|
Name |
Accession |
Description |
Interval |
E-value |
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5810-6488 |
0e+00 |
|
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: 797.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5810 AMLAVARHYRLDFSEEHVRVVINQESQSPHHLVLEDMARQLGLALRSVPADVSLIDPWRLPLVVELNDGQMAVLTHMDKH 5889
Cdd:TIGR03375 4 CLLLLARHYGRPVSREALVAGLPLEDGRLTPELLPRAARRAGLSARLVKRSLDDISPLLLPAILLLKDGRACVLLGIDED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5890 GQLSIQLSGDSGLETVVSREALSQRLKG-LFLLRPlNSIPDARVDDYVKPYQKNWFWTLALKDWKRYGDIMLVAMAANVL 5968
Cdd:TIGR03375 84 GKARVLLPETGDGEQELSLDALEALYSGyAIFVRP-QFRFDARADELISPRPKHWFWSTLKESWPLYRDVLIASLLINLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5969 ALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARALRIKNSARPKST 6048
Cdd:TIGR03375 163 ALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTLRSYFLDVAGKKADLILSAKLFERVLGLRMEARPASV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6049 GSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLVQRPLAHLSNEGMRESAI 6128
Cdd:TIGR03375 243 GSFANQLREFESVRDFFTSATLTALIDLPFALLFLLVIAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRESAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6129 RNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTG 6208
Cdd:TIGR03375 323 RNAVLVESLSGLETIKALNAEGRFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELTMG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6209 ALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLMQRPLDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEKVNdL 6288
Cdd:TIGR03375 403 GLIACVMLSGRALAPLGQLAGLLTRYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETPA-L 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6289 DIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTM 6368
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIAL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6369 GRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLV 6448
Cdd:TIGR03375 562 GAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFK 641
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 701771264 6449 ANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:TIGR03375 642 DRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADG 681
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5810-6482 |
0e+00 |
|
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: 644.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5810 AMLAVARHYRLDFSEEHVRVVINQESQSPHHLVLEDMARQLGLALRSVPADVSLIDPWRLPLVVELNDGQMAVLTHMDKh 5889
Cdd:COG2274 19 CLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPAILHWDGNHFVVLEGVDG- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5890 GQLSIQLSGDSglETVVSREALSQRLKG-LFLLRPLNSIPDARVddyvKPYQKNWFWTLALKDWKRYGDIMLVAMAANVL 5968
Cdd:COG2274 98 DKVTIADPATG--RRKLSLEEFAESWTGvALLLEPTPEFDKRGE----KPFGLRWFLRLLRRYRRLLLQVLLASLLINLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5969 ALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARALRIKNSARPK-S 6047
Cdd:COG2274 172 ALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESrS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6048 TGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLVQRPLAHLSNEGMRESA 6127
Cdd:COG2274 252 VGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6128 IRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTT 6207
Cdd:COG2274 332 KRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6208 GALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLMQRPLDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEKvND 6287
Cdd:COG2274 412 GQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSP-PV 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLT 6367
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENIT 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTlilqpqilllDEPTAWLDEISEQQL 6447
Cdd:COG2274 571 LGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARAllrnprililDEATSALDAETEAII 650
|
650 660 670
....*....|....*....|....*....|....*
gi 701771264 6448 VANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:COG2274 651 LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKG 685
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
5952-6244 |
1.65e-128 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 406.82 E-value: 1.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5952 WKRYGDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDR 6031
Cdd:cd18587 1 RRIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6032 VFARALRIKNSARPKSTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLV 6111
Cdd:cd18587 81 LFERVLGLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6112 QRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAV 6191
Cdd:cd18587 161 QKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6192 VLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGL 6244
Cdd:cd18587 241 IVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
34-410 |
1.47e-100 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 332.03 E-value: 1.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 34 LTLGESILFALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSRTTDSSG----SLKNSAAYGLSLTQLVYD 109
Cdd:TIGR01844 3 LTLLDAVLLALANNPELRAARAQRDAGEEQVAQARAALLPQLGLTANYGYSNTYPTESrgrnTDLNSGSSTLTLSQPLFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 110 FGKTNSNISQQQSQRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQ 189
Cdd:TIGR01844 83 GGSTWNAVRAAEAAALAARETLRATAQDLILRTAEAYMEVLRAQEILALAEANLAALKEQLDLARARFDVGLGTRTDVLQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 190 TQTRIAGMRSTLEQYRAARQSAKARLAVLTGVS---AANYQAMPVRLAleqEPLD---NIDYSLIPSVLAAEAMRESSGY 263
Cdd:TIGR01844 163 AEARYASARAQLIQAQNNLDDAKAQLRRLVGQPelaPLAVPSFPAELP---EPLDqllEIAEASNPLLLAAQAAVDAARY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 264 AVDKAKSGHWPTLSLRGGRTRYQSNNSAYWDD-----QIQLNVDAPIYQGGAVSAQVEQAQGARRIAASQVEQAKFDVLQ 338
Cdd:TIGR01844 240 QVEQARAGHLPTLSLTASTGNSDTSSGGSGNSdsdtySVGLNVSIPLYQGGATSAQVRQAAHQLNQSRSTLESQKRTVRQ 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 339 KASVAMADWNGARGRETAGALQLENARRAREVYKNEYKLSKRSLNDLLSIEQDVFQAAYAQINADFDGWQAA 410
Cdd:TIGR01844 320 QVRNAWSNLNAAAASVQAYEQQVASAQKALDAYRQEYQVGTRTLLDVLNAEQELYQARQELANARYDYLQAQ 391
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
35-411 |
1.94e-62 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 219.91 E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 35 TLGESILFALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQislngstghsrttdssgslknsaayglsltQLVYDFGKTN 114
Cdd:COG1538 1 TLDELIERALANNPDLRAARARVEAARAQLRQARAGLLPS------------------------------QELDLGGKRR 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 115 SNISQQQSQRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQTRI 194
Cdd:COG1538 51 ARIEAAKAQAEAAEADLRAARLDLAAEVAQAYFDLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 195 AGMRSTLEQYRAARQSAKARLAVLTGVSAANYQAMPVRLALEQEPLDNIDYSLI------PSVLAAEAMRESSGYAVDKA 268
Cdd:COG1538 131 AQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSealerrPDLRAAEAQLEAAEAEIGVA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 269 KSGHWPTLSLRGGRTRYQSNNSAYWDD---QIQLNVDAPIYQGGAVSAQVEQAQGARRIAASQVEQAKFDVLQKASVAMA 345
Cdd:COG1538 211 RAAFLPSLSLSASYGYSSSDDLFSGGSdtwSVGLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALA 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 346 DWNGARGRETAGALQLENARRAREVYKNEYKLSKRSLNDLLSIEQDVFQAAYAQINADFDGWQAAI 411
Cdd:COG1538 291 ALRAAREQLEALEEALEAAEEALELARARYRAGLASLLDVLDAQRELLQAQLNLIQARYDYLLALV 356
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6133-6482 |
1.52e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 185.80 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6133 LVEAVQSIEDIKLLRAEQRFQNQWNNTNdvaagvgmkQRWLTSllmtwtQEVQSIV----YAVVLLVGCYLV-------- 6200
Cdd:PRK11160 203 LTEWLQGQAELTLFGAEDRYRQQLEQTE---------QQWLAA------QRRQANLtglsQALMILANGLTVvlmlwlaa 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6201 --INGDMTTGALVGT---SILAS-RTIAPLA----QISGVLSrwqqakvARKGLDDLM-QRPldDPEEGKKVHKAHLQGN 6269
Cdd:PRK11160 268 ggVGGNAQPGALIALfvfAALAAfEALMPVAgafqHLGQVIA-------SARRINEITeQKP--EVTFPTTSTAAADQVS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6270 YQLNYAAF-YYDEEEKV-NDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRD 6347
Cdd:PRK11160 339 LTLNNVSFtYPDQPQPVlKGLS---LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6348 MTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGaLGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQP 6427
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG-LEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6428 QILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNG 549
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2127-3843 |
6.49e-33 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 142.60 E-value: 6.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2127 DGNGNWNVGIPASVINGLADGSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQ 2206
Cdd:COG3210 2 SGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2207 PAGTLITVTLNGINYQAVAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSALPTVIVNSVTSDN 2286
Cdd:COG3210 82 GAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2287 ILNITeIAGGQTLSGTVTGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSR 2366
Cdd:COG3210 162 TNTNN-SSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2367 DIVIDANLPGLRVDTVAGDDVINAIEHTQNLIINGTSSGLGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWAEG 2446
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2447 AVTIEVKGSSGAGNDVAIQHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELSGMTQNVEpgqTVNITFAGHTYTATVQ 2526
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVA---STVGTATASTGNASST 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2527 ADGSWKYTVPAADMVNLKEGDTAVQVSVTNKNGNSTDAAQNVSVDTLAPALTVDPVSQDNLLNAAEAKQDLVISGTSTAE 2606
Cdd:COG3210 398 TVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2607 AGQTVTVRLNGESYQATVKADGSWSLTVPAADVGKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDV 2686
Cdd:COG3210 478 NTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2687 INQTEHGQALVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGDTSHT 2766
Cdd:COG3210 558 ASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGS 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2767 VTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLGEAF 2846
Cdd:COG3210 638 AVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2847 YEVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDI---INAAELATGQTISGRVTGVQAGADVTINIGGVNYTAK 2923
Cdd:COG3210 718 QIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLsigLTANTTASGTTLTLANANGNTSAGATLDNAGAEISID 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2924 VQSDLTWSLTlgqdvltalgdGSLKINASVTDGagntgtgsrDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSS 3003
Cdd:COG3210 798 ITADGTITAA-----------GTTAINVTGSGG---------TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGA 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3004 GLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAG 3083
Cdd:COG3210 858 SGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTG 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3084 DDVLNAAEKGADLLLSGMTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKDGDTSVEVSVVNVTGNGASA 3163
Cdd:COG3210 938 AGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3164 GREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGD 3243
Cdd:COG3210 1018 GGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGI 1097
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3244 GVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTV 3323
Cdd:COG3210 1098 TNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTT 1177
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3324 DAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSAN 3403
Cdd:COG3210 1178 GSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDAT 1257
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3404 LAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTAD 3483
Cdd:COG3210 1258 TGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVN 1337
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3484 NVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHGNSGTAD 3563
Cdd:COG3210 1338 AGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGV 1417
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3564 REFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAA 3643
Cdd:COG3210 1418 SGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGA 1497
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3644 GNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEAGQTVTITFGGRTYTAQV 3723
Cdd:COG3210 1498 TASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGD 1577
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3724 ESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNA 3803
Cdd:COG3210 1578 TGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTL 1657
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|
gi 701771264 3804 QAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADN 3843
Cdd:COG3210 1658 SGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDTA 1697
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3165-3260 |
1.70e-31 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 120.86 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3165 REISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGDG 3244
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....*.
gi 701771264 3245 VYTVDASVSDAAGNGS 3260
Cdd:NF033510 82 TYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1962-2058 |
7.16e-30 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 116.24 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1962 TQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLIVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKD 2041
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 2042 GTLTVSASVADKAGNPA 2058
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2565-2661 |
7.89e-30 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 116.24 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2565 AQNVSVDTLAPALTVDPVSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSLTVPAADVGKLTD 2644
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 2645 GNITVTASVEDQAGNPG 2661
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1365-1461 |
4.40e-28 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 111.23 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1365 AREVLVDTQPPSITLNSITADNILNHAEAAQELVITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVADLANLTD 1444
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 1445 GSWSVSASVSDVAGNPA 1461
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
768-864 |
1.12e-27 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 110.07 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 768 SETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVTLKLNGKTYTATVGADGGWSMEVPAADVQAMAD 847
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 848 NSYTLNLSVSDKAGNTT 864
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3764-3857 |
1.53e-27 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 109.69 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3764 REFSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADN 3843
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....
gi 701771264 3844 QYVIKVDVSDAAGN 3857
Cdd:NF033510 82 TYTVTVTVTDAAGN 95
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
43-220 |
2.37e-27 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 112.23 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 43 ALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSR-TTDSSGSLKNSAAYGLSLTQLVYDFGKTNSNISQQQ 121
Cdd:pfam02321 3 ALENNPDLKAAEAEIEAAEANIKLAKSEFLPDLSLSGGYGYNSnNSESGGDDPGTGEVGLGLSQPLFDGGKRRARVKAAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 122 SQRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQTRIAGMRSTL 201
Cdd:pfam02321 83 AQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARLEL 162
|
170
....*....|....*....
gi 701771264 202 EQYRAARQSAKARLAVLTG 220
Cdd:pfam02321 163 LNAEADLELALAQLEQLLG 181
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
6288-6437 |
2.74e-27 |
|
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: 110.82 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLF-FGSIRDNL 6366
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6367 TMGRPL------ASDEEIHRALALSGALGFvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:pfam00005 81 RLGLLLkglskrEKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2664-2761 |
1.28e-26 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 106.99 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2664 SRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTgAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVSALG 2743
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2744 DNTYTVTASITDKAGNTG 2761
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
3547-5237 |
1.50e-26 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 121.41 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3547 TVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKSYLATVSAS 3626
Cdd:COG3210 11 NKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3627 GTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEA 3706
Cdd:COG3210 91 TLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3707 GQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVI 3786
Cdd:COG3210 171 TNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3787 NAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQYVIKVDVSDAAGNKTTGSQNMT 3866
Cdd:COG3210 251 LSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3867 LDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTGAAAGNkiIITLDGVQYVTQVDAKGNWSVGVPASAVSALKNGTAT 3946
Cdd:COG3210 331 DGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGG--LTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3947 ITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTLNGIQYTTTIQPGG 4026
Cdd:COG3210 409 NTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4027 GWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAG 4106
Cdd:COG3210 489 GIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLG 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4107 QKVTVKLGSESYEATVQADGSWSITVAAEDLAKLADGEFSVHAAVNDKAGNPGSADRTLTVDTTAPTITFDKVAGDDIIN 4186
Cdd:COG3210 569 VLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGS 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4187 SAEQQAGQAISGTTNAQPGQ-TITVTFNNHTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPTISiNTFA 4265
Cdd:COG3210 649 GTTGTASANGSNTTGVNTAGgTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALA-NANG 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4266 GDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSNSIGNSAG 4345
Cdd:COG3210 728 DTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAA 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4346 VDRTITVDTTPPqmTITIDSLQNDTGLSASDFITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTGTSWAYADG 4425
Cdd:COG3210 808 GTTAINVTGSGG--TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVA 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4426 PLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDTGLDAHDFITSDNTLTLSGKLGAPLAAGEHA 4505
Cdd:COG3210 886 TSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGD 965
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4506 QISIDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLRVVDDAGNIGSTASQLVTVDTVAPDASKTVTIDSISTDTGLSN 4585
Cdd:COG3210 966 TGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNG 1045
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4586 TDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYFNDGRTLSDGTYQYLVRVVDDAGNVGQSASKNV 4665
Cdd:COG3210 1046 VGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTT 1125
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4666 TVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLNGSLGAPLGSNEFVQISIDGGASWFYATSVNGTRWSYTDGRQ 4745
Cdd:COG3210 1126 TVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTG 1205
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4746 LADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGISDDTGQSASDFITMDTTLTLNGTLGHALASDERVQIS 4825
Cdd:COG3210 1206 GSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGST 1285
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4826 LDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNVGSTANQVVTVDTVAPDTVGSIVSYTDNNGERTGNFDS 4905
Cdd:COG3210 1286 VDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGA 1365
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4906 SYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTFADSGLLDGSYHYVLRVTDKAGNYTESNDFGLTV 4985
Cdd:COG3210 1366 GSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSV 1445
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4986 DTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVVTVNGKTYTSDRGGAVVVDPASNTWYLQIPDADVLSLKSYDV 5065
Cdd:COG3210 1446 AGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLE 1525
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5066 TAQVKSSAGNGNSVDVTHGTVVVGAEASMTPawAFTSATNAIAASFMLDANGMWTFASNQQFATANDRNSYSVSGNFSMT 5145
Cdd:COG3210 1526 GGEGTYGGSSVAEAGTGGGILGAVSGAGSEG--GAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAE 1603
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5146 GSYTTGAYADINRDGHADMLVESTNYSYITQLMNNGDGTYTSTSPGSSATVGALLWYGAVVSIDFQGDGYVDFVMGDAGG 5225
Cdd:COG3210 1604 GTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGA 1683
|
1690
....*....|..
gi 701771264 5226 PDSSTFVNNNAG 5237
Cdd:COG3210 1684 TTAAAGNVATGD 1695
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2167-2262 |
2.39e-26 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 106.22 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2167 RALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTTVPASAVSKLGEA 2246
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....*.
gi 701771264 2247 NYTVTAAVTDAHGNSS 2262
Cdd:NF033510 82 TYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4063-4159 |
2.19e-25 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 103.53 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4063 THNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGQKVTVKLGSESYEATVQADGSWSITVAAEDLAKLAD 4142
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 4143 GEFSVHAAVNDKAGNPG 4159
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3463-3560 |
8.88e-25 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 101.60 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3463 SASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKvSNAAAGDAVTINLGGKTYTATVQSDLSWSLDLPADVLTALG 3542
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGT-TTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3543 NGKLTVTASVTNGHGNSG 3560
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2764-2861 |
1.20e-24 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 101.21 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2764 SHTVTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGlAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLG 2843
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2844 EAFYEVSVSASNGVGNAG 2861
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
672-2388 |
2.14e-24 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 114.48 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 672 NVVTAQASLTAATTAGDNTLNAAEQANDFVISGSATELASGTALTVTLNGKTYATTVGSDGSWSVTVPAADAKSLADGSW 751
Cdd:COG3210 1 GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 752 TVTVSGKDAAGNNISASETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVTLKLNGKTYTATVGADG 831
Cdd:COG3210 81 IGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 832 GWSMEVPAADVQAMADNSYTLNLSVSDKAGNTTTTNASLLVDTTPPEASVNTVAGDDILSVSEQGQAQIISGTSQGAAPG 911
Cdd:COG3210 161 NTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 912 DKVTVSIGSETYQTTVQADGSWSVGVPKEVISSLPEGPNTITVAITDVAGNTGTTTHDITVSSTPPNVAFNAISQDNVLN 991
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 992 AIEATQPLILSGTSNLPDGSHVTVTLNNVNYTAQVQGGVWQVQVPVSDVVKLGDTTYTLSVSGTDTTGNTGTATATLQVD 1071
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1072 TALPTVIVSTFAGDNRVNNSEIANDQMLSGRVTGAHQGDTVTINIGGKNYTATVQSDLTWSTTVPAADLRALGDGDVSIV 1151
Cdd:COG3210 401 GSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1152 ASVTNAHGNTGSGSRDININAQLPGLRINTVSGDDVINAIEQHQDLTVTGTSTHLSAGTIITVRINGVDYQAAVSATGSW 1231
Cdd:COG3210 481 SATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1232 QIGIPAADVAGWPNGKLEMVASSADESGNPVAATRPVDVDLNAVAISINSVTSDGVLNAVEKAADLTLSGKTLGVEAGQT 1311
Cdd:COG3210 561 SNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1312 VVIKFAGHTYTTTVNQSGDWTFTVPAADMRDMIDGRADVSVSVTNVSGNGASGAREVLVDTQPPSITLN--SITADNILN 1389
Cdd:COG3210 641 AALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTIStgSITVTGQIG 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1390 HAEAAQELVITGTStAQPGQTVTVSLNNQSYTGlvladGTWSVTVPVADLANLTDGSWSVSASVSDVAGNPASTSHGMLV 1469
Cdd:COG3210 721 ALANANGDTVTFGN-LGTGATLTLNAGVTITSG-----NAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEI 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1470 DTTAPVVTINTFAGDNIVNRSEHAQAQVLSGKATGAAVGDSVKITVNGVEYSTVLDASGNWSLGLPAEVISGLADGKYTA 1549
Cdd:COG3210 795 SIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATA 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1550 TVVVTDKAGNVGGSSLAFDVATGLPQITINAIAQDDVINAAEKSAEVTVSGTSNQPDGTQITVNLNGVDYAAVVNGNAWS 1629
Cdd:COG3210 875 ASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1630 VKIPAPDVAKLGEASYTVSASVTDASGNANSASHSVLVDSSLPIITINAVAGDNIINLAEVNAGQVLTGSVINAAAGDEV 1709
Cdd:COG3210 955 SAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGT 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1710 TVILGGKSYTVIVQSDLSWNLPLSKEMLTALGDGDLTVHASVTNGRGNTGSTDHDITIDAQLPGLRLDTISGDDIINLAE 1789
Cdd:COG3210 1035 GTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTG 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1790 HNQDLVVSGTCSGLNAGSVVTVTLNGKDYLATVNADGSwsaavpaadvstwpdGVLTVTAKAQDGAQNPIGIDGIVDVDL 1869
Cdd:COG3210 1115 GVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVS---------------AVAGGASSASAGDTTAVAAATTTTTGS 1179
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1870 APVSISVNSVTADNVLNAAEKGVDLVLSGLTTNVEPGQTVTITFAGHRYTTSVNNDGSWSYTVPAADMARLKDGDAQVTV 1949
Cdd:COG3210 1180 AINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTG 1259
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1950 SVSNANGNPATSTQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLIVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSV 2029
Cdd:COG3210 1260 ATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAG 1339
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2030 SVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLSIDPVAGDDIINASEHSQAHTVGGTSTGAAAGDVVT 2109
Cdd:COG3210 1340 GGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSG 1419
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2110 VVVTNGQGTSFTFTTtlDGNGNWNVGIPASVINGLADGSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVI 2189
Cdd:COG3210 1420 TTVAGTTGSSATTGT--GGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGA 1497
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2190 NATEKGQDLVLSGTSNQPAGTLITVTLNGI--NYQAVAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHN 2267
Cdd:COG3210 1498 TASNGGTSTGAGGTAGGTTAEVAKASLEGGegTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGD 1577
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2268 VQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGE 2347
Cdd:COG3210 1578 TGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTL 1657
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|.
