGI--STFSFFRIYFIETSIEKITRRLRTHFFE 282
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLL---LLLLSVlsGLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 283 KVLNQDVHFFNKQKTGELINRLSNDI-EISSKFLIHLSFGIRNFISaLIGGIC-ALHISPR-NLFQSFLLPVSGclLIGT 359
Cdd:cd18572 78 SLLRQDIAFFDATKTGELTSRLTSDCqKVSDPLSTNLNVFLRNLVQ-LVGGLAfMFSLSWRlTLLAFITVPVIA--LITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 360 TYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLFFSIISLFL 439
Cdd:cd18572 155 VYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 440 LHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18572 235 VLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
205-489 |
1.92e-35 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 136.46 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINmYGGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIeTSI-EKITRRLRTHFFEK 283
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLID-QGFAAGNTALLNRAFLLLLAVALVLALASALRFYLV-SWLgERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 284 VLNQDVHFFNKQKTGELINRLSNDIEI------SSkflihLSFGIRNFISALIGGICALHISPRNLFQSFL-LPVSgcLL 356
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLiqtvvgSS-----LSIALRNLLLLIGGLVMLFITSPKLTLLVLLvIPLV--VL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 357 IGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSgnhFLFFSIIS 436
Cdd:cd18575 152 PIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARA---LLTALVIF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 437 LFLLHL---IYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLG 489
Cdd:cd18575 229 LVFGAIvfvLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAG 284
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
517-829 |
8.50e-34 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 138.03 E-value: 8.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 517 LKSNNFSITFHNVSFSYDNtkdninaninnERNkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEI 596
Cdd:COG5265 351 LVVGGGEVRFENVSFGYDP-----------ERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT-SGRI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLMY--PyKAYEEMLKEQIRLieqnqgAfinminnentkkekndd 674
Cdd:COG5265 416 LIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYgrP-DASEEEVEAAARA------A----------------- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 675 dntintydseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlHIDEF---LKNhfNYDNMnVGVNGT 751
Cdd:COG5265 472 -------------------------------------------------------QIHDFiesLPD--GYDTR-VGERGL 493
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQII 829
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
199-823 |
1.79e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 139.39 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 199 RKYLGFAMFCLIASSlGQMIFPMCISKII--NMYGGKEeslkylTNEIYKTvLLIIGISTF--SFFRIYFIETSIEKITR 274
Cdd:PTZ00265 59 RKLLGVSFVCATISG-GTLPFFVSVFGVImkNMNLGEN------VNDIIFS-LVLIGIFQFilSFISSFCMDVVTTKILK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 275 RLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIE-----ISSKFLIhlsfgIRNFISALIG-GICALHISPR-NLFQSF 347
Cdd:PTZ00265 131 TLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEqvnagIGTKFIT-----IFTYASAFLGlYIWSLFKNARlTLCITC 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 348 LLP-VSGCLLIGTTYAKFVKKISVLKQEKLSSCIDfasEKIHNISNVRLLNGESYEKKEFiNYLEDVYKigkKHSLVKSG 426
Cdd:PTZ00265 206 VFPlIYICGVICNKKVKINKKTSLLYNNNTMSIIE---EALVGIRTVVSYCGEKTILKKF-NLSEKLYS---KYILKANF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 427 NHFLFFSIISLFLLHL----IYYGNYLIAHKFINT--------GDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:PTZ00265 279 MESLHIGMINGFILASyafgFWYGTRIIISDLSNQqpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 495 LQIIKLPDNNFHNYWNKTSIDFLKsnnfsITFHNVSFSYDNTKDninANInnernkkfaLKNVSFFLPHNKSVAIVGKSG 574
Cdd:PTZ00265 359 YEIINRKPLVENNDDGKKLKDIKK-----IQFKNVRFHYDTRKD---VEI---------YKDLNFTLTEGKTYAFVGESG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 575 SGKTTILNLLTKKNDLNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLMYPYKAYE--EMLKEQIrlie 652
Cdd:PTZ00265 422 CGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKdlEALSNYY---- 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 653 qnqgafinminNENTKKEKnDDDNTINTYDSEQDINKNDMKNTYEIYTFLlkELQKVQEEIKNNlssdKMKNIYNDLHID 732
Cdd:PTZ00265 498 -----------NEDGNDSQ-ENKNKRNSCRAKCAGDLNDMSNTTDSNELI--EMRKNYQTIKDS----EVVDVSKKVLIH 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 733 EFLKNHFNYDNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAL--IKYMKDKTTIIFTHR 810
Cdd:PTZ00265 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHR 639
|
650
....*....|...
gi 124805679 811 LDLLNYVDYIGVI 823
Cdd:PTZ00265 640 LSTIRYANTIFVL 652
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
551-830 |
6.30e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 134.97 E-value: 6.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 551 KFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkkNDLNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVR 630
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL--GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 631 ENLmypykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfLLKELQKVQ 710
Cdd:PRK11174 441 DNV--------------------------------------------------------------------LLGNPDASD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 711 EEIKNNLssdkmkniyNDLHIDEFLKNHFNYDNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENI 790
Cdd:PRK11174 453 EQLQQAL---------ENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124805679 791 INKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:PRK11174 524 VMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
524-832 |
1.74e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 133.93 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnernKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPI 603
Cdd:PRK13657 335 VEFDDVSFSYDN--------------SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD-PQSGRILIDGTDI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLMY--PYKAYEEMLkeqiRLIEQNQGA-FInminnentkkEKNDDdntint 680
Cdd:PRK13657 400 RTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVgrPDATDEEMR----AAAERAQAHdFI----------ERKPD------ 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfNYDNMnVGVNGTSLSGGQKQR 760
Cdd:PRK13657 460 -----------------------------------------------------------GYDTV-VGERGRQLSGGERQR 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ---FD 832
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFD 554
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
526-827 |
2.75e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 121.81 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 526 FHNVSFSYDNTKdninaninnernkKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDLNA--SGEICVGNVPI 603
Cdd:cd03225 2 LKNLSFSYPDGA-------------RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLL---NGLLGptSGEVLVDGKDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPF--LFNLTVRE-------NLMYPykaYEEMLKEQIRLIEQnqgafinminnentkkekndd 674
Cdd:cd03225 66 TKLSLKELRRKVGLVFQNPDdqFFGPTVEEevafgleNLGLP---EEEIEERVEEALEL--------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 675 dntintydseqdinkndmkntyeiytFLLKELQKvqeeiknnlssdkmKNIYndlhideflknhfnydnmnvgvngtSLS 754
Cdd:cd03225 122 --------------------------VGLEGLRD--------------RSPF-------------------------TLS 136
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 755 GGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLL-NYVDYIGVIEEGQ 827
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIvTHDLDLLlELADRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
524-829 |
5.16e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 119.73 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKknDLNA-SGEICVGNVP 602
Cdd:cd03247 1 LSINNVSFSYPE-------------QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPqQGEITLDGVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAvLRSIVGVITQDPFLFNLTVRENLmypykayeemlkeqirlieqnqgafinminnentkkekndddntintyd 682
Cdd:cd03247 66 VSDLEKA-LSSLISVLNQRPYLFDTTLRNNL------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 683 seqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgvnGTSLSGGQKQRIY 762
Cdd:cd03247 96 -------------------------------------------------------------------GRRFSGGERQRLA 108
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 763 LAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQII 829
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
192-501 |
1.04e-30 |
|
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: 123.33 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 192 FNILKKERKYLGFAMFCLIASSLGQMIFPMCISKIINMYGgkEESLKYLTNEIYKTVL--LIIGISTF--SFFRIYFIET 267
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFS--LPDDDELRSEANFWALmfLVLAIVAGiaYFLQGYLFGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 268 SIEKITRRLRTHFFEKVLNQDVHFFNKQK--TGELINRLSNDIE----ISSKFlihLSFGIRNFISALIGGICALHISPR 341
Cdd:cd18578 79 AGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASdvrgLVGDR---LGLILQAIVTLVAGLIIAFVYGWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 342 nlfqsfL-LPVSGC--LLIGTTY--AKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKI 416
Cdd:cd18578 156 ------LaLVGLATvpLLLLAGYlrMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 417 GKKHSLVKSgnhfLFFSiISLFLLHLI-----YYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSC 491
Cdd:cd18578 230 GLRRALISG----LGFG-LSQSLTFFAyalafWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAA 304
|
330
....*....|
gi 124805679 492 SKVLQIIKLP 501
Cdd:cd18578 305 ARIFRLLDRK 314
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
523-820 |
3.28e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 126.25 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTKDninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVP 602
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRP--------------ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP-TEGSIAVNGVP 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPFLFNLTVRENL-MYPYKAYEEMLKEQIRLIEqnqgafinminnentkkekndddntinty 681
Cdd:TIGR02857 386 LADADADSWRDQIAWVPQHPFLFAGTIAENIrLARPDASDAEIREALERAG----------------------------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 682 dseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhIDEFLKNHFNYDNMNVGVNGTSLSGGQKQRI 761
Cdd:TIGR02857 437 -------------------------------------------------LDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 762 YLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYI 820
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
543-837 |
6.20e-30 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 118.44 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLN----ASGEICVGNVPINKINSAV--LRSIVG 616
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapDEGEVLLDGKDIYDLDVDVleLRRRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 617 VITQDPFLFNLTVRENLMYPYKAYEEMLKEQIRLIEQnqgafinminnentkkekndddntintydseqdinkndmknty 696
Cdd:cd03260 85 MVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVE------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 697 eiytfllKELQKVQ--EEIKNNLssdkmkniyndlhideflknhfnydnmnvgvNGTSLSGGQKQRIYLAQNLIKNNKIL 774
Cdd:cd03260 122 -------EALRKAAlwDEVKDRL-------------------------------HALGLSGGQQQRLCLARALANEPEVL 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 775 ILDEPTSSLDKLSENIINKaLIKYMKDKTTIIF-TH------RLdllnyVDYIGVIEEGQIIQFDKRQSV 837
Cdd:cd03260 164 LLDEPTSALDPISTAKIEE-LIAELKKEYTIVIvTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
202-490 |
6.91e-30 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 120.23 E-value: 6.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYltneIYKTVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFF 281
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGL----LALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 282 EKVLNQDVHFFNKQKTGELINRLSNDIEISSKFlihLSFGIRNFISALIGGICAL----HISPRNLFQSFL-LPVSGclL 356
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLREL---ITSGLPQLVTGVLTVVGAVvlmfLLDWVLTLVTLAvVPLAF--L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 357 IGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKS-----GNHFLF 431
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEAligplMGLAVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 432 FSIISLFLlhliyYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGS 490
Cdd:cd18551 232 LALLVVLG-----VGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGA 285
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
524-841 |
1.65e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 117.43 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnernKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLltkkndLNA-----SGEICV 598
Cdd:COG1122 1 IELENLSFSYPG--------------GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRL------LNGllkptSGEVLV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 GNVPINKINSAVLRSIVGVITQDPF--LFNLTVRENLMY-PykayeemlkeqirlieQNQGafinminnentkkeknddd 675
Cdd:COG1122 61 DGKDITKKNLRELRRKVGLVFQNPDdqLFAPTVEEDVAFgP----------------ENLG------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 ntintydseqdINKNDMKntyeiytfllkelQKVQEEIKnnlssdkmkniynDLHIDEFL-KNHFnydnmnvgvngtSLS 754
Cdd:COG1122 106 -----------LPREEIR-------------ERVEEALE-------------LVGLEHLAdRPPH------------ELS 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 755 GGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKD--KTTIIFTHRLDLL-NYVDYIGVIEEGQIIQ 830
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDpRGRRELLE--LLKRLNKegKTVIIVTHDLDLVaELADRVIVLDDGRIVA 214
|
330
....*....|.
gi 124805679 831 FDKRQSVLQKP 841
Cdd:COG1122 215 DGTPREVFSDY 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
524-827 |
1.70e-29 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 116.41 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNINaninnernkkFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkkNDLNA-SGEICVGNVp 602
Cdd:cd03250 1 ISVEDASFTWDSGEQETS----------FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL--GELEKlSGSVSVPGS- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 inkinsavlrsiVGVITQDPFLFNLTVRENLMYPYKAYEEMLKEQIR---Lieqnqgafinminnentkkekndddntin 679
Cdd:cd03250 68 ------------IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKacaL----------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 680 tydsEQDInkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhidEFLKNHfnyDNMNVGVNGTSLSGGQKQ 759
Cdd:cd03250 107 ----EPDL---------------------------------------------EILPDG---DLTEIGEKGINLSGGQKQ 134
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 760 RIYLAQNLIKNNKILILDEPTSSLD-----KLSENIINKALikyMKDKTTIIFTHRLDLLNYVDYIGVIEEGQ 827
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDahvgrHIFENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
205-465 |
2.82e-29 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 118.42 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIIN--MYGGKEESLKYLtNEIYKTVLLIIGI----STFSFFRIYFIETSIEKITRRLRT 278
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNviSRSLKETNGDFI-EDLKKPALKLLGLyllqSLLTFAYISLLSVVGERVAARLRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 279 HFFEKVLNQDVHFFNKQKTGELINRLSNDI-EISSKFLIHLSFGIRNFISAlIGGICAL-HISPRnLFQSFLLPVSGCLL 356
Cdd:cd18574 80 DLFSSLLRQDIAFFDTHRTGELVNRLTADVqEFKSSFKQCVSQGLRSVTQT-VGCVVSLyLISPK-LTLLLLVIVPVVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 357 IGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVykigkKHSLVKSGNHF-LFFSII 435
Cdd:cd18574 158 VGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKA-----AKLNEKLGLGIgIFQGLS 232
|
250 260 270
....*....|....*....|....*....|....
gi 124805679 436 SLFL----LHLIYYGNYLIAHKFINTGDLFSLIM 465
Cdd:cd18574 233 NLALngivLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
202-469 |
5.06e-29 |
|
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: 117.36 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYLTNeIYKTVLLIIGISTF--SFFRIYFIETSIEKITRRLRTH 279
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALN-VYSLALLLLGLAQFilSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 280 FFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIH-LSFGIRNFISALIGGICALHISPR-NLFQSFLLPVsgCLLI 357
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEkLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPL--YILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 358 GTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLFFSIISL 437
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|..
gi 124805679 438 FLLHLIYYGNYLIAHKFINTGDLFSLIMYSLF 469
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVAFLSLFAQ 269
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
186-830 |
5.12e-29 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 124.08 E-value: 5.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 186 SSLKDLFNILKKERKYLGFAMFCLIASSLGQMIFPMCISKIINMYGGKEeslkyLTNEIYKTVLLIIGI----STFSFFR 261
Cdd:TIGR01193 142 NSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHK-----MMGTLGIISIGLIIAyiiqQILSYIQ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 262 IYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEI-----SSKFLIHLSFGIRNFISALIGgical 336
Cdd:TIGR01193 217 IFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIidalaSTILSLFLDMWILVIVGLFLV----- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 337 hISPRNLFQSFLLPVSGCLLIGTTYAKFVKKISVLKQEK---LSSCIdfaSEKIHNISNVRLLNGESYEKK----EFINY 409
Cdd:TIGR01193 292 -RQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQAnavLNSSI---IEDLNGIETIKSLTSEAERYSkidsEFGDY 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 410 LEDVYKIGKK---HSLVKSGNHFlffsIISLFLLhliYYGNYLIAHKFINTGdlfSLIMYSLFCGSGIQGMMHAIgDIQK 486
Cdd:TIGR01193 368 LNKSFKYQKAdqgQQAIKAVTKL----ILNVVIL---WTGAYLVMRGKLTLG---QLITFNALLSYFLTPLENII-NLQP 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 487 CLGSCSKV---LQIIKLPDNNFHNywnKTSIDFLKSNNFSITFHNVSFSYdntkdNINANInnernkkfaLKNVSFFLPH 563
Cdd:TIGR01193 437 KLQAARVAnnrLNEVYLVDSEFIN---KKKRTELNNLNGDIVINDVSYSY-----GYGSNI---------LSDISLTIKM 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 564 NKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLMYPYK--AYE 641
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQ-ARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQ 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 642 EMLKEQIRLIEqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfLLKELQKVQEEIKNNLSSDk 721
Cdd:TIGR01193 579 DEIWAACEIAE-------------------------------------------------IKDDIENMPLGYQTELSEE- 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 722 mkniyndlhideflknhfnydnmnvgvnGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKyMKD 801
Cdd:TIGR01193 609 ----------------------------GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQD 659
|
650 660
....*....|....*....|....*....
gi 124805679 802 KTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:TIGR01193 660 KTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
524-828 |
3.28e-28 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 113.33 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPI 603
Cdd:cd03248 12 VKFQNVTFAYPT------------RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVLLDGKPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLMYPYKAYE-EMLKEQIRliEQNQGAFINMINNEntkkekndddntintYD 682
Cdd:cd03248 79 SQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSfECVKEAAQ--KAHAHSFISELASG---------------YD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 683 SEqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnVGVNGTSLSGGQKQRIY 762
Cdd:cd03248 142 TE-------------------------------------------------------------VGEKGSQLSGGQKQRVA 160
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 763 LAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQI 828
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
524-840 |
3.88e-28 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 113.74 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYdntkdninaninnERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNdLNASGEICVGNVPI 603
Cdd:cd03252 1 ITFEHVRFRY-------------KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-VPENGRVLVDGHDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLMYpykAYEEMLKEQIRLIEQNQGAfinminnentkkekndddntintyds 683
Cdd:cd03252 67 ALADPAWLRRQVGVVLQENVLFNRSIRDNIAL---ADPGMSMERVIEAAKLAGA-------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 684 eqdinkndmkntyeiYTFLLkELQKvqeeiknnlssdkmkniyndlhideflknhfNYDNMnVGVNGTSLSGGQKQRIYL 763
Cdd:cd03252 118 ---------------HDFIS-ELPE-------------------------------GYDTI-VGEQGAGLSGGQRQRIAI 149
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 764 AQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
554-781 |
8.90e-28 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 109.66 E-value: 8.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkKNDLNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFN-LTVREN 632
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIA-GLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 633 LMYPykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytFLLKELQKVQee 712
Cdd:pfam00005 80 LRLG----------------------------------------------------------------LLLKGLSKRE-- 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 713 iknnlSSDKMKNIYNDLHIDEFLKNHfnydnmnVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:pfam00005 94 -----KDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
202-494 |
2.85e-27 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 112.52 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIIN--MYGGKEESLKYLtneiyktVLLIIGIST----FSFFRIYFIETSIEKITRR 275
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDdiFVEKDLEALLLV-------PLAIIGLFLlrglASYLQTYLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 276 LRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIE-ISSKFLIHLSFGIRNFISALIGGICALHISPR-NLFQSFLLPVSG 353
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNqVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKlTLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 354 clLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFL--F 431
Cdd:cd18552 154 --LPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLmeL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 432 FSIISLFLlhLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18552 232 LGAIAIAL--VLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
524-828 |
3.77e-27 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 110.27 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYdntkdninaniNNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPI 603
Cdd:cd03255 1 IELKNLSKTY-----------GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVRVDGTDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSI----VGVITQDPFLF-NLTVRENLMYPYKAYEEMLKEQIRLIEQnqgafinminnentkkekndddnti 678
Cdd:cd03255 69 SKLSEKELAAFrrrhIGFVFQSFNLLpDLTALENVELPLLLAGVPKKERRERAEE------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 679 ntydseqdinkndmkntyeiytfLLKElqkvqeeiknnlssdkmkniyndLHIDEFLkNHFnydnmnvgvnGTSLSGGQK 758
Cdd:cd03255 124 -----------------------LLER-----------------------VGLGDRL-NHY----------PSELSGGQQ 146
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 759 QRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKDK--TTIIF-THRLDLLNYVDYIGVIEEGQI 828
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDsETGKEVME--LLRELNKEagTTIVVvTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
205-494 |
1.28e-26 |
|
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: 110.51 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINMYGGKeeslkYLTNEIYKTVLLI----IGISTFSFFRIYFIETSIEKITRRLRTHF 280
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGE-----YQHNAFTSAIGLMclfsLGSSLSAGLRGGLFMCTLSRLNLRLRHQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 281 FEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFL-IHLSFGIRNFISALigGICA--LHISPRNLFQSFL-LPVSGclL 356
Cdd:cd18590 76 FSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVaLNANVLLRSLVKTL--GMLGfmLSLSWQLTLLTLIeMPLTA--I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 357 IGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVkSGNHFLFFSIIS 436
Cdd:cd18590 152 AQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV-RAVYLLVRRVLQ 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 437 LFL-LHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18590 231 LGVqVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
202-466 |
2.27e-26 |
|
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: 109.95 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIINmYGGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFF 281
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLID-DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 282 EKVLNQDVHFFNKQKTGELINRLSNDI----EISSKFLIHLsfgIRNFISALIGGICALHISPR-NLFQSFLLPVSGclL 356
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVdavqNLVSSGLLQL---LSDVLTLIGALVILFYLNWKlTLVALLLLPLYV--L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 357 IGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLFFSIIS 436
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270
....*....|....*....|....*....|
gi 124805679 437 LFLLHLIYYGNYLIAHKFINTGDLFSLIMY 466
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAY 264
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
236-822 |
2.83e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 116.28 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 236 SLKYLTNEiYKTVLLIIGISTF--SFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKT--GELINRLSNDIEIs 311
Cdd:PTZ00265 860 NLEANSNK-YSLYILVIAIAMFisETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHL- 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 312 skflihLSFGIRNFISALIGGICALHISPRNLFqsFLLPVSGCLLIGTtYAKFVKKISVlkQEKLSSCIDFASEKIHNIS 391
Cdd:PTZ00265 938 ------LKTGLVNNIVIFTHFIVLFLVSMVMSF--YFCPIVAAVLTGT-YFIFMRVFAI--RARLTANKDVEKKEINQPG 1006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 392 NVRLLNGES--------------YEKKEFINY-LEDVY-----------KIGKKHSLVKSGNHFLFFSIISLFLLHLIY- 444
Cdd:PTZ00265 1007 TVFAYNSDDeifkdpsfliqeafYNMNTVIIYgLEDYFcnliekaidysNKGQKRKTLVNSMLWGFSQSAQLFINSFAYw 1086
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 445 YGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKVLQI------IKLPDNNFHNYWNKTSIDFlk 518
Cdd:PTZ00265 1087 FGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLiirksnIDVRDNGGIRIKNKNDIKG-- 1164
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 519 snnfSITFHNVSFSYDNtkdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNASGEICV 598
Cdd:PTZ00265 1165 ----KIEIMDVNFRYIS------------RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVF 1228
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 GNVPINkinsavlrsivgvitqdpflfnltvrenlmypykayeEMLKEQIRLIEQNQGAFINMINNENTKKEKNDDDNTI 678
Cdd:PTZ00265 1229 KNEHTN-------------------------------------DMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDST 1271
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 679 NTYDSEQ---------DINKNDMKNTYEIYT---FLLKelQKVQEEIK---NNLSSDKMKNIYNDLHIDEFLKNHFNYDN 743
Cdd:PTZ00265 1272 VFKNSGKilldgvdicDYNLKDLRNLFSIVSqepMLFN--MSIYENIKfgkEDATREDVKRACKFAAIDEFIESLPNKYD 1349
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 744 MNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAL--IKYMKDKTTIIFTHRLDLLNYVDYIG 821
Cdd:PTZ00265 1350 TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIV 1429
|
.
gi 124805679 822 V 822
Cdd:PTZ00265 1430 V 1430
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
524-840 |
7.88e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.69 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkkNDLNA-SGEICVGNVP 602
Cdd:COG1131 1 IEVRGLTKRYGDKT---------------ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL--GLLRPtSGEVRVLGED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIvGVITQDPFLF-NLTVRENLMYpYKAYEEMLKEQIRlieqnqgafinminnentkkekndddntinty 681
Cdd:COG1131 64 VARDPAEVRRRI-GYVPQEPALYpDLTVRENLRF-FARLYGLPRKEAR-------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 682 dseqdinkndmkntyeiytfllkelQKVQEEIKnnlssdkmkniynDLHIDEFLknhfnydNMNVGvngtSLSGGQKQRI 761
Cdd:COG1131 110 -------------------------ERIDELLE-------------LFGLTDAA-------DRKVG----TLSGGMKQRL 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 762 YLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQ 839
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLsTHYLEEAERLcDRVAIIDKGRIVADGTPDELKA 220
|
.
gi 124805679 840 K 840
Cdd:COG1131 221 R 221
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
205-486 |
8.30e-26 |
|
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: 108.17 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINMYGgKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFFEKV 284
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIV-IEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 285 LNQDVHFFNKQKTGELINRLSNDIEISSKFLI-HLSFGIRNFISALigGICAL--HISPR-NLFQSFLLPVsgCLLIGTT 360
Cdd:cd18784 80 VSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSlNLNIFLRSLVKAI--GVIVFmfKLSWQlSLVTLIGLPL--IAIVSKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 361 YAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLV----KSGNHFLFFSIIS 436
Cdd:cd18784 156 YGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAyggyVWSNELTELALTV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 437 LFLlhliYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQ-------GMMHAIGDIQK 486
Cdd:cd18784 236 STL----YYGGHLVITGQISGGNLISFILYQLELGSCLEsvgsvytGLMQAVGAAEK 288
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
524-846 |
1.19e-25 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 106.60 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT--KKNDlnaSGEICVGNV 601
Cdd:COG1127 6 IEVRNLTKSFGDRV---------------VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIglLRPD---SGEILVDGQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSI---VGVITQDPFLF-NLTVRENLMYPykayeemLKEQIRLieqnqgafinminnentkkekndddnt 677
Cdd:COG1127 68 DITGLSEKELYELrrrIGMLFQGGALFdSLTVFENVAFP-------LREHTDL--------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 678 intydSEQDINKN-DMKntyeiytfllkeLQKVqeeiknNLSS--DKMKNiyndlhideflknhfnydnmnvgvngtSLS 754
Cdd:COG1127 114 -----SEAEIRELvLEK------------LELV------GLPGaaDKMPS---------------------------ELS 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 755 GGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKaLIKYMKDK---TTIIFTHRLD-LLNYVDYIGVIEEGQIIQ 830
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDE-LIRELRDElglTSVVVTHDLDsAFAIADRVAVLADGKIIA 222
|
330
....*....|....*.