gi 701771264 2348 LTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDVI 2388
Cdd:COG3210 1658 SGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDTAP 1698
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1464-1561 |
7.32e-24 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 98.90 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1464 SHGMLVDTTAPVVTINTFAGDNIVNRSEHAQAQVLSGKATGAAvGDSVKITVNGVEYSTVLDASGNWSLGLPAEVISGLA 1543
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEA-GQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1544 DGKYTATVVVTDKAGNVG 1561
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1763-1858 |
1.19e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 98.52 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1763 HDITIDAQLPGLRLDTISGDDIINLAEHNQDLVVSGTcSGLNAGSVVTVTLNGKDYLATVNADGSWSAAVPAADVSTWPD 1842
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGT-TTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*.
gi 701771264 1843 GVLTVTAKAQDGAQNP 1858
Cdd:NF033510 81 GTYTVTVTVTDAAGNT 96
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
868-964 |
5.80e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 96.59 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 868 ASLLVDTTPPEASVNTVAGDDILSVSEQGQAQIISGTSQgAAPGDKVTVSIGSETYQTTVQADGSWSVGVPKEVISSLPE 947
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 948 GPNTITVAITDVAGNTG 964
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2465-2562 |
5.86e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 96.59 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2465 QHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELSGmTQNVEPGQTVNITFAGHTYTATVQADGSWKYTVPAADMVNLK 2544
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2545 EGDTAVQVSVTNKNGNST 2562
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3862-3957 |
6.33e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 96.21 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3862 SQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTgAAAGNKIIITLDGVQYVTQVDAKGNWSVGVPASAVSALK 3941
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*.
gi 701771264 3942 NGTATITATLTDSAGN 3957
Cdd:NF033510 80 DGTYTVTVTVTDAAGN 95
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4250-4344 |
1.17e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 95.44 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4250 VTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDa 4329
Cdd:NF033510 4 VTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADGT- 82
|
90
....*....|....*
gi 701771264 4330 YVIHASVSNSIGNSA 4344
Cdd:NF033510 83 YTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1865-1959 |
2.70e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 94.67 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1865 VDVDLAPVSISVNSVTADNVLNAAEKGVDLVLSGlTTNVEPGQTVTITFAGHRYTTSVNNDGSWSYTVPAADMARLKDGD 1944
Cdd:NF033510 4 VTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADGT 82
|
90
....*....|....*
gi 701771264 1945 AQVTVSVSNANGNPA 1959
Cdd:NF033510 83 YTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3564-3659 |
2.86e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 94.67 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3564 REFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGmSEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAA 3643
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*.
gi 701771264 3644 GNLTVTAAGSSSAGNP 3659
Cdd:NF033510 81 GTYTVTVTVTDAAGNT 96
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3363-3460 |
8.41e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 93.13 E-value: 8.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3363 SHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSaNLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLG 3442
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTT-TAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3443 EANYTLTATATSSIGNSA 3460
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2066-2163 |
9.26e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 93.13 E-value: 9.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2066 VDITEPKLSIDPVAGDDIINASEHSQAHTVGGTSTgAAAGDVVTVVVtNGQgtsfTFTTTLDGNGNWNVGIPASVINGLA 2145
Cdd:NF033510 6 VDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTL-NGK----TYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2146 DGSYTITASVTDAAGNSG 2163
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
670-763 |
1.05e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 92.74 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 670 TLNVVTAQASLTAATTAGDNTLNAAEQANDFVISGSATeLASGTALTVTLNGKTYATTVGSDGSWSVTVPAADAKSLADG 749
Cdd:NF033510 3 PVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....
gi 701771264 750 SWTVTVSGKDAAGN 763
Cdd:NF033510 82 TYTVTVTVTDAAGN 95
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3664-3760 |
2.78e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 91.58 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3664 RSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGkTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKD 3743
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 3744 GDASVKVSVTNVNGNGA 3760
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3065-3161 |
3.03e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 91.58 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3065 HTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGmTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKD 3144
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 3145 GDTSVEVSVVNVTGNGA 3161
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1068-1162 |
4.02e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 91.20 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1068 LQVDTALPTVIVSTFAGDNRVNNSEIANDQMLSGRVTGAhQGDTVTINIGGKNYTATVQSDLTWSTTVPAADLRALGDGD 1147
Cdd:NF033510 4 VTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAE-AGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADGT 82
|
90
....*....|....*
gi 701771264 1148 VSIVASVTNAHGNTG 1162
Cdd:NF033510 83 YTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1265-1362 |
3.01e-20 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 88.89 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1265 TRPVDVDLNAVAISINSVTSDGVLNAVEKAADLTLSGkTLGVEAGQTVVIKFAGHTYTTTVNQSGDWTFTVPAADMRDMI 1344
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1345 DGRADVSVSVTNVSGNGA 1362
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4163-4244 |
9.39e-20 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 87.35 E-value: 9.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4163 RTLTVDTTAPTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAV--------------DFLGAADG 4228
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATvdadgswsvtvpaaDLAALADG 81
|
90
....*....|....*.
gi 701771264 4229 SYQISASVSDKAGNSS 4244
Cdd:NF033510 82 TYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2365-2460 |
9.96e-20 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 87.35 E-value: 9.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2365 SRDIVIDANLPGLRVDTVAGDDVINAIEHTQNLIINGTSSGlGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWA 2444
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*.
gi 701771264 2445 EGAVTIEVKGSSGAGN 2460
Cdd:NF033510 80 DGTYTVTVTVTDAAGN 95
|
|
| tolC |
PRK09465 |
outer membrane channel protein; Reviewed |
43-338 |
1.04e-19 |
|
outer membrane channel protein; Reviewed
Pssm-ID: 236529 [Multi-domain] Cd Length: 446 Bit Score: 96.16 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 43 ALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSR-TTDSSGSLKNSAAYGLSLTQLVYDFGKTNS-NISQQ 120
Cdd:PRK09465 32 ARLSNPELLKAAADRDAAFEKINEARSPLLPQLGLGAGYTYSNgYRDANGIDSNGTSASLQLTQTIFDMSKWRAlTLAEK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 121 QSQRESYRYQlmATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQ--------T 192
Cdd:PRK09465 112 AAGIADVTYQ--TAQQTLILRTATAYFNVLRAIDNLSFTEAEKRAIYRQLDQTTQRFNVGLVAITDVQNAQaqydtvlaN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 193 RIAGmRSTLEQ-YRAARQ---SAKARLAVLTGVSAANYQAMPVRLALEQEPLDNIDysLIPSVLAAEAMRESsgyaVDKA 268
Cdd:PRK09465 190 EVLA-RNNLDNaYEALRQitgNYYPELAVLNTERFSTPKPQSVNALLKEAEKRNLS--LLSARLSQDLAREQ----IRLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 269 KSGHWPTLSL----------RGGRTRYQSNNSAYWDDQIQLNVDAPIYQGGAVSAQVEQAQGARRIAASQVEQAKFDVLQ 338
Cdd:PRK09465 263 QAGHMPTLDLtasygisdtsYSGANGTQYDDSDMGQNKVGLNLSLPLYSGGAVNSQVKQAQYNFVGASEQLESAHRSVVQ 342
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1165-1262 |
1.11e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.96 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1165 SRDININAQLPGLRINTVSGDDVINAIEQHQDLTVTGTSThLSAGTIITVRINGVDYQAAVSATGSWQIGIPAADVAGWP 1244
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1245 NGKLEMVASSADESGNPV 1262
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1564-1658 |
1.31e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.96 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1564 SLAFDVATGLPQITINAIAQDDVINAAEKSAEVTVSGTSNQPDGTQITVNLNGVDYAAVVNGN-AWSVKIPAPDVAKLGE 1642
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADgSWSVTVPAADLAALAD 80
|
90
....*....|....*.
gi 701771264 1643 ASYTVSASVTDASGNA 1658
Cdd:NF033510 81 GTYTVTVTVTDAAGNT 96
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2265-2362 |
1.89e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.58 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2265 SHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVkGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALG 2344
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEA-GQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2345 NGELTITASVTNGHGNTG 2362
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1662-1759 |
2.11e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.19 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1662 SHSVLVDSSLPIITINAVAGDNIINLAEVNAGQVLTGSViNAAAGDEVTVILGGKSYTVIVQSDLSWNLPLSKEMLTALG 1741
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTT-TAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1742 DGDLTVHASVTNGRGNTG 1759
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3962-4060 |
2.25e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.19 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3962 SHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTeLAVGTQVTVTLNGIQYTTTIQPGGGWSVTVPANQVQNLA 4041
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*....
gi 701771264 4042 HGSgYTVMASATDSANNAT 4060
Cdd:NF033510 80 DGT-YTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2964-3061 |
2.28e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.19 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2964 SRDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSSGlSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQ 3043
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3044 AGDITVSAGGTSSSGNPV 3061
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3263-3360 |
3.29e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 85.81 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3263 SHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAgDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLA 3342
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAG-QTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3343 DGKVTINASLTDSAGNTG 3360
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2864-2961 |
4.04e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 85.42 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2864 SSTLEVASTLPGVIINAVAIDDIINAAELATGQTISGRVTGvQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALG 2943
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2944 DGSLKINASVTDGAGNTG 2961
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
967-1053 |
2.08e-17 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 80.80 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 967 THDITVSSTPPNVAFNAISQDNVLNAIEATQPLILSGTSNLPDGSHVTVTLNNVNYTAQVQG-GVWQVQVPVSDVVKLGD 1045
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDAdGSWSVTVPAADLAALAD 80
|
....*...
gi 701771264 1046 TTYTLSVS 1053
Cdd:NF033510 81 GTYTVTVT 88
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4677-4776 |
4.39e-17 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 80.00 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4677 TVTVDSIT----TDSGFSNSDFITNDNTLTLNGSLGAplGSNEFVQISIDGGASWFYATSVNGTRWSYTDGRQLADGDHT 4752
Cdd:pfam19077 1 TLSIPTIDlaagSDTGVSDSDNITNDTTPTFTGTNED--GDVVTVTVSIDGNGVTGTATAGADGNWSFTPPAALADGTYT 78
|
90 100
....*....|....*....|....
gi 701771264 4753 WQVRVVDLAGNVGATTSQTVTVDT 4776
Cdd:pfam19077 79 LTVTVTDIAGNTATSSPLSFTIDT 102
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
6293-6479 |
9.32e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQIlldgislgqldTADLRRDMTLLSQQARL---FFGSIRDNLTMG 6369
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVpdsLPLTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 ---------RPLASDE-EIHRALALSGALGFVQKQKnglnyliteggAGLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:NF040873 82 rwarrglwrRLTRDDRaAVDDALERVGLADLAGRQL-----------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 701771264 6440 DEISEQQLVANLASWLG-NRTLVVATHRIPILQLVDRIIVL 6479
Cdd:NF040873 151 DAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| biofilm_BapA_N |
NF033677 |
BapA prefix-like domain; Two largely unrelated repetitive proteins, both named ... |
414-476 |
1.57e-15 |
|
BapA prefix-like domain; Two largely unrelated repetitive proteins, both named biofilm-associated protein BapA (from Salmonella enterica and from Paracoccus denitrificans) share homology domains at the two ends. Both lack a typical signal peptide for translocation by Sec, and instead depend on type I secretion for export and for contribution to biofilm formation. The conserved prefix (i.e. N-terminal) domain is shared by a number of other large, repetitive proteins of Proteobacteria thought to be associated with adhesion or biofilm formation.
Pssm-ID: 411274 [Multi-domain] Cd Length: 64 Bit Score: 74.13 E-value: 1.57e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 414 VISRKDAEKTLVTGDGNlsVALSSPSVIQIHGSAKDVAHYVRQGNDLLVYMKDGSVIRCNGYF 476
Cdd:NF033677 3 VISKETGVVLTQTQGEV--VLLNEPSVVKIKVSREDVASYTRQGNDLVITLKDGETIVIENFF 63
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
755-844 |
4.15e-14 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 71.75 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 755 VSGKDAAGNNISASE--TLVVDTQAP-SLTLDILAGDNIINAAE-HNAAVTVSGKT--DAEAGQVVTLKLNGKTYTATVG 828
Cdd:NF012196 1 VTSHDAAGNTATATAhhTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVggDVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|
gi 701771264 829 ADG----GWSMEVPAADVQA 844
Cdd:NF012196 81 DLGngqlGYSVDVDTSDLLN 100
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
428-963 |
5.59e-14 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 79.31 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 428 DGNL-SVALSSPSVIQIHGSAKDVAHYVRQGNDLLVYMKDGSVIRCNGYFmeEEGRPGHHSeLVF--DDGK-ALTHitFD 503
Cdd:NF040520 17 DGQLkKVVLNQPSIIQIGVNQKDIKSIEKQGNDLVITLKNGEKIVLENFF--NEANTTEHS-LAFptEDGKfVEAQ--FD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 504 EAGAAVGTQG---------TELTAIAVPIESIE---PFMDGSLLgdmpwgwvagavagGVGIGALLAHG---------GD 562
Cdd:NF040520 92 DSGKFIRYTGlthltqlayTETPTQAATMAAVDddpGISKSQLL--------------KAGLAALAAEGlylwavkddDK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 563 KSHTEVIDNTKPvesARPTfmvtdnkgdsqgllssnAVTDDSTPTFSGSGQPGATIQVKDANGNTIASTMVDSNGNWKVL 642
Cdd:NF040520 158 DDSNGPVDITPP---ATPT-----------------ATLADDTQTITGKAEANAKIYIKDATGKVIATGQADASGNYTIK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 643 LSEQPDGTHTYSVVQID-GNKITSAGEITLNVVT-AQASLTAATTAGDNTLNAAEQANDFVisgsATELASGTAL-TVTL 719
Cdd:NF040520 218 LDQPLVNGNKVNVTAIDaAGNASKATVVTGTKDTiAPDAPQAQLNADGTIVTGKTEANAKV----SVYDADGKLLgTVTA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 720 NgktyattvgSDGSWSV------------TVPAADA---KS-----------LADGSWTVTVSG---------------- 757
Cdd:NF040520 294 N---------KEGLYSIkvsppltsdkggTVIAEDAagnKSepskiiagkdtIAPDQPLVEVNKegtsiegraeanakvq 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 758 -KDAAGNNISaseTLVVDTQ-------APSLT-------------------LDILAGDNIIN----AAEHNAA-VTVSGK 805
Cdd:NF040520 365 iKDADGKVIG---TGTADAQgkfqitlSPALKtsqkgtiivedaagnqskpLEITAGKDTIApdkpTAQINAAgTSVTGT 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 806 tdAEAGQVVTLK-LNGKT-YTATVGADGGWSMEVPAadvqAMADNSYTlNLSVSDKAGN-TTTTNASLLVDTTPPEASVN 882
Cdd:NF040520 442 --AEANAKIEIKdSAGKViGTGTADADGKFTITISP----ALTDKNIG-KVYAIDAAGNrSDATDVTGTKDTIAPNKPVL 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 883 TVAGDDILSVSEQGQAqiiSGTSQGAAPgdKVTVSIGSETYQT-----------TVQADGSWSVGVPKEvissLPEGPNT 951
Cdd:NF040520 515 QKVTDDVGAVKGAIAA---GGETDDAKP--KLSGSGEAKATLTiydngqaigtvTVGDNGKWSFTLDKD----LALGKHK 585
|
650
....*....|..
gi 701771264 952 ITVAITDVAGNT 963
Cdd:NF040520 586 ITLTQTDAAGNT 597
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2752-2838 |
4.04e-13 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 68.67 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2752 SITDKAGNTGD--TSHTVTVDTVAP-TLSIDTIAGDNILNADE-KTGDVVISGTSTGLA-AGTSVTVNLNGKNYAATVGA 2826
Cdd:NF012196 2 TSHDAAGNTATatAHHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVGGDVkVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 2827 DGK----WTTTVPAGD 2838
Cdd:NF012196 82 LGNgqlgYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2254-2353 |
2.64e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 66.36 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2254 VTDAHGN--SSSDSHNVQVD-SALPTVIVNSVTSDNILNITEIAGGQTL-SGTVTGAVK-GDVVTINLGGKLYQATVQDD 2328
Cdd:NF012196 3 SHDAAGNtaTATAHHTVTIDtHADATITIDTVTGDNVLNAAESQQPTTTiTGTVGGDVKvGDPVTLTVNGHTYTGTVVDL 82
|
90 100
....*....|....*....|....*....
gi 701771264 2329 ----LSWSLPVSKeilTALGNGELTITAS 2353
Cdd:NF012196 83 gngqLGYSVDVDT---SDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3451-3549 |
3.33e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 66.36 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3451 TATSSIGNSAGASASLLV---DTAAPGITINPVTADNVLNAAEIAAGQTL-SGKVS-NAAAGDAVTINLGGKTYTATVQS 3525
Cdd:NF012196 2 TSHDAAGNTATATAHHTVtidTHADATITIDTVTGDNVLNAAESQQPTTTiTGTVGgDVKVGDPVTLTVNGHTYTGTVVD 81
|
90 100
....*....|....*....|....*...
gi 701771264 3526 D----LSWSLDLPADVLTAlGNGKLTVT 3549
Cdd:NF012196 82 LgngqLGYSVDVDTSDLLN-NPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3750-3837 |
4.25e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 65.97 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3750 VSVTNVNGN--GASAEREFSVDATAPG-LTINPIATDNVINAAEAGAGVT-VTGT--SNAQAGQTVTLTLDGKTYTGVVK 3823
Cdd:NF012196 1 VTSHDAAGNtaTATAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTvgGDVKVGDPVTLTVNGHTYTGTVV 80
|
90
....*....|....*...
gi 701771264 3824 ADG----TWSITLDSTAL 3837
Cdd:NF012196 81 DLGngqlGYSVDVDTSDL 98
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
4151-4238 |
9.70e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 64.81 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4151 VNDKAGNPGSA--DRTLTVDTTAP-TITFDKVAGDDIINSAE-QQAGQAISGTT--NAQPGQTITVTFNNHTYQA-VDFL 4223
Cdd:NF012196 3 SHDAAGNTATAtaHHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVggDVKVGDPVTLTVNGHTYTGtVVDL 82
|
90
....*....|....*
gi 701771264 4224 GAADGSYQISASVSD 4238
Cdd:NF012196 83 GNGQLGYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2655-2752 |
1.34e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 64.43 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2655 DQAGNPGSAS--RDVLVDVTVP-KVTIGTMATDDVINQTEHGQALV-ISGTSTG-AQAGDIVTVTLGNKQYTGVVDTNGN 2729
Cdd:NF012196 5 DAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTtITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLGN 84
|
90 100
....*....|....*....|....*..
gi 701771264 2730 ----WSVGVpraDVSALGDNTYTVTAS 2752
Cdd:NF012196 85 gqlgYSVDV---DTSDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3849-3950 |
2.44e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 63.66 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3849 VDVSDAAGNKTTGS--QNMTLDTTAP-TVSFNAVAGDDIINLEE-HAQAQIISGSSTG-AAAGNKIIITLDGVQYVTQVD 3923
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100 110
....*....|....*....|....*....|.
gi 701771264 3924 AKGN----WSVGVPasaVSALKNGTATITAT 3950
Cdd:NF012196 81 DLGNgqlgYSVDVD---TSDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1949-2038 |
2.86e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 63.66 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1949 VSVSNANGNPATST--QEYSVDASAP-TLIIDPLSGDNLLNAAEAKQPLI-VSGSSS--AEPGQEVTVTLNNVNYTATVG 2022
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|
gi 701771264 2023 ADG----RWSVSVPASDLAA 2038
Cdd:NF012196 81 DLGngqlGYSVDVDTSDLLN 100
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1352-1441 |
4.97e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 62.89 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1352 VSVTNVSGNGASGA--REVLVDTQPP-SITLNSITADNILNHAEAAQELV-ITGTST--AQPGQTVTVSLNNQSYTGLVL 1425
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|
gi 701771264 1426 ADG----TWSVTVPVADLAN 1441
Cdd:NF012196 81 DLGngqlGYSVDVDTSDLLN 100
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1452-1533 |
6.59e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 62.50 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1452 SVSDVAGNP--ASTSHGMLVDTTAPV-VTINTFAGDNIVNRSE-HAQAQVLSGKATG-AAVGDSVKITVNGVEYSTVLDA 1526
Cdd:NF012196 2 TSHDAAGNTatATAHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
....*..