gi 124805679 831 FDKRQSVLQKPCPILK 846
Cdd:COG1127 223 EGTPEELLASDDPWVR 238
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
204-494 |
1.26e-25 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 107.90 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 204 FAMFCLIASSLGQMIFPMCISKIINMYGGKeeslkYLTNEIYKTVLLIIGIST----FSFFRIYFIETSIEKITRRLRTH 279
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIGG-----GLRELLWLLALLILGVALlrgvFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 280 FFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFlihLSFGIRNFISALI----GGICALHISPR-NLFQSFLLPVsgC 354
Cdd:cd18542 78 LYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRF---LAFGLVELVRAVLlfigALIIMFSINWKlTLISLAIIPF--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 355 LLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVksgnHFLFFSI 434
Cdd:cd18542 153 ALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKL----LAKYWPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 435 ISLF----LLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18542 229 MDFLsglqIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
202-466 |
1.64e-25 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 107.50 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYLTNEIYKTVLLIIGISTFSFF-RIYFIETSIeKITRRLRTHF 280
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLwRYLIFGASR-RIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 281 FEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFlihLSFGIRNFISALIGGICAL----HISPRNLFQSfLLPVSGCLL 356
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMA---LGPGILYLVDALFLGVLVLvmmfTISPKLTLIA-LLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 357 IGTTYAKFVKKISVLKQEKLSSCIDFASEkihNISNVRLL---NGESYEKKEFINYLEDVYKigKKHSLVKSGNhfLFFS 433
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQE---SFSGIRVIkafVQEEAEIERFDKLNEEYVE--KNLRLARVDA--LFFP 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 124805679 434 IISLF----LLHLIYYGNYLIAHKFINTGDLFSLIMY 466
Cdd:cd18541 229 LIGLLiglsFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
538-829 |
2.16e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 105.28 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 538 DNINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKkndLNA--SGEICVGNVPINKINSA---VLR 612
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG---LLKptSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 613 SIVGVITQDPFL-FN--LTVRENLMYPYKAYEEMLKEQIRLieqnqgafinminnentkkekndddntintydseqdink 689
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIAEPLRIHGKLSKKEARK--------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 690 ndmkntyEIYTFLLKELqkvqeeiknNLSsdkmkniyndlhiDEFLKN--HfnydnmnvgvngtSLSGGQKQRIYLAQNL 767
Cdd:cd03257 123 -------EAVLLLLVGV---------GLP-------------EEVLNRypH-------------ELSGGQRQRVAIARAL 160
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 768 IKNNKILILDEPTSSLDKLSE-NIINkaLIKYMKDK--TTIIF-THRLDLLNYV-DYIGVIEEGQII 829
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElgLTLLFiTHDLGVVAKIaDRVAVMYAGKIV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
524-846 |
2.58e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 105.28 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnernkKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKkndLNA--SGEICVGNV 601
Cdd:cd03261 1 IELRGLTKSFGG---------------RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG---LLRpdSGEVLIDGE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSI---VGVITQDPFLFN-LTVRENLMYPYKAYEEMLKEQIRLIeqnqgafinminnentkkekndddnt 677
Cdd:cd03261 63 DISGLSEAELYRLrrrMGMLFQSGALFDsLTVFENVAFPLREHTRLSEEEIREI-------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 678 intydseqdinkndmkntyeiytfLLKELQKVqeeiknNLSSDKmkniynDLHIDEflknhfnydnmnvgvngtsLSGGQ 757
Cdd:cd03261 117 ------------------------VLEKLEAV------GLRGAE------DLYPAE-------------------LSGGM 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 758 KQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINkALIKYMKDK---TTIIFTHRLD-LLNYVDYIGVIEEGQIIQFDK 833
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVID-DLIRSLKKElglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGT 220
|
330
....*....|...
gi 124805679 834 RQSVLQKPCPILK 846
Cdd:cd03261 221 PEELRASDDPLVR 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
524-829 |
2.71e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 105.32 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYdntkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTK--KNDlnaSGEICVGNV 601
Cdd:COG4555 2 IEVENLSKKY---------------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllKPD---SGSILIDGE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSIvGVITQDPFLF-NLTVRENLMYPYKAYEEMLKEQIRLIEQnqgafinminnentkkekndddntint 680
Cdd:COG4555 64 DVRKEPREARRQI-GVLPDERGLYdRLTVRENIRYFAELYGLFDEELKKRIEE--------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfLLKELQkvqeeiknnlssdkmkniyndlhIDEFLknhfnydNMNVGvngtSLSGGQKQR 760
Cdd:COG4555 116 ---------------------LIELLG-----------------------LEEFL-------DRRVG----ELSTGMKKK 140
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLL-NYVDYIGVIEEGQII 829
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFsSHIMQEVeALCDRVVILHKGKVV 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
524-841 |
6.41e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 105.23 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYdntkdniNANINNERNkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlNA-----SGEICV 598
Cdd:TIGR04521 1 IKLKNVSYIY-------QPGTPFEKK---ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHL------NGllkptSGTVTI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 GNVPIN---KINSAVLRSIVGVITQDPF--LFNLTVRENLMY-PykayeemlkeqirlieQNQGAfinminnentkkekn 672
Cdd:TIGR04521 65 DGRDITakkKKKLKDLRKKVGLVFQFPEhqLFEETVYKDIAFgP----------------KNLGL--------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 673 dddntintydSEQDInkndmkntyeiytfllkeLQKVQEEIKnnlssdkmkniynDLHIDEFLKNH--Fnydnmnvgvng 750
Cdd:TIGR04521 114 ----------SEEEA------------------EERVKEALE-------------LVGLDEEYLERspF----------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 751 tSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYM---KDKTTIIFTHRL-DLLNYVDYIGVIEE 825
Cdd:TIGR04521 142 -ELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpKGRKEILD--LFKRLhkeKGLTVILVTHSMeDVAEYADRVIVMHK 218
|
330
....*....|....*.
gi 124805679 826 GQIIQFDKRQSVLQKP 841
Cdd:TIGR04521 219 GKIVLDGTPREVFSDV 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
528-828 |
6.51e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 102.29 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 528 NVSFSYDNTKDNInaninnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKkNDLNASGEICVGNVPINKIN 607
Cdd:cd03246 5 NVSFRYPGAEPPV-------------LRNVSFSIEPGESLAIIGPSGSGKSTLARLILG-LLRPTSGRVRLDGADISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 608 SAVLRSIVGVITQDPFLFNLTVRENLmypykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdi 687
Cdd:cd03246 71 PNELGDHVGYLPQDDELFSGSIAENI------------------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 688 nkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNL 767
Cdd:cd03246 97 -----------------------------------------------------------------LSGGQRQRLGLARAL 111
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 768 IKNNKILILDEPTSSLDKLSENIINKAlIKYMK--DKTTIIFTHRLDLLNYVDYIGVIEEGQI 828
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQA-IAALKaaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
550-840 |
4.83e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 107.53 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT---KkndlNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFN 626
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVgvwP----PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 627 LTVRENL--MY---PYKAYE--------EMLkeqIRLieqNQGafinminnentkkekndddntintYDSEqdinkndmk 693
Cdd:COG4618 420 GTIAENIarFGdadPEKVVAaaklagvhEMI---LRL---PDG------------------------YDTR--------- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 694 ntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnVGVNGTSLSGGQKQRIYLAQNLIKNNKI 773
Cdd:COG4618 461 ----------------------------------------------------IGEGGARLSGGQRQRIGLARALYGDPRL 488
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 774 LILDEPTSSLDKLSENIINKAlIKYMKD--KTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAA-IRALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
524-828 |
5.74e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 100.66 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDninaninnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDLN--ASGEICVGNV 601
Cdd:COG4619 1 LELEGLSFRVGGKPI---------------LSPVSLTLEAGECVAITGPSGSGKSTLLRAL---ADLDppTSGEIYLDGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSIVGVITQDPFLFNLTVRENLMYPYkayeemlkeQIRlieqnqgafinminnentkkEKNDDDNTINTy 681
Cdd:COG4619 63 PLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPF---------QLR--------------------ERKFDRERALE- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 682 dseqdinkndmkntyeiytfLLKELqkvqeeiknNLSsdkmkniyndlhiDEFLKNHFNydnmnvgvngtSLSGGQKQRI 761
Cdd:COG4619 113 --------------------LLERL---------GLP-------------PDILDKPVE-----------RLSGGERQRL 139
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 762 YLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDK--TTIIFTHRLDLLNYV-DYIGVIEEGQI 828
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
524-829 |
6.14e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 100.89 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLL------TkkndlnaSGEIC 597
Cdd:COG1136 5 LELRNLTKSYGTGE-----------GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrpT-------SGEVL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 598 VGNVPINKINSAVLRSI----VGVITQDPFLF-NLTVRENLMYPykayeemlkeqirlieqnqgafinminnentkkekn 672
Cdd:COG1136 67 IDGQDISSLSERELARLrrrhIGFVFQFFNLLpELTALENVALP------------------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 673 dddntintydseQDINKNDMKNTYEIYTFLLKElqkvqeeiknnlssdkmkniyndLHIDEFLkNHFnydnmnvgvnGTS 752
Cdd:COG1136 111 ------------LLLAGVSRKERRERARELLER-----------------------VGLGDRL-DHR----------PSQ 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKDK--TTIIF-THRLDLLNYVDYIGVIEEGQI 828
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDsKTGEEVLE--LLRELNRElgTTIVMvTHDPELAARADRVIRLRDGRI 222
|
.
gi 124805679 829 I 829
Cdd:COG1136 223 V 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
524-834 |
6.52e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.90 E-value: 6.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKknDLNA-SGEICVGNVP 602
Cdd:COG2884 2 IRFENVSKRYPGGRE--------------ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPtSGQVLVNGQD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINS---AVLRSIVGVITQD-PFLFNLTVRENLMYPYKAyeemlkeqirlieqnQGAfinminnentkkekndddnti 678
Cdd:COG2884 66 LSRLKRreiPYLRRRIGVVFQDfRLLPDRTVYENVALPLRV---------------TGK--------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 679 ntydSEQDINkndmKNTYEIytfllkeLQKVqeeiknNLsSDKMKNIyndlhIDEflknhfnydnmnvgvngtsLSGGQK 758
Cdd:COG2884 110 ----SRKEIR----RRVREV-------LDLV------GL-SDKAKAL-----PHE-------------------LSGGEQ 143
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 759 QRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInKALIKYMKDKTTIIF-THRLDLLNYVDY-IGVIEEGQIIQFDKR 834
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDpETSWEIM-ELLEEINRRGTTVLIaTHDLELVDRMPKrVLELEDGRLVRDEAR 221
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
442-840 |
9.04e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 107.14 E-value: 9.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 442 LIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKVLQIIKLPDNNFHNywnktSIDFLKSNN 521
Cdd:TIGR01846 379 LLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSA-----GLAALPELR 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 522 FSITFHNVSFSYDNTKDNINANINNErnkkfalknvsffLPHNKSVAIVGKSGSGKTTILNLLTKKNdLNASGEICVGNV 601
Cdd:TIGR01846 454 GAITFENIRFRYAPDSPEVLSNLNLD-------------IKPGEFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVDGV 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSIVGVITQDPFLFNLTVRENLMYpykAYEEMLKEQIRLIEQNQGAfinminnentkkekndddntinty 681
Cdd:TIGR01846 520 DLAIADPAWLRRQMGVVLQENVLFSRSIRDNIAL---CNPGAPFEHVIHAAKLAGA------------------------ 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 682 dseqdinkndmkntyeiYTFLLKELQKVQEEiknnlssdkmkniyndlhideflknhfnydnmnVGVNGTSLSGGQKQRI 761
Cdd:TIGR01846 573 -----------------HDFISELPQGYNTE---------------------------------VGEKGANLSGGQRQRI 602
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 762 YLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:TIGR01846 603 AIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL 681
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
524-841 |
9.25e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.14 E-value: 9.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDLNA--SGEICVGNV 601
Cdd:COG1123 261 LEVRNLSKRYPVRG----------KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLL---LGLLRptSGSILFDGK 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSI---VGVITQDPFL-FN--LTVRENLMYPYKAYEEMLKEQIRlieqnqgafinminnentkkeknddd 675
Cdd:COG1123 328 DLTKLSRRSLRELrrrVQMVFQDPYSsLNprMTVGDIIAEPLRLHGLLSRAERR-------------------------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 ntintydseqdinkndmKNTYEIytfllkeLQKVQeeiknnLSSDKMkniynDLHIDEFlknhfnydnmnvgvngtslSG 755
Cdd:COG1123 382 -----------------ERVAEL-------LERVG------LPPDLA-----DRYPHEL-------------------SG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 756 GQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKDKT--TIIF-THRLDLLNYV-DYIGVIEEGQIIQ 830
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDvSVQAQILN--LLRDLQRELglTYLFiSHDLAVVRYIaDRVAVMYDGRIVE 485
|
330
....*....|.
gi 124805679 831 FDKRQSVLQKP 841
Cdd:COG1123 486 DGPTEEVFANP 496
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
524-838 |
9.14e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 98.58 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDntkdninaninnernKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPI 603
Cdd:COG1120 2 LEAENLSVGYG---------------GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-SSGEVLLDGRDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFL-FNLTVRENLM---YPYkayeemlkeqirlieqnQGAFinminnentkkekndddntin 679
Cdd:COG1120 66 ASLSRRELARRIAYVPQEPPApFGLTVRELVAlgrYPH-----------------LGLF--------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 680 TYDSEQDInkndmkntyeiytfllkelQKVQEEIKnnlssdkmkniynDLHIDEFLKNHFnydnmnvgvngTSLSGGQKQ 759
Cdd:COG1120 108 GRPSAEDR-------------------EAVEEALE-------------RTGLEHLADRPV-----------DELSGGERQ 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 760 RIYLAQNLIKNNKILILDEPTSSLDklsenIINK-ALIKYMKD------KTTIIFTHRLDL-LNYVDYIGVIEEGQIIQF 831
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLD-----LAHQlEVLELLRRlarergRTVVMVLHDLNLaARYADRLVLLKDGRIVAQ 219
|
....*..
gi 124805679 832 DKRQSVL 838
Cdd:COG1120 220 GPPEEVL 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
543-827 |
9.63e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 96.10 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDLN--ASGEICVGNVPINKINSAV--LRSIVGVI 618
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCI---AGLEepDSGSILIDGEDLTDLEDELppLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 619 TQDPFLF-NLTVRENLMYPykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmkntye 697
Cdd:cd03229 82 FQDFALFpHLTVLENIALG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 698 iytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILD 777
Cdd:cd03229 101 -------------------------------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124805679 778 EPTSSLDKLSENIInKALIKYMKD---KTTIIFTHRLDLLNYV-DYIGVIEEGQ 827
Cdd:cd03229 126 EPTSALDPITRREV-RALLKSLQAqlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
524-828 |
1.29e-22 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 95.54 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDntkdninaninnernKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT--KKNDlnaSGEICVGNV 601
Cdd:cd03230 1 IEVRNLSKRYG---------------KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILglLKPD---SGEIKVLGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKiNSAVLRSIVGVITQDPFLF-NLTVRENLMYpykayeemlkeqirlieqnqgafinminnentkkekndddntint 680
Cdd:cd03230 63 DIKK-EPEEVKRRIGYLPEEPSLYeNLTVRENLKL--------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgvngtslSGGQKQR 760
Cdd:cd03230 97 -------------------------------------------------------------------------SGGMKQR 103
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRL-DLLNYVDYIGVIEEGQI 828
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLsSHILeEAERLCDRVAILNNGRI 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
244-840 |
1.85e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.90 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 244 IYKTVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDI--------EISSKFL 315
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIgdidrnvaNLMNMFM 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 316 IHLSFGIRNFisALIGGICAlhISPRNLFQSFLLPVSGCLLIGTTyAKFVKKISVLKQEKLSSCIdfaSEKIHNISNVRL 395
Cdd:PLN03232 1033 NQLWQLLSTF--ALIGTVST--ISLWAIMPLLILFYAAYLYYQST-SREVRRLDSVTRSPIYAQF---GEALNGLSSIRA 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 396 LngESYEKKEFIN--YLEDVYKIgkkhSLVK-SGNHFLFFSIISL--FLLHLIY------YGNYLIAHKFINTGDLfsLI 464
Cdd:PLN03232 1105 Y--KAYDRMAKINgkSMDNNIRF----TLANtSSNRWLTIRLETLggVMIWLTAtfavlrNGNAENQAGFASTMGL--LL 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 465 MYSLFCGSGIQGMMHAIGDIQKCLGSCSKVLQIIKLPDNNFHNYWNKTSIDFLKSNNfSITFHNVSFSYDNTKDNInani 544
Cdd:PLN03232 1177 SYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG-SIKFEDVHLRYRPGLPPV---- 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 545 nnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKINSAVLRSIVGVITQDPFL 624
Cdd:PLN03232 1252 ---------LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE-KGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 625 FNLTVRENLMyPYKayeemlkeqirlieqnqgafinminnentkkEKNDDDntintydseqdinkndmkntyeiytfLLK 704
Cdd:PLN03232 1322 FSGTVRFNID-PFS-------------------------------EHNDAD--------------------------LWE 1343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 705 ELQKVQeeIKNNLSsdkmkniyndlhideflKNHFNYDnMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PLN03232 1344 ALERAH--IKDVID-----------------RNPFGLD-AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 785 KLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
550-840 |
2.20e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 102.04 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNdLNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTV 629
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIW-PPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 630 RENLMypykayeemlkeqiRLieqnqgafinminnentkkekndDDNtintYDSEQDINKndmkntyeiytfllKELQKV 709
Cdd:TIGR01842 409 AENIA--------------RF-----------------------GEN----ADPEKIIEA--------------AKLAGV 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 710 QEEIKNnlssdkmkniyndlhidefLKNhfNYDNmNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSEN 789
Cdd:TIGR01842 434 HELILR-------------------LPD--GYDT-VIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 124805679 790 IINKALIKYMKDK-TTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:TIGR01842 492 ALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
532-841 |
2.92e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 102.10 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 532 SYDNTKDNINANINN---ERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPINKINS 608
Cdd:PRK10789 306 PVPEGRGELDVNIRQftyPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV-SEGDIRFHDIPLTKLQL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 609 AVLRSIVGVITQDPFLFNLTVRENLMypykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdin 688
Cdd:PRK10789 385 DSWRSRLAVVSQTPFLFSDTVANNIA------------------------------------------------------ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 689 kndmkntyeiytflLKELQKVQEEIKNnlsSDKMKNIYNDLhidefLKNHFNYDNmNVGVNGTSLSGGQKQRIYLAQNLI 768
Cdd:PRK10789 411 --------------LGRPDATQQEIEH---VARLASVHDDI-----LRLPQGYDT-EVGERGVMLSGGQKQRISIARALL 467
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 769 KNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
259-838 |
3.17e-22 |
|
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: 103.45 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 259 FFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHLSFGIRNFISALIGGICALHI 338
Cdd:TIGR01271 943 FFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSV 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 339 SPRNLFQSfLLPVSGCLLIGTTYakFVKKISVLKQ---EKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEdvyk 415
Cdd:TIGR01271 1023 LQPYIFIA-AIPVAVIFIMLRAY--FLRTSQQLKQlesEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALN---- 1095
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 416 igkkhslVKSGNHFLFFSIISLFLLHL-IYYGNYLIAHKFINT-------GDLFSLIMYSLFCGSGIQGMMHAIGDIQKC 487
Cdd:TIGR01271 1096 -------LHTANWFLYLSTLRWFQMRIdIIFVFFFIAVTFIAIgtnqdgeGEVGIILTLAMNILSTLQWAVNSSIDVDGL 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 488 LGSCSKVLQIIKLPD-----NNFHNYWNKTSIDFLKS--------NNFSITFHNVSFSYDNTKDNInaninnernkkfaL 554
Cdd:TIGR01271 1169 MRSVSRVFKFIDLPQeeprpSGGGGKYQLSTVLVIENphaqkcwpSGGQMDVQGLTAKYTEAGRAV-------------L 1235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 555 KNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKndLNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLM 634
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL--LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD 1313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 635 yPYKAYEEmlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfllKELQKVQEEIK 714
Cdd:TIGR01271 1314 -PYEQWSD-------------------------------------------------------------EEIWKVAEEVG 1331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 715 nnlssdkMKNIyndlhIDEFLknhfnyDNMNVGV--NGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIIN 792
Cdd:TIGR01271 1332 -------LKSV-----IEQFP------DKLDFVLvdGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 124805679 793 KALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVL 838
Cdd:TIGR01271 1394 KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
553-832 |
4.83e-22 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 95.17 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVREN 632
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-EEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 633 LMyPYkayeemlkeqirlieqnqgafinminnentkkekndddntiNTYDSEQdinkndmkntyeiytfllkelqkvqee 712
Cdd:cd03369 102 LD-PF-----------------------------------------DEYSDEE--------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 713 iknnlssdkmknIYNDLHIDEflknhfnydnmnvgvNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIIN 792
Cdd:cd03369 113 ------------IYGALRVSE---------------GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124805679 793 KALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFD 832
Cdd:cd03369 166 KTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
206-494 |
1.00e-21 |
|
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: 96.39 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 206 MFCLIASSLGQMIFPMCISKIINMYGGKEESLKYlTNEIYKTVLLII--GISTFSFFRIYFIETSieKITRRLRTHFFEK 283
Cdd:cd18589 2 LGLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAF-TAAITVMSLLTIasAVSEFVCDLIYNITMS--RIHSRLQGLVFAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 284 VLNQDVHFFNKQKTGELINRLSNDIEISSKFLIH-LSFGIRNFISALIGGICALHISPR-NLFQSFLLPVsgCLLIGTTY 361
Cdd:cd18589 79 VLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSEnLSLLMWYLARGLFLFIFMLWLSPKlALLTALGLPL--LLLVPKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 362 AKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLfFSIISLFL-L 440
Cdd:cd18589 157 GKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWT-SSFSGLALkV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124805679 441 HLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18589 236 GILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
525-827 |
2.38e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 91.54 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 525 TFHNVSFSYdntkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPIN 604
Cdd:cd00267 1 EIENLSFRY---------------GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP-TSGEILIDGKDIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 605 KINSAVLRSIVGVITQdpflfnltvrenlmypykayeemlkeqirlieqnqgafinminnentkkekndddntintydse 684
Cdd:cd00267 65 KLPLEELRRRIGYVPQ---------------------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 685 qdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLA 764
Cdd:cd00267 81 --------------------------------------------------------------------LSGGQRQRVALA 92
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 765 QNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLL-NYVDYIGVIEEGQ 827
Cdd:cd00267 93 RALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIvTHDPELAeLAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
538-841 |
2.43e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 94.10 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 538 DNINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkknDLNA--SGEICVGNVPINKINSAVLRSIV 615
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALA---GLERpwSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 616 GVITQDPFL-FN--LTVRENLMYPYKAYEEMlkeqirlieqnqgafinminnentkkekndddntintyDSEQDINKndm 692
Cdd:COG1124 82 QMVFQDPYAsLHprHTVDRILAEPLRIHGLP--------------------------------------DREERIAE--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 693 kntyeiytfLLKELqkvqeeiknNLSSDkmkniyndlhideFLknhFNYDNMnvgvngtsLSGGQKQRIYLAQNLIKNNK 772
Cdd:COG1124 121 ---------LLEQV---------GLPPS-------------FL---DRYPHQ--------LSGGQRQRVAIARALILEPE 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 773 ILILDEPTSSLDkLS---EnIINkaLIKYMKD--KTTIIF-THRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:COG1124 159 LLLLDEPTSALD-VSvqaE-ILN--LLKDLREerGLTYLFvSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
553-829 |
6.18e-21 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 92.18 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkkNDLNA-SGEICVGNVPINKINSAVLRSIvGVITQDPFLF-NLTVR 630
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLT--GELRPtSGTAYINGYSIRTDRKAARQSL-GYCPQFDALFdELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 631 ENLMypykayeemlkeqirlieqnqgaFINMINNENTKKEKNDDDNTINTYDSEQDINKndmkntyeiytfllkelqKVQ 710
Cdd:cd03263 94 EHLR-----------------------FYARLKGLPKSEIKEEVELLLRVLGLTDKANK------------------RAR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 711 EeiknnlssdkmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENI 790
Cdd:cd03263 133 T-----------------------------------------LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRA 171
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124805679 791 INKALIKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQII 829
Cdd:cd03263 172 IWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLR 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
553-811 |
1.47e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 96.28 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVREN 632
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 633 LMYpykayeemlkeqirlieqnqgafinminnenTKKEKNDDDntintydseqdinkndmkntyeiytfLLKELQKVQEE 712
Cdd:TIGR02868 429 LRL-------------------------------ARPDATDEE--------------------------LWAALERVGLA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 713 IknnlssdkmkniyndlHIDEFlknhfnYDNMN--VGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENI 790
Cdd:TIGR02868 452 D----------------WLRAL------PDGLDtvLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
250 260
....*....|....*....|.
gi 124805679 791 INKALIKYMKDKTTIIFTHRL 811
Cdd:TIGR02868 510 LLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
202-466 |
7.25e-20 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 90.91 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIINMYGgkeESLKYLTNEIYKTVLLIIGI----STFSFFRIYFIETSIEKITRRLR 277
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYI---VPGQGDLQGLLLLALLYLGLlllsFLLQYLQTYLLQKLGQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 278 THFFEKVLNQDVHFFNKQKTGELINRLSNDIE-IS---SKFLIHLsfgIRNFISaLIGGICA-LHISPR-NLFQSFLLPV 351
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEaLNelfTSGLVTL---IGDLLL-LIGILIAmFLLNWRlALISLLVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 352 sgcLLIGT-TYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVksgnHFL 430
Cdd:cd18544 154 ---LLLATyLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKL----FAL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124805679 431 FFSIISLF----LLHLIYYGNYLIAHKFINTGDLFSLIMY 466
Cdd:cd18544 227 FRPLVELLsslaLALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
524-812 |
8.75e-20 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 88.68 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkknDLNA--SGEICVGNV 601
Cdd:cd03293 1 LEVRNVSKTYGG-----------GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIA---GLERptSGEVLVDGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAvlrsiVGVITQDPFLFN-LTVRENLMYPYKAyEEMLKEQIRlieqnqgafinminnentkkekndddntint 680
Cdd:cd03293 67 PVTGPGPD-----RGYVFQQDALLPwLTVLDNVALGLEL-QGVPKAEAR------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfllkelQKVQEEIKnnlssdkmkniynDLHIDEFLkNHFNYDnmnvgvngtsLSGGQKQR 760
Cdd:cd03293 110 --------------------------ERAEELLE-------------LVGLSGFE-NAYPHQ----------LSGGMRQR 139
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIK-YMKDKTTIIF-THRLD 812
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiWRETGKTVLLvTHDID 193
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
554-854 |
1.24e-19 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 89.91 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKndLNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENL 633
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL--LNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 634 MyPYKAYEEmlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfllKELQKVQEEI 713
Cdd:cd03289 98 D-PYGKWSD-------------------------------------------------------------EEIWKVAEEV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 714 KnnlssdkMKNIyndlhIDEFlKNHFNYDNMNvgvNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINK 793
Cdd:cd03289 116 G-------LKSV-----IEQF-PGQLDFVLVD---GGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRK 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124805679 794 ALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQKpcpilKKILTQGVS 854
Cdd:cd03289 180 TLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE-----KSHFKQAIS 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
524-832 |
1.40e-19 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 88.78 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDLN--ASGEICVGNV 601
Cdd:cd03256 1 IEVENLSKTYPNGKK--------------ALKDVSLSINPGEFVALIGPSGAGKSTLLRCL---NGLVepTSGSVLIDGT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSI---VGVITQDPFLFN-LTVRENLMYPykayeemlkeqiRLieqNQGAFINMINNENTKKEKNDddnt 677
Cdd:cd03256 64 DINKLKGKALRQLrrqIGMIFQQFNLIErLSVLENVLSG------------RL---GRRSTWRSLFGLFPKEEKQR---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 678 intydseqdinkndmkntyeiytfLLKELQKVQEEIKNNLSSDKmkniyndlhideflknhfnydnmnvgvngtsLSGGQ 757
Cdd:cd03256 125 ------------------------ALAALERVGLLDKAYQRADQ-------------------------------LSGGQ 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 758 KQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkalikYMKD------KTTIIFTHRLDL-LNYVDYIGVIEEGQII 829
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDpASSRQVMD-----LLKRinreegITVIVSLHQVDLaREYADRIVGLKDGRIV 224
|
...
gi 124805679 830 qFD 832
Cdd:cd03256 225 -FD 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
549-832 |
1.58e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 87.96 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 549 NKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPINKInsAVLRSIVGVITQDPFLF-NL 627
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP-DSGEILIDGRDVTGV--PPERRNIGMVFQDYALFpHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 628 TVRENLMYPYKAyEEMLKEQIRlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfllkelQ 707
Cdd:cd03259 88 TVAENIAFGLKL-RGVPKAEIR---------------------------------------------------------A 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 708 KVQEEIKNnlssdkmkniyndLHIDEFLkNHFNYdnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KL 786
Cdd:cd03259 110 RVRELLEL-------------VGLEGLL-NRYPH----------ELSGGQQQRVALARALAREPSLLLLDEPLSALDaKL 165
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 124805679 787 SENIIN--KALIKYMKdKTTIIFTHRL-DLLNYVDYIGVIEEGQIIQFD 832
Cdd:cd03259 166 REELREelKELQRELG-ITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-469 |
2.39e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 89.52 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIINMYGGKEESLkyltNEIYKTVLLIIGI----STFSFFRIYFIETSIEKITRRLR 277
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL----GLLLGLALLLLGAyllrALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 278 THFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHlsfGIRNFISAL--IGGICA--LHISPRNLFQSfLLPVSG 353
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIAD---GIPQGITNVltLVGVAIilFSINPKLALLT-LIPIPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 354 CLLIGTTYAKFVKKISVLKQEKLSScidfASEKIH-NISNVRLL---NGESYEKKEFINYLEDVYKIGKKHSLVKSGNHF 429
Cdd:cd18778 153 LALGAWLYSKKVRPRYRKVREALGE----LNALLQdNLSGIREIqafGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124805679 430 LFFSIISLFLLHLIYYGNYLIAHKFINTGDLFSLIMY-SLF 469
Cdd:cd18778 229 LMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYlGLF 269
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
523-840 |
3.81e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.09 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYdntkdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVP 602
Cdd:PRK10790 340 RIDIDNVSFAY--------------RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-EGEIRLDGRP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPFLFNLTVRENLmypykayeemlkeqirlieqnqgafinminnentkkekndddnTINTYD 682
Cdd:PRK10790 405 LSSLSHSVLRQGVAMVQQDPVVLADTFLANV-------------------------------------------TLGRDI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 683 SEQDInkndmkntyeiytflLKELQKVQeeiKNNLSSDKMKNIYNDLhideflknhfnydnmnvGVNGTSLSGGQKQRIY 762
Cdd:PRK10790 442 SEEQV---------------WQALETVQ---LAELARSLPDGLYTPL-----------------GEQGNNLSVGQKQLLA 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 763 LAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
524-841 |
4.92e-19 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 91.50 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYdntkdninaninnERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTT----ILNLLTKKNDLnaSGEICVG 599
Cdd:COG1123 5 LEVRDLSVRY-------------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI--SGEVLLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 600 NVPINKINSAVLRSIVGVITQDPF--LFNLTVREnlmypykayeemlkeQIRLIEQNQGafinminnentkkekndddnt 677
Cdd:COG1123 70 GRDLLELSEALRGRRIGMVFQDPMtqLNPVTVGD---------------QIAEALENLG--------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 678 intydseqdINKNDMKntyeiytfllkelqkvqeeiknnlssDKMKNIYNDLHIDEFLKNHFNydnmnvgvngtSLSGGQ 757
Cdd:COG1123 114 ---------LSRAEAR--------------------------ARVLELLEAVGLERRLDRYPH-----------QLSGGQ 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 758 KQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDK-TTIIF-THRLDL-LNYVDYIGVIEEGQIIQFDKR 834
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLiTHDLGVvAEIADRVVVMDDGRIVEDGPP 227
|
....*..
gi 124805679 835 QSVLQKP 841
Cdd:COG1123 228 EEILAAP 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
524-828 |
6.05e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 87.07 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTT----ILNLLTKkndlnASGEICVG 599
Cdd:COG1121 7 IELENLTVSYGGRP---------------VLEDVSLTIPPGEFVAIVGPNGAGKSTllkaILGLLPP-----TSGTVRLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 600 NVPINKinsavLRSIVGVITQ----DPfLFNLTVRENLM---YPYKayeemlkeqirlieqnqGAFINMinnenTKKEKn 672
Cdd:COG1121 67 GKPPRR-----ARRRIGYVPQraevDW-DFPITVRDVVLmgrYGRR-----------------GLFRRP-----SRADR- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 673 dddntintydseqdinkndmkntyeiytfllkelQKVQEEIKnnlssdkmkniynDLHIDEFLKNHFNydnmnvgvngtS 752
Cdd:COG1121 118 ----------------------------------EAVDEALE-------------RVGLEDLADRPIG-----------E 139
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINkALIKYMKDK-TTIIF-THRLD-LLNYVDYIGVIEEGQI 828
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALY-ELLRELRREgKTILVvTHDLGaVREYFDRVLLLNRGLV 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
524-841 |
6.70e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.40 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLN----ASGEICVG 599
Cdd:COG1117 12 IEVRNLNVYYGDKQ---------------ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarVEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 600 NVPIN--KINSAVLRSIVGVITQDPFLFNLTVRENLMYPYKayeemlkeqirlieqnqgafINMINnentkkekndddnt 677
Cdd:COG1117 77 GEDIYdpDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLR--------------------LHGIK-------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 678 intydseqdiNKNDMKNTYEiytfllKELQKVQ--EEIKNNLSSdkmkniyndlhideflknhfnydnmnvgvNGTSLSG 755
Cdd:COG1117 123 ----------SKSELDEIVE------ESLRKAAlwDEVKDRLKK-----------------------------SALGLSG 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 756 GQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIInKALIKYMKDKTTIIF-TH------RLDllnyvDYIGVIEEGQI 828
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EELILELKKDYTIVIvTHnmqqaaRVS-----DYTAFFYLGEL 231
|
330
....*....|...
gi 124805679 829 IQFDKRQSVLQKP 841
Cdd:COG1117 232 VEFGPTEQIFTNP 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
523-829 |
7.40e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 85.30 E-value: 7.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNtkdninaniNNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT-KKNDLNASGEICVGNV 601
Cdd:cd03213 3 TLSFRNLTVTVKS---------SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGVSGEVLINGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINsavLRSIVGVITQDPFLF-NLTVRENLMYpykayeemlkeqirlieqnqgafinminnentkkekndddntint 680
Cdd:cd03213 74 PLDKRS---FRKIIGYVPQDDILHpTLTVRETLMF--------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfllkelqkvqeeiknnlsSDKMKniyndlhideflknhfnydnmnvgvngtSLSGGQKQR 760
Cdd:cd03213 106 --------------------------------------AAKLR----------------------------GLSGGERKR 119
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFT-HRL--DLLNYVDYIGVIEEGQII 829
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSiHQPssEIFELFDKLLLLSQGRVI 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
545-829 |
1.86e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.02 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 545 NNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKK--NDLNASGEICVGNVPINKinsAVLRSIVGVITQ-D 621
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQdD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 622 PFLFNLTVRENLmypykayeemlkeqirlieqnqgAFINMINNENTKKEKNDddntintydseqdinkndmknTYEIYTF 701
Cdd:cd03234 91 ILLPGLTVRETL-----------------------TYTAILRLPRKSSDAIR---------------------KKRVEDV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 LLKELqkvqeeiknnlssdkmkniyNDLHIdeflknhfnyDNMNVgvngTSLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:cd03234 127 LLRDL--------------------ALTRI----------GGNLV----KGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124805679 782 SLDKLSENIINKALIKYMKDKTTIIFT-H--RLDLLNYVDYIGVIEEGQII 829
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
517-838 |
2.96e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.81 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 517 LKSNNFSITFHNVSFSYDNtkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT---KKNdlnaS 593
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPN-------------SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTgllKPQ----S 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 594 GEICVGNVPINKINSAVLRSIVGVITQDPflfnltvrenlmypykayeemlkeqirlieQNQgaFINMinnentkkeknd 673
Cdd:PRK13632 64 GEIKIDGITISKENLKEIRKKIGIIFQNP------------------------------DNQ--FIGA------------ 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 674 ddntintyDSEQDInkndmkntyeiyTFLLKelqkvqeeiKNNLSSDKMKNIYNDL----HIDEFLKNHFNYdnmnvgvn 749
Cdd:PRK13632 100 --------TVEDDI------------AFGLE---------NKKVPPKKMKDIIDDLakkvGMEDYLDKEPQN-------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 750 gtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAL--IKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQ 827
Cdd:PRK13632 143 ---LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEAILADKVIVFSEGK 219
|
330
....*....|.
gi 124805679 828 IIQFDKRQSVL 838
Cdd:PRK13632 220 LIAQGKPKEIL 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
527-831 |
3.05e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 83.25 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 527 HNVSFSYdntkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPINKI 606
Cdd:cd03214 3 ENLSVGY---------------GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-SSGEILLDGKDLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 607 NSAVLRSIVGVITQdpflfnltvrenlmypykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqd 686
Cdd:cd03214 67 SPKELARKIAYVPQ------------------------------------------------------------------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 687 inkndmkntyeiytfLLKELQkvqeeiknnlssdkmkniyndlhIDEFLKNHFNydnmnvgvngtSLSGGQKQRIYLAQN 766
Cdd:cd03214 81 ---------------ALELLG-----------------------LAHLADRPFN-----------ELSGGERQRVLLARA 111
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 767 LIKNNKILILDEPTSSLDklseniINKAL--------IKYMKDKTTIIFTHRLDL-LNYVDYIGVIEEGQIIQF 831
Cdd:cd03214 112 LAQEPPILLLDEPTSHLD------IAHQIellellrrLARERGKTVVMVLHDLNLaARYADRVILLKDGRIVAQ 179
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
526-820 |
6.84e-18 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 82.97 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 526 FHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTT----ILNLLTKkndlnASGEICVGNV 601
Cdd:cd03235 2 VEDLTVSYGGHP---------------VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLKP-----TSGSIRVFGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKInsavlRSIVGVITQD---PFLFNLTVRENLM---YPYKayeemlkeqirlieqnqGAFINMinnenTKKEKnddd 675
Cdd:cd03235 62 PLEKE-----RKRIGYVPQRrsiDRDFPISVRDVVLmglYGHK-----------------GLFRRL-----SKADK---- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 ntintydseqdinkndmkntyeiytfllkelQKVQEEIKnnlssdkmkniynDLHIDEFLKNHFnydnmnvgvngTSLSG 755
Cdd:cd03235 111 -------------------------------AKVDEALE-------------RVGLSELADRQI-----------GELSG 135
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 756 GQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLD-LLNYVDYI 820
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVvTHDLGlVLEYFDRV 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
549-841 |
9.69e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 549 NKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLN----ASGEICVG--NVPINKINSAVLRSIVGVITQDP 622
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtITGSIVYNghNIYSPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 623 FLFNLTVRENLMYpykayeemlkeqirlieqnqGAFINMInnentkkekndddntintydseqdinkndmkntyeiytfl 702
Cdd:PRK14239 96 NPFPMSIYENVVY--------------------GLRLKGI---------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 703 lKELQKVQEEIKNNLssdKMKNIYNDLhideflKNHFnYDNmnvgvnGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSS 782
Cdd:PRK14239 116 -KDKQVLDEAVEKSL---KGASIWDEV------KDRL-HDS------ALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 783 LDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
524-841 |
2.03e-17 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 82.24 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNINAninnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTIL---NLLTKKNdlnaSGEICVGN 600
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTA-----------LKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLERPT----SGSVLVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 601 VPINKINSAVLRSI---VGVITQDpflFNL----TVRENLMYPYKAYEEMLKEQIRLIEQnqgafinminnentkkeknd 673
Cdd:cd03258 67 TDLTLLSGKELRKArrrIGMIFQH---FNLlssrTVFENVALPLEIAGVPKAEIEERVLE-------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 674 ddntintydseqdinkndmkntyeiytfLLKELqkvqeeiknNLSsDKMKNiyndlhideflknhfnYDnmnvgvngTSL 753
Cdd:cd03258 124 ----------------------------LLELV---------GLE-DKADA----------------YP--------AQL 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInkALIKYMKDK---TTIIFTHRLDLLNYV-DYIGVIEEGQI 828
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDpETTQSIL--ALLRDINRElglTIVLITHEMEVVKRIcDRVAVMEKGEV 219
|
330
....*....|...
gi 124805679 829 IQFDKRQSVLQKP 841
Cdd:cd03258 220 VEEGTVEEVFANP 232
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
202-467 |
2.28e-17 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 83.61 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIINMY-----GGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIETSIEKITRRL 276
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 277 RTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFlihLSFGIRNFISA---LIGGICA-LHISPRnLFQSFLLPVS 352
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQA---LSQSLTQLISSiltIVGTLIMmLYISPL-LTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 353 GCLLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVkSGnhfLFF 432
Cdd:cd18547 157 LSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY-SG---LLM 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124805679 433 SIISlFLLHLIY-----YGNYLIAHKFINTGDLFSLIMYS 467
Cdd:cd18547 233 PIMN-FINNLGYvlvavVGGLLVINGALTVGVIQAFLQYS 271
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
204-467 |
6.34e-17 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 82.06 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 204 FAMFCLIASSLGQMIFPMCISKIINmYGGKEESLKYltneIYKTVLLIIGISTFSFF----RIYFIETSIEKITRRLRTH 279
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIID-EGIANGDLSY----ILRTGLLMLLLALLGLIagilAGYFAAKASQGFGRDLRKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 280 FFEKVLNQDVHFFNKQKTGELINRLSNDIeisskFLIH--LSFGIRNFISA---LIGGIC-ALHISPRnlfQSFLLPVSG 353
Cdd:cd18548 78 LFEKIQSFSFAEIDKFGTSSLITRLTNDV-----TQVQnfVMMLLRMLVRApimLIGAIImAFRINPK---LALILLVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 354 CLLIGTTY--AKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLF 431
Cdd:cd18548 150 PILALVVFliMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLM 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 124805679 432 FSIISLFLLHLIYYGNYLIAHKFINTGDLFSLIMYS 467
Cdd:cd18548 230 MLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYL 265
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
524-843 |
6.89e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 80.81 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYdntkdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDL--NASGEICVGNV 601
Cdd:cd03295 1 IEFENVTKRY--------------GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI---NRLiePTSGEIFIDGE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSIVGVITQDPFLF-NLTVREN-------LMYPYKAYEEMLKEQIRLIeqnqgafinminnentkkeknd 673
Cdd:cd03295 64 DIREQDPVELRRKIGYVIQQIGLFpHMTVEENialvpklLKWPKEKIRERADELLALV---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 674 ddntintydseqdinkndmkntyeiytfllkelqkvqeeiknNLSSDKMKNIYNDlhideflknhfnydnmnvgvngtSL 753
Cdd:cd03295 122 ------------------------------------------GLDPAEFADRYPH-----------------------EL 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD--KTTIIFTHRLD-LLNYVDYIGVIEEGQIIQ 830
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDeAFRLADRIAIMKNGEIVQ 216
|
330
....*....|...
gi 124805679 831 FDKRQSVLQKPCP 843
Cdd:cd03295 217 VGTPDEILRSPAN 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
527-829 |
8.91e-17 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 79.61 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 527 HNVSFSYdntkdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNvpiNKI 606
Cdd:cd03226 3 ENISFSY--------------KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-ESSGSILLNG---KPI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 607 NSAVLRSIVGVITQDP--FLFNLTVRENLMYPYKayeemlkeqirlieqnqgafinminnentkkekndddntiNTYDSE 684
Cdd:cd03226 65 KAKERRKSIGYVMQDVdyQLFTDSVREELLLGLK----------------------------------------ELDAGN 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 685 QDINKndmkntyeiytfLLKelqkvqeeiknnlssdkmkniynDLHIDEFLKNHfnydnmnvgvnGTSLSGGQKQRIYLA 764
Cdd:cd03226 105 EQAET------------VLK-----------------------DLDLYALKERH-----------PLSLSGGQKQRLAIA 138
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 765 QNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLL-NYVDYIGVIEEGQII 829
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIViTHDYEFLaKVCDRVLLLANGAIV 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
523-841 |
1.06e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.45 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTkdninaninnernkkFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlnA------SGEI 596
Cdd:COG3842 5 ALELENVSKRYGDV---------------TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI-------AgfetpdSGRI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVG-----NVPINKinsavlRSIvGVITQDPFLF-NLTVRENLMYPykayeemLKEQirlieqnqgafinminnentkke 670
Cdd:COG3842 63 LLDgrdvtGLPPEK------RNV-GMVFQDYALFpHLTVAENVAFG-------LRMR----------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 671 kndddntintydseqDINKNDMKntyeiytfllkelQKVQEEIKnnlssdkMkniyndLHIDEFLKNHfnydnmnvgvnG 750
Cdd:COG3842 106 ---------------GVPKAEIR-------------ARVAELLE-------L------VGLEGLADRY-----------P 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIIN--KALIKymKDKTTIIF-TH-RLDLLNYVDYIGVIEE 825
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaKLREEMREelRRLQR--ELGITFIYvTHdQEEALALADRIAVMND 211
|
330
....*....|....*.
gi 124805679 826 GQIIQFDKRQSVLQKP 841
Cdd:COG3842 212 GRIEQVGTPEEIYERP 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
524-840 |
1.16e-16 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 80.72 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPI 603
Cdd:cd03288 20 IKIHDLCVRYEN-------------NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-FDGKIVIDGIDI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAVLRSIVGVITQDPFLFNLTVRENLmypykayeemlkeqirlieqnqgafinminnentkkekndddntintyDS 683
Cdd:cd03288 86 SKLPLHTLRSRLSIILQDPILFSGSIRFNL------------------------------------------------DP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 684 EQDINKNDMKNTYEIytfllKELQKVQEEIKNNLssdkmkniynDLHIDEflknhfnydnmnvgvNGTSLSGGQKQRIYL 763
Cdd:cd03288 118 ECKCTDDRLWEALEI-----AQLKNMVKSLPGGL----------DAVVTE---------------GGENFSVGQRQLFCL 167
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 764 AQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
550-843 |
2.63e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 79.30 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTK--KNDlnaSGEICVGNVPINKINSAvlRSIVGVITQDPFLF-N 626
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfiKPD---SGKILLNGKDITNLPPE--KRDISYVPQNYALFpH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 627 LTVRENLMYpykayeemlkeqirlieqnqgafiNMINNENTKKEKNDddntintydseqdinkndmkntyeiytfllkel 706
Cdd:cd03299 86 MTVYKNIAY------------------------GLKKRKVDKKEIER--------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 707 qkvqeeiknnlssdKMKNIYNDLHIDEFLKNhfnydnmnvgvNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-K 785
Cdd:cd03299 109 --------------KVLEIAEMLGIDHLLNR-----------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDvR 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124805679 786 LSENIIN--KALIKymKDKTTII-FTHRL-DLLNYVDYIGVIEEGQIIQFDKRQSVLQKPCP 843
Cdd:cd03299 164 TKEKLREelKKIRK--EFGVTVLhVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
524-829 |
4.11e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 79.40 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlNA-----SGEICV 598
Cdd:TIGR04520 1 IEVENVSFSYPE-------------SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLL------NGlllptSGKVTV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 GNvpINKINSAVL---RSIVGVITQDPflfnltvrenlmypykayeemlkeqirlieQNQgaFINMInnentkkeknddd 675
Cdd:TIGR04520 62 DG--LDTLDEENLweiRKKVGMVFQNP------------------------------DNQ--FVGAT------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 ntintydseqdinkndmkntyeiytfllkelqkVQEEI-----KNNLSSDKMKNIYND----LHIDEFLKN--HFnydnm 744
Cdd:TIGR04520 95 ---------------------------------VEDDVafgleNLGVPREEMRKRVDEalklVGMEDFRDRepHL----- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 745 nvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSeniiNKALIKYMK------DKTTIIFTHRLDLLNYVD 818
Cdd:TIGR04520 137 --------LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG----RKEVLETIRklnkeeGITVISITHDMEEAVLAD 204
|
330
....*....|.
gi 124805679 819 YIGVIEEGQII 829
Cdd:TIGR04520 205 RVIVMNKGKIV 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
554-840 |
1.29e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.71 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENL 633
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 634 MyPYKayeemlkeqirlieqnqgafinminnentkkEKNDDDntintydseqdinkndmkntyeiytfLLKELQKVqeei 713
Cdd:PLN03130 1334 D-PFN-------------------------------EHNDAD--------------------------LWESLERA---- 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 714 knnlssdkmkniyndlHI-DEFLKNHFNYDnMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIIN 792
Cdd:PLN03130 1352 ----------------HLkDVIRRNSLGLD-AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124805679 793 KALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:PLN03130 1415 KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
553-841 |
1.54e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 78.56 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTT----ILNLLtkKNDLNASGEICVGNVPINKINSAVLRSI----VGVITQDPFL 624
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLL--PPPGITSGEILFDGEDLLKLSEKELRKIrgreIQMIFQDPMT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 625 -FN--LTVRENLMYPYKAYEEMLKEQI--RLIEqnqgafinminnentkkekndddntintydseqdinkndmkntyeiy 699
Cdd:COG0444 98 sLNpvMTVGDQIAEPLRIHGGLSKAEAreRAIE----------------------------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 700 tfLLKELqkvqeeiknNLSSDkmkniyndlhiDEFLKN--HfnydnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILD 777
Cdd:COG0444 131 --LLERV---------GLPDP-----------ERRLDRypH-------------ELSGGMRQRVMIARALALEPKLLIAD 175
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 778 EPTSSLDKLSE-NIINkaLIKYMKDK--TTIIF-THRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:COG0444 176 EPTTALDVTIQaQILN--LLKDLQRElgLAILFiTHDLGVVAEIaDRVAVMYAGRIVEEGPVEELFENP 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
524-841 |
1.89e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 76.51 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPI 603
Cdd:cd03300 1 IELENVSKFYGGFV---------------ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-SGEILLDGKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 604 NKINSAvlRSIVGVITQDPFLF-NLTVRENLMYPYKayeemlkeqirlieqnqgafinminnenTKKEKNDDdntintyd 682
Cdd:cd03300 65 TNLPPH--KRPVNTVFQNYALFpHLTVFENIAFGLR----------------------------LKKLPKAE-------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 683 seqdinkndmkntyeiytfllkelqkVQEEIKNNLSSDKMKNiYNDLHIDEflknhfnydnmnvgvngtsLSGGQKQRIY 762
Cdd:cd03300 107 --------------------------IKERVAEALDLVQLEG-YANRKPSQ-------------------LSGGQQQRVA 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 763 LAQNLIKNNKILILDEPTSSLD-KLSENIinKALIKYMKDK--TTIIF-TH-RLDLLNYVDYIGVIEEGQIIQFDKRQSV 837
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDlKLRKDM--QLELKRLQKElgITFVFvTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
....
gi 124805679 838 LQKP 841
Cdd:cd03300 219 YEEP 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
539-830 |
2.89e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 75.41 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 539 NINANINnERNKKFALKnVSFFLPHNKsVAIVGKSGSGKTTILNLLT--KKNDlnaSGEICVGNVPI----NKINSAVLR 612
Cdd:cd03297 1 MLCVDIE-KRLPDFTLK-IDFDLNEEV-TGIFGASGAGKSTLLRCIAglEKPD---GGTIVLNGTVLfdsrKKINLPPQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 613 SIVGVITQDPFLF-NLTVRENLMYPYKAYEEMlkeqirlieqnqgafinminnentkkekndddntintydseqdinknd 691
Cdd:cd03297 75 RKIGLVFQQYALFpHLNVRENLAFGLKRKRNR------------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 692 mkntyeiytfllKELQKVQEeiknnlssdkmknIYNDLHIDEFLKNHFNydnmnvgvngtSLSGGQKQRIYLAQNLIKNN 771
Cdd:cd03297 107 ------------EDRISVDE-------------LLDLLGLDHLLNRYPA-----------QLSGGEKQRVALARALAAQP 150
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124805679 772 KILILDEPTSSLDKLSENIINKALIKYMKD--KTTIIFTHRLDLLNYV-DYIGVIEEGQIIQ 830
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQY 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
552-840 |
2.99e-15 |
|
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: 80.76 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 552 FALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRE 631
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-SAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 632 NLMyPYKAYEEMlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmkntyEIYTFLlkELQkvqe 711
Cdd:TIGR00957 1379 NLD-PFSQYSDE-----------------------------------------------------EVWWAL--ELA---- 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 712 eiknnlssdkmkniyndlHIDEFLKNHFNYDNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENII 791
Cdd:TIGR00957 1399 ------------------HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 124805679 792 NKALIKYMKDKTTIIFTHRLD-LLNYVDYIgVIEEGQIIQFDKRQSVLQK 840
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNtIMDYTRVI-VLDKGEVAEFGAPSNLLQQ 1509
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
520-840 |
4.80e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 520 NNFSITFHNVSFSYdntkdninaninnERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVG 599
Cdd:PRK13648 4 KNSIIVFKNVSFQY-------------QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIFYN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 600 NVPINKINSAVLRSIVGVITQDPflfnltvrenlmypykayeemlkeqirlieQNQgaFInminnentkkekndddNTIN 679
Cdd:PRK13648 70 NQAITDDNFEKLRKHIGIVFQNP------------------------------DNQ--FV----------------GSIV 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 680 TYDseqdinkndmkntyeiytfllkelqkVQEEIKNNL-SSDKMKNIYNDLHIDEFLKNHFNYDNmnvgvngTSLSGGQK 758
Cdd:PRK13648 102 KYD--------------------------VAFGLENHAvPYDEMHRRVSEALKQVDMLERADYEP-------NALSGGQK 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 759 QRIYLAQNLIKNNKILILDEPTSSLDKLSE----NIINKalIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKR 834
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARqnllDLVRK--VKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
....*.
gi 124805679 835 QSVLQK 840
Cdd:PRK13648 227 TEIFDH 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
524-832 |
5.24e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 75.48 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNtkdninaninnernKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDLNA--SGEICVGNV 601
Cdd:COG3638 3 LELRNLSKRYPG--------------GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCL---NGLVEptSGEILVDGQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSI---VGVITQDPFLF-NLTVRENLMYPYKAYEEMLKeqirlieqnqgAFINMInnentkkekndddnt 677
Cdd:COG3638 66 DVTALRGRALRRLrrrIGMIFQQFNLVpRLSVLTNVLAGRLGRTSTWR-----------SLLGLF--------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 678 intydSEQDINKndmkntyeiytfLLKELQKVqeeiknnlssdkmkniyndlHIDEFLknhfnydNMNVGvngtSLSGGQ 757
Cdd:COG3638 120 -----PPEDRER------------ALEALERV--------------------GLADKA-------YQRAD----QLSGGQ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 758 KQRIYLAQNLIKNNKILILDEPTSSLD-KLSENI------INKAlikymkDKTTIIFT-HRLDL-LNYVDYIGVIEEGQI 828
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDpKTARQVmdllrrIARE------DGITVVVNlHQVDLaRRYADRIIGLRDGRV 225
|
....
gi 124805679 829 IqFD 832
Cdd:COG3638 226 V-FD 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
523-841 |
6.08e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.04 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlnA------SGEI 596
Cdd:COG3839 3 SLELENVSKSYGGVE---------------ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI-------AgledptSGEI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVGNVPINKInSAVLRSIvGVITQDPFLF-NLTVRENLMYPykayeemLKeqirlieqNQGAfinminnentkkeknddd 675
Cdd:COG3839 61 LIGGRDVTDL-PPKDRNI-AMVFQSYALYpHMTVYENIAFP-------LK--------LRKV------------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 ntintydSEQDINKndmkntyeiytfllkelqKVQE--EIknnlssdkmkniyndLHIDEFL----KNhfnydnmnvgvn 749
Cdd:COG3839 106 -------PKAEIDR------------------RVREaaEL---------------LGLEDLLdrkpKQ------------ 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 750 gtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInkALIKYMKDK---TTIIFTHrlDllnYV------DY 819
Cdd:COG3839 134 ---LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaKLRVEMR--AEIKRLHRRlgtTTIYVTH--D---QVeamtlaDR 203
|
330 340
....*....|....*....|..