gi 701771264 1527 SGNWSLG 1533
Cdd:NF012196 82 LGNGQLG 88
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3551-3637 |
2.00e-10 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 60.96 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3551 SVTNGHGNSGTA--DREFTVDASLPG-IRINTVAGDDVVNAIE-HNQNLIISGSASG-MSEGSTVTVTINGKSYLATVSA 3625
Cdd:NF012196 2 TSHDAAGNTATAtaHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 3626 SG----TWSAAVPAGD 3637
Cdd:NF012196 82 LGngqlGYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3161-3251 |
5.93e-10 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 59.81 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3161 ASAGREISVDT-AAPTLQINTIAGDDVLNAAEAGQPLV-ITGT--SNAEPGQTVTVTLNNETYTGIVQANG----TWSIT 3232
Cdd:NF012196 13 ATAHHTVTIDThADATITIDTVTGDNVLNAAESQQPTTtITGTvgGDVKVGDPVTLTVNGHTYTGTVVDLGngqlGYSVD 92
|
90
....*....|....*....
gi 701771264 3233 VPadkASALGDGVYTVDAS 3251
Cdd:NF012196 93 VD---TSDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2952-3028 |
1.58e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.65 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2952 SVTDGAGNTGTGS--RDVTIDA-ALPGIRVNTIAGDDVINAIE-HGLNLVINGTSSG-LSEGSTVTVTINGKDYAATVRA 3026
Cdd:NF012196 2 TSHDAAGNTATATahHTVTIDThADATITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
..
gi 701771264 3027 DG 3028
Cdd:NF012196 82 LG 83
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3950-4033 |
1.85e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.27 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3950 TLTDSAGNEG--ANSHTVEV-NAARIGLTIDTISHDDVINAAEARQDLT-IGGSSTELA-VGTQVTVTLNGIQYTTTIQP 4024
Cdd:NF012196 2 TSHDAAGNTAtaTAHHTVTIdTHADATITIDTVTGDNVLNAAESQQPTTtITGTVGGDVkVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|...
gi 701771264 4025 GG----GWSVTVP 4033
Cdd:NF012196 82 LGngqlGYSVDVD 94
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1756-1836 |
2.00e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.27 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1756 GNTG--STDHDITIDAQLPG-LRLDTISGDDIINLAE-HNQDLVVSGTCSG-LNAGSVVTVTLNGKDYLATVNADG---- 1826
Cdd:NF012196 8 GNTAtaTAHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLGngql 87
|
90
....*....|
gi 701771264 1827 SWSAAVPAAD 1836
Cdd:NF012196 88 GYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2452-2553 |
2.02e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.27 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2452 VKGSSGAGNDV--AIQHQVTVDLT-EVVISINAVTGDNVLNAAE-KGANLELSG-MTQNVEPGQTVNITFAGHTYTATVQ 2526
Cdd:NF012196 1 VTSHDAAGNTAtaTAHHTVTIDTHaDATITIDTVTGDNVLNAAEsQQPTTTITGtVGGDVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|....*....
gi 701771264 2527 AD--GSWKYTVPaADMVNLKEGDTAVQVS 2553
Cdd:NF012196 81 DLgnGQLGYSVD-VDTSDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
854-954 |
3.69e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 57.50 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 854 LSVSDKAGNTTTTNAS--LLVDTTPPEA-SVNTVAGDDILSVSEQGQA-QIISGT-SQGAAPGDKVTVSIGSETYQTTVQ 928
Cdd:NF012196 1 VTSHDAAGNTATATAHhtVTIDTHADATiTIDTVTGDNVLNAAESQQPtTTITGTvGGDVKVGDPVTLTVNGHTYTGTVV 80
|
90 100 110
....*....|....*....|....*....|
gi 701771264 929 ADG----SWSVGVPkevISSLPEGPNTITV 954
Cdd:NF012196 81 DLGngqlGYSVDVD---TSDLLNNPNDVTA 107
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3053-3152 |
4.19e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 57.50 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3053 GTSSSGNPVTI--DHTVNVDLSA-VAITIGQIAGDDVLNAAEKGADLLL-SG-MTQNVEAGQTISITFAGHTYTTQV--A 3125
Cdd:NF012196 3 SHDAAGNTATAtaHHTVTIDTHAdATITIDTVTGDNVLNAAESQQPTTTiTGtVGGDVKVGDPVTLTVNGHTYTGTVvdL 82
|
90 100
....*....|....*....|....*..
gi 701771264 3126 SDGSWKFTVPAnDMKGLKDGDTSVEVS 3152
Cdd:NF012196 83 GNGQLGYSVDV-DTSDLLNNPNDVTAT 108
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
610-885 |
6.22e-09 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 63.13 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 610 GSGQPGATIQVKDANGNTIASTMVDSNGNWKVLLSEQPDGTHTYSVVQID--GNKIT----SAGEITLNVVTAQASLTAa 683
Cdd:NF040520 355 GRAEANAKVQIKDADGKVIGTGTADAQGKFQITLSPALKTSQKGTIIVEDaaGNQSKpleiTAGKDTIAPDKPTAQINA- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 684 ttAGDNTLNAAEQANDFVISGSAtelasgtaltvtlnGKTYAT-TVGSDGSWSVTV-PAADAKSLAdgswtvTVSGKDAA 761
Cdd:NF040520 434 --AGTSVTGTAEANAKIEIKDSA--------------GKVIGTgTADADGKFTITIsPALTDKNIG------KVYAIDAA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 762 GNNISASETL-VVDTQAP------SLTLDILAGDNIINAAEH--NAAVTVSGKtdAEAGQVVTLKLNGKTY-TATVGADG 831
Cdd:NF040520 492 GNRSDATDVTgTKDTIAPnkpvlqKVTDDVGAVKGAIAAGGEtdDAKPKLSGS--GEAKATLTIYDNGQAIgTVTVGDNG 569
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 832 GWSMEVpaadVQAMADNSYTLNLSVSDKAGNT--------------TTTNASLLVDTTPPEASVNTVA 885
Cdd:NF040520 570 KWSFTL----DKDLALGKHKITLTQTDAAGNTsevsdpftftvvapKTASASEQSEVDTSNTETASLA 633
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2552-2652 |
1.13e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.96 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2552 VSVTNKNGNSTDAA--QNVSVDTLAPA-LTVDPVSQDNLLNAAEAKQDLV-ISGTST--AEAGQTVTVRLNGESYQATVK 2625
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100 110
....*....|....*....|....*....|.
gi 701771264 2626 ADG----SWSLTVPAADvgkLTDGNITVTAS 2652
Cdd:NF012196 81 DLGngqlGYSVDVDTSD---LLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2353-2439 |
1.32e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.96 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2353 SVTNGHGNTG--SGSRDIVIDANLPG-LRVDTVAGDDVINAIE-HTQNLIINGTSSG-LGAGSAVTVTINGKDYAATVRA 2427
Cdd:NF012196 2 TSHDAAGNTAtaTAHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 2428 DG----SWQAAVPGED 2439
Cdd:NF012196 82 LGngqlGYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
4051-4138 |
1.47e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.96 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4051 SATDSANNATSAT--HNISVDTVAPI-VTIADISGDNAINAAEQQQPLT-IRGTSS--AEAGQKVTVKLGSESYEATVQA 4124
Cdd:NF012196 2 TSHDAAGNTATATahHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*...
gi 701771264 4125 DG----SWSITVAAEDLA 4138
Cdd:NF012196 82 LGngqlGYSVDVDTSDLL 99
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1256-1353 |
2.36e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.18 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1256 DESGNPVAAT--RPVDVDLNA-VAISINSVTSDGVLNAVEKAADLTL-SGKTLG-VEAGQTVVIKFAGHTYTTTV--NQS 1328
Cdd:NF012196 5 DAAGNTATATahHTVTIDTHAdATITIDTVTGDNVLNAAESQQPTTTiTGTVGGdVKVGDPVTLTVNGHTYTGTVvdLGN 84
|
90 100
....*....|....*....|....*
gi 701771264 1329 GDWTFTVPaADMRDMIDGRADVSVS 1353
Cdd:NF012196 85 GQLGYSVD-VDTSDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3353-3439 |
2.61e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.18 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3353 TDSAGNTG--SGSHEVTVNTGLP-SVNFNAISGDNVLNAIE-KGEVLTLSGT-SANLAPGTAVIVTLNGKNYTATTDASG 3427
Cdd:NF012196 4 HDAAGNTAtaTAHHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTvGGDVKVGDPVTLTVNGHTYTGTVVDLG 83
|
90
....*....|....*.
gi 701771264 3428 N----WRVDVQPGDLA 3439
Cdd:NF012196 84 NgqlgYSVDVDTSDLL 99
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3655-3751 |
3.49e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 54.80 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3655 SAGNP--ISIDRSVNVDLS-PVAVSVENITADNVLNAAEKGADLVL-SGK-TQNVEAGQTVTITFGGRTYTAQVESD--G 3727
Cdd:NF012196 6 AAGNTatATAHHTVTIDTHaDATITIDTVTGDNVLNAAESQQPTTTiTGTvGGDVKVGDPVTLTVNGHTYTGTVVDLgnG 85
|
90 100
....*....|....*....|....
gi 701771264 3728 SWHYTVPAsDIAGLKDGDASVKVS 3751
Cdd:NF012196 86 QLGYSVDV-DTSDLLNNPNDVTAT 108
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
3786-3957 |
3.91e-08 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 60.44 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3786 INAAeagaGVTVTGTSNAQAGQTVTLTlDGKT-YTGVVKADGTWSITLDStalgALADNQyVIKVDVSDAAGNKTTGSQ- 3863
Cdd:NF040520 431 INAA----GTSVTGTAEANAKIEIKDS-AGKViGTGTADADGKFTITISP----ALTDKN-IGKVYAIDAAGNRSDATDv 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3864 NMTLDTTAPTVSFNAVAGDDIINLeehaQAQIISGSST--------GAAAGNKIIITLDGVQYV--TQVDAKGNWSVgvp 3933
Cdd:NF040520 501 TGTKDTIAPNKPVLQKVTDDVGAV----KGAIAAGGETddakpklsGSGEAKATLTIYDNGQAIgtVTVGDNGKWSF--- 573
|
170 180
....*....|....*....|....
gi 701771264 3934 aSAVSALKNGTATITATLTDSAGN 3957
Cdd:NF040520 574 -TLDKDLALGKHKITLTQTDAAGN 596
|
|
| FG-GAP_3 |
pfam13517 |
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ... |
5270-5342 |
7.84e-08 |
|
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.
Pssm-ID: 433275 [Multi-domain] Cd Length: 61 Bit Score: 52.23 E-value: 7.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 5270 DLNNDGMVDIAQHTTNGGNIYalstmFNKGDGTFTWSQNFIntmysatgSAAANNAVSMTWADFDGDGYMDLY 5342
Cdd:pfam13517 1 DLDGDGKLDLVVANDGGLRLY-----LNNGDGTFTFITSVS--------LGGGGGGLSVAVGDLDGDGRLDLL 60
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
4859-5018 |
8.25e-08 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 59.28 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4859 VRIIDQAGNVGSTANQVVTVDTVAPDTvGSIVSYTDNNGERTGNFDSSYSTDDTSPVLNGTlnqaladGE---IAQIFRD 4935
Cdd:NF040520 485 VYAIDAAGNRSDATDVTGTKDTIAPNK-PVLQKVTDDVGAVKGAIAAGGETDDAKPKLSGS-------GEakaTLTIYDN 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4936 GVLVGNVTITGGTRWTFA-DSGLLDGSYHYVLRVTDKAGNYTE-SNDFGLTVDTSVPTTKALVNGLNTTDT-TPIITGSV 5012
Cdd:NF040520 557 GQAIGTVTVGDNGKWSFTlDKDLALGKHKITLTQTDAAGNTSEvSDPFTFTVVAPKTASASEQSEVDTSNTeTASLADSV 636
|
....*.
gi 701771264 5013 DANLVH 5018
Cdd:NF040520 637 GLNTLK 642
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
2523-2960 |
9.29e-08 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 59.28 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2523 ATVQADGSWKYTVPAADmvNLKEGDTaVQVSVTNKNGNSTDAAQNV-SVDTLAPaltVDPVSQdnlLNAaeakQDLVISG 2601
Cdd:NF040520 204 ATGQADASGNYTIKLDQ--PLVNGNK-VNVTAIDAAGNASKATVVTgTKDTIAP---DAPQAQ---LNA----DGTIVTG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2602 TstAEAGQTVTVrlngesYQA------TVKA--DGSWSLTVPAAdvgkLTDGNI-TVTAsvEDQAGNPGSASRDVLVDVT 2672
Cdd:NF040520 271 K--TEANAKVSV------YDAdgkllgTVTAnkEGLYSIKVSPP----LTSDKGgTVIA--EDAAGNKSEPSKIIAGKDT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2673 V----PKVTIGTMATddVINQTEHGQALVISGTSTGAQAGdivtvtlgnkqyTGVVDTNGNWSVGVPradvSALGDNTyT 2748
Cdd:NF040520 337 IapdqPLVEVNKEGT--SIEGRAEANAKVQIKDADGKVIG------------TGTADAQGKFQITLS----PALKTSQ-K 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2749 VTASITDKAGNTgdtSHTVTVdtvapTLSIDTIAGDNI---LNADektGDVVisgtsTGLA-AGTSVTV-NLNGKN-YAA 2822
Cdd:NF040520 398 GTIIVEDAAGNQ---SKPLEI-----TAGKDTIAPDKPtaqINAA---GTSV-----TGTAeANAKIEIkDSAGKViGTG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2823 TVGADGKWTTTV-PAGDVGKLGeafyevSVSASNGVGNagsQSSTLEVASTLPGV-----IINAVaIDDI--INAAELAT 2894
Cdd:NF040520 462 TADADGKFTITIsPALTDKNIG------KVYAIDAAGN---RSDATDVTGTKDTIapnkpVLQKV-TDDVgaVKGAIAAG 531
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 2895 GQT------ISGRvtgVQAGADVTINIGGVNY-TAKVQSDLTWSLTLGQDvltaLGDGSLKINASVTDGAGNT 2960
Cdd:NF040520 532 GETddakpkLSGS---GEAKATLTIYDNGQAIgTVTVGDNGKWSFTLDKD----LALGKHKITLTQTDAAGNT 597
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2679-2771 |
1.10e-07 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 53.04 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2679 GTMATDDVINQTehgqALVISGTstgAQAGDIVTVTL----GNKQYTGVVDTNGNWSVGVPradvSALGDNTYTVTASIT 2754
Cdd:pfam19077 16 GVSDSDNITNDT----TPTFTGT---NEDGDVVTVTVsidgNGVTGTATAGADGNWSFTPP----AALADGTYTLTVTVT 84
|
90
....*....|....*...
gi 701771264 2755 DKAGNTGDTSH-TVTVDT 2771
Cdd:pfam19077 85 DIAGNTATSSPlSFTIDT 102
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1650-1750 |
1.47e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.87 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1650 SVTDASGNA--NSASHSVLVDSSLPI-ITINAVAGDNIINLAEVNAGQVL-TGSVI-NAAAGDEVTVILGGKSYTVIVQS 1724
Cdd:NF012196 2 TSHDAAGNTatATAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTTiTGTVGgDVKVGDPVTLTVNGHTYTGTVVD 81
|
90 100 110
....*....|....*....|....*....|
gi 701771264 1725 D----LSWNLPLSKemlTALGDGDLTVHAS 1750
Cdd:NF012196 82 LgngqLGYSVDVDT---SDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1851-1950 |
1.59e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.87 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1851 AQDGAQNP--IGIDGIVDVDL-APVSISVNSVTADNVLNAAEKGVDLVL-SGLTT-NVEPGQTVTITFAGHRYTTSV--N 1923
Cdd:NF012196 3 SHDAAGNTatATAHHTVTIDThADATITIDTVTGDNVLNAAESQQPTTTiTGTVGgDVKVGDPVTLTVNGHTYTGTVvdL 82
|
90 100
....*....|....*....|....*..
gi 701771264 1924 NDGSWSYTVPaADMARLKDGDAQVTVS 1950
Cdd:NF012196 83 GNGQLGYSVD-VDTSDLLNNPNDVTAT 108
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
566-696 |
1.85e-07 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 58.13 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 566 TEVIDNTKPVESARPTFM-VTDNKGDSQGLLSSNAVTDDSTPTFSGSGQPGATIQVKDaNGNTIASTMVDSNGNWKVLLS 644
Cdd:NF040520 498 TDVTGTKDTIAPNKPVLQkVTDDVGAVKGAIAAGGETDDAKPKLSGSGEAKATLTIYD-NGQAIGTVTVGDNGKWSFTLD 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 645 -EQPDGTHTYSVVQIDGNKITS--AGEITLNVVTAQASLTAATTAGDnTLNAAEQ 696
Cdd:NF040520 577 kDLALGKHKITLTQTDAAGNTSevSDPFTFTVVAPKTASASEQSEVD-TSNTETA 630
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
954-1039 |
1.91e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.49 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 954 VAITDVAGNTGT--TTHDITVSSTPPN-VAFNAISQDNVLNAIEATQPLIL-SGT--SNLPDGSHVTVTLNNVNYTAQVQ 1027
Cdd:NF012196 1 VTSHDAAGNTATatAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTTiTGTvgGDVKVGDPVTLTVNGHTYTGTVV 80
|
90
....*....|....*..
gi 701771264 1028 GG-----VWQVQVPVSD 1039
Cdd:NF012196 81 DLgngqlGYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1076-1153 |
2.09e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.49 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1076 TVIVSTFAGDNRVNNSEIAND-QMLSGRVTG-AHQGDTVTINIGGKNYTATVQSD----LTWSTTVPAADLRalgDGDVS 1149
Cdd:NF012196 28 TITIDTVTGDNVLNAAESQQPtTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLgngqLGYSVDVDTSDLL---NNPND 104
|
....
gi 701771264 1150 IVAS 1153
Cdd:NF012196 105 VTAT 108
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
607-815 |
2.26e-07 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 57.74 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 607 TFSGSGQPGATIQVKDANGNTIASTMVDSNGNWKVLLSEQPDGTHTYSVVQID--GNKITSAGEITLNVVTAQASLTAAT 684
Cdd:NF040520 437 SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITISPALTDKNIGKVYAIDaaGNRSDATDVTGTKDTIAPNKPVLQK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 685 TAGDN-----TLNAAEQANDF--VISGSAtelASGTALTVTLNGKTYAT-TVGSDGSWSVTVpaadAKSLADGSWTVTVS 756
Cdd:NF040520 517 VTDDVgavkgAIAAGGETDDAkpKLSGSG---EAKATLTIYDNGQAIGTvTVGDNGKWSFTL----DKDLALGKHKITLT 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 757 GKDAAGNNISASETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVT 815
Cdd:NF040520 590 QTDAAGNTSEVSDPFTFTVVAPKTASASEQSEVDTSNTETASLADSVGLNTLKLAQETT 648
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2052-2154 |
3.43e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 51.72 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2052 DKAGNP--ANADRGMRVDIT-EPKLSIDPVAGDDIINASEHSQAHT-VGGTSTG-AAAGDVVTVVVtNGQgtsfTFTTTL 2126
Cdd:NF012196 5 DAAGNTatATAHHTVTIDTHaDATITIDTVTGDNVLNAAESQQPTTtITGTVGGdVKVGDPVTLTV-NGH----TYTGTV 79
|
90 100 110
....*....|....*....|....*....|..
gi 701771264 2127 DGNGN----WNVGIPASVingLADGSYTITAS 2154
Cdd:NF012196 80 VDLGNgqlgYSVDVDTSD---LLNNPNDVTAT 108
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
1504-1564 |
4.65e-07 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 51.50 E-value: 4.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 1504 GAAVGDSVKITVNGVEYSTVLDASGNWSLGLPAEvisgLADGKYTATVVVTDKAGNVGGSS 1564
Cdd:pfam19077 38 GDVVTVTVSIDGNGVTGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGNTATSS 94
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2875-2952 |
5.52e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 51.33 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2875 GVIINAVAIDDIINAAEL-ATGQTISGRVTG-VQAGADVTINIGGVNYTAKVQSD----LTWSLtlgqDVLT-ALGDGSL 2947
Cdd:NF012196 28 TITIDTVTGDNVLNAAESqQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLgngqLGYSV----DVDTsDLLNNPN 103
|
....*
gi 701771264 2948 KINAS 2952
Cdd:NF012196 104 DVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
4235-4316 |
1.49e-06 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 50.18 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4235 SVSDKAGN--SSSADKQVTLSGEVP-TISINTFAGDDIVSAAEHGTPLVL-SGVT--NAPAGQTVTITLNGQKYTTTV-- 4306
Cdd:NF012196 2 TSHDAAGNtaTATAHHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTTiTGTVggDVKVGDPVTLTVNGHTYTGTVvd 81
|
90
....*....|
gi 701771264 4307 NGDGTWSYTL 4316
Cdd:NF012196 82 LGNGQLGYSV 91
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
784-874 |
1.70e-06 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 49.57 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 784 ILAGDNIINaaehNAAVTVSGKTDAEAGQVVTLKL--NGKTYTATVGADGGWSMEVPAadvqAMADNSYTLNLSVSDKAG 861
Cdd:pfam19077 17 VSDSDNITN----DTTPTFTGTNEDGDVVTVTVSIdgNGVTGTATAGADGNWSFTPPA----ALADGTYTLTVTVTDIAG 88
|
90
....*....|....