gi 124805679 820 IGVIEEGQIIQFDKRQSVLQKP 841
Cdd:COG3839 204 IAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
549-838 |
6.12e-15 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 75.41 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 549 NKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKINSAVLRSI---VGVITQDPFLF 625
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-SGSILLEGTDITKLRGKKLRKLrrrIGMIFQHYNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 626 -NLTVRENLMYPYKAYEemlkeqirlieqnqgAFINMINNENTKKEKNDddntintydseqdinkndmkntyeiytfLLK 704
Cdd:TIGR02315 92 eRLTVLENVLHGRLGYK---------------PTWRSLLGRFSEEDKER----------------------------ALS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 705 ELQKVQEEIKNNLSSDKmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:TIGR02315 129 ALERVGLADKAYQRADQ-------------------------------LSGGQQQRVAIARALAQQPDLILADEPIASLD 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 785 KLSENIINKALIKYMKDK--TTIIFTHRLDL-LNYVDYIGVIEEGQIIqFDKRQSVL 838
Cdd:TIGR02315 178 PKTSKQVMDYLKRINKEDgiTVIINLHQVDLaKKYADRIVGLKAGEIV-FDGAPSEL 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
524-809 |
8.08e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 75.13 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNINAninnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkknDLNA--SGEICVGNV 601
Cdd:COG1116 8 LELRGVSKRFPTGGGGVTA-----------LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKptSGEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVlrsivGVITQDPFLFN-LTVRENLMYPYKAyeemlkeqirlieqnQGAfinminnenTKKEKNDddntint 680
Cdd:COG1116 74 PVTGPGPDR-----GVVFQEPALLPwLTVLDNVALGLEL---------------RGV---------PKAERRE------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkmkniyndlHIDEFLKNhfnydnmnVGVNG------TSLS 754
Cdd:COG1116 118 -------------------------------------------------RARELLEL--------VGLAGfedaypHQLS 140
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 755 GGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKY-MKDKTTIIF-TH 809
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFvTH 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
519-848 |
2.34e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.45 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 519 SNNFSITFHNVSFSYDNTKdninaninnernkKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTK--KNDLNASGEI 596
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSK-------------KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGllLPDDNPNSKI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVGNVPINKINSAVLRSIVGVITQDPflfnltvrenlmypykayeemlkeqirlieqnqgafinminnentkkeknddDN 676
Cdd:PRK13640 68 TVDGITLTAKTVWDIREKVGIVFQNP----------------------------------------------------DN 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 677 TINTYDSEQDInkndmkntyeiyTFLLKELQkvqeeiknnLSSDKMKNIYNDLHIDEFLKNHFNYDNMNvgvngtsLSGG 756
Cdd:PRK13640 96 QFVGATVGDDV------------AFGLENRA---------VPRPEMIKIVRDVLADVGMLDYIDSEPAN-------LSGG 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 757 QKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDK--TTIIFTHRLDLLNYVDYIGVIEEGQIIQFDKR 834
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
330
....*....|....
gi 124805679 835 QSVLQKPcPILKKI 848
Cdd:PRK13640 228 VEIFSKV-EMLKEI 240
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-494 |
2.54e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 74.47 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMcISKII----NMYGGKEESLKYLtneiYKTVLLIIGIST----FSFFRIYFIETSIEKIT 273
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPY-LTKILiddvLIQLGPGGNTSLL----LLLVLGLAGAYVlsalLGILRGRLLARLGERIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 274 RRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLI-HLSFGIRNFISALIGGICALHISPR-NLFqsFLLPV 351
Cdd:cd18563 76 ADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSdGLPDFLTNILMIIGIGVVLFSLNWKlALL--VLIPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 352 SgCLLIGTTYakFVKKISVL------KQEKLSSCIdfaSEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGkkhslVKS 425
Cdd:cd18563 154 P-LVVWGSYF--FWKKIRRLfhrqwrRWSRLNSVL---NDTLPGIRVVKAFGQEKREIKRFDEANQELLDAN-----IRA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 426 GNHFLFFSIISLFLLHLI-----YYGNYLIAHKFINTGDLFSLIMY-SLFCGSgIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18563 223 EKLWATFFPLLTFLTSLGtlivwYFGGRQVLSGTMTLGTLVAFLSYlGMFYGP-LQWLSRLNNWITRALTSAERI 296
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
543-841 |
3.84e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.28 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDL----NASGEICVGNVPIN--KINSAVLRSIVG 616
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfRVEGKVTFHGKNLYapDVDPVEVRRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 617 VITQDPFLFNLTVRENLMYpykayeemlkeqirlieqnqGAfinminnentkkekndddnTINTYdseqdinKNDMKNTY 696
Cdd:PRK14243 95 MVFQKPNPFPKSIYDNIAY--------------------GA-------------------RINGY-------KGDMDELV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 697 EiytfllKELQK--VQEEIKnnlssDKMKNiyndlhideflknhfnydnmnvgvNGTSLSGGQKQRIYLAQNLIKNNKIL 774
Cdd:PRK14243 129 E------RSLRQaaLWDEVK-----DKLKQ------------------------SGLSLSGGQQQRLCIARAIAVQPEVI 173
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 775 ILDEPTSSLDKLSENIINKaLIKYMKDKTTI-IFTHRLDLLNYV-DYI---------GVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEE-LMHELKEQYTIiIVTHNMQQAARVsDMTaffnvelteGGGRYGYLVEFDRTEKIFNSP 250
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
204-494 |
3.85e-14 |
|
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: 74.24 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 204 FAMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYLTNE-----------------IYKTVLLIIGISTF--SFFRIYF 264
Cdd:cd18558 3 VGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSglnssagpfekleeemtLYAYYYLIIGAIVLitAYIQGSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 265 IETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDI-EISSKFLIHLSFGIRNfISALIGGICALHISPRNL 343
Cdd:cd18558 83 WGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVsKINEGIGDKIGVIFQN-IATFGTGFIIGFIRGWKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 344 fQSFLLPVSGCL-LIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSL 422
Cdd:cd18558 162 -TLVILAISPVLgLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124805679 423 VKSGNHFLFFSIISLFLLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGIQGMMHAIGDIQKCLGSCSKV 494
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
742-826 |
5.77e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 71.98 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 742 DNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINKALIKYMKD--KTTIIFTHRLDLLNYVD 818
Cdd:cd03290 130 DQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHAD 209
|
....*...
gi 124805679 819 YIGVIEEG 826
Cdd:cd03290 210 WIIAMKDG 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
549-841 |
8.89e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.39 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 549 NKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTK-----KNDLNASGEICVGNVPINKINSAVLRSIVGVITQDPF 623
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 624 LF-NLTVRENLMYPYKAYEemLKEQirlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfl 702
Cdd:PRK14246 101 PFpHLSIYDNIAYPLKSHG--IKEK------------------------------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 703 lKELQKVQEEiknnlsSDKMKNIYNDLHideflknhfnyDNMNVgvNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSS 782
Cdd:PRK14246 124 -REIKKIVEE------CLRKVGLWKEVY-----------DRLNS--PASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 783 LDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
524-848 |
1.80e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILN----LLTKKndlnaSGEICVG 599
Cdd:COG4604 2 IEIKNVSKRYGGKV---------------VLDDVSLTIPKGGITALIGPNGAGKSTLLSmisrLLPPD-----SGEVLVD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 600 NVPINKINSAVLRSIVGVITQDPFL-FNLTVRENLM---YPYkayeemlkeqirlieqNQGafinminnentkKEKNDDD 675
Cdd:COG4604 62 GLDVATTPSRELAKRLAILRQENHInSRLTVRELVAfgrFPY----------------SKG------------RLTAEDR 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 NTINTYdseqdinkndmkntyeIYTFLLKELQkvqeeiknnlssdkmkniynDLHIDEflknhfnydnmnvgvngtsLSG 755
Cdd:COG4604 114 EIIDEA----------------IAYLDLEDLA--------------------DRYLDE-------------------LSG 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 756 GQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInKALIKYMKD--KTTIIFTHrlDlLN----YVDYIGVIEEGQI 828
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMM-KLLRRLADElgKTVVIVLH--D-INfascYADHIVAMKDGRV 214
|
330 340
....*....|....*....|
gi 124805679 829 IQFDKRQSVLQKpcPILKKI 848
Cdd:COG4604 215 VAQGTPEEIITP--EVLSDI 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
524-829 |
1.84e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.42 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNINAninnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTT---ILNLL---TkkndlnaSGEIC 597
Cdd:COG1135 2 IELENLSKTFPTKGGPVTA-----------LDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLerpT-------SGSVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 598 VGNVPINKINSAVLRSI---VGVITQDpflFNL----TVRENLMYPYKaYEEMLKEQIRlieqnqgafinminnentkke 670
Cdd:COG1135 64 VDGVDLTALSERELRAArrkIGMIFQH---FNLlssrTVAENVALPLE-IAGVPKAEIR--------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 671 kndddntintydseqdinkndmkntyeiytfllkelQKVQEEIKN-NLsSDKMKNiYNDlhideflknhfnydnmnvgvn 749
Cdd:COG1135 119 ------------------------------------KRVAELLELvGL-SDKADA-YPS--------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 750 gtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENI------INKALikymkdKTTIIF-THRLDllnyV---- 817
Cdd:COG1135 140 --QLSGGQKQRVGIARALANNPKVLLCDEATSALDpETTRSIldllkdINREL------GLTIVLiTHEMD----Vvrri 207
|
330
....*....|...
gi 124805679 818 -DYIGVIEEGQII 829
Cdd:COG1135 208 cDRVAVLENGRIV 220
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
199-466 |
1.87e-13 |
|
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: 71.71 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 199 RKYLGFAMFCLIASSLGQMIFPMCISKIINmyggkeeslKYLTNEIYKTVLLIIGI--------STFSFFRIYFIETSIE 270
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIID---------DLLPSKNLRLILIIGAIllalyilrTLLNYFVTYWGHVMGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 271 KITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHlsfGIRN-FISA--LIGGICAL-HISPR-NLFQ 345
Cdd:cd18549 72 RIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHH---GPEDlFISIitIIGSFIILlTINVPlTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 346 SFLLPVsgCLLIGTTYAKFVKKISVLKQEKLSsciDFASEKIHNISNVRLL---NGESYEKKEFInyledvyKIGKKHSL 422
Cdd:cd18549 149 FALLPL--MIIFTIYFNKKMKKAFRRVREKIG---EINAQLEDSLSGIRVVkafANEEYEIEKFD-------EGNDRFLE 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124805679 423 VKSGNHF---LFFSIISLF--LLHL--IYYGNYLIAHKFINTGDLFSLIMY 466
Cdd:cd18549 217 SKKKAYKamaYFFSGMNFFtnLLNLvvLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
551-829 |
2.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 71.62 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 551 KFALKNVSFFLPHNKSVAIVGKSGSGKTTI---LNLLTKKNdlnaSGEICVGNVPI--NKINSAVLRSIVGVITQdpflf 625
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLiqhLNGLLKPT----SGKIIIDGVDItdKKVKLSDIRKKVGLVFQ----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 626 nltvrenlmYP-YKAYEEMLKEQIRLIEQNQGAfinminnentkkekndddntintydSEQDINKndmkntyeiytfllk 704
Cdd:PRK13637 91 ---------YPeYQLFEETIEKDIAFGPINLGL-------------------------SEEEIEN--------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 705 elqKVQEEIKN-NLSSDKMKNiyndlhideflKNHFNydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSL 783
Cdd:PRK13637 122 ---RVKRAMNIvGLDYEDYKD-----------KSPFE------------LSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124805679 784 D-KLSENIINKalIKYMKDK---TTIIFTHRL-DLLNYVDYIGVIEEGQII 829
Cdd:PRK13637 176 DpKGRDEILNK--IKELHKEynmTIILVSHSMeDVAKLADRIIVMNKGKCE 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
524-831 |
3.22e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.53 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPhNKSVAIVGKSGSGKTTILNLLT--KKNDlnaSGEICVGNV 601
Cdd:cd03264 1 LQLENLTKRYGKKR---------------ALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILAtlTPPS---SGTIRIDGQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAvLRSIVGVITQDPFLF-NLTVRENLMYPykayeemlkeqirlieqnqgAFINMINNentKKEKNDDDNTInt 680
Cdd:cd03264 62 DVLKQPQK-LRRRIGYLPQEFGVYpNFTVREFLDYI--------------------AWLKGIPS---KEVKARVDEVL-- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydseQDINKNDMKNtyeiytfllkelqkvqeeiknnlssDKMKniyndlhideflknhfnydnmnvgvngtSLSGGQKQR 760
Cdd:cd03264 116 ----ELVNLGDRAK-------------------------KKIG----------------------------SLSGGMRRR 138
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124805679 761 IYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRL-DLLNYVDYIGVIEEGQIIQF 831
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVeDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
549-828 |
3.40e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 69.48 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 549 NKKF----ALKNVSFFLPHNKSVAIVGKSGSGKTTIL---NLLTKKNdlnaSGEICVGNVPIN--KINSAVLRSIVGVIT 619
Cdd:cd03262 7 HKSFgdfhVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrciNLLEEPD----SGTIIIDGLKLTddKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 620 QDPFLF-NLTVRENLMYPykayeemlkeQIRLieqnqgafinminnentkkekndddntintydseQDINKNDMKNTYEi 698
Cdd:cd03262 83 QQFNLFpHLTVLENITLA----------PIKV----------------------------------KGMSKAEAEERAL- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 699 ytfllKELQKVQEEiknnlssDKmKNIYNDlhideflknhfnydnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILDE 778
Cdd:cd03262 118 -----ELLEKVGLA-------DK-ADAYPA-----------------------QLSGGQQQRVAIARALAMNPKVMLFDE 161
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 779 PTSSLDKlseNIINKALiKYMKD-----KTTIIFTHRLDLLNYV-DYIGVIEEGQI 828
Cdd:cd03262 162 PTSALDP---ELVGEVL-DVMKDlaeegMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
524-829 |
4.53e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDL--NASGEICVGNV 601
Cdd:PRK13635 6 IRVEHISFRYPDAA-------------TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLL---NGLllPEAGTITVGGM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PINKINSAVLRSIVGVITQDP---FLfNLTVRENLMYpykAYEemlkeqirlieqNQGafinminnentkkekndddnti 678
Cdd:PRK13635 70 VLSEETVWDVRRQVGMVFQNPdnqFV-GATVQDDVAF---GLE------------NIG---------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 679 ntydseqdINKNDMkntyeiytfllkeLQKVQEEIKNnlssdkmkniyndLHIDEFLKNHfnydnmnvgvnGTSLSGGQK 758
Cdd:PRK13635 112 --------VPREEM-------------VERVDQALRQ-------------VGMEDFLNRE-----------PHRLSGGQK 146
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 759 QRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInkALIKYMKDK---TTIIFTHRLDLLNYVDYIGVIEEGQII 829
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDpRGRREVL--ETVRQLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
554-841 |
5.23e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.94 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDL----NASGEICVGNVPINKINSAVLRSIVGVITQDPF-LFNLT 628
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 629 VRENLMYPYKayeemlkeqirlieqnqgafINMInnentkkekndddntintydseqdinkndMKNTYEIYTFLLKELQK 708
Cdd:PRK14247 99 IFENVALGLK--------------------LNRL-----------------------------VKSKKELQERVRWALEK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 709 VQ--EEIKNNLssdkmkniyndlhideflknhfnydnmnvGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKL 786
Cdd:PRK14247 130 AQlwDEVKDRL-----------------------------DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPE 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 787 SENIINKALIKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK14247 181 NTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
523-840 |
5.68e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNtkdninaninneRNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlnasgeicVGNVP 602
Cdd:PLN03232 614 AISIKNGYFSWDS------------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-------------LGELS 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPFLFNLTVRENLMYPYKayeemlkeqirlieqnqgafinminnentkkekndddntintYD 682
Cdd:PLN03232 669 HAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSD------------------------------------------FE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 683 SEQDINKNDMkntyeiyTFLLKELqkvqeeiknnlssdkmkniyndlhidEFLKNHfnyDNMNVGVNGTSLSGGQKQRIY 762
Cdd:PLN03232 707 SERYWRAIDV-------TALQHDL--------------------------DLLPGR---DLTEIGERGVNISGGQKQRVS 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 763 LAQNLIKNNKILILDEPTSSLD-KLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYI-----GVI-EEGQIIQFDKRQ 835
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDaHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIilvseGMIkEEGTFAELSKSG 830
|
....*
gi 124805679 836 SVLQK 840
Cdd:PLN03232 831 SLFKK 835
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
523-828 |
5.92e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.23 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTkdninaninnerNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlnasgeicVGNVP 602
Cdd:PLN03130 614 AISIKNGYFSWDSK------------AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-------------LGELP 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPFLFNLTVRENLMY--PYKA--YEemlkeqiRLIEqnqgafinminnentkkekndddnti 678
Cdd:PLN03130 669 PRSDASVVIRGTVAYVPQVSWIFNATVRDNILFgsPFDPerYE-------RAID-------------------------- 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 679 ntydseqdinkndmkntyeiytflLKELQKvqeeiknnlssdkmkniynDLhidEFLKNHfnyDNMNVGVNGTSLSGGQK 758
Cdd:PLN03130 716 ------------------------VTALQH-------------------DL---DLLPGG---DLTEIGERGVNISGGQK 746
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124805679 759 QRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQI 828
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALDaHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
567-833 |
6.23e-13 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 68.73 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 567 VAIVGKSGSGKTTILNLLTKkNDLNASGEICVGNVpiNKINSAVLRSIVGVITQDPFLF-NLTVRENLMYPykayeemLK 645
Cdd:TIGR01277 27 VAIMGPSGAGKSTLLNLIAG-FIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFaHLTVRQNIGLG-------LH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 646 EQIRLieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfllkelqkvqeeikNNLSSDKMKNI 725
Cdd:TIGR01277 97 PGLKL----------------------------------------------------------------NAEQQEKVVDA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 726 YNDLHIDEFLKNHFNydnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInkALIKYM---KD 801
Cdd:TIGR01277 113 AQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDpLLREEML--ALVKQLcseRQ 179
|
250 260 270
....*....|....*....|....*....|...
gi 124805679 802 KTTIIFTHRL-DLLNYVDYIGVIEEGQIIQFDK 833
Cdd:TIGR01277 180 RTLLMVTHHLsDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
553-815 |
1.14e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 67.82 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKnDLNASGEICVGNVPINKINS---AVLRSIVGVITQD-PFLFNLT 628
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-ELPTSGTIRVNGQDVSDLRGraiPYLRRKIGVVFQDfRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 629 VRENLMYPYKAyeemlkeqirlieqnqgafinminnentkkekndddntinTYDSEQDINKndmkntyeiytfllkelqK 708
Cdd:cd03292 95 VYENVAFALEV----------------------------------------TGVPPREIRK------------------R 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 709 VQEEIKNNLSSDKMKNIYNDlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSE 788
Cdd:cd03292 117 VPAALELVGLSHKHRALPAE------------------------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
250 260
....*....|....*....|....*...
gi 124805679 789 NIINKALIKYMKDKTTIIF-THRLDLLN 815
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVaTHAKELVD 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
543-830 |
1.20e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.37 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDL-NASGEIcVGNVPINKINSAVLR-SIVGviTQ 620
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYePTSGRI-IYHVALCEKCGYVERpSKVG--EP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 621 DPflfnltvrenlmypyKAYEEMLKEQIRLIEQNQGAFINMinnenTKKEKNDDDNTINTYDsEQDINKNDMKNTYEIYT 700
Cdd:TIGR03269 82 CP---------------VCGGTLEPEEVDFWNLSDKLRRRI-----RKRIAIMLQRTFALYG-DDTVLDNVLEALEEIGY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 701 FLLKELQKVQEEIKNNLSSDKMKNIYNDLhideflknhfnydnmnvgvngtslSGGQKQRIYLAQNLIKNNKILILDEPT 780
Cdd:TIGR03269 141 EGKEAVGRAVDLIEMVQLSHRITHIARDL------------------------SGGEKQRVVLARQLAKEPFLFLADEPT 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124805679 781 SSLDKLSENIINKALIKYMKDK--TTIIFTHRLDLL-NYVDYIGVIEEGQIIQ 830
Cdd:TIGR03269 197 GTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIeDLSDKAIWLENGEIKE 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
554-784 |
1.28e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNAsgeicvGNVPINKinsavlRSIVGVITQDPFLF-NLTVREN 632
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS------GEVSIPK------GLRIGYLPQEPPLDdDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 633 LMYPYKAYEEMLKEqIRLIEQnQGAFINMINNENTKKEknDDDNTINTYDSEQDINKndmkntyeiytfLLKELqkvqee 712
Cdd:COG0488 82 VLDGDAELRALEAE-LEELEA-KLAEPDEDLERLAELQ--EEFEALGGWEAEARAEE------------ILSGL------ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124805679 713 iknnlssdkmkNIYNDLHideflknhfnydNMNVGvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:COG0488 140 -----------GFPEEDL------------DRPVS----ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
546-829 |
1.50e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 546 NERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNASGEicvGNVPIN--KINSAVLRSIVGVITQDP- 622
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS---GSVLLNgmPIDAKEMRAISAYVQQDDl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 623 FLFNLTVRENLMypykaYEEMLKEQIRLieqnqgafinminnenTKKEKndddntintydseqdinkndmkntyeiytfl 702
Cdd:TIGR00955 110 FIPTLTVREHLM-----FQAHLRMPRRV----------------TKKEK------------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 703 lkeLQKVQEEIKN-NLSSDKmkniyndlhideflknhfnydNMNVGVNGT--SLSGGQKQRIYLAQNLIKNNKILILDEP 779
Cdd:TIGR00955 138 ---RERVDEVLQAlGLRKCA---------------------NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124805679 780 TSSLDKLSENIINKALIKY-MKDKTTIIFTHR--LDLLNYVDYIGVIEEGQII 829
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQpsSELFELFDKIILMAEGRVA 246
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
543-832 |
3.08e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 66.51 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKInSAVLRSIvGVITQDP 622
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGGRDVTDL-PPKDRDI-AMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 623 FLF-NLTVRENLMYPykayeemLKEQIRlieqnqgafinminnentkkekndddntintydSEQDINKndmkntyeiytf 701
Cdd:cd03301 82 ALYpHMTVYDNIAFG-------LKLRKV---------------------------------PKDEIDE------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 llkelqKVQEEIKNnlssdkmkniyndLHIDEFLKNHfnydnmnvgvnGTSLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:cd03301 110 ------RVREVAEL-------------LQIEHLLDRK-----------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 782 SLD-KLSENIinKALIK--YMKDKTTIIF-TH-RLDLLNYVDYIGVIEEGQIIQFD 832
Cdd:cd03301 160 NLDaKLRVQM--RAELKrlQQRLGTTTIYvTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
752-829 |
3.29e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.21 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIInKALIKYMKDK-TTIIF-THRLDLlnyV----DYIGVIEE 825
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELL-KDVIRELAAKgTTVIFsSHQMEL---VeelcDRIVIINK 204
|
....
gi 124805679 826 GQII 829
Cdd:COG4152 205 GRKV 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
550-829 |
7.34e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNdLNASGEICVGNVPINKINSAVL-RSIVGVITQDPFLFNLT 628
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL-TPQSGTVFLGDKPISMLSSRQLaRRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 629 VRENLMY---PYKAYEEMLkeqirlieqnqgafinminnentkkekNDDDNtintydseqdinkndmkntyeiytfllke 705
Cdd:PRK11231 93 VRELVAYgrsPWLSLWGRL---------------------------SAEDN----------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 706 lQKVQEEIknnlssdkmkniyNDLHIDEFLKNHFnydnmnvgvngTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDk 785
Cdd:PRK11231 117 -ARVNQAM-------------EQTRINHLADRRL-----------TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD- 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124805679 786 LSENIINKALIKYMKD--KTTIIFTHRLD-LLNYVDYIGVIEEGQII 829
Cdd:PRK11231 171 INHQVELMRLMRELNTqgKTVVTVLHDLNqASRYCDHLVVLANGHVM 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
553-841 |
8.28e-12 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 66.51 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDL--NASGEICVGNVPINKINSAVLRSI----VGVITQDPFLF- 625
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCI---NRLiePTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 626 NLTVRENLMYPYkayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfllkE 705
Cdd:cd03294 116 HRTVLENVAFGL-------------------------------------------------------------------E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 706 LQKVQEEIKNNLSSDKMKNI----YNDLHIDEflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:cd03294 129 VQGVPRAEREERAAEALELVglegWEHKYPDE-------------------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 782 SLDKLSENIINKALIKYMKD-KTTIIF-THRLD-LLNYVDYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAElQKTIVFiTHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
742-840 |
1.24e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 742 DNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK-LSENIINKAL--IKYMKDKTTIIFTHRLDLLNYVD 818
Cdd:TIGR00957 750 DRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVD 829
|
90 100
....*....|....*....|..
gi 124805679 819 YIGVIEEGQIIQFDKRQSVLQK 840
Cdd:TIGR00957 830 VIIVMSGGKISEMGSYQELLQR 851
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
548-841 |
1.27e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.98 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 548 RNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTI---LNLLTKKndlnASGEICVGNVPINKINSAVLRSIVGVITQDPfl 624
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLfrhFNGILKP----TSGSVLIRGEPITKENIREVRKFVGLVFQNP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 625 fnltvrenlmypykayeemlkeqirlieqnqgafinminnentkkeknddDNTINTYDSEQDInkndmkntyeiyTFLLK 704
Cdd:PRK13652 88 --------------------------------------------------DDQIFSPTVEQDI------------AFGPI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 705 ELQKVQEEIKNNLSSD-KMKNIYndlHIDEFLKNHfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSL 783
Cdd:PRK13652 106 NLGLDEETVAHRVSSAlHMLGLE---ELRDRVPHH--------------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 784 DKLSEniinKALIKYMKD-----KTTIIF-THRLDLL-NYVDYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK13652 169 DPQGV----KELIDFLNDlpetyGMTVIFsTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
554-818 |
1.28e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTIL----NLLTKKndlnaSGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTV 629
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLkivaSLISPT-----SGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 630 RENLMYPYkayeemlkeQIRlieqNQgafinminnentkkekndddntintydseqdinKNDMKNtyeiytfLLKELQKv 709
Cdd:PRK10247 98 YDNLIFPW---------QIR----NQ---------------------------------QPDPAI-------FLDDLER- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 710 qeeiknnlssdkmkniyndlhideflknhFNYDNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSEN 789
Cdd:PRK10247 124 -----------------------------FALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
250 260 270
....*....|....*....|....*....|.
gi 124805679 790 IINKALIKYMKDKTTIIF--THRLDLLNYVD 818
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLwvTHDKDEINHAD 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
547-817 |
1.62e-11 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 64.42 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 547 ERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKkndLN--ASGEICVGNVPINKINSAVLRSIVGVITQDPFL 624
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG---LLppSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 625 FNLTVRENLmypykayeemlkeqirlieqnqgAFINMINNENTKKEKNDDdntintydseqdinkndmkntyeiytfLLK 704
Cdd:COG4133 88 PELTVRENL-----------------------RFWAALYGLRADREAIDE---------------------------ALE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 705 ELqkvqeeiknNLSSdkmkniyndlHIDEFLKNhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:COG4133 118 AV---------GLAG----------LADLPVRQ---------------LSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 124805679 785 KLSENIINKALIKYMKDKTTIIFT----------HRLDLLNYV 817
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLTthqplelaaaRVLDLGDFK 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
538-841 |
1.85e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 538 DNINANINNERNKkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNAS----GEICV--GNVPINKINSAVL 611
Cdd:PRK14267 6 ETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEarveGEVRLfgRNIYSPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 612 RSIVGVITQDPFLF-NLTVRENLMYPYKaYEEMLKEQIRLIEQNQGAFinminnentKKekndddntintydseqdinkn 690
Cdd:PRK14267 84 RREVGMVFQYPNPFpHLTIYDNVAIGVK-LNGLVKSKKELDERVEWAL---------KK--------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 691 dmkntyeiytfllkelQKVQEEIKNNLSsDKMKNiyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKN 770
Cdd:PRK14267 133 ----------------AALWDEVKDRLN-DYPSN----------------------------LSGGQRQRLVIARALAMK 167
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124805679 771 NKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
553-829 |
2.05e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNdLNASGEICVGNVPINKINSAVLRSIVGVITQDP--FLFNLTVR 630
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 631 ENLmypykayeemlkeqirlieqnqgAFiNMINNENTKKEkndddntintydseqdinkndmkntyeiytfllkelqkVQ 710
Cdd:PRK13647 99 DDV-----------------------AF-GPVNMGLDKDE--------------------------------------VE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 711 EEIKNNLSSDKMKNiyndlhidefLKNHFNYdnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENI 790
Cdd:PRK13647 117 RRVEEALKAVRMWD----------FRDKPPY----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124805679 791 INKALIKYMKD-KTTIIFTHRLDL-LNYVDYIGVIEEGQII 829
Cdd:PRK13647 177 LMEILDRLHNQgKTVIVATHDVDLaAEWADQVIVLKEGRVL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
553-784 |
2.18e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.40 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTT----ILNLLTkkndlnASGEICVGNVPINKINSAVLRSI---VGVITQDPF-L 624
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP------SEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDPFgS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 625 FN--LTVRENLMYPYKAYEEMLKEQIRlieqnqgafinminnentkkekndddntintydsEQDInkndmkntyeiytfl 702
Cdd:COG4172 375 LSprMTVGQIIAEGLRVHGPGLSAAER----------------------------------RARV--------------- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 703 LKELQKVqeeiknNLSSDkMKNIYndlhIDEFlknhfnydnmnvgvngtslSGGQKQRIYLAQNLIKNNKILILDEPTSS 782
Cdd:COG4172 406 AEALEEV------GLDPA-ARHRY----PHEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
..