gi 701771264 862 NT-TTTNASLLVDT 874
Cdd:pfam19077 89 NTaTSSPLSFTIDT 102
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
580-666 |
1.93e-06 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 49.57 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 580 PTFMVTDNKGDSQGLLSSNAVTDDSTPTFSGSGQPGATIQV--KDANGNTIASTMVDSNGNWKV-LLSEQPDGTHTYSVV 656
Cdd:pfam19077 3 SIPTIDLAAGSDTGVSDSDNITNDTTPTFTGTNEDGDVVTVtvSIDGNGVTGTATAGADGNWSFtPPAALADGTYTLTVT 82
|
90
....*....|..
gi 701771264 657 QID--GNKITSA 666
Cdd:pfam19077 83 VTDiaGNTATSS 94
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2711-2866 |
4.73e-06 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 50.75 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2711 VTVTLGNKQYTGVVDTnGNWSVGVPRADVSALGDNTYTVTAS-ITDKAGNTG--DTSHTVTVdtvAPTLSIDTIagdNIL 2787
Cdd:NF032891 33 ATATLGGVAVTSLTDT-ADKKVWTGEVVVPASSELTVGLVVSgYQDLSGNVGeeDTSHSLPI---TPTITITPI---GDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2788 NADEKTgDVVISGTSTGLAAGTSVTV-------NLNGKNYAATVGADGKWTTTvpAGDVGKLGEAFYEVSVSASNGVGNA 2860
Cdd:NF032891 106 DESEAA-TVVISGTSTRFEDGQTLTVevkaqgsETVEVTGTATVQSDGSWTTN--ELDLSSWPDGTITVTVTGTNNLGVA 182
|
....*.
gi 701771264 2861 GSQSST 2866
Cdd:NF032891 183 AEEAST 188
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
1374-1471 |
1.32e-05 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 47.26 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1374 PPSITLN------SITADNILNHAeaAQELVITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVAdlanLTDGSW 1447
Cdd:pfam19077 4 IPTIDLAagsdtgVSDSDNITNDT--TPTFTGTNEDGDVVTVTVSIDGNGVTGTATAGADGNWSFTPPAA----LADGTY 77
|
90 100
....*....|....*....|....*
gi 701771264 1448 SVSASVSDVAGNPASTSHGML-VDT 1471
Cdd:pfam19077 78 TLTVTVTDIAGNTATSSPLSFtIDT 102
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
2522-2775 |
1.42e-05 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 51.96 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2522 TATVQADGSWKYTVPAAdmvnLKEGDTAvQVSVTNKNGNSTDAAQ-NVSVDTLAPAltvDPVSQdnlLNAAeakQDLVis 2600
Cdd:NF040520 375 TGTADAQGKFQITLSPA----LKTSQKG-TIIVEDAAGNQSKPLEiTAGKDTIAPD---KPTAQ---INAA---GTSV-- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2601 gTSTAEAGQTVTVRLNGES--YQATVKADGSWSLTVPAAdvgkLTDGNITvTASVEDQAGNPgSASRDVL--VDVTVPKV 2676
Cdd:NF040520 439 -TGTAEANAKIEIKDSAGKviGTGTADADGKFTITISPA----LTDKNIG-KVYAIDAAGNR-SDATDVTgtKDTIAPNK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2677 TIGTMATDDVinQTEHGQALVISGT-------STGAQAGDIVTVtLGNKQYTGVVD--TNGNWSVGVPRaDVsALGDNTY 2747
Cdd:NF040520 512 PVLQKVTDDV--GAVKGAIAAGGETddakpklSGSGEAKATLTI-YDNGQAIGTVTvgDNGKWSFTLDK-DL-ALGKHKI 586
|
250 260
....*....|....*....|....*...
gi 701771264 2748 TVTAsiTDKAGNTGDTSHTVTVDTVAPT 2775
Cdd:NF040520 587 TLTQ--TDAAGNTSEVSDPFTFTVVAPK 612
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2006-2160 |
1.71e-05 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 49.21 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2006 QEVTVTL--NNVNYTATVGADGRW--SVSVPASDLAALkdgTLTVSaSVADKAGNPANADRGMRVDITePKLSIDPVaGD 2081
Cdd:NF032891 31 QEATATLggVAVTSLTDTADKKVWtgEVVVPASSELTV---GLVVS-GYQDLSGNVGEEDTSHSLPIT-PTITITPI-GD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2082 diINASEHSQAhTVGGTSTGAAAGDVVTVVVT--NGQGTSFTFTTTLDGNGNWNVgiPASVINGLADGSYTITASVTDAA 2159
Cdd:NF032891 105 --VDESEAATV-VISGTSTRFEDGQTLTVEVKaqGSETVEVTGTATVQSDGSWTT--NELDLSSWPDGTITVTVTGTNNL 179
|
.
gi 701771264 2160 G 2160
Cdd:NF032891 180 G 180
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
660-756 |
2.09e-05 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 46.71 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 660 GNKITSAGEITLNVVT-AQASLTAATTAGDNTLNAAEQANDFV-ISGSATELA-SGTALTVTLNGKTYATTVGSDG---- 732
Cdd:NF012196 8 GNTATATAHHTVTIDThADATITIDTVTGDNVLNAAESQQPTTtITGTVGGDVkVGDPVTLTVNGHTYTGTVVDLGngql 87
|
90 100
....*....|....*....|....
gi 701771264 733 SWSVTVPAADaksLADGSWTVTVS 756
Cdd:NF012196 88 GYSVDVDTSD---LLNNPNDVTAT 108
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
6298-6482 |
2.93e-05 |
|
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: 47.75 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLdgislgqLDTADLRRDMTLLSQqarlffgsirdnltmgrplasdee 6377
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLL------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6378 ihralalsgalgfvqkqknglNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWL-- 6455
Cdd:smart00382 51 ---------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 701771264 6456 -----GNRTLVVATHRIPILQ------LVDRIIVLDNG 6482
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGpallrrRFDRRIVLLLI 147
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2893-3062 |
4.32e-05 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 48.05 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2893 ATGQTISGRVTGVQAGADVTINIGGVNYTakvqsdlTWSLTLGQDVLTALGDGSLKINASVT-------DGAGNTGTGSR 2965
Cdd:NF032891 15 AIGQSVTVTLTFDKAVQEATATLGGVAVT-------SLTDTADKKVWTGEVVVPASSELTVGlvvsgyqDLSGNVGEEDT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2966 DVTIDAAlPGIRVNTIAGDDVINAIehglNLVINGTSSGLSEGSTVTVTINGKDYA-------ATVRADGSWQTvvPGNE 3038
Cdd:NF032891 88 SHSLPIT-PTITITPIGDVDESEAA----TVVISGTSTRFEDGQTLTVEVKAQGSEtvevtgtATVQSDGSWTT--NELD 160
|
170 180
....*....|....*....|....
gi 701771264 3039 VSQWQAGDITVSAGGTSSSGNPVT 3062
Cdd:NF032891 161 LSSWPDGTITVTVTGTNNLGVAAE 184
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
801-954 |
6.11e-05 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 47.67 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 801 TVSGKTDAEAGQVVTLKLNG----KTYTATVGAD--GGWSMEVPA----ADVQAMADNSYTLNLSVS---DKAGNTTTTN 867
Cdd:NF032891 7 VTFNPTHQAIGQSVTVTLTFdkavQEATATLGGVavTSLTDTADKkvwtGEVVVPASSELTVGLVVSgyqDLSGNVGEED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 868 ASLLVDTTPpeasvnTVAGDDILSVSEQGQAQ-IISGTSQGAAPGDKVTVSI---GSETYQ----TTVQADGSWSvgVPK 939
Cdd:NF032891 87 TSHSLPITP------TITITPIGDVDESEAATvVISGTSTRFEDGQTLTVEVkaqGSETVEvtgtATVQSDGSWT--TNE 158
|
170
....*....|....*
gi 701771264 940 EVISSLPEGPNTITV 954
Cdd:NF032891 159 LDLSSWPDGTITVTV 173
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2001-2061 |
6.17e-05 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 45.33 E-value: 6.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 2001 SAEPGQEVTVTL----NNVNYTATVGADGRWSVSVPasdlAALKDGTLTVSASVADKAGNPANAD 2061
Cdd:pfam19077 34 TNEDGDVVTVTVsidgNGVTGTATAGADGNWSFTPP----AALADGTYTLTVTVTDIAGNTATSS 94
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3251-3351 |
6.98e-05 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 45.17 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3251 SVSDAAGN--GSSASHNLSVDVTVP-SISFGVVAGDDVINLAEHGQAQ--IISGSSSGAAAGDKITVTIGANSWTTTVDA 3325
Cdd:NF012196 2 TSHDAAGNtaTATAHHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTttITGTVGGDVKVGDPVTLTVNGHTYTGTVVD 81
|
90 100 110
....*....|....*....|....*....|
gi 701771264 3326 AGN----WSIGVPASVvsqLADGKVTINAS 3351
Cdd:NF012196 82 LGNgqlgYSVDVDTSD---LLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1153-1239 |
8.31e-05 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 45.17 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1153 SVTNAHGNTG--SGSRDININAQLPG-LRINTVSGDDVINAIEQHQDLT-VTGT-STHLSAGTIITVRINGVDYQAAVSA 1227
Cdd:NF012196 2 TSHDAAGNTAtaTAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTvGGDVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 1228 TG----SWQIGIPAAD 1239
Cdd:NF012196 82 LGngqlGYSVDVDTSD 97
|
|
| FG-GAP_3 |
pfam13517 |
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ... |
5332-5393 |
9.03e-05 |
|
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.
Pssm-ID: 433275 [Multi-domain] Cd Length: 61 Bit Score: 43.37 E-value: 9.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 5332 DFDGDGYMDLYMGMSRAGTgglLMMNDGKGNLLTGTAVGSEKYNGTVSVAV-DWNMDGRMDII 5393
Cdd:pfam13517 1 DLDGDGKLDLVVANDGGLR---LYLNNGDGTFTFITSVSLGGGGGGLSVAVgDLDGDGRLDLL 60
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
3745-4220 |
1.50e-04 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 48.50 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3745 DASVKVSVTNVNGN-----GASAEREFSVDATAP---GLTINPIATDNVINAAEAGAgvtVTGTSNAQA--GQTVTLTLD 3814
Cdd:NF040520 188 EANAKIYIKDATGKviatgQADASGNYTIKLDQPlvnGNKVNVTAIDAAGNASKATV---VTGTKDTIApdAPQAQLNAD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3815 GKTYTGVVKADGTWSI-TLDSTALG---ALADNQYVIK------------VDVSDAAGNKTTGSQNM----TLDTTAPTV 3874
Cdd:NF040520 265 GTIVTGKTEANAKVSVyDADGKLLGtvtANKEGLYSIKvsppltsdkggtVIAEDAAGNKSEPSKIIagkdTIAPDQPLV 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3875 SFNAvAGDDIINLEEhAQAQIISGSSTGaaagnKIIITldGVqyvtqVDAKGNWSVGVPasavSALKNG-TATItaTLTD 3953
Cdd:NF040520 345 EVNK-EGTSIEGRAE-ANAKVQIKDADG-----KVIGT--GT-----ADAQGKFQITLS----PALKTSqKGTI--IVED 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3954 SAGNEganSHTVEVNAARigltiDTISHDDV---INA--------AEARQDLTIGGSSTELaVGTQvTVTLNGiQYTTTI 4022
Cdd:NF040520 405 AAGNQ---SKPLEITAGK-----DTIAPDKPtaqINAagtsvtgtAEANAKIEIKDSAGKV-IGTG-TADADG-KFTITI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4023 QpgggwsvtvPANQVQNlaHGSGYtvmasATDSANNATSATHNISV-DTVAP----IVTIADISGD--NAINAAEQQQPL 4095
Cdd:NF040520 474 S---------PALTDKN--IGKVY-----AIDAAGNRSDATDVTGTkDTIAPnkpvLQKVTDDVGAvkGAIAAGGETDDA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4096 TIRGTSSAEAGQKVT-----VKLGSesyeATVQADGSWSITVAAEdlakLADGEFSVHAAVNDKAGNPGSADRTLTVDTT 4170
Cdd:NF040520 538 KPKLSGSGEAKATLTiydngQAIGT----VTVGDNGKWSFTLDKD----LALGKHKITLTQTDAAGNTSEVSDPFTFTVV 609
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 701771264 4171 APTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAV 4220
Cdd:NF040520 610 APKTASASEQSEVDTSNTETASLADSVGLNTLKLAQETTNETNSQQQESV 659
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
3492-3657 |
1.60e-04 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 46.13 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3492 AAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLS--W--SLDLPADVLTALGngkLTVTaSVTNGHGNSGTADREFT 3567
Cdd:NF032891 15 AIGQSVTVTLTFDKAVQEATATLGGVAVTSLTDTADKkvWtgEVVVPASSELTVG---LVVS-GYQDLSGNVGEEDTSHS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3568 VDASlPGIRINTVAGDDVVNAiehnQNLIISGSASGMSEGSTVTVTI---NGKSYL----ATVSASGTWSaaVPAGDVSL 3640
Cdd:NF032891 91 LPIT-PTITITPIGDVDESEA----ATVVISGTSTRFEDGQTLTVEVkaqGSETVEvtgtATVQSDGSWT--TNELDLSS 163
|
170
....*....|....*..
gi 701771264 3641 WAAGNLTVTAAGSSSAG 3657
Cdd:NF032891 164 WPDGTITVTVTGTNNLG 180
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
5282-5704 |
2.26e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 48.02 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5282 HTTNGGNIYALSTMFNKGDGTFTWSQNFINTMYSATGSAAANNAVSMTWADFDGDGYMDLYMGMSRAGTGGLLMMNDGKG 5361
Cdd:COG3468 17 TGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGGGGNS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5362 NLLTGTAVGSEKYNGTVSVAVDWNMDGRMDIIKLANTGQSYMYTNDGLKGVASF--TSSKFGSATTSQVSGAALVDYDWD 5439
Cdd:COG3468 97 GTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGgtGAAAAGGGTGSGGGGSGGGGGAGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5440 GAQDLLIFRQNGSVTLERNTNAVAPGTAIHLKIVDSQGINVFFGNTVKLYNAAGELVASQVINAQSGIGINDASALVSFY 5519
Cdd:COG3468 177 GGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5520 GLNPNETYHAELVRAINGVSSNTTWNGLTAGDGRESYALTADAATGVHAGTLTGTGYNDTFIAEQGTYVYNGGGGWETSS 5599
Cdd:COG3468 257 GAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5600 DHQTWSATGGMDVVDFRNSTVGVTVDLGKTGAQNTGFNTATFSNIEGIVGSSHDDVITGNSGNNTFEGGGGNDTFNIGSG 5679
Cdd:COG3468 337 GGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGL 416
|
410 420
....*....|....*....|....*
gi 701771264 5680 GHDTllYKLLNGSDATGGNGHDVVN 5704
Cdd:COG3468 417 TLTG--GTLTVNGNYTGNNGTLVLN 439
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
1942-2060 |
3.77e-04 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 45.36 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1942 DGDAQVTVSVSN---ANGNPATSTQEYSVDASaPTLIIDPLSGDNLLNAAEakqpLIVSGSSSA-EPGQEVTVTLN---- 2013
Cdd:NF032891 63 SSELTVGLVVSGyqdLSGNVGEEDTSHSLPIT-PTITITPIGDVDESEAAT----VVISGTSTRfEDGQTLTVEVKaqgs 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 701771264 2014 ---NVNYTATVGADGRWSVSvpASDLAALKDGTLTVSASVADKAGNPANA 2060
Cdd:NF032891 138 etvEVTGTATVQSDGSWTTN--ELDLSSWPDGTITVTVTGTNNLGVAAEE 185
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
4378-4445 |
7.74e-04 |
|
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).
Pssm-ID: 239028 [Multi-domain] Cd Length: 317 Bit Score: 45.37 E-value: 7.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 4378 ITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTG-----TSWA--YADGPLPDGTVTYHVRVVDNAGNV 4445
Cdd:cd02110 219 LVSGGRVEIGGVAWSGGRGIRRVEVSLDGGRTWQEARLEGplagpRAWRqwELDWDLPPGEYELVARATDSTGNV 293
|
|
| FG-GAP_3 |
pfam13517 |
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ... |
5383-5446 |
9.00e-04 |
|
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.
Pssm-ID: 433275 [Multi-domain] Cd Length: 61 Bit Score: 40.67 E-value: 9.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 5383 DWNMDGRMDIIkLANTGQSYMYTNDGlKGVASFtSSKFGSATTSQVSGAALVDYDWDGAQDLLI 5446
Cdd:pfam13517 1 DLDGDGKLDLV-VANDGGLRLYLNNG-DGTFTF-ITSVSLGGGGGGLSVAVGDLDGDGRLDLLV 61
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2605-2758 |
1.13e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 43.82 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2605 AEAGQTVTVRLNGESYQATVKAdgswslTVPAADVGKLTD--------GNITVTASVE-----------DQAGNPGSASR 2665
Cdd:NF032891 14 QAIGQSVTVTLTFDKAVQEATA------TLGGVAVTSLTDtadkkvwtGEVVVPASSEltvglvvsgyqDLSGNVGEEDT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2666 DVLVDVTvPKVTIGTMATDDVINQTEhgqaLVISGTSTGAQAGDIVTVTL-------GNKQYTGVVDTNGNWSvgVPRAD 2738
Cdd:NF032891 88 SHSLPIT-PTITITPIGDVDESEAAT----VVISGTSTRFEDGQTLTVEVkaqgsetVEVTGTATVQSDGSWT--TNELD 160
|
170 180
....*....|....*....|
gi 701771264 2739 VSALGDNTYTVTASITDKAG 2758
Cdd:NF032891 161 LSSWPDGTITVTVTGTNNLG 180
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
1398-1567 |
1.51e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 45.41 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1398 VITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVAdlanLTDGSwSVSASVSDVAGN-PASTSHGMLVDTTAPVV 1476
Cdd:NF040520 437 SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITISPA----LTDKN-IGKVYAIDAAGNrSDATDVTGTKDTIAPNK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1477 -TINTFAGDN------IVNRSEHAQAQ-VLSGKATGAAVgdsVKITVNGVEYSTV-LDASGNWSLGLPAEvisgLADGKY 1547
Cdd:NF040520 512 pVLQKVTDDVgavkgaIAAGGETDDAKpKLSGSGEAKAT---LTIYDNGQAIGTVtVGDNGKWSFTLDKD----LALGKH 584
|
170 180
....*....|....*....|
gi 701771264 1548 TATVVVTDKAGNVGGSSLAF 1567
Cdd:NF040520 585 KITLTQTDAAGNTSEVSDPF 604
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1551-1623 |
1.59e-03 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 41.32 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1551 VVVTDKAGNVGGSSLAFDV-----ATGlpQITINAIAQDDVINAAE-KSAEVTVSGT--SNQPDGTQITVNLNGVDYAAV 1622
Cdd:NF012196 1 VTSHDAAGNTATATAHHTVtidthADA--TITIDTVTGDNVLNAAEsQQPTTTITGTvgGDVKVGDPVTLTVNGHTYTGT 78
|
.
gi 701771264 1623 V 1623
Cdd:NF012196 79 V 79
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
1756-1850 |
1.92e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 43.05 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1756 GNTGSTDHDITIDAQlPGLRLDTISGDDIINLAehnqDLVVSGTCSGLNAGSVVTVTLN-------GKDYLATVNADGSW 1828
Cdd:NF032891 80 GNVGEEDTSHSLPIT-PTITITPIGDVDESEAA----TVVISGTSTRFEDGQTLTVEVKaqgsetvEVTGTATVQSDGSW 154
|
90 100
....*....|....*....|..
gi 701771264 1829 SaaVPAADVSTWPDGVLTVTAK 1850
Cdd:NF032891 155 T--TNELDLSSWPDGTITVTVT 174
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
3166-3359 |
1.96e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 45.03 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3166 EISV--DTAAP---TLQINTiAGDdvlnaaeagqplVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVpadkASA 3240
Cdd:NF040520 414 EITAgkDTIAPdkpTAQINA-AGT------------SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITI----SPA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3241 LGDG----VYtvdasVSDAAGNGSSASHNLSV-DVTVPSISFGVVAGDDVinLAEHGQaqiISGSSSGAAAGDKITVTIG 3315
Cdd:NF040520 477 LTDKnigkVY-----AIDAAGNRSDATDVTGTkDTIAPNKPVLQKVTDDV--GAVKGA---IAAGGETDDAKPKLSGSGE 546
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 3316 ANSWTT-----------TVDAAGNWSIgvpaSVVSQLADGKVTINASLTDSAGNT 3359
Cdd:NF040520 547 AKATLTiydngqaigtvTVGDNGKWSF----TLDKDLALGKHKITLTQTDAAGNT 597
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
1995-2194 |
2.25e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 44.64 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1995 IVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPAsdlaALKDGTLTvSASVADKAGNPANA-DRGMRVDITEPKL 2073
Cdd:NF040520 437 SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITISP----ALTDKNIG-KVYAIDAAGNRSDAtDVTGTKDTIAPNK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2074 SIDPVAGDDIinaSEHSQAHTVGGTS-------TGAAAGDVVTVVVTNGQGTSftfTTTLDGNGNWNVgipaSVINGLAD 2146
Cdd:NF040520 512 PVLQKVTDDV---GAVKGAIAAGGETddakpklSGSGEAKATLTIYDNGQAIG---TVTVGDNGKWSF----TLDKDLAL 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 2147 GSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEK 2194
Cdd:NF040520 582 GKHKITLTQTDAAGNTSEVSDPFTFTVVAPKTASASEQSEVDTSNTET 629
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
2476-2692 |
2.45e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 44.64 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2476 VISINAvTGDNVLNAAEKGANLELSGMTQNVepgqtvnitfaghTYTATVQADGswKYTV---PAadmvnLKEGDTAvQV 2552
Cdd:NF040520 428 TAQINA-AGTSVTGTAEANAKIEIKDSAGKV-------------IGTGTADADG--KFTItisPA-----LTDKNIG-KV 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2553 SVTNKNGNSTDAAQNVSV-DTLAPALTVDPVSQDNL------LNAAEAKQDLVISGTSTAEAGQTVTVRLNGesyQA--- 2622
Cdd:NF040520 486 YAIDAAGNRSDATDVTGTkDTIAPNKPVLQKVTDDVgavkgaIAAGGETDDAKPKLSGSGEAKATLTIYDNG---QAigt 562
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 2623 -TVKADGSWSLTVpaadVGKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDVINQTEH 2692
Cdd:NF040520 563 vTVGDNGKWSFTL----DKDLALGKHKITLTQTDAAGNTSEVSDPFTFTVVAPKTASASEQSEVDTSNTET 629
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
689-769 |
3.84e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 42.28 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 689 NTLNAAEQANdFVISGSATELASGTALTVTLN-------GKTYATTVGSDGSWSVTvpAADAKSLADGSWTVTVSGKDAa 761
Cdd:NF032891 103 GDVDESEAAT-VVISGTSTRFEDGQTLTVEVKaqgsetvEVTGTATVQSDGSWTTN--ELDLSSWPDGTITVTVTGTNN- 178
|
....*...
gi 701771264 762 gNNISASE 769
Cdd:NF032891 179 -LGVAAEE 185
|
|
| PRK08026 |
PRK08026 |
FliC/FljB family flagellin; |
648-881 |
5.67e-03 |
|
FliC/FljB family flagellin;
Pssm-ID: 236140 [Multi-domain] Cd Length: 529 Bit Score: 43.19 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 648 DGTHTYSVvqIDGNKITSAGEItLNVVTAQASLTAATTAGDNTLNAAeqANDFVISGSATELASGTALTVTLNGKTYatt 727
Cdd:PRK08026 199 DTTGLYDV--KTKNAALTTADA-LAKLGDGDKVTATATGGDYTYNAK--SGKYQAADLAATLTPDVGGTAGASYTIK--- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 728 vgsDGSWSVTVpAADAKSLADGSWTVTVSGKDAAGNNISAsetlvvdtqAPSLTLDILAGDNIINAAEHNAAVTVSGKTD 807
Cdd:PRK08026 271 ---DGTYEVNV-DSDGKITLGGSALYIDATGNLTTNNAGA---------ATKATLDALKKTASEGAATAKAALAAAGVTV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 808 AEAGQVVTLKLNGkTYTATVGADGGWSMEVPaADVQAMADN------SYTLNLSVSDKAGNTTTTNASLLVDTTPPEASV 881
Cdd:PRK08026 338 ADGVTAKTVKMSY-TDKNGKVIDGGYAVKTG-DDYYAADYDeitgaiSATTTYYTAKDGTTKTAANKLGGADGKTEVVTI 415
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4556-4658 |
5.77e-03 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 39.58 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4556 SQLVTVDTVAPdaskTVTIDSISTDTGLSNTDfvtSDTSLTVHGSLGAPllAGEYVQISLDGgTVWQTVVTIGSTWYFN- 4634
Cdd:NF033510 1 THPVTVDTTAP----ALTINPVAGDDVLNAAE---QGQGLTLSGTTTAE--AGQTVTVTLNG-KTYTATVDADGSWSVTv 70
|
90 100
....*....|....*....|....*..
gi 701771264 4635 ---DGRTLSDGTYQYLVRVVDDAGNVG 4658
Cdd:NF033510 71 paaDLAALADGTYTVTVTVTDAAGNTS 97
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
4065-4579 |
6.47e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 43.10 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4065 NISVDTVAPIVTIADISGDNainaaeqqqpLTIRGTssAEAGQKVTVKLGSESYEATVQADGSWSITVAAEDlaKLADGE 4144
Cdd:NF040520 161 NGPVDITPPATPTATLADDT----------QTITGK--AEANAKIYIKDATGKVIATGQADASGNYTIKLDQ--PLVNGN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4145 fSVHAAVNDKAGNPGSADR-TLTVDTTAPtitfdkvagdDIINSAEQQAGQAISGttNAQPGQTITVtfnnhtYQAVD-F 4222
Cdd:NF040520 227 -KVNVTAIDAAGNASKATVvTGTKDTIAP----------DAPQAQLNADGTIVTG--KTEANAKVSV------YDADGkL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4223 LGAA----DGSYQISAS------------VSDKAGNSSSADKQV----TLSGEVPTISINTfAGDDIVSAAEHGTPLVLS 4282
Cdd:NF040520 288 LGTVtankEGLYSIKVSppltsdkggtviAEDAAGNKSEPSKIIagkdTIAPDQPLVEVNK-EGTSIEGRAEANAKVQIK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4283 GVTNAPAGqtvtitlngqkyTTTVNGDGTWSYTLGSsavsALADGD-AYVIhasVSNSIGNSagvdrtitvdTTPPQMTI 4361
Cdd:NF040520 367 DADGKVIG------------TGTADAQGKFQITLSP----ALKTSQkGTII---VEDAAGNQ----------SKPLEITA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4362 TIDSLQNDtglSASDFITADNKVVvkgslSGALGNNEKAQISLDGGKTwtdlVVTGTswAYADG--------PLPDGTVT 4433
Cdd:NF040520 418 GKDTIAPD---KPTAQINAAGTSV-----TGTAEANAKIEIKDSAGKV----IGTGT--ADADGkftitispALTDKNIG 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4434 YhVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDT-GLDAHDFITSDNTLTLSGKlgaplaaGE-HAQISI-D 4510
Cdd:NF040520 484 K-VYAIDAAGNRSDATDVTGTKDTIAPNKPVLQKVTDDVGAVkGAIAAGGETDDAKPKLSGS-------GEaKATLTIyD 555
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4511 GGKTWVDVSV-SGTSWSYVDGRQLADGDHLYQLRVVDDAGNIgSTASQLVTVDTVAPDASKTVTIDSIST 4579
Cdd:NF040520 556 NGQAIGTVTVgDNGKWSFTLDKDLALGKHKITLTQTDAAGNT-SEVSDPFTFTVVAPKTASASEQSEVDT 624
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2344-2459 |
6.82e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 41.51 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2344 GNGELTITASVTN---GHGNTGSGSRDIVIDANlPGLRVDTVAGDDVINAiehtQNLIINGTSSGLGAGSAVTVTINGKD 2420
Cdd:NF032891 62 ASSELTVGLVVSGyqdLSGNVGEEDTSHSLPIT-PTITITPIGDVDESEA----ATVVISGTSTRFEDGQTLTVEVKAQG 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 701771264 2421 YA-------ATVRADGSWqaAVPGEDVARWAEGAVTIEVKGSSGAG 2459
Cdd:NF032891 137 SEtvevtgtATVQSDGSW--TTNELDLSSWPDGTITVTVTGTNNLG 180
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
4007-4147 |
7.15e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 41.51 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4007 TQVTVTLNGIQYTTTIQPGGG--W--SVTVPANQVqnlaHGSGYTVmASATDSANNATSATHNISVDtVAPIVTIADISG 4082
Cdd:NF032891 31 QEATATLGGVAVTSLTDTADKkvWtgEVVVPASSE----LTVGLVV-SGYQDLSGNVGEEDTSHSLP-ITPTITITPIGD 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 4083 DNAINAAEqqqpLTIRGTSSA-EAGQKVTVKL---GSESYE----ATVQADGSWsiTVAAEDLAKLADGEFSV 4147
Cdd:NF032891 105 VDESEAAT----VVISGTSTRfEDGQTLTVEVkaqGSETVEvtgtATVQSDGSW--TTNELDLSSWPDGTITV 171
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5810-6488 |
0e+00 |
|
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: 797.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5810 AMLAVARHYRLDFSEEHVRVVINQESQSPHHLVLEDMARQLGLALRSVPADVSLIDPWRLPLVVELNDGQMAVLTHMDKH 5889
Cdd:TIGR03375 4 CLLLLARHYGRPVSREALVAGLPLEDGRLTPELLPRAARRAGLSARLVKRSLDDISPLLLPAILLLKDGRACVLLGIDED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5890 GQLSIQLSGDSGLETVVSREALSQRLKG-LFLLRPlNSIPDARVDDYVKPYQKNWFWTLALKDWKRYGDIMLVAMAANVL 5968
Cdd:TIGR03375 84 GKARVLLPETGDGEQELSLDALEALYSGyAIFVRP-QFRFDARADELISPRPKHWFWSTLKESWPLYRDVLIASLLINLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5969 ALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARALRIKNSARPKST 6048
Cdd:TIGR03375 163 ALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTLRSYFLDVAGKKADLILSAKLFERVLGLRMEARPASV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6049 GSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLVQRPLAHLSNEGMRESAI 6128
Cdd:TIGR03375 243 GSFANQLREFESVRDFFTSATLTALIDLPFALLFLLVIAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRESAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6129 RNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTG 6208
Cdd:TIGR03375 323 RNAVLVESLSGLETIKALNAEGRFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELTMG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6209 ALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLMQRPLDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEKVNdL 6288
Cdd:TIGR03375 403 GLIACVMLSGRALAPLGQLAGLLTRYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETPA-L 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6289 DIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTM 6368
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIAL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6369 GRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLV 6448
Cdd:TIGR03375 562 GAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFK 641
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 701771264 6449 ANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:TIGR03375 642 DRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADG 681
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5810-6482 |
0e+00 |
|
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: 644.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5810 AMLAVARHYRLDFSEEHVRVVINQESQSPHHLVLEDMARQLGLALRSVPADVSLIDPWRLPLVVELNDGQMAVLTHMDKh 5889
Cdd:COG2274 19 CLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPAILHWDGNHFVVLEGVDG- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5890 GQLSIQLSGDSglETVVSREALSQRLKG-LFLLRPLNSIPDARVddyvKPYQKNWFWTLALKDWKRYGDIMLVAMAANVL 5968
Cdd:COG2274 98 DKVTIADPATG--RRKLSLEEFAESWTGvALLLEPTPEFDKRGE----KPFGLRWFLRLLRRYRRLLLQVLLASLLINLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5969 ALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARALRIKNSARPK-S 6047
Cdd:COG2274 172 ALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESrS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6048 TGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLVQRPLAHLSNEGMRESA 6127
Cdd:COG2274 252 VGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6128 IRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTT 6207
Cdd:COG2274 332 KRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6208 GALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLMQRPLDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEKvND 6287
Cdd:COG2274 412 GQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSP-PV 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLT 6367
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENIT 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTlilqpqilllDEPTAWLDEISEQQL 6447
Cdd:COG2274 571 LGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARAllrnprililDEATSALDAETEAII 650
|
650 660 670
....*....|....*....|....*....|....*
gi 701771264 6448 VANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:COG2274 651 LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKG 685
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
5952-6244 |
1.65e-128 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 406.82 E-value: 1.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5952 WKRYGDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDR 6031
Cdd:cd18587 1 RRIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6032 VFARALRIKNSARPKSTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLV 6111
Cdd:cd18587 81 LFERVLGLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6112 QRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAV 6191
Cdd:cd18587 161 QKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6192 VLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGL 6244
Cdd:cd18587 241 IVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
34-410 |
1.47e-100 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 332.03 E-value: 1.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 34 LTLGESILFALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSRTTDSSG----SLKNSAAYGLSLTQLVYD 109
Cdd:TIGR01844 3 LTLLDAVLLALANNPELRAARAQRDAGEEQVAQARAALLPQLGLTANYGYSNTYPTESrgrnTDLNSGSSTLTLSQPLFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 110 FGKTNSNISQQQSQRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQ 189
Cdd:TIGR01844 83 GGSTWNAVRAAEAAALAARETLRATAQDLILRTAEAYMEVLRAQEILALAEANLAALKEQLDLARARFDVGLGTRTDVLQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 190 TQTRIAGMRSTLEQYRAARQSAKARLAVLTGVS---AANYQAMPVRLAleqEPLD---NIDYSLIPSVLAAEAMRESSGY 263
Cdd:TIGR01844 163 AEARYASARAQLIQAQNNLDDAKAQLRRLVGQPelaPLAVPSFPAELP---EPLDqllEIAEASNPLLLAAQAAVDAARY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 264 AVDKAKSGHWPTLSLRGGRTRYQSNNSAYWDD-----QIQLNVDAPIYQGGAVSAQVEQAQGARRIAASQVEQAKFDVLQ 338
Cdd:TIGR01844 240 QVEQARAGHLPTLSLTASTGNSDTSSGGSGNSdsdtySVGLNVSIPLYQGGATSAQVRQAAHQLNQSRSTLESQKRTVRQ 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 339 KASVAMADWNGARGRETAGALQLENARRAREVYKNEYKLSKRSLNDLLSIEQDVFQAAYAQINADFDGWQAA 410
Cdd:TIGR01844 320 QVRNAWSNLNAAAASVQAYEQQVASAQKALDAYRQEYQVGTRTLLDVLNAEQELYQARQELANARYDYLQAQ 391
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5943-6482 |
2.51e-93 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 317.11 E-value: 2.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5943 WFWTLALKDWKRYGDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGK 6022
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6023 RADLRISDRVFARALRIKNS--ARpKSTGSFISQI-RELESVRELITSTTIGTVSD-IPFFLLFVFILW---------LI 6089
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSffDR-RRTGDLLSRLtNDVDAVEQFLAHGLPQLVRSvVTLIGALVVLFVidwrlalivLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6090 GGPLVFVVLLAiplllipgllVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMK 6169
Cdd:COG1132 170 VLPLLLLVLRL----------FGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6170 QRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLMQ 6249
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6250 RPLDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEKV-NDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQ 6328
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVlKDIS---LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6329 ILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAG 6408
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6409 LSGGQRQALLLARTlilqpqilllDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:COG1132 477 LSGGQRQRIAIARAllkdppililDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6268-6482 |
1.12e-83 |
|
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: 275.24 E-value: 1.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6268 GNYQLNYAAFYYDEEEkVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRD 6347
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6348 MTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQP 6427
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6428 QILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5948-6482 |
7.17e-79 |
|
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: 274.70 E-value: 7.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5948 ALKDWKRY-GDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADL 6026
Cdd:COG4618 14 ALRACRRAfLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGARLDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6027 RISDRVFARALRiknSARPKSTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLI---------GGPLVfvv 6097
Cdd:COG4618 94 RLGPRVFDAAFR---AALRGGGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFhpllgllalVGALV--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6098 llAIPLLLIPGLLVQRPLAHLSNEGMR-----ESAIRNATLVEAVQSIEDI--KLLRAEQRFQNQWNNTNDVAAGVGMKQ 6170
Cdd:COG4618 168 --LVALALLNERLTRKPLKEANEAAIRanafaEAALRNAEVIEAMGMLPALrrRWQRANARALALQARASDRAGGFSALS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6171 RWLTSLLmtwtqevQSIVYAvvllVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLMQr 6250
Cdd:COG4618 246 KFLRLLL-------QSAVLG----LGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLA- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6251 plDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEK--VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQ 6328
Cdd:COG4618 314 --AVPAEPERMPLPRPKGRLSVENLTVVPPGSKRpiLRGVS---FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6329 ILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLtmGR-PLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGA 6407
Cdd:COG4618 389 VRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGA 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6408 GLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASW-LGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6127-6482 |
1.00e-70 |
|
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: 250.84 E-value: 1.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6127 AIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMT 6206
Cdd:COG4987 192 AALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6207 tGALVGTSILASRTIA-PLAQISGVLSRWQQAKVARKGLDDLMQRPLDDPEEGkkvHKAHLQGNY--QLNYAAFYYDEEE 6283
Cdd:COG4987 272 -GPLLALLVLAALALFeALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPA---EPAPAPGGPslELEDVSFRYPGAG 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 K--VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGS 6361
Cdd:COG4987 348 RpvLDGLS---LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTT 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 IRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDE 6441
Cdd:COG4987 425 LRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 701771264 6442 ISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:COG4987 505 ATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDG 545
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5958-6482 |
3.27e-70 |
|
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: 248.80 E-value: 3.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLfgGVMLAILFEFTMRM--LRVHIADVVGKRADLRISDRVFAR 6035
Cdd:TIGR01842 11 VGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLML--TVLALGLYLFLGLLdaLRSFVLVRIGEKLDGALNQPIFAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6036 ALRiKNSARPKSTGSFIsqIRELESVRELITSTTIGTVSDIPFFLLFVFILWL----IGGPLVFVVLLAIPLLLIPGLLV 6111
Cdd:TIGR01842 89 SFS-ATLRRGSGDGLQA--LRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLlhpwIGILALGGAVVLVGLALLNNRAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6112 QRPLAHLSNEGMR-----ESAIRNATLVEAVQSIEDI--KLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLmtwtqev 6184
Cdd:TIGR01842 166 KKPLKEATEASIRannlaDSALRNAEVIEAMGMMGNLtkRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVL------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6185 QSIVyavvLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLM-QRPLDDPeegkKVHK 6263
Cdd:TIGR01842 239 QSLV----LGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLaNYPSRDP----AMPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6264 AHLQGNYQLNYAAFYYDEEEKVNDLDIArLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD 6343
Cdd:TIGR01842 311 PEPEGHLSVENVTIVPPGGKKPTLRGIS-FSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRET 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6344 LRRDMTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTL 6423
Cdd:TIGR01842 390 FGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARAL 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6424 ILQPQILLLDEPTAWLDEISEQQLV-ANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALAnAIKALKARGITVVVITHRPSLLGCVDKILVLQDG 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5937-6489 |
2.11e-68 |
|
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: 243.90 E-value: 2.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5937 KPYQKNWFWTLAlKDWKRYgdiMLVAMAANVLALAGMI-----FSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRM 6011
Cdd:COG4988 1 QKPLDKRLKRLA-RGARRW---LALAVLLGLLSGLLIIaqawlLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6012 LRVHIADVVGKRADLRISDRVFARALRIK-NSARPKSTGSFIS----QIRELESVRELITSTTIGTVSdIPFfLLFVFIL 6086
Cdd:COG4988 77 LRERAAFRAAARVKRRLRRRLLEKLLALGpAWLRGKSTGELATllteGVEALDGYFARYLPQLFLAAL-VPL-LILVAVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6087 W---------LIGGPL--VFVVLlaiplllipgllVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQ 6155
Cdd:COG4988 155 PldwlsglilLVTAPLipLFMIL------------VGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6156 WNNTND-----------VAagvgmkqrWLTSLLMTWtqeVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPL 6224
Cdd:COG4988 223 IAEASEdfrkrtmkvlrVA--------FLSSAVLEF---FASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6225 AQISgvlSRW---QQAKVARKGLDDLMQRPLDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEKV-NDLDiarLTITAGEK 6300
Cdd:COG4988 292 RDLG---SFYharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPAlDGLS---LTIPPGER 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6301 IAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPLASDEEIHR 6380
Cdd:COG4988 366 VALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6381 ALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTL 6460
Cdd:COG4988 446 ALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV 525
|
570 580
....*....|....*....|....*....