gi 124805679 783 LD 784
Cdd:COG4172 456 LD 457
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
523-841 |
2.59e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlnA------SGEI 596
Cdd:COG1118 2 SIEVRNISKRFGSFT---------------LLDDVSLEIASGELVALLGPSGSGKTTLLRII-------AgletpdSGRI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVGNVPINkINSAVLRSIVGVITQDPFLF-NLTVRENLMY-----PYKayeemlKEQIRlieqnqgafinminnentkke 670
Cdd:COG1118 60 VLNGRDLF-TNLPPRERRVGFVFQHYALFpHMTVAENIAFglrvrPPS------KAEIR--------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 671 kndddntintydseqdinkndmkntyeiytfllkelQKVQEEIKnnlssdkmkniynDLHIDEfLKNHFNydnmnvgvng 750
Cdd:COG1118 112 ------------------------------------ARVEELLE-------------LVQLEG-LADRYP---------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-----KLSENiinkaLIKYMKD--KTTIIFTH-RLDLLNYVDYIGV 822
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkELRRW-----LRRLHDElgGTTVFVTHdQEEALELADRVVV 206
|
330
....*....|....*....
gi 124805679 823 IEEGQIIQFDKRQSVLQKP 841
Cdd:COG1118 207 MNQGRIEQVGTPDEVYDRP 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
220-826 |
3.82e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 220 PMCISKIINMYGGKEeslkylTNEIYKTVLLIIGISTFSFFRIYFIETSI---EKITRRLRTHFF----EKVLNQDVHFF 292
Cdd:TIGR01271 100 PLLLGRIIASYDPFN------APEREIAYYLALGLCLLFIVRTLLLHPAIfglHHLGMQMRIALFsliyKKTLKLSSRVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 293 NKQKTGELINRLSNDIeisSKFLIHLSFGIRNFISALIGGICALHIspRNLFQSFLLPVSGCL-LIGTTYAKFVKKISVL 371
Cdd:TIGR01271 174 DKISTGQLVSLLSNNL---NKFDEGLALAHFVWIAPLQVILLMGLI--WELLEVNGFCGLGFLiLLALFQACLGQKMMPY 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 372 KQE---KLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVK--SGNHFLFFSIISLFLlhliyyg 446
Cdd:TIGR01271 249 RDKragKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRyfYSSAFFFSGFFVVFL------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 447 nYLIAHKFINTGDL---FSLIMYSLFCGSGIQGMMHaiGDIQKCLGSCSKVLQIiklpdnnfHNYWNKTSIDFLKSN--N 521
Cdd:TIGR01271 322 -SVVPYALIKGIILrriFTTISYCIVLRMTVTRQFP--GAIQTWYDSLGAITKI--------QDFLCKEEYKTLEYNltT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 522 FSITFHNVSFSYD----------NTKDNINANINNERNKKFA---------LKNVSFFLPHNKSVAIVGKSGSGKTTIL- 581
Cdd:TIGR01271 391 TEVEMVNVTASWDegigelfekiKQNNKARKQPNGDDGLFFSnfslyvtpvLKNISFKLEKGQLLAVAGSTGSGKSSLLm 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 582 ----NLLTKKNDLNASGEICVGnvpinkinsavlrsivgviTQDPFLFNLTVRENLMYPYkayeemlkeqirlieqnqga 657
Cdd:TIGR01271 471 mimgELEPSEGKIKHSGRISFS-------------------PQTSWIMPGTIKDNIIFGL-------------------- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 658 finminnentkkekndddntinTYDSEQdinkndmkntyeiYTFLLKELQkvqeeiknnlssdkmkniyndlhIDEFLKN 737
Cdd:TIGR01271 512 ----------------------SYDEYR-------------YTSVIKACQ-----------------------LEEDIAL 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 738 HFNYDNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSE-NIINKALIKYMKDKTTIIFTHRLDLLNY 816
Cdd:TIGR01271 534 FPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKK 613
|
650
....*....|
gi 124805679 817 VDYIGVIEEG 826
Cdd:TIGR01271 614 ADKILLLHEG 623
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
524-841 |
5.02e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYdntkdniNANINNERNkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNlltkknDLNA-----SGEICV 598
Cdd:PRK13634 3 ITFQKVEHRY-------QYKTPFERR---ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQ------HLNGllqptSGTVTI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 GNVPI-----NKiNSAVLRSIVGVITQDPflfnltvrENLMYpykayEEMLKEQIRLIEQNQGAfinminnentkkeknd 673
Cdd:PRK13634 67 GERVItagkkNK-KLKPLRKKVGIVFQFP--------EHQLF-----EETVEKDICFGPMNFGV---------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 674 ddntintydSEQDinkndmkntyeiytfllkELQKVQEEIKnnlssdkmkniynDLHIDEFLKNHFNYDnmnvgvngtsL 753
Cdd:PRK13634 117 ---------SEED------------------AKQKAREMIE-------------LVGLPEELLARSPFE----------L 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDK--TTIIFTHRL-DLLNYVDYIGVIEEGQIIQ 830
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMeDAARYADQIVVMHKGTVFL 226
|
330
....*....|.
gi 124805679 831 FDKRQSVLQKP 841
Cdd:PRK13634 227 QGTPREIFADP 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
550-829 |
5.75e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKF----ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT---KKNdlnaSGEICVGNVPINKIN-SAVLRSIVGVITQD 621
Cdd:COG1129 12 KSFggvkALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyQPD----SGEILLDGEPVRFRSpRDAQAAGIAIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 622 PFLF-NLTVRENLMypykayeemlkeqirlieqnqgafinmINNENTKKEKndddntintydseqdINKNDMkntYEIYT 700
Cdd:COG1129 88 LNLVpNLSVAENIF---------------------------LGREPRRGGL---------------IDWRAM---RRRAR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 701 FLLKELqkvqeeiknnlssdkmkniynDLHIDEflknhfnydNMNVGvngtSLSGGQKQRIYLAQNLIKNNKILILDEPT 780
Cdd:COG1129 123 ELLARL---------------------GLDIDP---------DTPVG----DLSVAQQQLVEIARALSRDARVLILDEPT 168
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124805679 781 SSLDKlSEniINK--ALIKYMKDK-TTIIF-THRLD-LLNYVDYIGVIEEGQII 829
Cdd:COG1129 169 ASLTE-RE--VERlfRIIRRLKAQgVAIIYiSHRLDeVFEIADRVTVLRDGRLV 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
753-829 |
9.02e-11 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 61.29 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSL-DKLSENIInkALIKYMKDK-TTIIF-THRLD-LLNYVDYIGVIEEGQI 828
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALtPAEVERLF--KVIRRLRAQgVAVIFiSHRLDeVFEIADRVTVLRDGRV 160
|
.
gi 124805679 829 I 829
Cdd:cd03216 161 V 161
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
735-828 |
1.04e-10 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 62.34 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 735 LKNHFNYDNMNvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDK--TTIIFTHRLD 812
Cdd:TIGR02982 131 LGDHLNYYPHN-------LSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQgcTILMVTHDNR 203
|
90
....*....|....*.
gi 124805679 813 LLNYVDYIGVIEEGQI 828
Cdd:TIGR02982 204 ILDVADRILQMEDGKL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
569-841 |
1.13e-10 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 63.67 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 569 IVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKInSAVLRSIvGVITQDPFLF-NLTVRENLMYPYKayeemlkeq 647
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-SGSIMLDGEDVTNV-PPHLRHI-NMVFQSYALFpHMTVEENVAFGLK--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 648 irlieqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfllkeLQKV-QEEIKnnlssDKMKNIY 726
Cdd:TIGR01187 69 ----------------------------------------------------------MRKVpRAEIK-----PRVLEAL 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 727 NDLHIDEFLKNHFnydnmnvgvngTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINKalIKYMKDK--- 802
Cdd:TIGR01187 86 RLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDkKLRDQMQLE--LKTIQEQlgi 152
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124805679 803 TTIIFTH-RLDLLNYVDYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:TIGR01187 153 TFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
523-841 |
1.23e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNtkdninaninNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTIL---NLLTKKndlnASGEICVG 599
Cdd:PRK13641 2 SIKFENVDYIYSP----------GTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLKP----SSGTITIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 600 NVPI-----NKiNSAVLRSIVGVITQDPF--LFNLTVRENLMYPYKayeemlkeqirlieqNQGAfinminNENTKKEKn 672
Cdd:PRK13641 68 GYHItpetgNK-NLKKLRKKVSLVFQFPEaqLFENTVLKDVEFGPK---------------NFGF------SEDEAKEK- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 673 dddntintydseqdinkndmkntyeiytfLLKELQKVQeeiknnlssdkmkniyndlhIDEFLKNHFNYDnmnvgvngts 752
Cdd:PRK13641 125 -----------------------------ALKWLKKVG--------------------LSEDLISKSPFE---------- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD-KTTIIFTHRL-DLLNYVDYIGVIEEGQIIQ 830
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMdDVAEYADDVLVLEHGKLIK 225
|
330
....*....|.
gi 124805679 831 FDKRQSVLQKP 841
Cdd:PRK13641 226 HASPKEIFSDK 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
548-841 |
1.26e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 62.93 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 548 RNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLL---TKKndlnASGEICVGNVPINKINSAVLRSIVGVITQDP-- 622
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLagiIEP----TSGEILINGHKLEYGDYKYRCKHIRMIFQDPnt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 623 -FLFNLTVREnlmypykayeeMLKEQIRLieqnqgafinminneNTKkekndddntintydseqdinkndmkntyeiytf 701
Cdd:COG4167 99 sLNPRLNIGQ-----------ILEEPLRL---------------NTD--------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 lLKELQKvQEEIKNNLssdKMKNIYNDlhideflknHFN-YDNMnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPT 780
Cdd:COG4167 120 -LTAEER-EERIFATL---RLVGLLPE---------HANfYPHM--------LSSGQKQRVALARALILQPKIIIADEAL 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 781 SSLD-KLSENIINKALIKYMKDKTTIIF-THRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:COG4167 178 AALDmSVRSQIINLMLELQEKLGISYIYvSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
743-829 |
1.32e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.77 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 743 NMNVGvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAlIKYMKDKTT--IIFTHRLDLLNYV--D 818
Cdd:cd03217 100 YVNEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-INKLREEGKsvLIITHYQRLLDYIkpD 173
|
90
....*....|.
gi 124805679 819 YIGVIEEGQII 829
Cdd:cd03217 174 RVHVLYDGRIV 184
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
753-838 |
1.77e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD--KTTIIFTHRLDLLNYV-DYIGVIEEGQII 829
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDVcDRAALMRDGKIV 507
|
....*....
gi 124805679 830 QFDKRQSVL 838
Cdd:TIGR03269 508 KIGDPEEIV 516
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
523-840 |
2.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYdntkdniNANINNERNkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkNDLN--ASGEICVGN 600
Cdd:PRK13649 2 GINLQNVSYTY-------QAGTPFEGR---ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL---NGLHvpTQGSVRVDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 601 VPI-----NK-INSavLRSIVGVITQDPflfnltvrENlmypyKAYEEMLKEQIRLIEQNQGafINMINNENTKKEKndd 674
Cdd:PRK13649 69 TLItstskNKdIKQ--IRKKVGLVFQFP--------ES-----QLFEETVLKDVAFGPQNFG--VSQEEAEALAREK--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 675 dntintydseqdinkndmkntyeiytfllKELQKVQEEIknnlssdkmkniyndlhideFLKNHFNydnmnvgvngtsLS 754
Cdd:PRK13649 129 -----------------------------LALVGISESL--------------------FEKNPFE------------LS 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 755 GGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRL-DLLNYVDYIGVIEEGQIIQFD 832
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLvTHLMdDVANYADFVYVLEKGKLVLSG 227
|
....*...
gi 124805679 833 KRQSVLQK 840
Cdd:PRK13649 228 KPKDIFQD 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
523-841 |
2.83e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnaSGEICV---- 598
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---------------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL--ESEVRVegrv 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 ----GNVPINKINSAVLRSIVGVITQDPFLFNLTVRENLMYPYKAYEEMLKEQIrlieqnqgafinminnentkkekndd 674
Cdd:PRK14258 70 effnQNIYERRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEI-------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 675 dntintydseQDINKNDMKNTyeiytfllkelqKVQEEIKNNLSSDKMKniyndlhideflknhfnydnmnvgvngtsLS 754
Cdd:PRK14258 124 ----------DDIVESALKDA------------DLWDEIKHKIHKSALD-----------------------------LS 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 755 GGQKQRIYLAQNLIKNNKILILDEPTSSLDKLS----ENIINKALIKymKDKTTIIFTHRLDLLNYV-DYIGVIEE---- 825
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLR--SELTMVIVSHNLHQVSRLsDFTAFFKGnenr 230
|
330
....*....|....*..
gi 124805679 826 -GQIIQFDKRQSVLQKP 841
Cdd:PRK14258 231 iGQLVEFGLTKKIFNSP 247
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-490 |
5.19e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 61.34 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 202 LGFAMFCLIASSLGQMIFPMCISKIIN--MYGGKEESLKYLtneiyktVLLIIGI----STFSFFRIYFIeTSI-EKITR 274
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDdaLPQGDLGLLVLL-------ALGMVAVavasALLGVVQTYLS-ARIgQGVMY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 275 RLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIE-ISSKFLIHLSFGIRNFISALIGGICALHISPR-NLFQSFLLPVS 352
Cdd:cd18550 73 DLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGgAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRlALLSLVLLPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 353 gcLLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIhNISN---VRLLNGESYEKKEFINYLEDVYKIGKKHSLVksgnHF 429
Cdd:cd18550 153 --VLPTRRVGRRRRKLTREQQEKLAELNSIMQETL-SVSGallVKLFGREDDEAARFARRSRELRDLGVRQALA----GR 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 430 LFFSIISLFL---LHLIY-YGNYLIAHKFINTGDLFSLIMY--SLFcgSGIQGMMHAIGDIQKCLGS 490
Cdd:cd18550 226 WFFAALGLFTaigPALVYwVGGLLVIGGGLTIGTLVAFTALlgRLY--GPLTQLLNIQVDLMTSLAL 290
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
523-585 |
5.82e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 5.82e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSY-------DNTKDNINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT 585
Cdd:COG1134 4 MIEVENVSKSYrlyhepsRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA 73
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
524-829 |
6.84e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNINAninnernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTIL---NLLTKKndlnASGEICVGN 600
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHA-----------LNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLERP----TSGRVLVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 601 VPINKINSAVLRSI---VGVITQDpflFNL----TVRENLMYPYKAyeemlkeqirlieqnqgafinminnENTKKEknd 673
Cdd:PRK11153 67 QDLTALSEKELRKArrqIGMIFQH---FNLlssrTVFDNVALPLEL-------------------------AGTPKA--- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 674 ddntintydseqDINKndmkntyeiytfllkelqKVQEEIKNNLSSDKMkniyndlhiDEFLKNhfnydnmnvgvngtsL 753
Cdd:PRK11153 116 ------------EIKA------------------RVTELLELVGLSDKA---------DRYPAQ---------------L 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLDK---------LSEniINKALikymkdKTTIIF-THRLDLLNYV-DYIGV 822
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPattrsilelLKD--INREL------GLTIVLiTHEMDVVKRIcDRVAV 213
|
....*..
gi 124805679 823 IEEGQII 829
Cdd:PRK11153 214 IDAGRLV 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
753-829 |
6.92e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 6.92e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLLN-YVDYIGVIEEGQII 829
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIsTHDVDLVPvYADKVYVMSDGKII 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
700-830 |
7.14e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.47 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 700 TFLLKELQKV-QEEIKNNLSSDKMKNIYNDLHIDE-FLKNhfnydNMNVGvngtsLSGGQKQRIYLAQNLIKNNKILILD 777
Cdd:COG0396 96 NFLRTALNARrGEELSAREFLKLLKEKMKELGLDEdFLDR-----YVNEG-----FSGGEKKRNEILQMLLLEPKLAILD 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 778 EPTSSLD-----KLSENIinKALIKymKDKTTIIFTHRLDLLNYV--DYIGVIEEGQIIQ 830
Cdd:COG0396 166 ETDSGLDidalrIVAEGV--NKLRS--PDRGILIITHYQRILDYIkpDFVHVLVDGRIVK 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
550-829 |
9.30e-10 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 59.76 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKF----ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKndLNA-SGEICVGNVPINKInSAVLRSIVGVI-T-QDP 622
Cdd:cd03219 8 KRFgglvALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPtSGSVLFDGEDITGL-PPHEIARLGIGrTfQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 623 FLF-NLTVRENLMypykayeemLKEQIRlieqnQGAFINMINNENTKKEKNDDdntintydseqdinkndmknTYEIYTF 701
Cdd:cd03219 85 RLFpELTVLENVM---------VAAQAR-----TGSGLLLARARREEREARER--------------------AEELLER 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 LlkELQKVQEEIknnlssdkmkniyndlhideflknhfnydnmnVGvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:cd03219 131 V--GLADLADRP--------------------------------AG----ELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 124805679 782 SL-DKLSENIINkaLIKYMKDK-TTIIFT-HRLDL-LNYVDYIGVIEEGQII 829
Cdd:cd03219 173 GLnPEETEELAE--LIRELRERgITVLLVeHDMDVvMSLADRVTVLDQGRVI 222
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
217-466 |
1.01e-09 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 60.51 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 217 MIFPMCISKII-NMYGGKEeslkYLTNEIYKTVLLIIGISTFSF---------FRIYFIETSIEKITRRLRTHFFEKVLN 286
Cdd:cd18554 16 LLLPLILKYIVdDVIQGSS----LTLDEKVYKLFTIIGIMFFIFlilrppveyYRQYFAQWIANKILYDIRKDLFDHLQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 287 QDVHFFNKQKTGELINRLSNDIEISSKFLIHLSFGIRNFISALIGGIC-ALHISPRNLFQS-FLLPVSGcLLIGTTYAKF 364
Cdd:cd18554 92 LSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICiMLVLNPKLTFVSlVIFPFYI-LAVKYFFGRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 365 vKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLFFSIISLFLLHLIY 444
Cdd:cd18554 171 -RKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIG 249
|
250 260
....*....|....*....|..
gi 124805679 445 YGNYLIAHKFINTGDLFSLIMY 466
Cdd:cd18554 250 FAAYLVIEGNLTVGTLVAFVGY 271
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
530-829 |
1.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 530 SFSYDNTKDNINANINNERNKKF-ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLlTKKNDLNASGEICVGN--VP--IN 604
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEFkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQL-TNGLIISETGQTIVGDyaIPanLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 605 KINSAV-LRSIVGVITQDPflfnltvrenlmyPYKAYEEMLKEQIRLIEQNQGAfinminnentkkekndddntintyds 683
Cdd:PRK13645 81 KIKEVKrLRKEIGLVFQFP-------------EYQLFQETIEKDIAFGPVNLGE-------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 684 eqdinknDMKNTYEIYTFLLKELQKVQEEIKnnlssdkmkniyndlhideflKNHFnydnmnvgvngtSLSGGQKQRIYL 763
Cdd:PRK13645 122 -------NKQEAYKKVPELLKLVQLPEDYVK---------------------RSPF------------ELSGGQKRRVAL 161
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 764 AQNLIKNNKILILDEPTSSLD-KLSENIINKAL-IKYMKDKTTIIFTHRLD-LLNYVDYIGVIEEGQII 829
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDpKGEEDFINLFErLNKEYKKRIIMVTHNMDqVLRIADEVIVMHEGKVI 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
248-626 |
1.20e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 61.74 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 248 VLLIIGISTFSFFRIyfiETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHLSFGIRNFis 327
Cdd:COG4615 58 LVLLLLSRLASQLLL---TRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSV-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 328 ALIGGiCAL---HISPrnlfQSFLLpVSGCLLIGT-TYAKFVKKI-----------SVLkQEKLSSCIDFASE-KIHNIS 391
Cdd:COG4615 133 ALVLG-CLAylaWLSP----PLFLL-TLVLLGLGVaGYRLLVRRArrhlrrareaeDRL-FKHFRALLEGFKElKLNRRR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 392 NVRLLNGEsyekkefinYLEDVYKIgkKHSLVKSGNHFLF---FSIISLFLL--HLIYYGNYLIAhkfINTGDLFSLIMY 466
Cdd:COG4615 206 RRAFFDED---------LQPTAERY--RDLRIRADTIFALannWGNLLFFALigLILFLLPALGW---ADPAVLSGFVLV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 467 SLFCGSGIQGMMHAIGDIQKCLGSCSKVLQIiKLPDNNFHNYWNKTSIDFLKSNNFSITFHNVSFSYDNTKDninaninn 546
Cdd:COG4615 272 LLFLRGPLSQLVGALPTLSRANVALRKIEEL-ELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDG-------- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 547 ERNkkFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkknDLNA--SGEICVGNVPINKINSAVLRSIVGVITQDPFL 624
Cdd:COG4615 343 DEG--FTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLT---GLYRpeSGEILLDGQPVTADNREAYRQLFSAVFSDFHL 417
|
..
gi 124805679 625 FN 626
Cdd:COG4615 418 FD 419
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
753-829 |
1.27e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 58.83 E-value: 1.27e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLLNYV-DYIGVIEEGQII 829
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEELcDRVLLLNKGRAV 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
551-841 |
1.48e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 551 KFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKND----LNASGEICVGNVPI-NKINSAVLRSIVGVITQDPFLF 625
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgYRYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 626 NLTVRENLMYPYKAYEEMLKEQIRLIEQNQgafinminnentkkekndddntintydseqdinkndmkntyeiytflLKE 705
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQAR-----------------------------------------------LTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 706 LqKVQEEIKNNLSSDKMKniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK 785
Cdd:PRK14271 147 V-GLWDAVKDRLSDSPFR-----------------------------LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 786 LSENIINKaLIKYMKDK-TTIIFTHRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK14271 197 TTTEKIEE-FIRSLADRlTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
751-841 |
1.49e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.01 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDkLSENIINKALIKYMKD--KTTIIFTHRLDL-LNYVDYIGVIEEGQ 827
Cdd:PRK09536 138 TSLSGGERQRVLLARALAQATPVLLLDEPTASLD-INHQVRTLELVRRLVDdgKTAVAAIHDLDLaARYCDELVLLADGR 216
|
90
....*....|....
gi 124805679 828 IIQFDKRQSVLQKP 841
Cdd:PRK09536 217 VRAAGPPADVLTAD 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
553-841 |
1.55e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 59.28 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT--KKNDlnaSGEICVGNVPINKINsaVLRSIVGVITQDPFLF-NLTV 629
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglERPD---SGTILFGGEDATDVP--VQERNVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 630 RENLMYPykayeemLKEQIRLIEQNqgafinminnENTKKEKNDDdntintydseqdinkndmkntyeiytfLLKELQKv 709
Cdd:cd03296 92 FDNVAFG-------LRVKPRSERPP----------EAEIRAKVHE---------------------------LLKLVQL- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 710 qeeiknnlssDKMKNIYNdlhideflknhfnydnmnvgvngTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSE 788
Cdd:cd03296 127 ----------DWLADRYP-----------------------AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDaKVRK 173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 789 NIinKALIKYMKDK---TTIIFTH-RLDLLNYVDYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:cd03296 174 EL--RRWLRRLHDElhvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
552-638 |
1.93e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 60.11 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 552 FALkNVSFFLPHNKSVAIVGKSGSGKTTILNL---LTKKndlnASGEICVG-----------NVPINKinsavlRSIvGV 617
Cdd:COG4148 14 FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP----DSGRIRLGgevlqdsargiFLPPHR------RRI-GY 81
|
90 100
....*....|....*....|..
gi 124805679 618 ITQDPFLF-NLTVRENLMYPYK 638
Cdd:COG4148 82 VFQEARLFpHLSVRGNLLYGRK 103
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
543-833 |
2.23e-09 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 58.56 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKndLN-ASGEICVGNVPINKINsavLRSIVGVITQD 621
Cdd:TIGR03740 5 NLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI--LRpTSGEIIFDGHPWTRKD---LHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 622 PFLFNLTVRENLmypyKAYEEMLKEQIRLIEQnqgaFINMINNENTKKEKNDDdntintydseqdinkndmkntyeiytf 701
Cdd:TIGR03740 80 PLYENLTARENL----KVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQ--------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 llkelqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:TIGR03740 125 ---------------------------------------------------FSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 782 SLDKLSENIINKaLIKYMKDK--TTIIFTHRL-DLLNYVDYIGVIEEGQIIQFDK 833
Cdd:TIGR03740 154 GLDPIGIQELRE-LIRSFPEQgiTVILSSHILsEVQQLADHIGIISEGVLGYQGK 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
524-838 |
2.44e-09 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 58.94 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTK--DNINANIN-NERnkkfalknvsfflphnksVAIVGKSGSGKTTILNLLTKKNDLNASGEICV-- 598
Cdd:COG1119 4 LELRNVTVRRGGKTilDDISWTVKpGEH------------------WAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 599 ---GNVPINKInsavlRSIVGVIT---QDPFLFNLTVRE-------NLMYPYKAYEEmlkEQIRLIEQnqgafinminne 665
Cdd:COG1119 66 errGGEDVWEL-----RKRIGLVSpalQLRFPRDETVLDvvlsgffDSIGLYREPTD---EQRERARE------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 666 ntkkekndddntintydseqdinkndmkntyeiytfLLKELqkvqeeiknnlssdkmkniyndlHIDEFLKNHFNydnmn 745
Cdd:COG1119 126 ------------------------------------LLELL-----------------------GLAHLADRPFG----- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 746 vgvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD-KTTIIF-THRL-DLLNYVDYIGV 822
Cdd:COG1119 142 ------TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLvTHHVeEIPPGITHVLL 215
|
330
....*....|....*.
gi 124805679 823 IEEGQIIQFDKRQSVL 838
Cdd:COG1119 216 LKDGRVVAAGPKEEVL 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
553-829 |
2.80e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 58.21 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILN----LLTKKndlnaSGEICVGNVPINKINS-AVLRSIVGVITQDPFLF-N 626
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKtimgLLPPR-----SGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 627 LTVRENLmypykayeEMlkeqirlieqnqGAfinminnentkkekndddntintYDSEQDINKNDMKNTYEIYTfLLKEL 706
Cdd:cd03224 90 LTVEENL--------LL------------GA-----------------------YARRRAKRKARLERVYELFP-RLKER 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 707 QKVQeeiknnlssdkmkniyndlhideflknhfnydnmnvgvnGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-K 785
Cdd:cd03224 126 RKQL---------------------------------------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLApK 166
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124805679 786 LSENIInkALIKYMKDK-TTIIFT-HRLDL-LNYVDYIGVIEEGQII 829
Cdd:cd03224 167 IVEEIF--EAIRELRDEgVTILLVeQNARFaLEIADRAYVLERGRVV 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
517-829 |
3.20e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 517 LKSNNFSITFhnvsfsydntkdniNANINNERNkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEI 596
Cdd:COG1101 2 LELKNLSKTF--------------NPGTVNEKR---ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-SGSI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVGNVPINKInSAVLRS-IVGVITQDPFL---FNLTVRENLmypykayeemlkeqirLIEQNQGAFINmINNENTKKEKn 672
Cdd:COG1101 64 LIDGKDVTKL-PEYKRAkYIGRVFQDPMMgtaPSMTIEENL----------------ALAYRRGKRRG-LRRGLTKKRR- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 673 dddntintydseqdinkndmkntyEIYTFLLKELqkvqeeiknNLSsdkmkniyndlhidefLKNHFNydnMNVGvngtS 752
Cdd:COG1101 125 ------------------------ELFRELLATL---------GLG----------------LENRLD---TKVG----L 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIIN--KALIKymKDK-TTIIFTHRL-DLLNYVDYIGVIEEGQ 827
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDpKTAALVLEltEKIVE--ENNlTTLMVTHNMeQALDYGNRLIMMHEGR 226
|
..