gi 701771264 6461 VVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:COG4988 526 ILITHRLALLAQADRILVLDDGRIVEQGT 554
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
35-411 |
1.94e-62 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 219.91 E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 35 TLGESILFALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQislngstghsrttdssgslknsaayglsltQLVYDFGKTN 114
Cdd:COG1538 1 TLDELIERALANNPDLRAARARVEAARAQLRQARAGLLPS------------------------------QELDLGGKRR 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 115 SNISQQQSQRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQTRI 194
Cdd:COG1538 51 ARIEAAKAQAEAAEADLRAARLDLAAEVAQAYFDLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 195 AGMRSTLEQYRAARQSAKARLAVLTGVSAANYQAMPVRLALEQEPLDNIDYSLI------PSVLAAEAMRESSGYAVDKA 268
Cdd:COG1538 131 AQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSealerrPDLRAAEAQLEAAEAEIGVA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 269 KSGHWPTLSLRGGRTRYQSNNSAYWDD---QIQLNVDAPIYQGGAVSAQVEQAQGARRIAASQVEQAKFDVLQKASVAMA 345
Cdd:COG1538 211 RAAFLPSLSLSASYGYSSSDDLFSGGSdtwSVGLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALA 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 346 DWNGARGRETAGALQLENARRAREVYKNEYKLSKRSLNDLLSIEQDVFQAAYAQINADFDGWQAAI 411
Cdd:COG1538 291 ALRAAREQLEALEEALEAAEEALELARARYRAGLASLLDVLDAQRELLQAQLNLIQARYDYLLALV 356
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
5953-6242 |
6.45e-62 |
|
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: 215.91 E-value: 6.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5953 KRYGDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRV 6032
Cdd:cd18566 2 PLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6033 FARALRIKNSA-RPKSTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLV 6111
Cdd:cd18566 82 FEHLLSLPLSFfEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6112 QRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAV 6191
Cdd:cd18566 162 GPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6192 VLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARK 6242
Cdd:cd18566 242 VVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVR 292
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5810-6488 |
2.98e-55 |
|
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: 208.83 E-value: 2.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5810 AMLAVARHYRLDFSEEHVRVVINQESQSPHHLVLEDMARQLGLALRSVPADVSLIDPWRLPLvvelndgqmAVLTHMDKH 5889
Cdd:TIGR01193 11 ALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADMSLFEDKNLPL---------PFIAHVIKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5890 GQLS-----IQLSGDSGL---------ETVVSREALSQRLKGlfllrplNSIPDARVDDYVKPYQKNW----FWTLALKD 5951
Cdd:TIGR01193 82 GKLPhyyvvYGVTKNHLIiadpdptvgITKISKEDFYEEWTG-------IAIFISPTPEYKPIKEKENsllkFIPLITRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5952 WKRYGDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRIS-- 6029
Cdd:TIGR01193 155 KKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIIls 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6030 --DRVFARALRIKNSARpksTGSFISQIRELESVRELITSTTIGTVSD------IPFFLLF----VFILWLIGGPLVfvv 6097
Cdd:TIGR01193 235 yiKHLFELPMSFFSTRR---TGEIVSRFTDASSIIDALASTILSLFLDmwilviVGLFLVRqnmlLFLLSLLSIPVY--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6098 llaipllLIPGLLVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQ--------RFQNQWNN--TNDVAAGVG 6167
Cdd:TIGR01193 309 -------AVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAeryskidsEFGDYLNKsfKYQKADQGQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6168 MKQRWLTSLLMTwtqevqsivyAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDL 6247
Cdd:TIGR01193 382 QAIKAVTKLILN----------VVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6248 MQRPLDDPEEGKKVHKAHLQGNYQLNYAAFYYDEEEKVndLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHG 6327
Cdd:TIGR01193 452 YLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6328 QILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMG-RPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGG 6406
Cdd:TIGR01193 530 EILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEG 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6407 AGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASwLGNRTLVVATHRIPILQLVDRIIVLDNGPARD 6486
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
..
gi 701771264 6487 DG 6488
Cdd:TIGR01193 689 QG 690
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5992-6482 |
2.99e-49 |
|
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: 187.62 E-value: 2.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5992 LWVLFGGVMLAIL-----FEFTMRMLRVHIADVVGKRADLrisdrvFARALRIKNSARPK-STGSFISQI-RELESVREL 6064
Cdd:TIGR02203 54 WWVPLVVIGLAVLrgicsFVSTYLLSWVSNKVVRDIRVRM------FEKLLGLPVSFFDRqPTGTLLSRItFDSEQVASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6065 ITSTTIGTVSD-IPFFLLFVFILWLiGGPLVFVVLLAIPLLLIPGLLVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDI 6143
Cdd:TIGR02203 128 ATDAFIVLVREtLTVIGLFIVLLYY-SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6144 KLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAP 6223
Cdd:TIGR02203 207 KLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6224 LAQISGVLSRWQQAKVARKGLDDLMQRPlDDPEEGKKvHKAHLQGNYQLNYAAFYYDEEEkVNDLDIARLTITAGEKIAV 6303
Cdd:TIGR02203 287 LKSLTNVNAPMQRGLAAAESLFTLLDSP-PEKDTGTR-AIERARGDVEFRNVTFRYPGRD-RPALDSISLVIEPGETVAL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6304 LGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPL-ASDEEIHRAL 6382
Cdd:TIGR02203 364 VGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERAL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6383 ALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLVV 6462
Cdd:TIGR02203 444 AAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLV 523
|
490 500
....*....|....*....|
gi 701771264 6463 ATHRIPILQLVDRIIVLDNG 6482
Cdd:TIGR02203 524 IAHRLSTIEKADRIVVMDDG 543
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6133-6482 |
1.52e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 185.80 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6133 LVEAVQSIEDIKLLRAEQRFQNQWNNTNdvaagvgmkQRWLTSllmtwtQEVQSIV----YAVVLLVGCYLV-------- 6200
Cdd:PRK11160 203 LTEWLQGQAELTLFGAEDRYRQQLEQTE---------QQWLAA------QRRQANLtglsQALMILANGLTVvlmlwlaa 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6201 --INGDMTTGALVGT---SILAS-RTIAPLA----QISGVLSrwqqakvARKGLDDLM-QRPldDPEEGKKVHKAHLQGN 6269
Cdd:PRK11160 268 ggVGGNAQPGALIALfvfAALAAfEALMPVAgafqHLGQVIA-------SARRINEITeQKP--EVTFPTTSTAAADQVS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6270 YQLNYAAF-YYDEEEKV-NDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRD 6347
Cdd:PRK11160 339 LTLNNVSFtYPDQPQPVlKGLS---LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6348 MTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGaLGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQP 6427
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG-LEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6428 QILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNG 549
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6273-6482 |
8.35e-47 |
|
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: 169.60 E-value: 8.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6273 NYAAFYYDEEEKVNDlDIaRLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLS 6352
Cdd:cd03244 7 NVSLRYRPNLPPVLK-NI-SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6353 QQARLFFGSIRDNLTmgrPL--ASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQIL 6430
Cdd:cd03244 85 QDPVLFSGTIRSNLD---PFgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6431 LLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6277-6482 |
9.49e-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: 169.71 E-value: 9.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVndLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR 6356
Cdd:cd03254 10 FSYDEKKPV--LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPT 6436
Cdd:cd03254 88 LFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 701771264 6437 AWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6293-6479 |
5.86e-46 |
|
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: 176.71 E-value: 5.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPL 6372
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 ASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLA 6452
Cdd:TIGR02857 423 ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALR 502
|
170 180
....*....|....*....|....*..
gi 701771264 6453 SWLGNRTLVVATHRIPILQLVDRIIVL 6479
Cdd:TIGR02857 503 ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6293-6482 |
2.36e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.49 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMqTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPL 6372
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 ASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLA 6452
Cdd:PRK11174 450 ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN 529
|
170 180 190
....*....|....*....|....*....|
gi 701771264 6453 SWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK11174 530 AASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
5956-6240 |
2.88e-44 |
|
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: 165.00 E-value: 2.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5956 GDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFAR 6035
Cdd:cd18783 5 RDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6036 ALRI------KNSArpkstGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGL 6109
Cdd:cd18783 85 LLSLpidffeRTPA-----GVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6110 LVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVY 6189
Cdd:cd18783 160 AFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6190 AVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18783 240 VGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLS 290
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6277-6482 |
2.19e-43 |
|
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: 157.54 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEK--VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQ 6354
Cdd:cd03228 8 FSYPGRPKpvLKDVS---LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 ARLFFGSIRDNLtmgrplasdeeihralalsgalgfvqkqknglnyliteggagLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:cd03228 85 PFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6435 PTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6288-6489 |
3.70e-42 |
|
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: 156.88 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLT 6367
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQL 6447
Cdd:cd03252 98 LADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701771264 6448 VANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:cd03252 178 MRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
5966-6240 |
6.75e-42 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 157.77 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5966 NVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARALRIKNSARP 6045
Cdd:cd18586 15 NLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6046 KSTGSfiSQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPL----VFVVLLAIPLLLIPGLLVQRPLAhlsnE 6121
Cdd:cd18586 95 SGYWQ--QLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLgwvaLVGAPVLVGLAWLNHRATRKPLG----E 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6122 GMRESAIRNATLVEAVQSIEDIK---LLRA-EQRFQNQWNNTNDVAAGVGMkqrwLTSLLMTWTQEVQSIVYAVVLLVGC 6197
Cdd:cd18586 169 ANEAQAARDALAAETLRNAETIKalgMLGNlRRRWEARHAETLELQIRASD----LAGAISAIGKTLRMALQSLILGVGA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 701771264 6198 YLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18586 245 YLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQA 287
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
5952-6240 |
1.19e-41 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 157.28 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5952 WKRYGDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDR 6031
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6032 VFARALRIKNS---ARPksTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPG 6108
Cdd:cd18588 81 LFRHLLRLPLSyfeSRQ--VGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6109 LLVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNN--TNDVAAGVGMKQrwLTSLLMTWTQEVQS 6186
Cdd:cd18588 159 LLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEEllARYVKASFKTAN--LSNLASQIVQLIQK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6187 IVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18588 237 LTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVS 290
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6131-6466 |
3.96e-41 |
|
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: 162.53 E-value: 3.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6131 ATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSllmtWTQEVQSIVYAVVLLVGCYLVINGDMTtGAL 6210
Cdd:TIGR02868 194 AQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA----LGAALTLLAAGLAVLGALWAGGPAVAD-GRL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6211 VGTsILASRTIAPLA------QISGVLSRWQQAKVARKGLDDLMqrpldDPEEGKKVHKAHLQGNY-------QLNYAAF 6277
Cdd:TIGR02868 269 APV-TLAVLVLLPLAafeafaALPAAAQQLTRVRAAAERIVEVL-----DAAGPVAEGSAPAAGAVglgkptlELRDLSA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVndLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARL 6357
Cdd:TIGR02868 343 GYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 FFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:TIGR02868 421 FDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
330 340
....*....|....*....|....*....
gi 701771264 6438 WLDEISEQQLVANLASWLGNRTLVVATHR 6466
Cdd:TIGR02868 501 HLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6118-6482 |
2.34e-40 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 161.28 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6118 LSNEGMRESAIRNATLVEAVQSIEDiKLLRAEQRFQNQWnntndvaAGVGMKQRWLTSLLMTwtqevqsivyaVVLLVGC 6197
Cdd:PRK13657 202 IGNVSVVQSYNRIEAETQALRDIAD-NLLAAQMPVLSWW-------ALASVLNRAASTITML-----------AILVLGA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6198 YLVINGDMTTGALVGTSILASRTIAPLAQISGVLSrwqQAKVARKGLDDLMQ-----RPLDDPEEGKKVhkAHLQGNYQL 6272
Cdd:PRK13657 263 ALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFIN---QVFMAAPKLEEFFEvedavPDVRDPPGAIDL--GRVKGAVEF 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6273 NYAAFYYD-EEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLL 6351
Cdd:PRK13657 338 DDVSFSYDnSRQGVEDVS---FEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6352 SQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILL 6431
Cdd:PRK13657 415 FQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6432 LDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5951-6489 |
2.79e-40 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 163.35 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5951 DWKRYGD-IMLVAMAAnvlaLAGMI---FSMQVYDRVVPSQSVPTL----WVL----FGGVMLAIL----FEFTMrmlrv 6014
Cdd:TIGR00958 159 DWPWLISaFVFLTLSS----LGEMFipfYTGRVIDTLGGDKGPPALasaiFFMcllsIASSVSAGLrggsFNYTM----- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6015 hiadvvgKRADLRISDRVFARALR------IKNSarpksTGSFISQIRELESV--RELITSTTIGTVSDIPFFLLFVFIL 6086
Cdd:TIGR00958 230 -------ARINLRIREDLFRSLLRqdlgffDENK-----TGELTSRLSSDTQTmsRSLSLNVNVLLRNLVMLLGLLGFML 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6087 W---------LIGGPLVFVVLLaiplllipgllVQRPLAHLSNEGMREsAIRNATLV--EAVQSIEDIKLLRAE----QR 6151
Cdd:TIGR00958 298 WlsprltmvtLINLPLVFLAEK-----------VFGKRYQLLSEELQE-AVAKANQVaeEALSGMRTVRSFAAEegeaSR 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6152 FQNQWNNTNDVAagvgmKQRWLTSLLMTWTQEV-QSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGV 6230
Cdd:TIGR00958 366 FKEALEETLQLN-----KRKALAYAGYLWTTSVlGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6231 LSRWQQAKVARKGLDDLMQRPLDDPEEGKKVHKaHLQGNYQLNYAAFYYDEEEKVNDLDIARLTITAGEKIAVLGRNGSG 6310
Cdd:TIGR00958 441 YSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPL-NLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6311 KSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGF 6390
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDF 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6391 VQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEqQLVANLASWlGNRTLVVATHRIPIL 6470
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE-QLLQESRSR-ASRTVLLIAHRLSTV 677
|
570
....*....|....*....
gi 701771264 6471 QLVDRIIVLDNGPARDDGK 6489
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGT 696
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6277-6488 |
2.01e-39 |
|
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: 148.92 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEK--VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQ 6354
Cdd:cd03251 8 FRYPGDGPpvLRDIS---LDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 ARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:cd03251 85 VFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6435 PTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERG 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6265-6482 |
1.04e-37 |
|
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: 143.77 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6265 HLQGNYQLNYAAFYYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL 6344
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6345 RRDMTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLI 6424
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6425 LQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6271-6482 |
1.75e-36 |
|
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: 138.21 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVNdLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAdLRRDMTL 6350
Cdd:cd03247 2 SINNVSFSYPEQEQQV-LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQARLFFGSIRDNLtmgrplasdeeihralalsgalgfvqkqknglnylitegGAGLSGGQRQALLLARTLILQPQIL 6430
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6431 LLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENG 172
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6182-6482 |
2.49e-36 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 149.01 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6182 QEVQSIVYAVVLLVGCYLVINGDMTTG--ALVGTSILAsrTIAPLAQISGVLSRWQQAKVARKGLDDLmqrpLD-DPE-- 6256
Cdd:PRK11176 256 QLIASLALAFVLYAASFPSVMDTLTAGtiTVVFSSMIA--LMRPLKSLTNVNAQFQRGMAACQTLFAI----LDlEQEkd 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6257 EGKKVHKaHLQGNYQLNYAAFYYDEEEKVNDLDIArLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL 6336
Cdd:PRK11176 330 EGKRVIE-RAKGDIEFRNVTFTYPGKEVPALRNIN-FKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6337 GQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRP-LASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQ 6415
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6416 ALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6293-6482 |
3.94e-36 |
|
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: 139.60 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPL 6372
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 ASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLA 6452
Cdd:cd03249 104 ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALD 183
|
170 180 190
....*....|....*....|....*....|
gi 701771264 6453 SWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03249 184 RAMKGRTTIVIAHRLSTIRNADLIAVLQNG 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6277-6489 |
6.79e-36 |
|
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: 138.52 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVndLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR 6356
Cdd:cd03253 8 FAYDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPT 6436
Cdd:cd03253 86 LFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6437 AWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGT 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
5958-6244 |
3.15e-33 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 133.10 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARAL 6037
Cdd:cd18782 7 VLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6038 RIKNS---ARPksTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLVQRP 6114
Cdd:cd18782 87 RLPLGffdKRP--VGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6115 LAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLL 6194
Cdd:cd18782 165 LRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLW 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6195 VGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGL 6244
Cdd:cd18782 245 VGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6276-6482 |
5.08e-33 |
|
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: 130.93 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6276 AFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQA 6355
Cdd:COG1120 8 SVGYGGRPVLDDVS---LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLFFG-SIRDNLTMGR---------PLASDEEI-HRALALSGALGFVQKqknglnyLITEggagLSGGQRQALLLARTli 6424
Cdd:COG1120 85 PAPFGlTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADR-------PVDE----LSGGERQRVLIARAla 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6425 lqpqilllDEPTAWLDeISEQ----QLVANLASWLGnRTLVVATHRIPI-LQLVDRIIVLDNG 6482
Cdd:COG1120 154 qeppllllDEPTSHLD-LAHQlevlELLRRLARERG-RTVVMVLHDLNLaARYADRLVLLKDG 214
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2127-3843 |
6.49e-33 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 142.60 E-value: 6.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2127 DGNGNWNVGIPASVINGLADGSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQ 2206
Cdd:COG3210 2 SGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2207 PAGTLITVTLNGINYQAVAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSALPTVIVNSVTSDN 2286
Cdd:COG3210 82 GAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2287 ILNITeIAGGQTLSGTVTGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSR 2366
Cdd:COG3210 162 TNTNN-SSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2367 DIVIDANLPGLRVDTVAGDDVINAIEHTQNLIINGTSSGLGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWAEG 2446
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2447 AVTIEVKGSSGAGNDVAIQHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELSGMTQNVEpgqTVNITFAGHTYTATVQ 2526
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVA---STVGTATASTGNASST 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2527 ADGSWKYTVPAADMVNLKEGDTAVQVSVTNKNGNSTDAAQNVSVDTLAPALTVDPVSQDNLLNAAEAKQDLVISGTSTAE 2606
Cdd:COG3210 398 TVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2607 AGQTVTVRLNGESYQATVKADGSWSLTVPAADVGKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDV 2686
Cdd:COG3210 478 NTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2687 INQTEHGQALVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGDTSHT 2766
Cdd:COG3210 558 ASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGS 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2767 VTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLGEAF 2846
Cdd:COG3210 638 AVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2847 YEVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDI---INAAELATGQTISGRVTGVQAGADVTINIGGVNYTAK 2923
Cdd:COG3210 718 QIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLsigLTANTTASGTTLTLANANGNTSAGATLDNAGAEISID 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2924 VQSDLTWSLTlgqdvltalgdGSLKINASVTDGagntgtgsrDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSS 3003
Cdd:COG3210 798 ITADGTITAA-----------GTTAINVTGSGG---------TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGA 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3004 GLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAG 3083
Cdd:COG3210 858 SGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTG 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3084 DDVLNAAEKGADLLLSGMTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKDGDTSVEVSVVNVTGNGASA 3163
Cdd:COG3210 938 AGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3164 GREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGD 3243
Cdd:COG3210 1018 GGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGI 1097
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3244 GVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTV 3323
Cdd:COG3210 1098 TNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTT 1177
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3324 DAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSAN 3403
Cdd:COG3210 1178 GSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDAT 1257
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3404 LAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTAD 3483
Cdd:COG3210 1258 TGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVN 1337
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3484 NVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHGNSGTAD 3563
Cdd:COG3210 1338 AGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGV 1417
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3564 REFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAA 3643
Cdd:COG3210 1418 SGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGA 1497
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3644 GNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEAGQTVTITFGGRTYTAQV 3723
Cdd:COG3210 1498 TASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGD 1577
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3724 ESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNA 3803
Cdd:COG3210 1578 TGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTL 1657
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|
gi 701771264 3804 QAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADN 3843
Cdd:COG3210 1658 SGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDTA 1697
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2553-4243 |
8.85e-33 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 142.21 E-value: 8.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2553 SVTNKNGNSTDAAQNVSVDTLAPALTVDPVSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSL 2632
Cdd:COG3210 19 AVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAGTLETGLTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2633 TVPAADVGKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTGAQAGDIVT 2712
Cdd:COG3210 99 NIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIGNSIP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2713 VTLGNKQYTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGDTSHTVTVDTVAPTLSIDTIAGDNILNADEK 2792
Cdd:COG3210 179 TTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSVAAGAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2793 TGDVVISGTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLGEAFYEVSVSASNGVGNAGSQSSTLEVAST 2872
Cdd:COG3210 259 TGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTAN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2873 LPGVIINAVAIDDIINAaelatGQTISGRVTGVQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINAS 2952
Cdd:COG3210 339 SGAGLVSGGTGGNNGTT-----GTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2953 VTDGAGNTGTGSRDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQT 3032
Cdd:COG3210 414 IAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTV 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3033 VVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQTIS 3112
Cdd:COG3210 494 TTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAAT 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3113 ITFAGHTYTTQVASDGSWKFTVPANDMKGLKDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEA 3192
Cdd:COG3210 574 GGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGT 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3193 GQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGDGVYTVDASVSDAAGNG---SSASHNLSVD 3269
Cdd:COG3210 654 ASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGalaNANGDTVTFG 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3270 VTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTIN 3349
Cdd:COG3210 734 NLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGTTAIN 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3350 ASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNW 3429
Cdd:COG3210 814 VTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANA 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3430 RVDVQPGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAAGDA 3509
Cdd:COG3210 894 GTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAG 973
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3510 VTINLGGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAI 3589
Cdd:COG3210 974 SSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGI 1053
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3590 EHNQNLIISGSASGMSEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVD 3669
Cdd:COG3210 1054 SGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTS 1133
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3670 LSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVK 3749
Cdd:COG3210 1134 TASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGT 1213
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3750 VSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWS 3829
Cdd:COG3210 1214 TNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSA 1293
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3830 ITLDSTALGALADNQYVIKVDVSDAAGNKTTGSQNMTLDTTAPTVSFNAVAGDDIINleehaQAQIISGSSTGAAAGNKI 3909
Cdd:COG3210 1294 TSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANT-----GLNGGNGATDSAAGAGSG 1368
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3910 IITLDGVQYVTQVDAKGNWSVGVPASAVSALKNGTATITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAE 3989
Cdd:COG3210 1369 GAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGA 1448
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3990 ARQDLTIGGSSTELAVGTQVTVTLNGIQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNISVD 4069
Cdd:COG3210 1449 GGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGE 1528
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4070 TVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGqkvtVKLGSESYEATVQADGSWSITVAAEDLAKLADGEFSVHA 4149
Cdd:COG3210 1529 GTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGS----VGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEG 1604
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4150 AVNDKAGNPGSADRTLTVDTTAPTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAVDFLGAADGS 4229
Cdd:COG3210 1605 TNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGAT 1684
|
1690
....*....|....