gi 124805679 828 II 829
Cdd:COG1101 227 II 228
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
539-635 |
3.42e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 539 NINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTK-KNDLNASGEICVGNVPINKinsAVLRSIVGV 617
Cdd:cd03232 8 NLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrKTAGVITGEILINGRPLDK---NFQRSTGYV 84
|
90
....*....|....*...
gi 124805679 618 ITQDPFLFNLTVRENLMY 635
Cdd:cd03232 85 EQQDVHSPNLTVREALRF 102
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
742-827 |
3.53e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.71 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 742 DNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSEN-IINKALIKYMKDKTTIIFTHRLDLLNYVDYI 820
Cdd:cd03291 149 DNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKI 228
|
....*..
gi 124805679 821 GVIEEGQ 827
Cdd:cd03291 229 LILHEGS 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
523-831 |
3.59e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTT---ILNLLtkknDLNASGEICVG 599
Cdd:COG4161 2 SIQLKNINCFYGSHQ---------------ALFDINLECPSGETLVLLGPSGAGKSSllrVLNLL----ETPDSGQLNIA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 600 NVPIN---KINSA---VLRSIVGVITQDPFLF-NLTVRENLmypykayeemLKEQIRLIEQNQgafinminnentkkekn 672
Cdd:COG4161 63 GHQFDfsqKPSEKairLLRQKVGMVFQQYNLWpHLTVMENL----------IEAPCKVLGLSK----------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 673 dddntintydseQDINKNDMKntyeiytfLLKELQkvqeeiknnlssdkmkniyndlhIDEFLK---NHfnydnmnvgvn 749
Cdd:COG4161 116 ------------EQAREKAMK--------LLARLR-----------------------LTDKADrfpLH----------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 750 gtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKDK--TTIIFTHRLDL----LNYVDYigv 822
Cdd:COG4161 142 ---LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpEITAQVVE--IIRELSQTgiTQVIVTHEVEFarkvASQVVY--- 213
|
....*....
gi 124805679 823 IEEGQIIQF 831
Cdd:COG4161 214 MEKGRIIEQ 222
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
248-486 |
3.76e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 59.00 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 248 VLLIIGISTFSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLsNDI----EISSKFLIHLsfgIR 323
Cdd:cd18570 49 ILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDAnkirEAISSTTISL---FL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 324 NFISALIGGICALHISPRnLFQSFLLPVSGCLLIGTTYAKFVKKI--SVLKQE-KLSSCIdfaSEKIHNISNVRLLNGES 400
Cdd:cd18570 125 DLLMVIISGIILFFYNWK-LFLITLLIIPLYILIILLFNKPFKKKnrEVMESNaELNSYL---IESLKGIETIKSLNAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 401 YEKKE----FINYLEDVYKIGKKhslvksGNHFLFFSII--SLFLLHLIYYGNYLIAHKFINTGDLFSLIMYSLFCGSGI 474
Cdd:cd18570 201 QFLKKiekkFSKLLKKSFKLGKL------SNLQSSIKGLisLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPI 274
|
250
....*....|..
gi 124805679 475 QGMMHAIGDIQK 486
Cdd:cd18570 275 ENLINLQPKIQE 286
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
746-828 |
4.78e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.56 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 746 VGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIE 824
Cdd:PTZ00243 776 IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDaHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALG 855
|
....
gi 124805679 825 EGQI 828
Cdd:PTZ00243 856 DGRV 859
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
752-829 |
5.82e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 56.99 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLLNYV-DYIGVIEEGQII 829
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFsTHIMQEVERLcDRVVVLHRGRVV 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
558-849 |
6.12e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 57.46 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 558 SFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlnA------SGEICVGNVPINKINSAvLRSiVGVITQDPFLFN-LTVR 630
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLI-------AgflppdSGRILWNGQDLTALPPA-ERP-VSMLFQENNLFPhLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 631 ENL---MYPykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdinknDMKntyeiytflLKELQ 707
Cdd:COG3840 90 QNIglgLRP------------------------------------------------------GLK---------LTAEQ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 708 KVQeeiknnlssdkmkniyndlhIDEFLKNhfnydnmnVGVNG------TSLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:COG3840 107 RAQ--------------------VEQALER--------VGLAGlldrlpGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 782 SLD-KLSENIInkALIKYMKDKT--TIIF-THRL-DLLNYVDYIGVIEEGQIIQFDKRQSVLQK-PCPILKKIL 849
Cdd:COG3840 159 ALDpALRQEML--DLVDELCRERglTVLMvTHDPeDAARIADRVLLVADGRIAADGPTAALLDGePPPALAAYL 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
553-829 |
8.44e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTI---LNLLTKKndlnASGEICVGNVPINKINSAV--LRSIVGVITQDPflfnl 627
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLfqnLNGILKP----SSGRILFDGKPIDYSRKGLmkLRESVGMVFQDP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 628 tvrenlmypykayeemlkeqirlieqnqgafinminnentkkeknddDNTINTYDSEQDInkndmknTYEIYTFLLKElQ 707
Cdd:PRK13636 92 -----------------------------------------------DNQLFSASVYQDV-------SFGAVNLKLPE-D 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 708 KVQEEIKNNLSSDKMkniyndlhidEFLKNHFNYdnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLS 787
Cdd:PRK13636 117 EVRKRVDNALKRTGI----------EHLKDKPTH----------CLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124805679 788 ENIINKALIKYMK--DKTTIIFTHRLDLLN-YVDYIGVIEEGQII 829
Cdd:PRK13636 177 VSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVI 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
752-814 |
1.02e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 55.70 E-value: 1.02e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLL 814
Cdd:NF040873 119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVvTHDLELV 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
753-827 |
1.06e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 54.76 E-value: 1.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYmkdKTTIIF-THRLDLLNYV-DYIGVIEEGQ 827
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY---PGTVILvSHDRYFLDQVaTKIIELEDGK 144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
551-811 |
1.19e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 551 KFALKNVSFFLPHNKSVAIVGKSGSGK-TTILNLLTKkndLNASGEICVGNVPINKINSAVL---RSIVGVITQDPFlFN 626
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKsTTGLALLRL---INSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN-SS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 627 LTVRENLmypykayEEMLKEQIRLIEqnqgafinminnentkkekndddntintydseqdinkndmkntyeiytfllKEL 706
Cdd:PRK15134 375 LNPRLNV-------LQIIEEGLRVHQ---------------------------------------------------PTL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 707 QKVQEEiknnlssDKMKNIYNDLHIDEFLKNHFNydnmnvgvngTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKL 786
Cdd:PRK15134 397 SAAQRE-------QQVIAVMEEVGLDPETRHRYP----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
|
250 260
....*....|....*....|....*
gi 124805679 787 SENIInKALIKYMKDKttiiftHRL 811
Cdd:PRK15134 460 VQAQI-LALLKSLQQK------HQL 477
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
544-830 |
1.27e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 56.74 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 544 INNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSI---VGVITQ 620
Cdd:TIGR02769 17 LFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEK-PAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 621 D-PFLFN--LTVRENLMYPYKAYEEMLK-EQIRLIEQnqgafinminnentkkekndddntintydseqdinkndmknty 696
Cdd:TIGR02769 96 DsPSAVNprMTVRQIIGEPLRHLTSLDEsEQKARIAE------------------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 697 eiytfLLKELqkvqeeiknNLSSDKMKNIyndlhideflknhfnydnmnvgvnGTSLSGGQKQRIYLAQNLIKNNKILIL 776
Cdd:TIGR02769 133 -----LLDMV---------GLRSEDADKL------------------------PRQLSGGQLQRINIARALAVKPKLIVL 174
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 777 DEPTSSLDKLSENIInKALIKYMKDKTTIIF---THRLDLLNYV-DYIGVIEEGQIIQ 830
Cdd:TIGR02769 175 DEAVSNLDMVLQAVI-LELLRKLQQAFGTAYlfiTHDLRLVQSFcQRVAVMDKGQIVE 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
553-784 |
1.36e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.43 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTT----ILNLLTKkndlnASGEICVGNVPINKINSAVLRSI---VGVITQDPF-- 623
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTlgrlLLRLEEP-----TSGEILFDGQDITGLSGRELRPLrrrMQMVFQDPYas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 624 LfN--LTVRENLMYPYKayeemlkeqirlieqnqgafinmINNENTKKEKNDddntintydseqdinkndmkNTYEIytf 701
Cdd:COG4608 108 L-NprMTVGDIIAEPLR-----------------------IHGLASKAERRE--------------------RVAEL--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 llkeLQKVQeeiknnLSSDkmkniyndlHID----EFlknhfnydnmnvgvngtslSGGQKQRIYLAQNLIKNNKILILD 777
Cdd:COG4608 141 ----LELVG------LRPE---------HADryphEF-------------------SGGQRQRIGIARALALNPKLIVCD 182
|
....*..
gi 124805679 778 EPTSSLD 784
Cdd:COG4608 183 EPVSALD 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
752-837 |
1.69e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.19 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD------------KLSENIinkalikymkdKTTIIF-THRLD-LLNYV 817
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellpyleRLAREI-----------NIPILYvSHSLDeILRLA 196
|
90 100
....*....|....*....|
gi 124805679 818 DYIGVIEEGQIIQFDKRQSV 837
Cdd:PRK11144 197 DRVVVLEQGKVKAFGPLEEV 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
552-841 |
2.08e-08 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 57.04 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 552 FALKnVSFFLPHNKSVAIVGKSGSGKTTILNL---LTKKndlnASGEICVGNVPIN----KINSAVLRSIVGVITQDPFL 624
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRP----DEGEIVLNGRTLFdsrkGIFLPPEKRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 625 F-NLTVRENLMYPYKayeemlkeqirlieqnqgafinminnentkkeKNDDDNTINTYDSeqdinkndmkntyeiytflL 703
Cdd:TIGR02142 87 FpHLSVRGNLRYGMK--------------------------------RARPSERRISFER-------------------V 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 704 KELqkvqeeiknnlssdkmkniyndLHIDEFLKNHFNydnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSL 783
Cdd:TIGR02142 116 IEL----------------------LGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 784 DKLSENIInkalIKYMKD-----KTTIIF-THRLD-LLNYVDYIGVIEEGQIIQFDKRQSVLQKP 841
Cdd:TIGR02142 163 DDPRKYEI----LPYLERlhaefGIPILYvSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
515-808 |
2.40e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 515 DFLKSNNFSITFHNVSFSYDNTKD---------NINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLT 585
Cdd:TIGR00956 731 EVLGSTDLTDESDDVNDEKDMEKEsgedifhwrNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 586 KKNDlnaSGEICVGNVPIN--KINSAVLRSIVGVITQDPFLFNLTVRENLMypYKAYeemlkeqIRLieqnqgafinmiN 663
Cdd:TIGR00956 811 ERVT---TGVITGGDRLVNgrPLDSSFQRSIGYVQQQDLHLPTSTVRESLR--FSAY-------LRQ------------P 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 664 NENTKKEKNDddntintydseqdinkndmkntYEIYTFLLKELQKVQEEIknnlssdkmkniyndlhideflknhfnydn 743
Cdd:TIGR00956 867 KSVSKSEKME----------------------YVEEVIKLLEMESYADAV------------------------------ 894
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 744 mnVGVNGTSLSGGQKQRIYLAQNLIKNNKILI-LDEPTSSLDKLSENIINKALIKYMKDKTTIIFT 808
Cdd:TIGR00956 895 --VGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCT 958
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
524-830 |
2.45e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTK--DNINANINNERnkkfalknvsfFLphnksvAIVGKSGSGKTTILNLLTKKNDLNaSGEI----- 596
Cdd:PRK09452 15 VELRGISKSFDGKEviSNLDLTINNGE-----------FL------TLLGPSGCGKTTVLRLIAGFETPD-SGRImldgq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVGNVPINKINsavlrsiVGVITQDPFLF-NLTVRENLmypykayeemlkeqirlieqnqgafinminnentkkeknddd 675
Cdd:PRK09452 77 DITHVPAENRH-------VNTVFQSYALFpHMTVFENV------------------------------------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 ntintydseqdinkndmkntyeiyTFLLKeLQKV-QEEIKNN-LSSDKMkniyndLHIDEFLKNhfnydnmnvgvNGTSL 753
Cdd:PRK09452 108 ------------------------AFGLR-MQKTpAAEITPRvMEALRM------VQLEEFAQR-----------KPHQL 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINKalIKYMKDKTTIIF---TH-RLDLLNYVDYIGVIEEGQI 828
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDyKLRKQMQNE--LKALQRKLGITFvfvTHdQEEALTMSDRIVVMRDGRI 223
|
..
gi 124805679 829 IQ 830
Cdd:PRK09452 224 EQ 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
753-830 |
2.48e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKaLIKYMK--DKTTIIFTHRLD-LLNYVDYIGVIEEGQII 829
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKanNKTVFVITHTMEhVLEVADEVIVMDKGKIL 255
|
.
gi 124805679 830 Q 830
Cdd:PRK13631 256 K 256
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
735-829 |
2.49e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 735 LKNHFNYDNMNVGvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM-KDKTTIIFTHRLDL 813
Cdd:CHL00131 139 MDPSFLSRNVNEG-----FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRL 213
|
90
....*....|....*...
gi 124805679 814 LNYV--DYIGVIEEGQII 829
Cdd:CHL00131 214 LDYIkpDYVHVMQNGKII 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
550-829 |
2.59e-08 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 54.92 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNL---LTKKNdlnaSGEICVGNVPINKINSAVLRsiVGVITQDPFLF- 625
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIilgLIKPD----SGEITFDGKSYQKNIEALRR--IGALIEAPGFYp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 626 NLTVRENLMypYKAYEEMLKEQIrlIEQnqgaFINMINNENTKKEKndddntintydseqdinkndmkntyeiytfllke 705
Cdd:cd03268 86 NLTARENLR--LLARLLGIRKKR--IDE----VLDVVGLKDSAKKK---------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 706 lqkvqeeiknnlssdkmkniyndlhideflknhfnydnmnvgVNGTSLsgGQKQRIYLAQNLIKNNKILILDEPTSSLDK 785
Cdd:cd03268 124 ------------------------------------------VKGFSL--GMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 124805679 786 LSENIINKALIKYMKDKTTIIF-THRL-DLLNYVDYIGVIEEGQII 829
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLIsSHLLsEIQKVADRIGIINKGKLI 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
524-854 |
2.62e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.48 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTK--DNINANINnernkkfalknvsfflpHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNV 601
Cdd:PRK09493 2 IEFKNVSKHFGPTQvlHNIDLNID-----------------QGEVVVIIGPSGSGKSTLLRCINKLEEIT-SGDLIVDGL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 PIN--KINSAVLRSIVGVITQDPFLF-NLTVRENLMY-PYkayeemlkeQIRlieqnqGAfinminnenTKKEKNDddnt 677
Cdd:PRK09493 64 KVNdpKVDERLIRQEAGMVFQQFYLFpHLTALENVMFgPL---------RVR------GA---------SKEEAEK---- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 678 intydseqdinkndmkntyeiytfLLKELQKvqeeiKNNLSSDKmkniyndlhideflkNHFNydnmnvgvngTSLSGGQ 757
Cdd:PRK09493 116 ------------------------QARELLA-----KVGLAERA---------------HHYP----------SELSGGQ 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 758 KQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIinkalIKYMKD-----KTTIIFTHRLDLLNYV-DYIGVIEEGQIIQ 830
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDpELRHEV-----LKVMQDlaeegMTMVIVTHEIGFAEKVaSRLIFIDKGRIAE 216
|
330 340
....*....|....*....|....*
gi 124805679 831 FDKRQSVLQKPC-PILKKILtQGVS 854
Cdd:PRK09493 217 DGDPQVLIKNPPsQRLQEFL-QHVS 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
743-829 |
2.81e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 743 NMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKlSENIINKALIKYMKDK--TTIIFTHRLDLLNYV-DY 819
Cdd:PRK13549 134 DINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTE-SETAVLLDIIRDLKAHgiACIYISHKLNEVKAIsDT 212
|
90
....*....|
gi 124805679 820 IGVIEEGQII 829
Cdd:PRK13549 213 ICVIRDGRHI 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
753-840 |
3.53e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.90 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKlseniinKALIKYMK--------DKTTIIFTHRL-DLLNYVDYIGVI 823
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP-------KARIEMMQlfesihqsGQTVVLVTHLMdDVADYADYVYLL 217
|
90
....*....|....*..
gi 124805679 824 EEGQIIQFDKRQSVLQK 840
Cdd:PRK13643 218 EKGHIISCGTPSDVFQE 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
524-829 |
4.43e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 54.65 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYD------NTKDNINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkkndlnasgeic 597
Cdd:cd03267 1 IEVSNLSKSYRvyskepGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 598 vgnvpinkinsavlrsivGVITQDpflfNLTVRENLMYPYKAYEEMLKeQIRLI--EQNQGAFinminnentkkekndDD 675
Cdd:cd03267 69 ------------------GLLQPT----SGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWW---------------DL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 NTINTYDSEQDInkndmkntYEIYTFllkelqkvqeEIKNNLssDKMKNIyndLHIDEFLKnhfnydnmnvgVNGTSLSG 755
Cdd:cd03267 111 PVIDSFYLLAAI--------YDLPPA----------RFKKRL--DELSEL---LDLEELLD-----------TPVRQLSL 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 756 GQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD-KTTIIFT-HRL-DLLNYVDYIGVIEEGQII 829
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTsHYMkDIEALARRVLVIDKGRLL 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
553-849 |
4.45e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSIVGVITQDPflfnltvrEN 632
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-PTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP--------ST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 633 LMYPYKAYEEMLKEQIRLieqnqgafinminneNTKKEkndddntintydseqdinkndmkntyeiytfllkelqkvqee 712
Cdd:PRK15112 99 SLNPRQRISQILDFPLRL---------------NTDLE------------------------------------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 713 iknnlSSDKMKNIYNDLHIDEFLKNHFNY-DNMnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENI 790
Cdd:PRK15112 122 -----PEQREKQIIETLRQVGLLPDHASYyPHM--------LAPGQKQRLGLARALILRPKVIIADEALASLDmSMRSQL 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 791 INkaLIKYMKDKTTIIF---THRLDLLNYV-DYIGVIEEGQIIQFDKRQSVLQKPCPILKKIL 849
Cdd:PRK15112 189 IN--LMLELQEKQGISYiyvTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLASPLHELTKRL 249
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
201-466 |
4.68e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 55.55 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 201 YLGFAMFCLIASSLGQMIFPMCISKIINMYGGKEeSLKYLTNEIYKTVLLIIGISTFSFFRIYFIETSIEKITRRLRTHF 280
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNG-DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 281 FEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFlihLSFGIRNFISALIGGICA----LHISPRNLFQSF-LLPVsgcL 355
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDL---LSNGLINLIPDLLTLVGIviimFSLNVRLALVTLaVLPL---L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 356 LIGTTY-AKFVKKISVLKQEKLSSCIDFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVksgNHFLFFSI 434
Cdd:cd18545 154 VLVVFLlRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRL---NALFWPLV 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 124805679 435 -----ISLFLlhLIYYGNYLIAHKFINTGDLFSLIMY 466
Cdd:cd18545 231 elisaLGTAL--VYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
754-784 |
4.81e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 54.75 E-value: 4.81e-08
10 20 30
....*....|....*....|....*....|.
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
554-636 |
5.06e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 54.75 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKnDLNASGEICVGNVPINKINS---AVLRS-IVGVITQD-PFLFNLT 628
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGQDLFALDEdarARLRArHVGFVFQSfQLLPTLT 106
|
....*...
gi 124805679 629 VRENLMYP 636
Cdd:COG4181 107 ALENVMLP 114
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
567-829 |
5.76e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 54.04 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 567 VAIVGKSGSGKTTILNLLTKkNDLNASGEICVGNVPINKINSAvlRSIVGVITQDPFLF-NLTVRENLMYPykayeemLK 645
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAG-FETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG-------LS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 646 EQIRLIEQNQGAfinminnentkkekndddntintydseqdinkndmkntyeiytfllkelqkvqeeiknnlssdkMKNI 725
Cdd:cd03298 97 PGLKLTAEDRQA----------------------------------------------------------------IEVA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 726 YNDLHIDEFLKNHfnydnmnvgvnGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDK--T 803
Cdd:cd03298 113 LARVGLAGLEKRL-----------PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmT 181
|
250 260
....*....|....*....|....*..
gi 124805679 804 TIIFTHRL-DLLNYVDYIGVIEEGQII 829
Cdd:cd03298 182 VLMVTHQPeDAKRLAQRVVFLDNGRIA 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
556-828 |
6.46e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 556 NVSFFlpHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPInKINSAVLRSIVGVITQDPFLFN-LTVRENLM 634
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLP-PTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 635 YpykaYEEMlkeQIRLIEQNQGAFINMINNENTKKEKNDDdntintydsEQDinkndmkntyeiytfllkelqkvqeeik 714
Cdd:TIGR01257 1026 F----YAQL---KGRSWEEAQLEMEAMLEDTGLHHKRNEE---------AQD---------------------------- 1061
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 715 nnlssdkmkniyndlhideflknhfnydnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKA 794
Cdd:TIGR01257 1062 --------------------------------------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
250 260 270
....*....|....*....|....*....|....*
gi 124805679 795 LIKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQI 828
Cdd:TIGR01257 1104 LLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRL 1138
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
524-832 |
7.18e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.84 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKndLNA-SGEICVG-NV 601
Cdd:COG0488 316 LELEGLSKSYGDKT---------------LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE--LEPdSGTVKLGeTV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 602 pinkinsavlrsIVGVITQDpflfnltvRENLmypykayeemlkeqirlieqnqgafinminnentkkeknDDDNTIntY 681
Cdd:COG0488 379 ------------KIGYFDQH--------QEEL---------------------------------------DPDKTV--L 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 682 DSEQDINKNdmKNTYEIYTFLLKelqkvqeeiknnlssdkmkniyndlhideFLknhFNYDNMN--VGVngtsLSGGQKQ 759
Cdd:COG0488 398 DELRDGAPG--GTEQEVRGYLGR-----------------------------FL---FSGDDAFkpVGV----LSGGEKA 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 760 RIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYmkdKTTIIF-TH-R--LDLLnyVDYIGVIEEGQIIQFD 832
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF---PGTVLLvSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
550-829 |
1.06e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKFALKNVSF-FLPHNKsVAIVGKSGSGKTTILNLLTKKnDLNASGEIcvgnVPINKINsavlrsiVGVITQDPFL-FNL 627
Cdd:TIGR03719 17 KKEILKDISLsFFPGAK-IGVLGLNGAGKSTLLRIMAGV-DKDFNGEA----RPQPGIK-------VGYLPQEPQLdPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 628 TVRENLMypyKAYEEMLKEQIRLIEqnqgafINMINNENtkkeknDDDntintydseqdinkndmkntyeiYTFLLKELQ 707
Cdd:TIGR03719 84 TVRENVE---EGVAEIKDALDRFNE------ISAKYAEP------DAD-----------------------FDKLAAEQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 708 KVQEEIKN----NLSSdKMKNIYNDLHIDEflknhfnyDNMNVgvngTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSL 783
Cdd:TIGR03719 126 ELQEIIDAadawDLDS-QLEIAMDALRCPP--------WDADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124805679 784 DKLSENIINKALIKYmkDKTTIIFTH-RLDLLNYVDYIGVIEEGQII 829
Cdd:TIGR03719 193 DAESVAWLERHLQEY--PGTVVAVTHdRYFLDNVAGWILELDRGRGI 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
712-839 |
1.07e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 712 EIKNNLSSDKMKNIYNDLhIDEFLKNHFNyDNMnvgvnGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENII 791
Cdd:PRK10895 104 QIRDDLSAEQREDRANEL-MEEFHIEHLR-DSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 124805679 792 NKaLIKYMKDK--TTIIFTHRL-DLLNYVDYIGVIEEGQIIQFDKRQSVLQ 839
Cdd:PRK10895 177 KR-IIEHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
752-828 |
1.37e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.53 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSEnIINKALIKYMKDK---TTIIFTHrlDLLNYV---DYIGVIEE 825
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR-IEMQDLIESLWQQhgfTVLLVTH--DVSEAVamaDRVLLIEE 209
|
...
gi 124805679 826 GQI 828
Cdd:PRK11247 210 GKI 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
753-853 |
1.77e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.27 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM-KDKTTIIF-THRLD-LLNYVDYIGVIEEGQII 829
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFiSHDLDeAMRIGDRIAIMQNGEVV 244
|
90 100
....*....|....*....|....
gi 124805679 830 QFDKRQSVLQKPCPILKKILTQGV 853
Cdd:PRK10070 245 QVGTPDEILNNPANDYVRTFFRGV 268
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
738-832 |
2.15e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.09 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 738 HFNYDNMnvgvngTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAL--IKYMKDKTTIIFTHRLDL-L 814
Cdd:PRK09984 144 HFAHQRV------STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYaL 217
|
90 100
....*....|....*....|....
gi 124805679 815 NYVDYIGVIEEGQII------QFD 832
Cdd:PRK09984 218 RYCERIVALRQGHVFydgssqQFD 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
753-848 |
2.54e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.34 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLS-ENIInkALIKYMKDK--TTIIFTHRLDLLNYVDYIGVIEEGQII 829
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
90 100
....*....|....*....|..
gi 124805679 830 Q---FDKRQSVLQKPCPILKKI 848
Cdd:PRK10535 223 RnppAQEKVNVAGGTEPVVNTA 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
524-828 |
2.83e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSYDNTKDNinaninnernkkFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkKNDLNA-SGEICVGNVP 602
Cdd:PRK13650 5 IEVKNLTFKYKEDQEK------------YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI--DGLLEAeSGQIIIDGDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRSIVGVITQDPflfnltvrenlmypykayeemlkeqirlieQNQ--GAFInminnentkkeknDDDNTINT 680
Cdd:PRK13650 71 LTEENVWDIRHKIGMVFQNP------------------------------DNQfvGATV-------------EDDVAFGL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 681 ydSEQDINKNDMKNtyeiytfllkelqKVQEEIK-NNLSSDKMKNiyndlhideflknhfnydnmnvgvnGTSLSGGQKQ 759
Cdd:PRK13650 108 --ENKGIPHEEMKE-------------RVNEALElVGMQDFKERE-------------------------PARLSGGQKQ 147
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 760 RIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKDK---TTIIFTHRLDLLNYVDYIGVIEEGQI 828
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDpEGRLELIK--TIKGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
524-635 |
3.47e-07 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 51.76 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 524 ITFHNVSFSY-------DNTKDNINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEI 596
Cdd:cd03220 1 IELENVSKSYptykggsSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD-SGTV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 124805679 597 CV-GNVpinkinSAVLRSIVGvitqdpFLFNLTVRENLMY 635
Cdd:cd03220 80 TVrGRV------SSLLGLGGG------FNPELTGRENIYL 107
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
753-829 |
3.80e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 3.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM-KDKTTIIFTHRLDLLNYV-DYIGVIEEGQII 829
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGRKI 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
752-820 |
3.84e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 3.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 752 SLSGGQKQRIYLAQNLIKN--NKILILDEPTSSLDklsENIINKAL--IKYMKDK--TTIIFTHRLDLLNYVDYI 820
Cdd:cd03238 87 TLSGGELQRVKLASELFSEppGTLFILDEPSTGLH---QQDINQLLevIKGLIDLgnTVILIEHNLDVLSSADWI 158
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
753-829 |
3.99e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 3.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIK-YMKDKTTIIFTHRLD-LLNYVDYIGVIEEGQII 829
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDnVLEWTKRTIFFKDGKII 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
554-633 |
4.66e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPINKINSAVLRSIVGVITQDPFLFNLTVRENL 633
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV-CGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
752-829 |
5.30e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.10 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDkLSENIINKALIKYMKDK---TTIIFTHRLDL-LNYVDYIGVIEEGQ 827
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IAHQVDVLALVHRLSQErglTVIAVLHDINMaARYCDYLVALRGGE 225
|
..
gi 124805679 828 II 829
Cdd:PRK10575 226 MI 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
520-829 |
6.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.01 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 520 NNFSITFHNVSFSYDNtkdninaniNNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTI---LNLLTkkndLNASGEI 596
Cdd:PRK13633 1 MNEMIKCKNVSYKYES---------NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL----IPSEGKV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 597 CVGNVPINKI-NSAVLRSIVGVITQDPflfnltvrenlmypykayeemlkeqirlieqnqgafinminnentkkeknddD 675
Cdd:PRK13633 68 YVDGLDTSDEeNLWDIRNKAGMVFQNP----------------------------------------------------D 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 676 NTINTYDSEQDInkndmkntyeiyTFLLKELQKVQEEIKnnlssdkmkniyndLHIDEFLK--NHFNYDNMNVGVngtsL 753
Cdd:PRK13633 96 NQIVATIVEEDV------------AFGPENLGIPPEEIR--------------ERVDESLKkvGMYEYRRHAPHL----L 145
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAlIKYMKDK---TTIIFTHRLDLLNYVDYIGVIEEGQII 829
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
753-816 |
6.12e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 6.12e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDLLNY 816
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAF 549
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
752-830 |
6.44e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.61 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK-LSENIInkALIKYMKDKTTIIF---THRLDLLNY-VDYIGVIEEG 826
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvLQAGVI--RLLKKLQQQFGTAClfiTHDLRLVERfCQRVMVMDNG 228
|
....
gi 124805679 827 QIIQ 830
Cdd:PRK10419 229 QIVE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
752-841 |
7.33e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.53 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLS-ENIINKALIKYMKDKTTIIFTHRLDLLNYVDYIGVIEEGQIIQ 830
Cdd:PRK13644 136 TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVL 215
|
90
....*....|.
gi 124805679 831 FDKRQSVLQKP 841
Cdd:PRK13644 216 EGEPENVLSDV 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
744-830 |
7.43e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 744 MNVGVngtslsgGQKQRIYLAQNLIKNNKILILDEPTSSL-DKLSENIINkaLIKYMKDK--TTIIFTHRLDLLNYV-DY 819
Cdd:NF040905 138 TDIGV-------GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD--LLLELKAQgiTSIIISHKLNEIRRVaDS 208
|
90
....*....|.
gi 124805679 820 IGVIEEGQIIQ 830
Cdd:NF040905 209 ITVLRDGRTIE 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
538-622 |
9.49e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.38 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 538 DNINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKT----TILNLLTkKNDLNASGEICVGNVPINKINSAVLRS 613
Cdd:COG4172 10 EDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLP-DPAAHPSGSILFDGQDLLGLSERELRR 88
|
90
....*....|...
gi 124805679 614 I----VGVITQDP 622
Cdd:COG4172 89 IrgnrIAMIFQEP 101
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
753-830 |
1.09e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.32 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD--KTTIIFTHRL-DLLNYVDYIGVIEEGQII 829
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMnEVARYADEVIVMKEGSIV 225
|
.
gi 124805679 830 Q 830
Cdd:PRK13646 226 S 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
753-820 |
1.25e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.07 E-value: 1.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSEN----IINKALIkymkdktTIIF-THRLDLLNYVDYI 820
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDrlyqLLKELGI-------TVISvGHRPSLWKFHDRV 157
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
753-829 |
1.45e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.37 E-value: 1.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM-KDKTTIIFTHRLDLLNYV-DYIGVIEEGQII 829
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGRKI 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
742-829 |
1.47e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 742 DNMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKlSENIINKALIKYMKDK--TTIIFTHRLDLLNYV-D 818
Cdd:TIGR02633 131 DADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE-KETEILLDIIRDLKAHgvACVYISHKLNEVKAVcD 209
|
90
....*....|.
gi 124805679 819 YIGVIEEGQII 829
Cdd:TIGR02633 210 TICVIRDGQHV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
554-636 |
1.70e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.20 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKnDLNASGEICVGNVPINKINS---AVLRSI-VGVITQ-DPFLFNLT 628
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQfHHLLPDFT 103
|
....*...
gi 124805679 629 VRENLMYP 636
Cdd:PRK11629 104 ALENVAMP 111
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
541-820 |
1.76e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 541 NANINNernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILN---LLTKKNDLNAsgeicvgnvpiNKINSAVLRSIVGV 617
Cdd:TIGR00630 618 GARENN-------LKNITVSIPLGLFTCITGVSGSGKSTLINdtlYPALANRLNG-----------AKTVPGRYTSIEGL 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 618 --------ITQDPFlfNLTVRENLMYPYKAYEEmlkeqIR-LIEQ---------NQGAFinminNENTKK---EKNDDDN 676
Cdd:TIGR00630 680 ehldkvihIDQSPI--GRTPRSNPATYTGVFDE-----IReLFAEtpeakvrgyTPGRF-----SFNVKGgrcEACQGDG 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 677 TINTydseqdinknDMKNTYEIYT---------FLLKELqkvqeEIKNnlssdKMKNIYN--DLHIDE---FLKNH---- 738
Cdd:TIGR00630 748 VIKI----------EMHFLPDVYVpcevckgkrYNRETL-----EVKY-----KGKNIADvlDMTVEEayeFFEAVpsis 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 739 ----------FNYdnMNVGVNGTSLSGGQKQRIYLAQNLIKNNK---ILILDEPTSSL---DklseniINKAL--IKYMK 800
Cdd:TIGR00630 808 rklqtlcdvgLGY--IRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdD------IKKLLevLQRLV 879
|
330 340
....*....|....*....|..
gi 124805679 801 DK--TTIIFTHRLDLLNYVDYI 820
Cdd:TIGR00630 880 DKgnTVVVIEHNLDVIKTADYI 901
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
523-841 |
1.76e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 523 SITFHNVSFSYDNTKdninaninnernkkfALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVP 602
Cdd:PRK10851 2 SIEIANIKKSFGRTQ---------------VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-SGHIRFHGTD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 603 INKINSAVLRsiVGVITQDPFLF-NLTVRENLMYPYKayeeMLKEQIRLieqnqgafinminnentkkekndddntinty 681
Cdd:PRK10851 66 VSRLHARDRK--VGFVFQHYALFrHMTVFDNIAFGLT----VLPRRERP------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 682 dseqdinkndmkNTYEIYTFLLKELQKVQEEiknnlssdkmkniyndlHidefLKNHFNydnmnvgvngTSLSGGQKQRI 761
Cdd:PRK10851 109 ------------NAAAIKAKVTQLLEMVQLA-----------------H----LADRYP----------AQLSGGQKQRV 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 762 YLAQNLIKNNKILILDEPTSSLDKLseniINKALIKYMKD-----KTTIIF-TH-RLDLLNYVDYIGVIEEGQIIQFDKR 834
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQ----VRKELRRWLRQlheelKFTSVFvTHdQEEAMEVADRVVVMSQGNIEQAGTP 221
|
....*..
gi 124805679 835 QSVLQKP 841
Cdd:PRK10851 222 DQVWREP 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
543-829 |
2.05e-06 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 49.85 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNL---LTKKNdlnaSGEICVGNVPINK--INSAVLRSIvGV 617
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMivgLVKPD----SGKILLDGQDITKlpMHKRARLGI-GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 618 ITQDPFLF-NLTVRENLMypykayeemlkeqirlieqnqgafinminnentkkekndddntintydseqdinkndmknty 696
Cdd:cd03218 80 LPQEASIFrKLTVEENIL-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 697 eiytfLLKELQKVQEEIKnnlsSDKMKNIYNDLHIDEFLKNhfnydnmnvgvNGTSLSGGQKQRIYLAQNLIKNNKILIL 776
Cdd:cd03218 98 -----AVLEIRGLSKKER----EEKLEELLEEFHITHLRKS-----------KASSLSGGERRRVEIARALATNPKFLLL 157
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 777 DEPTSSLDKLSENIInKALIKYMKDKT--TIIFTHRL-DLLNYVDYIGVIEEGQII 829
Cdd:cd03218 158 DEPFAGVDPIAVQDI-QKIIKILKDRGigVLITDHNVrETLSITDRAYIIYEGKVL 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
754-784 |
2.37e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 2.37e-06
10 20 30
....*....|....*....|....*....|.
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
753-784 |
2.85e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 2.85e-06
10 20 30
....*....|....*....|....*....|..
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
753-830 |
3.08e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.71 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKaLIKYMKDK---TTIIFTHRLDLLNYVDYIGVIEEGQII 829
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR-VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEII 219
|
.
gi 124805679 830 Q 830
Cdd:PRK13642 220 K 220
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
247-368 |
3.28e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 49.87 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 247 TVLLIIGI----STFSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFlihLSFGI 322
Cdd:cd18565 56 LGGLTVAAflleSLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERF---LDDGA 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124805679 323 RNFI-----SALIGGICALhISPR-NLFQsfLLPVSgcLLIGTTYaKFVKKI 368
Cdd:cd18565 133 NSIIrvvvtVLGIGAILFY-LNWQlALVA--LLPVP--LIIAGTY-WFQRRI 178
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
539-633 |
3.38e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.80 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 539 NINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNAS--GEICVGNVPINKINSAVLRSIVG 616
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSveGDIHYNGIPYKEFAEKYPGEIIY 87
|
90
....*....|....*..
gi 124805679 617 VITQDPFLFNLTVRENL 633
Cdd:cd03233 88 VSEEDVHFPTLTVRETL 104
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
199-462 |
3.52e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 49.82 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 199 RKYLGFAMFCLIASSLGQMIFPMCISKIINmYGGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFI---ETSIEKitrR 275
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVID-NVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIiklQTKLDK---S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 276 LRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHLSFGIRNFISALIGGICALHISPRnlfQSFLLPVSGCL 355
Cdd:cd18555 77 LMSDFFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPL---LTLIVLLLGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 356 LIGTTY--AKFVKKIS---VLKQEKLSScidFASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKH----SLVKSG 426
Cdd:cd18555 154 IVLLLLltRKKIKKLNqeeIVAQTKVQS---YLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKerlsNILNSI 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 124805679 427 NHFLFFsIISLFLLhliYYGNYLIAHKFINTGDLFS 462
Cdd:cd18555 231 SSSIQF-IAPLLIL---WIGAYLVINGELTLGELIA 262
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
753-785 |
3.81e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.22 E-value: 3.81e-06
10 20 30
....*....|....*....|....*....|...
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK 785
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
753-830 |
4.16e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKDK--TTIIFTHRLDL----LNYVDYigvIEE 825
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpEITAQIVS--IIRELAETgiTQVIVTHEVEVarktASRVVY---MEN 216
|
....*
gi 124805679 826 GQIIQ 830
Cdd:PRK11124 217 GHIVE 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
751-812 |
4.21e-06 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 49.00 E-value: 4.21e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDK--TTIIFTHRLD 812
Cdd:TIGR01184 113 GQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVD 176
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
553-634 |
4.57e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 48.83 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILN----LLTKKndlnaSGEICVGNVPINKINS-AVLRSIVGVITQDPFLF-N 626
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKaisgLLPPR-----SGSIRFDGEDITGLPPhRIARLGIGYVPEGRRIFpS 92
|
....*...
gi 124805679 627 LTVRENLM 634
Cdd:COG0410 93 LTVEENLL 100
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
550-829 |
4.78e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 48.52 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKF----ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTK--KNDlnaSGEICVGNVPINKINSAVLRSIvGVITQDPF 623
Cdd:cd03265 8 KKYgdfeAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPT---SGRATVAGHDVVREPREVRRRI-GIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 624 LFN-LTVRENL-----MYPYKAYEemLKEQIRlieqnqgafinminnentkkekndddntintydseqdinkndmkntyE 697
Cdd:cd03265 84 VDDeLTGWENLyiharLYGVPGAE--RRERID-----------------------------------------------E 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 698 IYTFLlkELQKVQeeiknnlssdkmkniyndlhiDEFLKNHfnydnmnvgvngtslSGGQKQRIYLAQNLIKNNKILILD 777
Cdd:cd03265 115 LLDFV--GLLEAA---------------------DRLVKTY---------------SGGMRRRLEIARSLVHRPEVLFLD 156
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 778 EPTSSLDKLSENIINKaLIKYMKDK--TTIIF-THRL---DLLnyVDYIGVIEEGQII 829
Cdd:cd03265 157 EPTIGLDPQTRAHVWE-YIEKLKEEfgMTILLtTHYMeeaEQL--CDRVAIIDHGRII 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
567-785 |
5.26e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 48.25 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 567 VAIVGKSGSGKTTILNLL--TKKNDLNASGEICVGNVPINKINsaVLRSIVGVITQDPFLF-NLTVRENLMYPykayeem 643
Cdd:COG4136 30 LTLMGPSGSGKSTLLAAIagTLSPAFSASGEVLLNGRRLTALP--AEQRRIGILFQDDLLFpHLSVGENLAFA------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 644 LKEQIrlieqnqgafinminnenTKKEKndddntintydseqdinkndmkntyeiytfllkelqkvQEEIKNNLSSDKMK 723
Cdd:COG4136 101 LPPTI------------------GRAQR--------------------------------------RARVEQALEEAGLA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 724 NIYN-DLHideflknhfnydnmnvgvngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK 785
Cdd:COG4136 125 GFADrDPA---------------------TLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
567-830 |
5.69e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.59 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 567 VAIVGKSGSGKTTIL---NLLTKKNdlnaSGEICVGNV------PINKINSAV--LRSIVGVITQDpflFNL----TVRE 631
Cdd:PRK11264 32 VAIIGPSGSGKTTLLrciNLLEQPE----AGTIRVGDItidtarSLSQQKGLIrqLRQHVGFVFQN---FNLfphrTVLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 632 NLMypykayeemlkeqirlieqnQGAFInminnenTKKEKNDDdntintydseqdinkndmkntyeiYTFLLKELQKvqe 711
Cdd:PRK11264 105 NII--------------------EGPVI-------VKGEPKEE------------------------ATARARELLA--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 712 eiknnlssdkmkniyndlhideflknhfnydnmNVGVNGTS------LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD- 784
Cdd:PRK11264 131 ---------------------------------KVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDp 177
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124805679 785 KLSENIINKALIKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQIIQ 830
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVE 224
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
541-820 |
8.03e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.38 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 541 NANINNernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILN-LLTK--KNDLNASGEiCVGNVpiNKINSAVLRSIVGV 617
Cdd:cd03271 5 GARENN-------LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYPalARRLHLKKE-QPGNH--DRIEGLEHIDKVIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 618 ITQDPFlfNLTVRENLMYPYKAYEEmlkeqIRLI--EQNQGAFINMINNENTKKEKNDDDNTintydseqdinknDMkNT 695
Cdd:cd03271 75 IDQSPI--GRTPRSNPATYTGVFDE-----IRELfcEVCKGKRYNRETLEVRYKGKSIADVL-------------DM-TV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 696 YEIYTFLLKelqkvQEEIKNNLSSDKmkniynDLHIDeflknhfnYdnMNVGVNGTSLSGGQKQRIYLAQNLIK---NNK 772
Cdd:cd03271 134 EEALEFFEN-----IPKIARKLQTLC------DVGLG--------Y--IKLGQPATTLSGGEAQRIKLAKELSKrstGKT 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124805679 773 ILILDEPTSSLDklSENIinKALIKYM-----KDKTTIIFTHRLDLLNYVDYI 820
Cdd:cd03271 193 LYILDEPTTGLH--FHDV--KKLLEVLqrlvdKGNTVVVIEHNLDVIKCADWI 241
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
204-481 |
8.59e-06 |
|
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: 48.64 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 204 FAMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYltnEIYKTVLLIIGISTFS--FFRIYFIETSieKITRRLRTHF- 280
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLS---EGYLLALALFLVSLLQslLLHQYFFLSF--RLGMRVRSALs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 281 ---FEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHLSFGIRNFISaLIGGICALHispRNLFQSFLLPVSGCLLI 357
Cdd:cd18579 76 sliYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQ-IIVALYLLY---RLLGWAALAGLGVLLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 358 GTTYAKFVKKISVLkQEKLSSCID----FASEKIHNISNVRLLngeSYEKKeFINYLEDV----YKIGKKHSLVKSGNHF 429
Cdd:cd18579 152 IPLQAFLAKLISKL-RKKLMKATDervkLTNEILSGIKVIKLY---AWEKP-FLKRIEELrkkeLKALRKFGYLRALNSF 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 430 LFFSIISL-----FLLHlIYYGNYLIAHKFINTGDLFSLIMYSLFC-GSGIQGMMHAI 481
Cdd:cd18579 227 LFFSTPVLvslatFATY-VLLGNPLTAAKVFTALSLFNLLRFPLLMlPQAISSLIEAL 283
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
753-841 |
8.85e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.95 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDklseniinKALIKYMKDK----------TTIIFTH-RLDLLNYVDYIG 821
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLD--------ANLRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVI 208
|
90 100
....*....|....*....|
gi 124805679 822 VIEEGQIIQFDKRQSVLQKP 841
Cdd:PRK11432 209 VMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
741-828 |
8.93e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 47.04 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 741 YDNMNVGVngtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDklsenIINKA----LIKYMKD--KTTIIFTHRLD-L 813
Cdd:cd03215 96 AENIALSS---LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD-----VGAKAeiyrLIRELADagKAVLLISSELDeL 167
|
90
....*....|....*
gi 124805679 814 LNYVDYIGVIEEGQI 828
Cdd:cd03215 168 LGLCDRILVMYEGRI 182
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
567-833 |
9.21e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.49 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 567 VAIVGKSGSGKTTILNLLTKKNDLNA-SGEICVGNvpiNKINSAVLRSIvGVITQDPFLF-NLTVRENLMYPykayeeml 644
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRIQGNNfTGTILANN---RKPTKQILKRT-GFVTQDDILYpHLTVRETLVFC-------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 645 kEQIRLieqnqgafinmiNNENTKKEKNdddntintydseqdinkndmkntyeiytfllkelqKVQEEIKNNLSSDKMKN 724
Cdd:PLN03211 165 -SLLRL------------PKSLTKQEKI-----------------------------------LVAESVISELGLTKCEN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 725 IyndlhideFLKNHFnydnmnvgVNGtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM-KDKT 803
Cdd:PLN03211 197 T--------IIGNSF--------IRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAqKGKT 258
|
250 260 270
....*....|....*....|....*....|..
gi 124805679 804 TIIFTHRLDLLNY--VDYIGVIEEGQIIQFDK 833
Cdd:PLN03211 259 IVTSMHQPSSRVYqmFDSVLVLSEGRCLFFGK 290
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
750-830 |
1.02e-05 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 47.52 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 750 GTSLSGGQKQRIYLAQNLIKNNKILILDEPTS----SLDKLSENIINKalIKYMKDKTTIIFTHRLDL-LNYVDYIGVIE 824
Cdd:TIGR03410 129 GGDLSGGQQQQLAIARALVTRPKLLLLDEPTEgiqpSIIKDIGRVIRR--LRAEGGMAILLVEQYLDFaRELADRYYVME 206
|
....*.
gi 124805679 825 EGQIIQ 830
Cdd:TIGR03410 207 RGRVVA 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
524-599 |
1.13e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 45.90 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 524 ITFHNVSFSYDNtkdninaninnernkKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKnDLNASGEICVG 599
Cdd:cd03221 1 IELENLSKTYGG---------------KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE-LEPDEGIVTWG 60
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
543-631 |
1.18e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 47.84 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkkNDLNA-SGEICVGNVPINKINSAVLRSIVGVITQD 621
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPdSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90
....*....|.
gi 124805679 622 PFL-FNLTVRE 631
Cdd:PRK13548 85 SSLsFPFTVEE 95
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
753-825 |
1.19e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 47.66 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD-KTTIIFTHRLDLLNYVD------YIGVIEE 825
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSshviflHQGKIEE 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
753-819 |
1.19e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 1.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInkALIKYMKD--KTTIIFTHRL-DLLNYVDY 819
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvKTEARII--SLLRELRDegKTMLVSTHNLgSVTEFCDY 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
707-839 |
1.35e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 707 QKVQEEIKNNLSSDKMKNIyndLHIDEFLKNHFNYdnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKL 786
Cdd:PRK10938 104 EIIQDEVKDPARCEQLAQQ---FGITALLDRRFKY-----------LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 787 SENIINKALIKYMKDKTTI--IFTHRLDLLNYVDYIGVIEEGQIIQFDKRQSVLQ 839
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLvlVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
752-812 |
1.96e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSL-----DKLseniinKALIKYMKDK-TTIIF-THRLD 812
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLtpqeaDEL------FEILRRLAAEgKSIIFiTHKLR 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
752-827 |
2.02e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDklSENIINKA-LIKYM---KDKTTIIFTHRLDLLNYVDYIGVIEEGQ 827
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD--IEQRLNAArAIRRLseeGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
752-820 |
2.17e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQ------RIYLAQNLIKNNKILILDEPTSSLDKlsENIINK--ALIKYMKDKTT---IIFTHRLDLLNYVDYI 820
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE--ENIEESlaEIIEERKSQKNfqlIVITHDEELVDAADHI 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
754-849 |
2.62e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINkALIKYMKDK--TTIIFTHRLDLLNYVDY-IGVIEEGQII 829
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIIN-LLLDLQRDFgiAYLFISHDMAVVERISHrVAVMYLGQIV 543
|
90 100
....*....|....*....|.
gi 124805679 830 QFDKRQSVLQKPC-PILKKIL 849
Cdd:PRK10261 544 EIGPRRAVFENPQhPYTRKLM 564
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
753-784 |
2.82e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.82e-05
10 20 30
....*....|....*....|....*....|..
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
248-406 |
3.10e-05 |
|
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: 46.74 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 248 VLLIIGIST-FSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIE-------------ISSK 313
Cdd:cd18564 60 LVGIALLRGlASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGaiqdllvsgvlplLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 314 FLIHLSFGIRNFIS---ALIggicALHISPrnLFqsfllpvsgcLLIGTTYAKFVKKISVLKQEKLSSCIDFASEKIHNI 390
Cdd:cd18564 140 LTLVGMLGVMFWLDwqlALI----ALAVAP--LL----------LLAARRFSRRIKEASREQRRREGALASVAQESLSAI 203
|
170
....*....|....*.
gi 124805679 391 SNVRLLNGESYEKKEF 406
Cdd:cd18564 204 RVVQAFGREEHEERRF 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
538-786 |
3.81e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.39 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 538 DNINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLtkkndlnA------SGEICVGNVPINKinSAVL 611
Cdd:COG4525 7 RHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLI-------AgflapsSGEITLDGVPVTG--PGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 612 RsivGVITQDPFLFN-LTVRENLMYPykayeemLKEQ-IRLIEQNQGAfinminnentkkekndddntintydseqdink 689
Cdd:COG4525 78 R---GVVFQKDALLPwLNVLDNVAFG-------LRLRgVPKAERRARA-------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 690 ndmkntyeiytflLKELQKVqeeiknNLSSDKMKNIYndlhideflknhfnydnmnvgvngtSLSGGQKQRIYLAQNLIK 769
Cdd:COG4525 116 -------------EELLALV------GLADFARRRIW-------------------------QLSGGMRQRVGIARALAA 151
|
250
....*....|....*..
gi 124805679 770 NNKILILDEPTSSLDKL 786
Cdd:COG4525 152 DPRFLLMDEPFGALDAL 168
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
204-336 |
3.83e-05 |
|
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: 46.34 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 204 FAMFCLIASSLGQMIFPMCISKII--NMYGGKEESLKYLTneIYkTVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFF 281
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWLDWWSsdWSSSPNSSSGYYLG--VY-AALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 282 EKVLNQDVHFFNKQKTGELINRLSNDIEisskfLI--HLSFGIRNFISALIGGICAL 336
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIG-----LIdeELPLALLDFLQSLFSVLGSL 131
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
753-851 |
4.08e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.15 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIInKALIKYM--KDKTTIIFTHRLDLLNYV-DYIGVIEEGQII 829
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM-IAIIRRIvaQGNHVIISSHDIDLIYEIsDAVYVLRQGQIL 215
|
90 100
....*....|....*....|..
gi 124805679 830 QFDKRQSVLQKPCPILKKILTQ 851
Cdd:PRK13638 216 THGAPGEVFACTEAMEQAGLTQ 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
753-831 |
5.67e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.95 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSE-NIINKalIKYMKD--KTTIIFT---HRLDLLNYVDYIGVIEEG 826
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAlEILKC--IRTMADvlKTTTFVSlyqASDEIYDLFDKVLVLYEG 196
|
....*
gi 124805679 827 QIIQF 831
Cdd:cd03233 197 RQIYY 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
702-832 |
6.06e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 702 LLKELQKV-QEEIKNNLssDKMKNIyndLHIDEFLknhfnydnmNVGVNgtSLSGGQKQRIYLAQNLIKNNKILILDEPT 780
Cdd:COG4586 119 LLKAIYRIpDAEYKKRL--DELVEL---LDLGELL---------DTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 781 SSLDKLS-ENIINkaLIKYM--KDKTTIIFT-HRL-DLLNYVDYIGVIEEGQIIqFD 832
Cdd:COG4586 183 IGLDVVSkEAIRE--FLKEYnrERGTTILLTsHDMdDIEALCDRVIVIDHGRII-YD 236
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
245-410 |
6.30e-05 |
|
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: 46.02 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 245 YKTVLLIIGIST--FSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDI-EISSKFLIHLSFG 321
Cdd:cd18599 60 YQLVYGGSILVIllLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLdEVDVRLPFTLENF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 322 IRNFISAL--IGGICAlhisprnLFQSFLLPVSGCLLIGTTYAK-FVKKISVLKQ---EKLSSCIDFASEKIHNISNVRL 395
Cdd:cd18599 140 LQNVLLVVfsLIIIAI-------VFPWFLIALIPLAIIFVFLSKiFRRAIRELKRlenISRSPLFSHLTATIQGLSTIHA 212
|
170
....*....|....*
gi 124805679 396 LNGESYEKKEFINYL 410
Cdd:cd18599 213 FNKEKEFLSKFKKLL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
753-785 |
6.40e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.86 E-value: 6.40e-05
10 20 30
....*....|....*....|....*....|...