gi 701771264 4230 YQISASVSDKAGNS 4243
Cdd:COG3210 1685 TAAAGNVATGDTAP 1698
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6293-6482 |
4.70e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.47 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMG--- 6369
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPfql 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 RPLASDEEihRALALSGALGFvqkQKNGLNYLITEggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVA 6449
Cdd:COG4619 101 RERKFDRE--RALELLERLGL---PPDILDKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 701771264 6450 NLASWL--GNRTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:COG4619 172 LLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAG 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6277-6482 |
6.17e-32 |
|
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: 127.06 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVndLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR 6356
Cdd:COG1122 8 FSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 --LFFGSIRDNLTMGrPLA---SDEEIHR----ALALSGALGFvqKQKNGLNyliteggagLSGGQRQ----A------- 6416
Cdd:COG1122 86 dqLFAPTVEEDVAFG-PENlglPREEIRErveeALELVGLEHL--ADRPPHE---------LSGGQKQrvaiAgvlamep 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6417 --LLLartlilqpqilllDEPTAWLDEISEQQLVANLASW-LGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG1122 154 evLVL-------------DEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDlVAELADRVIVLDDG 210
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
1942-3633 |
1.51e-31 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 137.98 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1942 DGDAQVTVSVSNANGNPATSTQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLIVSGSSSAEPGQEVTVTLNNVNYTATV 2021
Cdd:COG3210 3 GGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2022 GADGRWSVSVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLSIDPVAGDDIINASEHSQAHTVGGTSTG 2101
Cdd:COG3210 83 AAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2102 AAAGDVVTVVVTNGQGTSFTFTTTLDGNGNWNVGIPASVINGLADGSYTITASVTDAAGNSGSADRALTVNTALPVISLA 2181
Cdd:COG3210 163 NTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVIS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2182 TIAGDDVINATEKGQDLVLSGTSNqpAGTLITVTLNGINYQAVAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNS 2261
Cdd:COG3210 243 TGGTDISSLSVAAGAGTGGAGGTG--NAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2262 SSDSHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILT 2341
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2342 ALGNGELTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDVINAIEHTQNLIINGTSSGLGAGSAVTVTINGKDY 2421
Cdd:COG3210 401 GSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2422 AATVRADGSWQAAVPGEDVARWAEGAVTIEVKGSSGAGNDVAIQHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELSG 2501
Cdd:COG3210 481 SATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2502 MTQNVEPGQTVNITFAGHTYTATVQADGSWKYTVPAADMVNLKEGDTAVQVSVTNKNGNSTDAAQNVSVDTLAPALTVDP 2581
Cdd:COG3210 561 SNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2582 VSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSLTVPAADVGKLTDGNITVTASVEDQAGNPG 2661
Cdd:COG3210 641 AALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIG 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2662 S----ASRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRA 2737
Cdd:COG3210 721 AlanaNGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITA 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2738 DVSALGDNTYTVTA-----SITDKAGNTGDTSHTVTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVT 2812
Cdd:COG3210 801 DGTITAAGTTAINVtgsggTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2813 VNLNGKNYAATVGADGKWTTTVPAGDVGklgeafyeVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAEL 2892
Cdd:COG3210 881 SGGVATSTGTANAGTLTNLGTTTNAASG--------NGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNA 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2893 ATGQTISGRVTGVQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINASVTDGAGNTGTGSRDVTIDAA 2972
Cdd:COG3210 953 GLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASAT 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2973 LPGIRVNTIAGDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAG 3052
Cdd:COG3210 1033 GTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTS 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3053 GTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQTISITFAGHTYTTQVASDGSWKF 3132
Cdd:COG3210 1113 TGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEG 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3133 TVPANDMKGLKDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTV 3212
Cdd:COG3210 1193 TAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATST 1272
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3213 TLNNETYTGIVQANGTWSITVPADKASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHG 3292
Cdd:COG3210 1273 VAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGL 1352
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3293 QAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGL 3372
Cdd:COG3210 1353 NGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATT 1432
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3373 PSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATA 3452
Cdd:COG3210 1433 GTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTA 1512
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3453 TSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLSWSLD 3532
Cdd:COG3210 1513 GGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAG 1592
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3533 LPADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTV 3612
Cdd:COG3210 1593 NTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDL 1672
|
1690 1700
....*....|....*....|.
gi 701771264 3613 TINGKSYLATVSASGTWSAAV 3633
Cdd:COG3210 1673 TDATLAGLGGATTAAAGNVAT 1693
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3165-3260 |
1.70e-31 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 120.86 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3165 REISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGDG 3244
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....*.
gi 701771264 3245 VYTVDASVSDAAGNGS 3260
Cdd:NF033510 82 TYTVTVTVTDAAGNTS 97
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2940-4643 |
2.37e-31 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 137.21 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2940 TALGDGSLKINASVTDGAGNTGTGSRDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKD 3019
Cdd:COG3210 3 GGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3020 YAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLS 3099
Cdd:COG3210 83 AAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3100 GMTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQIN 3179
Cdd:COG3210 163 NTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVIS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3180 TIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGDGVYTVDASVSDAAGNG 3259
Cdd:COG3210 243 TGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3260 SSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVS 3339
Cdd:COG3210 323 TNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3340 QLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNY 3419
Cdd:COG3210 403 GSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3420 TATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSG 3499
Cdd:COG3210 483 TTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSN 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3500 KVSNAAAGDAVTINLGGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINT 3579
Cdd:COG3210 563 TANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3580 VAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGksyLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNP 3659
Cdd:COG3210 643 LSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVT---SGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQI 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3660 ISIDRSV--NVDLSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEAGQTVTITFGGRTytaqvesdgswhytvpASD 3737
Cdd:COG3210 720 GALANANgdTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGN----------------TSA 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3738 IAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKT 3817
Cdd:COG3210 784 GATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTA 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3818 YTGVVKADGTWSITLDSTALGALADNQYVIKVDVSDAAGNKTTGSQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIIS 3897
Cdd:COG3210 864 GANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTT 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3898 GSSTGAAAGNKIIITLDGVQYVTQVDAKGNWSVGVPASAVSALKNGTATITATLTDSAGNEGANSHTVEVNAARIGLTID 3977
Cdd:COG3210 944 ALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVT 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3978 TISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTLNGIQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSAN 4057
Cdd:COG3210 1024 GTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGAT 1103
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4058 NATSATHNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGQKVTVKLGSESYEATVQADGSWSITVAAE-- 4135
Cdd:COG3210 1104 GTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAIng 1183
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4136 -DLAKLADGEFSVHAAVNDKAGNPGSADRTLTVDTTAPTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNN 4214
Cdd:COG3210 1184 gADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAG 1263
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4215 HTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVT 4294
Cdd:COG3210 1264 AVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTI 1343
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4295 ITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSNSIGNSAGVDRTITVDTTPPQMTITIDSLQNDTGLSA 4374
Cdd:COG3210 1344 NTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVA 1423
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4375 SDFITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTGTSWAYADGPLPDGTVTYHVRVVDNAGNVGSTATKNVT 4454
Cdd:COG3210 1424 GTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGG 1503
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4455 VDTVAPDAGTTITVEAISRDTGLDAHDFITSDNTLTLSGKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSWSYVDGRQLA 4534
Cdd:COG3210 1504 TSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADD 1583
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4535 DGDHLYQLRVVDDAGNIGSTASQLVTVDTVAPDASKTVTIDSISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQIS 4614
Cdd:COG3210 1584 TGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNG 1663
|
1690 1700
....*....|....*....|....*....
gi 701771264 4615 LDGGTVWQTVVTIGSTWYFNDGRTLSDGT 4643
Cdd:COG3210 1664 AGNGWAVDLTDATLAGLGGATTAAAGNVA 1692
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2341-4036 |
5.69e-31 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 136.05 E-value: 5.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2341 TALGNGELTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDVINAIEHTQNLIINGTSSGLGAGSAVTVTINGKD 2420
Cdd:COG3210 1 GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2421 YAATVRADGSWQAAVPGEDVARWAEGAVTIEVKGSSGAGNDVAIQHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELS 2500
Cdd:COG3210 81 IGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2501 GMTQNVEPGQTVNITFAGHTYTATVQADGSWKYTVPAADMVNLKEGDTAVQVSVTNKNGNSTDAAQNVSVDTLAPALTVD 2580
Cdd:COG3210 161 NTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2581 PVSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSLTVPAADVGKLTDGNITVTASVEDQAGNP 2660
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2661 GSASRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVS 2740
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2741 ALGDNTYTVTASITDKAGNTGDTSHTVTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVTVNLNGKNY 2820
Cdd:COG3210 401 GSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2821 AATVGADGKWTTTVPAGDVGKLGEAFYEVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAELATGQTISG 2900
Cdd:COG3210 481 SATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2901 RVTGVQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINASVTDGAGNTGTGSRDVTIDAALPGIRVNT 2980
Cdd:COG3210 561 SNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2981 IAGDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQwQAGDITVSAGGTSSSGNP 3060
Cdd:COG3210 641 AALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNN-AGNTLTISTGSITVTGQI 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3061 VTIDHTVNVDLSAVAITIGQ--IAGDDVLNAAEKGADLLLSGMTQNVEAGQTISITFAG--HTYTTQVASDGSWKFTVPA 3136
Cdd:COG3210 720 GALANANGDTVTFGNLGTGAtlTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANgnTSAGATLDNAGAEISIDIT 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3137 NDMKGLKDGDTSVevsvvNVTGNG-------ASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQT 3209
Cdd:COG3210 800 ADGTITAAGTTAI-----NVTGSGgtitintATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATA 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3210 VTVTLNNETYTGIVQANGTWSITVPADKASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLA 3289
Cdd:COG3210 875 ASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3290 EHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVN 3369
Cdd:COG3210 955 SAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGT 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3370 TGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLT 3449
Cdd:COG3210 1035 GTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTG 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3450 ATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLSW 3529
Cdd:COG3210 1115 GVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTA 1194
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3530 SLDLPADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGST 3609
Cdd:COG3210 1195 GTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVA 1274
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3610 VTVTINGKSYLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAA 3689
Cdd:COG3210 1275 GNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNG 1354
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3690 EKGADLV--LSGKTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFS 3767
Cdd:COG3210 1355 GNGATDSaaGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGT 1434
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3768 VDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQYVI 3847
Cdd:COG3210 1435 GGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGG 1514
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3848 KVDVSDAAGNKTTGSQNMTLDTTAPTVSFNAVAGDDIINleehaqAQIISGSSTGAAAGNKIIITLDGVQYVTQVDAKGN 3927
Cdd:COG3210 1515 TTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAG------SEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQA 1588
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3928 WSVGVPASAVSALKNGTATITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGT 4007
Cdd:COG3210 1589 PTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGW 1668
|
1690 1700
....*....|....*....|....*....
gi 701771264 4008 QVTVTLNGIQYTTTIQPGGGWSVTVPANQ 4036
Cdd:COG3210 1669 AVDLTDATLAGLGGATTAAAGNVATGDTA 1697
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
5958-6240 |
1.56e-30 |
|
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: 125.25 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARAL 6037
Cdd:cd18570 7 ILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6038 RIknsarPKS------TGSFISQIRELESVRELITSTTIGTVSDIpFFLLFVFI-LWLIGGPLVFVVLLAIPLLLIPGLL 6110
Cdd:cd18570 87 KL-----PLSffetrkTGEIISRFNDANKIREAISSTTISLFLDL-LMVIISGIiLFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6111 VQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAE----QRFQNQWNNTNDVAagvgMKQRWLTSLLMTWTQEVQS 6186
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEeqflKKIEKKFSKLLKKS----FKLGKLSNLQSSIKGLISL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6187 IVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18570 237 IGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVA 290
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
1756-3465 |
1.88e-30 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 134.51 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1756 GNTGSTDHDITIDAQLPGLRLDTISGDDIINLAEHNQDLVVSGTCSGLNAGSVVTVTLNGKDYLATVNADGSWSAAVPAA 1835
Cdd:COG3210 1 GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1836 DVSTWPDGVLTVTAKAQDGAQNPIGIDGIVDVDLAPVSISVNSVTADNVLNAAEKGVDLVLSGLTTNVEPGQTVTITFAG 1915
Cdd:COG3210 81 IGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1916 HRYTTSVNNDGSWSYTVPAADmarLKDGDAQVTVSVSNANGNPATSTQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLI 1995
Cdd:COG3210 161 NTNTNNSSSGTNIGNSIPTTG---GSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1996 VSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLSI 2075
Cdd:COG3210 238 AGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2076 DPVAGDDIINASEHSQAHTVGGTSTGAAAGDVVTVVVTNGQGTSFTFTTTLDGNGNWNVGIPASVINGLADGSYTITASV 2155
Cdd:COG3210 318 AGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASST 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2156 TDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTTV 2235
Cdd:COG3210 398 TVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2236 PASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDVVTIN 2315
Cdd:COG3210 478 NTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2316 LGGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDVINAIEHTQ 2395
Cdd:COG3210 558 ASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGS 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2396 NLIINGTSSGLGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWAEGAVTIEVKGSSGAGNDVAIQHQV-TVDLTE 2474
Cdd:COG3210 638 AVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTgSITVTG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2475 VVISINAVTGDNV-LNAAEKGANLELSGMTqNVEPGQTVNITFAGHTYTATVQADGSWKYTV-PAADMVNLKEGDTAVQV 2552
Cdd:COG3210 718 QIGALANANGDTVtFGNLGTGATLTLNAGV-TITSGNAGTLSIGLTANTTASGTTLTLANANgNTSAGATLDNAGAEISI 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2553 SVTNKNGNSTDAAQNVSVDTLAPALTVDPVSQDNLLNaaeakqdlVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSL 2632
Cdd:COG3210 797 DITADGTITAAGTTAINVTGSGGTITINTATTGLTGT--------GDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSG 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2633 TVPAADVGKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTGAQAGDIVT 2712
Cdd:COG3210 869 SLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGT 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2713 VTLGNKQYTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGDTSHTVTVDTVAPTLSIDTIAGDNILNADek 2792
Cdd:COG3210 949 QGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTT-- 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2793 TGDVVISGTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLGEAFYEVSVSASNGVGNAGSQSSTLEVAST 2872
Cdd:COG3210 1027 GTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTS 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2873 LPGVIINAVAIDDIINAAELATGQTISGRVTGVQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINAS 2952
Cdd:COG3210 1107 GGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGAD 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2953 VTDGAGNTGTGSRDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQT 3032
Cdd:COG3210 1187 SAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVS 1266
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3033 VVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQTIS 3112
Cdd:COG3210 1267 NGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTT 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3113 ITFAGHTYTTQVASDGSWkfTVPANDMKGLKDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEA 3192
Cdd:COG3210 1347 AANTGLNGGNGATDSAAG--AGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAG 1424
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3193 GQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTV 3272
Cdd:COG3210 1425 TTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGT 1504
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3273 PSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASL 3352
Cdd:COG3210 1505 STGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDT 1584
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3353 TDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVD 3432
Cdd:COG3210 1585 GAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGA 1664
|
1690 1700 1710
....*....|....*....|....*....|...
gi 701771264 3433 VQPGDLAGLGEANYTLTATATSSIGNSAGASAS 3465
Cdd:COG3210 1665 GNGWAVDLTDATLAGLGGATTAAAGNVATGDTA 1697
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6293-6482 |
3.80e-30 |
|
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: 120.01 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLtmgrpl 6372
Cdd:cd03246 23 FSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 asdeeihralalsgalgfvqkqknglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLA 6452
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|.
gi 701771264 6453 SW-LGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03246 141 ALkAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
5952-6240 |
6.28e-30 |
|
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: 123.44 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5952 WKRYGDIMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDR 6031
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6032 VFARALRIKNS---ARPksTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPG 6108
Cdd:cd18568 81 FYKHLLSLPLSffaSRK--VGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6109 LLVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIV 6188
Cdd:cd18568 159 LLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6189 YAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18568 239 TIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRIS 290
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1962-2058 |
7.16e-30 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 116.24 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1962 TQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLIVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKD 2041
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 2042 GTLTVSASVADKAGNPA 2058
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2565-2661 |
7.89e-30 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 116.24 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2565 AQNVSVDTLAPALTVDPVSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSLTVPAADVGKLTD 2644
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 2645 GNITVTASVEDQAGNPG 2661
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6278-6482 |
4.29e-29 |
|
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: 118.34 E-value: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKV-NDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR 6356
Cdd:cd03225 9 YPDGARPAlDDIS---LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 --LFFGSIRD-------NLTMGRPLAsDEEIHRALALSGALGFvqkqkngLNYLITEggagLSGGQRQ------------ 6415
Cdd:cd03225 86 dqFFGPTVEEevafgleNLGLPEEEI-EERVEEALELVGLEGL-------RDRSPFT----LSGGQKQrvaiagvlamdp 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6416 -ALLLartlilqpqilllDEPTAWLDEISEQQLVANLASWLG-NRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:cd03225 154 dILLL-------------DEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLdLLLELADRVIVLEDG 210
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2983-4683 |
4.70e-29 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 129.89 E-value: 4.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2983 GDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVT 3062
Cdd:COG3210 1 GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3063 IDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQ--TISITFAGHTYTTQVASDGSWKFTVPANDMK 3140
Cdd:COG3210 81 IGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNntGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3141 GLKDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYT 3220
Cdd:COG3210 161 NTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3221 GIVQANGTWSITVPADKASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGS 3300
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3301 SSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAI 3380
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3381 SGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSA 3460
Cdd:COG3210 401 GSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3461 GASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLSwsLDLPADVLTA 3540
Cdd:COG3210 481 SATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTV--SGGASGTTAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3541 LGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKSYL 3620
Cdd:COG3210 559 SGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3621 ATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGK 3700
Cdd:COG3210 639 VGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQ 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3701 TQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSvTNVNGNGASAEREFSVDATAPGLTINPI 3780
Cdd:COG3210 719 IGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASG-TTLTLANANGNTSAGATLDNAGAEISID 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3781 ATDNVINAAEAGAGVTVTGTSNA-QAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQYVIKVDVSDAAGNKT 3859
Cdd:COG3210 798 ITADGTITAAGTTAINVTGSGGTiTINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASI 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3860 TGSQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTGAAAGNKIIITLDGVQYVTQVDAKGNWSVGVPASAVSA 3939
Cdd:COG3210 878 TVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAA 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3940 LKNGTATITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTLNGIQYT 4019
Cdd:COG3210 958 SASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTA 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4020 TTIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRG 4099
Cdd:COG3210 1038 ATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVT 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4100 TSSAEAGQKVTVKLGSESYEATVQADGSWSITVAAEDLAKLADGEFSVHAAVNDKAGNPGSADRTLTVDTTAPTITFDKV 4179
Cdd:COG3210 1118 ASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTD 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4180 AGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPTI 4259
Cdd:COG3210 1198 LKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNA 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4260 SINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSNS 4339
Cdd:COG3210 1278 GATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNG 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4340 IGNSAGVDRTITVDTTPPQMTITIDSLQNDTGLSASDFITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTGTS 4419
Cdd:COG3210 1358 ATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGT 1437
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4420 WAYADGPLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDTGLDAHDFITSDNTLTLSGKLGAPL 4499
Cdd:COG3210 1438 GNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTA 1517
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4500 AAGEHAQISIDGGKTWVDVSVSGTSWSYVDGRQLADGDhlyQLRVVDDAGNIGSTASQLVTVDTVAPDASKTVTIDSIST 4579
Cdd:COG3210 1518 EVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSE---GGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNT 1594
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4580 DTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYFNDGRTLSDGTYQYLVRVVDDAGNVGQ 4659
Cdd:COG3210 1595 ATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTD 1674
|
1690 1700
....*....|....*....|....