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK 785
Cdd:PRK13539 128 LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
753-825 |
7.39e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 45.18 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK--LSEniinkaLIKYMKD-----KTTIIFTHRL----DLLNYVDYI- 820
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPelVGE------VLKVMRDlaeegRTMLVVTHEMgfarDVSSHVVFLh 228
|
....*.
gi 124805679 821 -GVIEE 825
Cdd:COG4598 229 qGRIEE 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
710-813 |
7.88e-05 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 44.41 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 710 QEEIKNNLSSDKMKNIYNDLHIDEFLKNHFNydnmNVGVNG------TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSL 783
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALA----RVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
90 100 110
....*....|....*....|....*....|
gi 124805679 784 DKLSENIINKALIKYMKDKTTIIFTHRLDL 813
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDL 186
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
753-841 |
8.83e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIINKAL-IKYMKDKTTIIFTHRLDLLNYV-DYIGVIEEGQII 829
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLeLQQKENMALVLITHDLALVAEAaHKIIVMYAGQVV 233
|
90
....*....|..
gi 124805679 830 QFDKRQSVLQKP 841
Cdd:PRK11022 234 ETGKAHDIFRAP 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
752-837 |
9.79e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKlSENIINKALIKYMKDKTTIIF--THRLD-LLNYVDYIGVIEEGQI 828
Cdd:PRK11288 140 YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA-REIEQLFRVIRELRAEGRVILyvSHRMEeIFALCDAITVFKDGRY 218
|
90
....*....|
gi 124805679 829 IQ-FDKRQSV 837
Cdd:PRK11288 219 VAtFDDMAQV 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
751-784 |
9.83e-05 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 45.11 E-value: 9.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 124805679 751 TSLSGGQKQRIYLA-------QNLIKNNKILILDEPTSSLD 784
Cdd:COG4559 132 QTLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEPTSALD 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
753-841 |
1.22e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIInkALIKYMK---DKTTIIFTHRLDLLNYV-DYIGVIEEGQ 827
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQIL--QLLRELQqelNMGLLFITHNLSIVRKLaDRVAVMQNGR 234
|
90
....*....|....
gi 124805679 828 IIQFDKRQSVLQKP 841
Cdd:PRK15134 235 CVEQNRAATLFSAP 248
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
753-825 |
1.36e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.18 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD--KTTIIFTHRLDLLN--------YVDYIGV 822
Cdd:COG2401 137 LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRagITLVVATHHYDVIDdlqpdlliFVGYGGV 216
|
...
gi 124805679 823 IEE 825
Cdd:COG2401 217 PEE 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
753-809 |
1.51e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.31 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD--KTTIIFTH 809
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
205-484 |
1.54e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 44.41 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYLTneiyktVLLIIGISTFSFFRIYFIE-------TSIEKITRRLR 277
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVP------LLLLLAYGLARILSSLFNElrdalfaRVSQRAVRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 278 THFFEKVLNQDVHFFNKQKTGEL---INRLSNDIEisskFLihLSFGIRNFIS-----ALIGGICALHISPrnlfqSFLL 349
Cdd:cd18582 75 LRVFRHLHSLSLRFHLSRKTGALsraIERGTRGIE----FL--LRFLLFNILPtilelLLVCGILWYLYGW-----SYAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 350 PVSGCL-------LIGTTY-AKFVKKISvlKQEKLSSciDFASEKIHNISNVRLLNGESYEKKEFINYLEDvykigKKHS 421
Cdd:cd18582 144 ITLVTValyvaftIKVTEWrTKFRREMN--EADNEAN--AKAVDSLLNYETVKYFNNEEYEAERYDKALAK-----YEKA 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 422 LVKsgnhflffSIISLFLLHLiyyGNYLIahkfINTGdlFSLIMYslFCGSGI-QGMMHaIGDI 484
Cdd:cd18582 215 AVK--------SQTSLALLNI---GQALI----ISLG--LTAIML--LAAQGVvAGTLT-VGDF 258
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
751-784 |
1.57e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 1.57e-04
10 20 30
....*....|....*....|....*....|....
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
752-823 |
1.89e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.89 E-value: 1.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD---KLSENIINKALIKymKDKTTIIFTHRLDLLNYV-DYIGVI 823
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqRLNAARLIRELAE--DDNYVLVVEHDLAVLDYLsDYIHCL 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
751-828 |
1.98e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.82 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF--THRLDLLNYVDYIGVIEEGQI 828
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVvsSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
756-817 |
2.14e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 2.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 756 GQKQRIYLAQNLIKNNKILILDEPTSSLD----KLSENIINKalikymKDKTTIIFTHRLDLLNYV 817
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDintiRWLEDVLNE------RNSTMIIISHDRHFLNSV 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
515-625 |
2.20e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.96 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 515 DFLKSNNFS----ITFHNVSFSYDNTKdninaninnernkkFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTkknDL 590
Cdd:PRK10522 310 EFPRPQAFPdwqtLELRNVTFAYQDNG--------------FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT---GL 372
|
90 100 110
....*....|....*....|....*....|....*..
gi 124805679 591 N--ASGEICVGNVPINKINSAVLRSIVGVITQDPFLF 625
Cdd:PRK10522 373 YqpQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF 409
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
753-835 |
2.31e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF--THRLDLLNYVDYIGVIEEGQII- 829
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILvsSEMPEVLGMSDRILVMHEGRISg 475
|
....*.
gi 124805679 830 QFDKRQ 835
Cdd:PRK10762 476 EFTREQ 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
751-831 |
2.34e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYmkDKTTIIFTHRLDLLN-YVDYIGVIEEGQII 829
Cdd:PRK10636 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILISHDRDFLDpIVDKIIHIEQQSLF 225
|
..
gi 124805679 830 QF 831
Cdd:PRK10636 226 EY 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
751-817 |
2.36e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 2.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM--KDKTTIIFTHRLDLLNYV 817
Cdd:COG1245 454 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLIDYI 522
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
708-823 |
2.63e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 708 KVQEEIKNNLSSDKMKNIYNDLHIDEFLKNHFNYdnmnvgvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDkLS 787
Cdd:PRK13409 179 KVRELLKKVDERGKLDEVVERLGLENILDRDISE-----------LSGGELQRVAIAAALLRDADFYFFDEPTSYLD-IR 246
|
90 100 110
....*....|....*....|....*....|....*...
gi 124805679 788 ENI-INKALIKYMKDKTTIIFTHRLDLLNYV-DYIGVI 823
Cdd:PRK13409 247 QRLnVARLIRELAEGKYVLVVEHDLAVLDYLaDNVHIA 284
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
239-364 |
2.86e-04 |
|
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: 43.61 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 239 YLTneIYktVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIE-ISSKFLIH 317
Cdd:cd18604 45 YLG--IY--ALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIEtIDSELADS 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124805679 318 LSFGIRNFISALIGGICALHISPrnlfqSFLLPVSGCLLIGTTYAKF 364
Cdd:cd18604 121 LSSLLESTLSLLVILIAIVVVSP-----AFLLPAVVLAALYVYIGRL 162
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
754-799 |
2.88e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 43.93 E-value: 2.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLD-KLSENIIN--KALIKYM 799
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDvSIQAQVVNllQQLQREM 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
751-817 |
3.56e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.17 E-value: 3.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM--KDKTTIIFTHRLDLLNYV 817
Cdd:cd03237 114 PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYL 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
553-584 |
4.33e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.99 E-value: 4.33e-04
10 20 30
....*....|....*....|....*....|..
gi 124805679 553 ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLL 584
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNAL 52
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
554-784 |
4.35e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEIcvgnvpinKINSAVlrsIVGVITQDPflfnltVR--E 631
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD-DGRI--------IYEQDL---IVARLQQDP------PRnvE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 632 NLMYPYKAyeEMLKEQIRLIEQNQGAFINMinnENTKKEKNdddntintydseqdinkndmkntyeiytflLKELQKVQE 711
Cdd:PRK11147 81 GTVYDFVA--EGIEEQAEYLKRYHDISHLV---ETDPSEKN------------------------------LNELAKLQE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 712 EIKNNlssdkmkNIYN-DLHIDEFLKNhfnydnmnVGVNG----TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK11147 126 QLDHH-------NLWQlENRINEVLAQ--------LGLDPdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
752-784 |
5.13e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 42.67 E-value: 5.13e-04
10 20 30
....*....|....*....|....*....|...
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK10253 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
753-817 |
5.27e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 5.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM--KDKTTIIFTHRLDLLNYV 817
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeeREATALVVDHDIYMIDYI 520
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
753-813 |
5.34e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.46 E-value: 5.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTT--IIFTHRLDL 813
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTtlILVTHDLQL 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
752-833 |
5.35e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.09 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD---KLSENI-INKaLIKYMKdKTTIIFTH-RLDLLNYVDYIGVIEEG 826
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalRVQMRIeISR-LHKRLG-RTMIYVTHdQVEAMTLADKIVVLDAG 210
|
....*..
gi 124805679 827 QIIQFDK 833
Cdd:PRK11000 211 RVAQVGK 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
752-785 |
5.53e-04 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 41.96 E-value: 5.53e-04
10 20 30
....*....|....*....|....*....|....
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK 785
Cdd:TIGR01189 127 QLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
547-633 |
6.91e-04 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 41.58 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 547 ERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLnASGEICVGNVPINKINSAVLRSIVGVITQDPFLFN 626
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPE 87
|
....*..
gi 124805679 627 LTVRENL 633
Cdd:TIGR01189 88 LSALENL 94
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
547-635 |
7.18e-04 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 41.71 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 547 ERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSIVGVITQDPFLFN 626
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-PLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTT 87
|
....*....
gi 124805679 627 LTVRENLMY 635
Cdd:cd03231 88 LSVLENLRF 96
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
752-823 |
7.95e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.85 E-value: 7.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDklsenI---INKA-LIKYM--KDKTTIIFTHRLDLLNYV-DYIGVI 823
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-----IyqrLNVArLIRELaeEGKYVLVVEHDLAILDYLaDYVHIL 285
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
516-608 |
8.69e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.87 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 516 FLKSNNFSITFHNVSFSYDNTKDNINA-NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKnDLNASG 594
Cdd:COG2401 7 FFVLMRVTKVYSSVLDLSERVAIVLEAfGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-LKGTPV 85
|
90
....*....|....
gi 124805679 595 EICVgNVPINKINS 608
Cdd:COG2401 86 AGCV-DVPDNQFGR 98
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
753-841 |
9.05e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKT--TIIFTHRLDLL-NYVDYIGVIEEGQII 829
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIV 220
|
90
....*....|..
gi 124805679 830 QFDKRQSVLQKP 841
Cdd:PRK10418 221 EQGDVETLFNAP 232
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
249-465 |
1.04e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 42.16 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 249 LLIIGIS--TFSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSkFLIHLSFG-IRNF 325
Cdd:cd18568 48 LLIVGIFqiLLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRR-FLTRSALTtILDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 326 ISALIGGICALHISPR--NLFQSFLLPVSGCLLIGTTYAK-FVKKISVLKQEKLSSCIdfasEKIHNISNVRLLNGE--- 399
Cdd:cd18568 127 LMVFIYLGLMFYYNLQltLIVLAFIPLYVLLTLLSSPKLKrNSREIFQANAEQQSFLV----EALTGIATIKALAAErpi 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124805679 400 -SYEKKEFINYLEDVYKIGKKHSLVKSGNHFLfFSIISLFLLhliYYGNYLIAHKFINTGDLFSLIM 465
Cdd:cd18568 203 rWRWENKFAKALNTRFRGQKLSIVLQLISSLI-NHLGTIAVL---WYGAYLVISGQLTIGQLVAFNM 265
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
749-851 |
1.11e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 749 NGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKD-KTTIIFTHRL-DLLNYVDYIGVIEEG 826
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEG 485
|
90 100
....*....|....*....|....*.
gi 124805679 827 QIIQ-FDKRQSVLQKpcPILKKILTQ 851
Cdd:PRK09700 486 RLTQiLTNRDDMSEE--EIMAWALPQ 509
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
752-817 |
1.16e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYmkDKTTIIFTHRLDLLNYV 817
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSHAREFLNTV 407
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
751-784 |
1.21e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 1.21e-03
10 20 30
....*....|....*....|....*....|....
gi 124805679 751 TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
539-841 |
1.32e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 539 NINANINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKT----TILNLLTKKNDLNASGEICVGN-----VPINKINSA 609
Cdd:PRK10261 17 NLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRrsrqvIELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 610 VLRSIVG----VITQDPFlfnltvreNLMYPYKAYEEMLKEQIRLieqNQGAfinminnenTKKEKndddntintydseq 685
Cdd:PRK10261 97 QMRHVRGadmaMIFQEPM--------TSLNPVFTVGEQIAESIRL---HQGA---------SREEA-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 686 dinkndmkntyeiytflLKELQKVQEEIKnnlssdkmkniyndlhIDEFLKNHFNYDNmnvgvngtSLSGGQKQRIYLAQ 765
Cdd:PRK10261 143 -----------------MVEAKRMLDQVR----------------IPEAQTILSRYPH--------QLSGGMRQRVMIAM 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 766 NLIKNNKILILDEPTSSLD-KLSENIINkaLIKYMKDKTT--IIF-THRLDLL-NYVDYIGVIEEGQIIQFDKRQSVLQK 840
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDvTIQAQILQ--LIKVLQKEMSmgVIFiTHDMGVVaEIADRVLVMYQGEAVETGSVEQIFHA 259
|
.
gi 124805679 841 P 841
Cdd:PRK10261 260 P 260
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
747-829 |
1.33e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 747 GVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRL--DLLNYVDYIGVIE 824
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
....*
gi 124805679 825 EGQII 829
Cdd:NF000106 219 RGRVI 223
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
248-341 |
1.45e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 41.70 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 248 VLLIIGISTF--SFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSNDIEISSKFLIHLSFGIRNF 325
Cdd:cd18543 44 LLLALGVAEAvlSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNL 123
|
90
....*....|....*.
gi 124805679 326 ISALIGGICALHISPR 341
Cdd:cd18543 124 LTLVVGLVVMLVLSPP 139
|
|
| VirB4_CagE |
TIGR00929 |
type IV secretion/conjugal transfer ATPase, VirB4 family; Type IV secretion systems are found ... |
499-584 |
1.70e-03 |
|
type IV secretion/conjugal transfer ATPase, VirB4 family; Type IV secretion systems are found in Gram-negative pathogens. They export proteins, DNA, or complexes in different systems and are related to plasmid conjugation systems. This model represents related ATPases that include VirB4 in Agrobacterium tumefaciens (DNA export) CagE in Helicobacter pylori (protein export) and plasmid TraB (conjugation).
Pssm-ID: 273346 [Multi-domain] Cd Length: 785 Bit Score: 41.92 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 499 KLPdNNFHnyWNkTSIDFLKSNNFS--ITFHNVS--FSYDNTKDNINANINNERNKKFalknvsFFLPHNKSV------A 568
Cdd:TIGR00929 369 QLP-GNFS--WN-PRKSLITSRNFAslIPFHNFNlgKLRGNPWGPALTLLKTQSGTPF------YFNFHVRDAkvlghtL 438
|
90
....*....|....*.
gi 124805679 569 IVGKSGSGKTTILNLL 584
Cdd:TIGR00929 439 IFGPTGSGKTTLLNFL 454
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
550-809 |
1.71e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKFALKNVSF-FLPHNKsVAIVGKSGSGKTTILNLLTKKnDLNASGEIcvgnVPINKINsavlrsiVGVITQDPFL-FNL 627
Cdd:PRK11819 19 KKQILKDISLsFFPGAK-IGVLGLNGAGKSTLLRIMAGV-DKEFEGEA----RPAPGIK-------VGYLPQEPQLdPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 628 TVRENLmypykayEEMLKEqirlieqnqgafinminnentKKEKNDDDNTINTYDSEQDINKNDmkntyeiytfLLKELQ 707
Cdd:PRK11819 86 TVRENV-------EEGVAE---------------------VKAALDRFNEIYAAYAEPDADFDA----------LAAEQG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 708 KVQEEIKN----NLSSdKMKNIYNDLHIDEflknhfnyDNMNVGVngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSL 783
Cdd:PRK11819 128 ELQEIIDAadawDLDS-QLEIAMDALRCPP--------WDAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHL 194
|
250 260
....*....|....*....|....*.
gi 124805679 784 DKLSENIINKALIKYmkDKTTIIFTH 809
Cdd:PRK11819 195 DAESVAWLEQFLHDY--PGTVVAVTH 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
754-811 |
1.80e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.25 E-value: 1.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124805679 754 SGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIInKALIKYMKDK--TTIIF-THRL 811
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI-MTLLNELKREfnTAIIMiTHDL 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
753-791 |
1.82e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 40.63 E-value: 1.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDK-LSENII 791
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDaLSEGIL 177
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
543-635 |
1.97e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.32 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 543 NINNERNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKndLN-ASGEICVGNVPINKINSAVLRSIVGVITQD 621
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL--LNpEKGEILFERQSIKKDLCTYQKQLCFVGHRS 83
|
90
....*....|....
gi 124805679 622 PFLFNLTVRENLMY 635
Cdd:PRK13540 84 GINPYLTLRENCLY 97
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
720-829 |
2.01e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 720 DKM----KNIYNDLHIDeflknhfnydnMNVGVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTSSldkLSENIINK-- 793
Cdd:PRK10982 109 DKMyrdtKAIFDELDID-----------IDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS---LTEKEVNHlf 174
|
90 100 110
....*....|....*....|....*....|....*....
gi 124805679 794 ALIKYMKDK--TTIIFTHRLD-LLNYVDYIGVIEEGQII 829
Cdd:PRK10982 175 TIIRKLKERgcGIVYISHKMEeIFQLCDEITILRDGQWI 213
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
199-452 |
2.18e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 41.09 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 199 RKYLGFAMFCLIASSLGQMIFPMCISKIINMYGGKEESLKYLTNEIYKTVLLIIGISTFSFFRIYFIETSIE-KITRRLR 277
Cdd:cd18556 1 KLLFFSILFISLLSSILISISPVILAKITDLLTSSSSDSYNYIVVLAALYVITISATKLLGFLSLYLQSSLRvELIISIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 278 THFFEKVLNQDVHFFNKQKTGEL---INRLSNDIEISskflihlsfgIRNFISALIGGICALHISPRNLFQSFLLPVSGC 354
Cdd:cd18556 81 SSYFRYLYEQPKTFFVKENSGDItqrLNQASNDLYTL----------VRNLSTNILPPLLQLIIAIVVILSSGDYFVAAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 355 LLI-----GTTYAKFVKKISVLKQEKLSSCID---FASEKIHNISNVRLLNGESYEKKEFINYLE-------DVYKIGKK 419
Cdd:cd18556 151 FLLyavlfVINNTIFTKKIVSLRNDLMDAGRKsysLLTDSVKNIVAAKQNNAFDFLFKRYEATLTndrnsqkRYWKLTFK 230
|
250 260 270
....*....|....*....|....*....|...
gi 124805679 420 HSLVKSGNHFLFFSIISLFLLHLIYYGNYLIAH 452
Cdd:cd18556 231 MLILNSLLNVILFGLSFFYSLYGVVNGQVSIGH 263
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
712-812 |
2.26e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 712 EIKNNLSSDKMKNIYNDLhidEFLKNHFNYDNMNVGVNGTSLSGGQKQRIYLAQNLIKNN--KILILDEPTSSLDKLSEN 789
Cdd:smart00382 21 ALARELGPPGGGVIYIDG---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLkpDVLILDEITSLLDAEQEA 97
|
90 100
....*....|....*....|....*....
gi 124805679 790 IINKA------LIKYMKDKTTIIFTHRLD 812
Cdd:smart00382 98 LLLLLeelrllLLLKSEKNLTVILTTNDE 126
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
238-348 |
2.36e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 40.96 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 238 KYLTNEIYKT-VLLIIGI-------STFSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLSndiE 309
Cdd:cd18783 31 KVLVHQSYSTlYVLTIGVviallfeGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQ---Q 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 124805679 310 IsskflihlsFGIRNFISaliggicalhispRNLFQSFL 348
Cdd:cd18783 108 I---------ERIRQFLT-------------GQLFGTLL 124
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
753-784 |
2.37e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 41.46 E-value: 2.37e-03
10 20 30
....*....|....*....|....*....|..
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
746-820 |
2.52e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 746 VGVNGTSLSGGQKQRIYLAQNLIK--NNKIL-ILDEPTSSL-----DKLSEnIINKaLIkymkDK--TTIIFTHRLDLLN 815
Cdd:PRK00349 824 LGQPATTLSGGEAQRVKLAKELSKrsTGKTLyILDEPTTGLhfediRKLLE-VLHR-LV----DKgnTVVVIEHNLDVIK 897
|
....*
gi 124805679 816 YVDYI 820
Cdd:PRK00349 898 TADWI 902
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
753-807 |
2.52e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.19 E-value: 2.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF 807
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF 458
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
739-807 |
2.69e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 2.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 739 FNYDNMNVGVNgtSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYmkdKTTIIF 807
Cdd:PRK15064 427 FSQDDIKKSVK--VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY---EGTLIF 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
707-828 |
2.72e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.19 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 707 QKVQEEI-----KNNLSSDKMKNIYNDLHIdeflknHFNYDnmnvgVNGTSLSGGQKQRIYLAQNLIKNNKILILDEPTS 781
Cdd:PRK15439 101 LSVKENIlfglpKRQASMQKMKQLLAALGC------QLDLD-----SSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 124805679 782 SLDKL-SENIINKalIKYMKDKTT-IIF-THRL-DLLNYVDYIGVIEEGQI 828
Cdd:PRK15439 170 SLTPAeTERLFSR--IRELLAQGVgIVFiSHKLpEIRQLADRISVMRDGTI 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
753-784 |
2.72e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.48 E-value: 2.72e-03
10 20 30
....*....|....*....|....*....|..
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
548-653 |
2.88e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.52 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 548 RNKKFALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDLNaSGEICVGNVPINKINSAVL---RSIVGVITQDPFL 624
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110
....*....|....*....|....*....|
gi 124805679 625 F-NLTVRENLMYPykayeemLKEQIRLIEQ 653
Cdd:PRK11831 96 FtDMNVFDNVAYP-------LREHTQLPAP 118
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
742-828 |
3.29e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 742 DNMNVGVNG-----TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYM-KDKTTIIFTHRL-DLL 814
Cdd:PRK10982 376 DSMRVKTPGhrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELL 455
|
90
....*....|....
gi 124805679 815 NYVDYIGVIEEGQI 828
Cdd:PRK10982 456 GITDRILVMSNGLV 469
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
746-795 |
3.43e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 3.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124805679 746 VGVNG-TSLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAL 795
Cdd:PLN03140 1012 VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
752-780 |
3.88e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.77 E-value: 3.88e-03
10 20
....*....|....*....|....*....
gi 124805679 752 SLSGGQKQRIYLAQNLIKNNKILILDEPT 780
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
753-787 |
4.15e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 4.15e-03
10 20 30
....*....|....*....|....*....|....*
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLS 787
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
554-636 |
4.79e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 39.38 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 554 LKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINS---AVLRSI-VGVITQDPFLF-NLT 628
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD-GSSGEVSLVGQPLHQMDEearAKLRAKhVGFVFQSFMLIpTLN 104
|
....*...
gi 124805679 629 VRENLMYP 636
Cdd:PRK10584 105 ALENVELP 112
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
753-815 |
5.02e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 5.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 753 LSGGQKQRIYLAQNLIKNNK----ILILDEPTSSLDKLSENIINKALIKYMKDKTTIIF-THRLDLLN 815
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIViTHLPELAE 145
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
746-784 |
5.34e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 5.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 124805679 746 VGVngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLD 784
Cdd:PRK11819 443 VGV----LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
235-485 |
6.23e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 39.49 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 235 ESLKYLTNEIyktVLLIIGISTFSFFRIYFIETSIEKITRRLRTHFFEKVLNQDVHFFNKQKTGELINRLsNDIEISSKF 314
Cdd:cd18566 39 PTLQVLVIGV---VIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 315 --------LIHLSF-GIRNFISALIGGIcaLHISPRNLFQSFLLpVSgcLLIGTTYAKFVKKISVLKQEKLSscidFASE 385
Cdd:cd18566 115 ltgqallaLLDLPFvLIFLGLIWYLGGK--LVLVPLVLLGLFVL-VA--ILLGPILRRALKERSRADERRQN----FLIE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 386 KIHNISNVRLLNGES-----YEKKEfINYLEDVYKIGKKHSLVKSGNHflFFSIISLFLlhLIYYGNYLIAHKFINTGDL 460
Cdd:cd18566 186 TLTGIHTIKAMAMEPqmlrrYERLQ-ANAAYAGFKVAKINAVAQTLGQ--LFSQVSMVA--VVAFGALLVINGDLTVGAL 260
|
250 260
....*....|....*....|....*
gi 124805679 461 FSLIMYSLFCGSGIQGMMHAIGDIQ 485
Cdd:cd18566 261 IACTMLSGRVLQPLQRAFGLWTRFQ 285
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
743-830 |
6.23e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 743 NMNVGvngtsLSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKAlIKYMKD--KTTIIFTHRLDLLNYV--D 818
Cdd:PRK09580 141 SVNVG-----FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADG-VNSLRDgkRSFIIVTHYQRILDYIkpD 214
|
90
....*....|..
gi 124805679 819 YIGVIEEGQIIQ 830
Cdd:PRK09580 215 YVHVLYQGRIVK 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
540-582 |
6.80e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 6.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124805679 540 INANINNernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTILN 582
Cdd:PRK00349 618 KGARENN-------LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
752-811 |
6.88e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 6.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124805679 752 SLSGGQkQRIYL-AQNLIKNNKILILDEPTSSLDKLseniiNKALIKYMKD------KTTIIF------------THRL 811
Cdd:PRK10938 401 SLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPL-----NRQLVRRFVDvlisegETQLLFvshhaedapaciTHRL 473
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
751-820 |
7.52e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 751 TSLSGGQKQRIYLAQNLIK---NNKILILDEPTSSL-----DKLSEnIINKaLIkymkDK--TTIIFTHRLDLLNYVDYI 820
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLhfhdiRKLLE-VLHR-LV----DKgnTVVVIEHNLDVIKTADWI 898
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
753-819 |
7.60e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.78 E-value: 7.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124805679 753 LSGGQKQRIYLAQNLIKNNKILILDEPTSSLDKLSENIINKALIKYMKDKTTIIFTHRLDL-LNYVDY 819
Cdd:PRK13540 128 LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLpLNKADY 195
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
541-580 |
7.73e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 7.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124805679 541 NANINNernkkfaLKNVSFFLPHNKSVAIVGKSGSGKTTI 580
Cdd:cd03270 5 GAREHN-------LKNVDVDIPRNKLVVITGVSGSGKSSL 37
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
550-826 |
8.63e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 550 KKF----ALKNVSFFLPHNKSVAIVGKSGSGKTTILNLLTKKNDlNASGEICVGNVPINKINSAVLRSI-VGVITQDPFL 624
Cdd:PRK09700 13 KSFgpvhALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-PTKGTITINNINYNKLDHKLAAQLgIGIIYQELSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 625 FN-LTVRENLMypykayeemlkeqirlieqnqgafinmINNENTKKEKNdddntINTYDseqdinkndmkntyeiytflL 703
Cdd:PRK09700 92 IDeLTVLENLY---------------------------IGRHLTKKVCG-----VNIID--------------------W 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 704 KELQKVQEEIKNNLssdkmkniynDLHIDeflknhfnydnMNVGVNGTSLSggQKQRIYLAQNLIKNNKILILDEPTSSL 783
Cdd:PRK09700 120 REMRVRAAMMLLRV----------GLKVD-----------LDEKVANLSIS--HKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124805679 784 DKLSENIINKALIKYMKDKTTIIF-THRL-DLLNYVDYIGVIEEG 826
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYiSHKLaEIRRICDRYTVMKDG 221
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
751-820 |
9.09e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 9.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124805679 751 TSLSGGQKQRIYLAQNLIKN--NKILILDEPTSSLDKLSENIINKALiKYMKDK--TTIIFTHRLDLLNYVDYI 820
Cdd:cd03270 136 PTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETL-KRLRDLgnTVLVVEHDEDTIRAADHV 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
751-784 |
9.14e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.76 E-value: 9.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 124805679 751 TSLSGGQKQRIYLAQNLIK-------NNKILILDEPTSSLD 784
Cdd:PRK03695 125 NQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
205-466 |
9.27e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 39.13 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 205 AMFCLIASSLGQMIFPMCISKIIN-MYGGKEESL-KYLTNEIYKTVLLIIGISTFSFFRIYFIETSiEKITRRLRTHFFE 282
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNaLTLAKVKDLeSAVTLILLYALLRFSSKLLKELRSLLYRRVQ-QNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 283 KVLNQDVHFFNKQKTGELINRLSNDIEISSKFlihLSFGIRNFISALIGGICALHIsprnLFQSFLLPVSGCLLIGTT-Y 361
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTL---LSYLVFYLVPTLLELIVVSVV----FAFHFGAWLALIVFLSVLlY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124805679 362 AKFVKKISV--LKQEKLSSCID-----FASEKIHNISNVRLLNGESYEKKEFINYLEDVYKIGKKHSLVKSGNHFLFFSI 434
Cdd:cd18560 153 GVFTIKVTEwrTKFRRAANKKDneahdIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLI 232
|
250 260 270
....*....|....*....|....*....|..
gi 124805679 435 ISLFLLHLIYYGNYLIAHKFINTGDLFSLIMY 466
Cdd:cd18560 233 IQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTY 264
|
|
| |