gi 701771264 4660 SASKNVTVDTTPPDASVTVTVDSI 4683
Cdd:COG3210 1675 ATLAGLGGATTAAAGNVATGDTAP 1698
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
5958-6240 |
6.70e-29 |
|
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: 120.35 E-value: 6.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARAL 6037
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6038 RIKNSARPK-STGSFISQIRE-LESVRELITSTTIGTVSDIpFFLLFVFILW-----------LIGGPLVFVVLLAipll 6104
Cdd:cd07346 84 RLSLSFFDRnRTGDLMSRLTSdVDAVQNLVSSGLLQLLSDV-LTLIGALVILfylnwkltlvaLLLLPLYVLILRY---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6105 lipgllVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEV 6184
Cdd:cd07346 159 ------FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6185 QSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd07346 233 TALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALAS 288
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6277-6482 |
1.22e-28 |
|
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: 118.04 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAdLRRDMTLLSQQAR 6356
Cdd:COG4555 9 KKYGKVPALKDVS---FTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFG-SIRDNLT---MGRPLASDEEIHRALALSGALGFVQKQKNGLnyliteggAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:COG4555 85 LYDRlTVRENIRyfaELYGLFDEELKKRIEELIELLGLEEFLDRRV--------GELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6433 DEPTAWLDEISEQQLVANLASWLG-NRTLVVATHripILQLV----DRIIVLDNG 6482
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKeGKTVLFSSH---IMQEVealcDRVVILHKG 208
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
5958-6240 |
1.38e-28 |
|
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: 119.54 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARAL 6037
Cdd:cd18555 7 ILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6038 RIknsarP------KSTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLV 6111
Cdd:cd18555 87 KL-----PysffenRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6112 QRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNT-NDVAAGVGMKQRWlTSLLMTWTQEVQSIVYA 6190
Cdd:cd18555 162 RKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLfKKQLKAFKKKERL-SNILNSISSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6191 VVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18555 241 LILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSY 290
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6223-6489 |
1.83e-28 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 125.22 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6223 PLAQISGVLSRWQQAKVARKGLDDLMqrplDDPEEGKKVHKAHLQ-GNYQLNYAAFYYDEEEKVndLDIARLTITAGEKI 6301
Cdd:PRK10790 297 PLIELTTQQSMLQQAVVAGERVFELM----DGPRQQYGNDDRPLQsGRIDIDNVSFAYRDDNLV--LQNINLSVPSRGFV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6302 AVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPLaSDEEIHRA 6381
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDI-SEEQVWQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6382 LALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLV 6461
Cdd:PRK10790 450 LETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLV 529
|
250 260
....*....|....*....|....*...
gi 701771264 6462 VATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:PRK10790 530 VIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1365-1461 |
4.40e-28 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 111.23 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1365 AREVLVDTQPPSITLNSITADNILNHAEAAQELVITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVADLANLTD 1444
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 1445 GSWSVSASVSDVAGNPA 1461
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6276-6482 |
7.43e-28 |
|
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: 113.68 E-value: 7.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6276 AFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQqa 6355
Cdd:cd03214 6 SVGYGGRTVLDDLS---LSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 rlffgsirdnltmgrplasdeeihrALALSGALGFVQKQknglnylITEggagLSGGQRQALLLARTLILQPQILLLDEP 6435
Cdd:cd03214 81 -------------------------ALELLGLAHLADRP-------FNE----LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6436 TAWLDeISEQ----QLVANLASWLGnRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:cd03214 125 TSHLD-IAHQiellELLRRLARERG-KTVVMVLHDLnLAARYADRVILLKDG 174
|
|
| outer_NodT |
TIGR01845 |
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this ... |
43-402 |
7.99e-28 |
|
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins]
Pssm-ID: 273830 [Multi-domain] Cd Length: 460 Bit Score: 120.98 E-value: 7.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 43 ALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSRT------TDSSGSLKNSAAYGLSLTQLVYDFGKTNSN 116
Cdd:TIGR01845 66 ALADNPDLQVAEARLRAARANLRAARADFFPSLGLSASATRQKSsedasgTTSGGSLSNTSTLTLDVSYELDLFGKVRRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 117 ISQQQSQRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQTRIAG 196
Cdd:TIGR01845 146 VESALAQLEAAEADSQAARLTLSASIANAYVQLAALRAQLDVYHAALASRRKTLELTQKRYAAGVAAASDVRQAEAAVAS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 197 MRSTLEQYRAARQSAKARLAVLTGVSAANYQAMPVRLALEQEPLD---NIDYSLI---PSVLAAEAMRESSGYAVDKAKS 270
Cdd:TIGR01845 226 AEAELPSLDVQIAQARNALAALLGKGPSRGLAIARPLLLDQLPPDlplSLPSDLLrrrPDIRAAERRLAAANAQIGVAKA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 271 GHWPTLSLRG--GRTRYQ-----SNNSAYWddQIQLNVDAPIYQGGAVSAQVEQAQGARRIAASQVEQAKFDVLQKAS-- 341
Cdd:TIGR01845 306 AFFPSITLSAsiGLSASQlsrlfDGGSRFW--SIGPALALPIFDGGSLRAALDSAKATYDAAVAQYRQTVLTAFQEVAda 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 342 VAMADWNGARGRETAGALQleNARRAREVYKNEYKLSKRSLNDLLSIEQDVFQAAYAQINA 402
Cdd:TIGR01845 384 LVALQALARRLDAQRQAVE--QAQEALSLAQTRYRAGLDSYLTVLEAQRSLLTAQRSLATL 442
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6271-6483 |
1.09e-27 |
|
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: 114.17 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqLDTADLRRDMTL 6350
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVS---FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQA---RLFFGSIRDNLTMGR---------PLASD-EEIHRALALSGALGFVQKQknglnylITEggagLSGGQRQAL 6417
Cdd:cd03235 73 VPQRRsidRDFPISVRDVVLMGLyghkglfrrLSKADkAKVDEALERVGLSELADRQ-------IGE----LSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6418 LLARTLILQPQILLLDEPTAWLDEISEQQLVANLASW-LGNRTLVVATHRI-PILQLVDRIIVLDNGP 6483
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLgLVLEYFDRVLLLNRTV 209
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
768-864 |
1.12e-27 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 110.07 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 768 SETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVTLKLNGKTYTATVGADGGWSMEVPAADVQAMAD 847
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 848 NSYTLNLSVSDKAGNTT 864
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3764-3857 |
1.53e-27 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 109.69 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3764 REFSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADN 3843
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....
gi 701771264 3844 QYVIKVDVSDAAGN 3857
Cdd:NF033510 82 TYTVTVTVTDAAGN 95
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
43-220 |
2.37e-27 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 112.23 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 43 ALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSR-TTDSSGSLKNSAAYGLSLTQLVYDFGKTNSNISQQQ 121
Cdd:pfam02321 3 ALENNPDLKAAEAEIEAAEANIKLAKSEFLPDLSLSGGYGYNSnNSESGGDDPGTGEVGLGLSQPLFDGGKRRARVKAAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 122 SQRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQTRIAGMRSTL 201
Cdd:pfam02321 83 AQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARLEL 162
|
170
....*....|....*....
gi 701771264 202 EQYRAARQSAKARLAVLTG 220
Cdd:pfam02321 163 LNAEADLELALAQLEQLLG 181
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
6288-6437 |
2.74e-27 |
|
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: 110.82 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLF-FGSIRDNL 6366
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6367 TMGRPL------ASDEEIHRALALSGALGFvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:pfam00005 81 RLGLLLkglskrEKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2664-2761 |
1.28e-26 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 106.99 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2664 SRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTgAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVSALG 2743
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2744 DNTYTVTASITDKAGNTG 2761
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6278-6482 |
1.34e-26 |
|
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: 111.43 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL----RRDMTLLSQ 6353
Cdd:cd03255 10 YGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 QARL--FFgSIRDNLTM-----GRPLASDEEihRALALSGALGFVQKqkngLNYLITEggagLSGGQRQ----------- 6415
Cdd:cd03255 90 SFNLlpDL-TALENVELplllaGVPKKERRE--RAEELLERVGLGDR----LNHYPSE----LSGGQQQrvaiaraland 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6416 -ALLLArtlilqpqilllDEPTAWLD-EISEQ--QLVANLASWLGnRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03255 159 pKIILA------------DEPTGNLDsETGKEvmELLRELNKEAG-TTIVVVTHDPELAEYADRIIELRDG 216
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
3547-5237 |
1.50e-26 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 121.41 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3547 TVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKSYLATVSAS 3626
Cdd:COG3210 11 NKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3627 GTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEA 3706
Cdd:COG3210 91 TLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3707 GQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVI 3786
Cdd:COG3210 171 TNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3787 NAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQYVIKVDVSDAAGNKTTGSQNMT 3866
Cdd:COG3210 251 LSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3867 LDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTGAAAGNkiIITLDGVQYVTQVDAKGNWSVGVPASAVSALKNGTAT 3946
Cdd:COG3210 331 DGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGG--LTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3947 ITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTLNGIQYTTTIQPGG 4026
Cdd:COG3210 409 NTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4027 GWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAG 4106
Cdd:COG3210 489 GIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLG 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4107 QKVTVKLGSESYEATVQADGSWSITVAAEDLAKLADGEFSVHAAVNDKAGNPGSADRTLTVDTTAPTITFDKVAGDDIIN 4186
Cdd:COG3210 569 VLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGS 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4187 SAEQQAGQAISGTTNAQPGQ-TITVTFNNHTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPTISiNTFA 4265
Cdd:COG3210 649 GTTGTASANGSNTTGVNTAGgTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALA-NANG 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4266 GDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSNSIGNSAG 4345
Cdd:COG3210 728 DTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAA 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4346 VDRTITVDTTPPqmTITIDSLQNDTGLSASDFITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTGTSWAYADG 4425
Cdd:COG3210 808 GTTAINVTGSGG--TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVA 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4426 PLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDTGLDAHDFITSDNTLTLSGKLGAPLAAGEHA 4505
Cdd:COG3210 886 TSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGD 965
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4506 QISIDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLRVVDDAGNIGSTASQLVTVDTVAPDASKTVTIDSISTDTGLSN 4585
Cdd:COG3210 966 TGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNG 1045
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4586 TDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYFNDGRTLSDGTYQYLVRVVDDAGNVGQSASKNV 4665
Cdd:COG3210 1046 VGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTT 1125
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4666 TVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLNGSLGAPLGSNEFVQISIDGGASWFYATSVNGTRWSYTDGRQ 4745
Cdd:COG3210 1126 TVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTG 1205
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4746 LADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGISDDTGQSASDFITMDTTLTLNGTLGHALASDERVQIS 4825
Cdd:COG3210 1206 GSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGST 1285
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4826 LDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNVGSTANQVVTVDTVAPDTVGSIVSYTDNNGERTGNFDS 4905
Cdd:COG3210 1286 VDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGA 1365
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4906 SYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTFADSGLLDGSYHYVLRVTDKAGNYTESNDFGLTV 4985
Cdd:COG3210 1366 GSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSV 1445
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4986 DTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVVTVNGKTYTSDRGGAVVVDPASNTWYLQIPDADVLSLKSYDV 5065
Cdd:COG3210 1446 AGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLE 1525
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5066 TAQVKSSAGNGNSVDVTHGTVVVGAEASMTPawAFTSATNAIAASFMLDANGMWTFASNQQFATANDRNSYSVSGNFSMT 5145
Cdd:COG3210 1526 GGEGTYGGSSVAEAGTGGGILGAVSGAGSEG--GAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAE 1603
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5146 GSYTTGAYADINRDGHADMLVESTNYSYITQLMNNGDGTYTSTSPGSSATVGALLWYGAVVSIDFQGDGYVDFVMGDAGG 5225
Cdd:COG3210 1604 GTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGA 1683
|
1690
....*....|..
gi 701771264 5226 PDSSTFVNNNAG 5237
Cdd:COG3210 1684 TTAAAGNVATGD 1695
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6295-6482 |
2.00e-26 |
|
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: 110.58 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTmgrPLA- 6373
Cdd:cd03369 31 VKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLD---PFDe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6374 -SDEEIHRALAlsgalgfvqkqknglnylITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLA 6452
Cdd:cd03369 108 ySDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190
....*....|....*....|....*....|
gi 701771264 6453 SWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03369 170 EEFTNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6275-6482 |
2.33e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.33 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6275 AAFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLdtadlRRDMTLLSQQ 6354
Cdd:COG1121 12 LTVSYGGRPVLEDVS---LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 A---RLFFGSIRDNLTMG---------RPLASD-EEIHRALALSGALGFVQKQknglnylITEggagLSGGQRQALLLAR 6421
Cdd:COG1121 84 AevdWDFPITVRDVVLMGrygrrglfrRPSRADrEAVDEALERVGLEDLADRP-------IGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6422 tlilqpqilllDEPTAWLDEISEQQLVANLASWLG-NRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:COG1121 153 alaqdpdllllDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLgAVREYFDRVLLLNRG 215
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2167-2262 |
2.39e-26 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 106.22 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2167 RALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTTVPASAVSKLGEA 2246
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....*.
gi 701771264 2247 NYTVTAAVTDAHGNSS 2262
Cdd:NF033510 82 TYTVTVTVTDAAGNTS 97
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6278-6482 |
2.49e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.90 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL----RRDMTLLSQ 6353
Cdd:COG1136 14 YGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 QARLF-FGSIRDNLTM-----GRPLASDEEihRALALSGALGFVQKqkngLNYLITEggagLSGGQRQ------------ 6415
Cdd:COG1136 94 FFNLLpELTALENVALplllaGVSRKERRE--RARELLERVGLGDR----LDHRPSQ----LSGGQQQrvaiaralvnrp 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6416 ALLLArtlilqpqilllDEPTAWLD-EISEQ--QLVANLASWLGnRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:COG1136 164 KLILA------------DEPTGNLDsKTGEEvlELLRELNRELG-TTIVMVTHDPELAARADRVIRLRDG 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6287-6488 |
3.12e-26 |
|
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: 120.44 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6287 DLDIA----RLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSI 6362
Cdd:TIGR00957 1297 DLDLVlrhiNVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6363 RDNLTmgrPLA--SDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:TIGR00957 1377 RMNLD---PFSqySDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6441 EISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFG 1501
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
5958-6237 |
4.69e-26 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 111.87 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARAL 6037
Cdd:cd18779 7 ILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6038 RIknsarP------KSTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLV 6111
Cdd:cd18779 87 RL-----PyrffqqRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6112 QRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAV 6191
Cdd:cd18779 162 RRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 701771264 6192 VLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQA 6237
Cdd:cd18779 242 LLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLL 287
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6277-6482 |
5.28e-26 |
|
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: 117.61 E-value: 5.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKV-NDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQA 6355
Cdd:COG5265 365 FGYDPERPIlKGVS---FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEP 6435
Cdd:COG5265 442 VLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6436 TAWLDEISEQQLVANLASWLGNRT-LVVAtHRIPILQLVDRIIVLDNG 6482
Cdd:COG5265 522 TSALDSRTERAIQAALREVARGRTtLVIA-HRLSTIVDADEILVLEAG 568
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
43-220 |
9.81e-26 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 112.82 E-value: 9.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 43 ALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSRTTDSSGSLKNSAAYGLSLTQLVYDFGKTNSNISQQQS 122
Cdd:COG1538 186 ALERRPDLRAAEAQLEAAEAEIGVARAAFLPSLSLSASYGYSSSDDLFSGGSDTWSVGLSLSLPLFDGGRNRARVRAAKA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 123 QRESYRYQLMATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQTRIAGMRSTLE 202
Cdd:COG1538 266 QLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAEEALELARARYRAGLASLLDVLDAQRELLQAQLNLI 345
|
170
....*....|....*...
gi 701771264 203 QYRAARQSAKARLAVLTG 220
Cdd:COG1538 346 QARYDYLLALVQLYRALG 363
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6285-6488 |
1.56e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.43 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFG-SIR 6363
Cdd:COG4559 17 LDDVS---LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAFPfTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTMGR-----PLASDEEI-HRALALSGALGFVQKqknglNYLiteggaGLSGGQRQALLLARTLILQPQILLL----- 6432
Cdd:COG4559 94 EVVALGRaphgsSAAQDRQIvREALALVGLAHLAGR-----SYQ------TLSGGEQQRVQLARVLAQLWEPVDGgprwl 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6433 --DEPTAWLDeISEQQLVANLASWLGNRTL-VVAthripIL-------QLVDRIIVLDNGPARDDG 6488
Cdd:COG4559 163 flDEPTSALD-LAHQHAVLRLARQLARRGGgVVA-----VLhdlnlaaQYADRILLLHQGRLVAQG 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6293-6481 |
1.83e-25 |
|
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: 107.56 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQARLFFG-SIRDNLT---- 6367
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVRENLRfwaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLASDEEIHRALALSGALGFVQKQknglnylitegGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQL 6447
Cdd:COG4133 102 LYGLRADREAIDEALEAVGLAGLADLP-----------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|....
gi 701771264 6448 VANLASWLGNRTLVVATHRIPILQLVDRIIVLDN 6481
Cdd:COG4133 171 AELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6277-6482 |
1.87e-25 |
|
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: 108.42 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVND--LDIARLTITAgekiaVLGRNGSGKSTLLQLLAGM-----QTPQHGQILLDG--ISLGQLDTADLRRD 6347
Cdd:cd03260 8 VYYGDKHALKDisLDIPKGEITA-----LIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkdIYDLDVDVLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6348 MTLLSQQARLFFGSIRDNLTMGRPL-------ASDEEIHRALALSGALGFVQKQKNGLnyliteggaGLSGGQRQALLLA 6420
Cdd:cd03260 83 VGMVFQKPNPFPGSIYDNVAYGLRLhgiklkeELDERVEEALRKAALWDEVKDRLHAL---------GLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6421 RTLILQPQILLLDEPTAWLDEISEQ---QLVANLAswlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAkieELIAELK---KEYTIVIVTHNMQqAARVADRTAFLLNG 216
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4063-4159 |
2.19e-25 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 103.53 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4063 THNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGQKVTVKLGSESYEATVQADGSWSITVAAEDLAKLAD 4142
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 4143 GEFSVHAAVNDKAGNPG 4159
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6277-6482 |
5.09e-25 |
|
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: 104.63 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQqar 6356
Cdd:cd00267 7 FRYGGRTALDNVS---LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 lffgsirdnltmgrplasdeeihralalsgalgfvqkqknglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPT 6436
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6437 AWLDEISEQQLVANLASWL-GNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd00267 109 SGLDPASRERLLELLRELAeEGRTVIIVTHDPElAELAADRVIVLKDG 156
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3463-3560 |
8.88e-25 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 101.60 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3463 SASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKvSNAAAGDAVTINLGGKTYTATVQSDLSWSLDLPADVLTALG 3542
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGT-TTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3543 NGKLTVTASVTNGHGNSG 3560
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2764-2861 |
1.20e-24 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 101.21 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2764 SHTVTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGlAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLG 2843
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2844 EAFYEVSVSASNGVGNAG 2861
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6277-6482 |
1.28e-24 |
|
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: 106.05 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQ 6353
Cdd:cd03261 8 KSFGGRTVLKGVD---LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 QARLFFG-SIRDNltMGRPLA-----SDEEIhRALALSgALGFVqkqknGL----NYLITEggagLSGGQRQALLLARTL 6423
Cdd:cd03261 85 SGALFDSlTVFEN--VAFPLRehtrlSEEEI-REIVLE-KLEAV-----GLrgaeDLYPAE----LSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6424 ILQPQILLLDEPTAWLDEISE---QQLVANLASWLGNRTLVVaTHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASgviDDLIRSLKKELGLTSIMV-THDLDtAFAIADRIAVLYDG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6279-6482 |
1.60e-24 |
|
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: 104.91 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAdlRRDMTLLSQQARLF 6358
Cdd:cd03259 10 YGSVRALDDLS---LTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 -FGSIRDN----LTMGRPLASDEE--IHRALALSGALGFvqkqkngLNYLITEggagLSGGQRQALLLARTLILQPQILL 6431
Cdd:cd03259 85 pHLTVAENiafgLKLRGVPKAEIRarVRELLELVGLEGL-------LNRYPHE----LSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6432 LDEPTAWLDEISEQQLVANLASWLGNR--TLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELgiTTIYVTHdQEEALALADRIAVMNEG 207
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
672-2388 |
2.14e-24 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 114.48 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 672 NVVTAQASLTAATTAGDNTLNAAEQANDFVISGSATELASGTALTVTLNGKTYATTVGSDGSWSVTVPAADAKSLADGSW 751
Cdd:COG3210 1 GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 752 TVTVSGKDAAGNNISASETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVTLKLNGKTYTATVGADG 831
Cdd:COG3210 81 IGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 832 GWSMEVPAADVQAMADNSYTLNLSVSDKAGNTTTTNASLLVDTTPPEASVNTVAGDDILSVSEQGQAQIISGTSQGAAPG 911
Cdd:COG3210 161 NTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 912 DKVTVSIGSETYQTTVQADGSWSVGVPKEVISSLPEGPNTITVAITDVAGNTGTTTHDITVSSTPPNVAFNAISQDNVLN 991
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 992 AIEATQPLILSGTSNLPDGSHVTVTLNNVNYTAQVQGGVWQVQVPVSDVVKLGDTTYTLSVSGTDTTGNTGTATATLQVD 1071
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1072 TALPTVIVSTFAGDNRVNNSEIANDQMLSGRVTGAHQGDTVTINIGGKNYTATVQSDLTWSTTVPAADLRALGDGDVSIV 1151
Cdd:COG3210 401 GSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1152 ASVTNAHGNTGSGSRDININAQLPGLRINTVSGDDVINAIEQHQDLTVTGTSTHLSAGTIITVRINGVDYQAAVSATGSW 1231
Cdd:COG3210 481 SATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1232 QIGIPAADVAGWPNGKLEMVASSADESGNPVAATRPVDVDLNAVAISINSVTSDGVLNAVEKAADLTLSGKTLGVEAGQT 1311
Cdd:COG3210 561 SNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1312 VVIKFAGHTYTTTVNQSGDWTFTVPAADMRDMIDGRADVSVSVTNVSGNGASGAREVLVDTQPPSITLN--SITADNILN 1389
Cdd:COG3210 641 AALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTIStgSITVTGQIG 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1390 HAEAAQELVITGTStAQPGQTVTVSLNNQSYTGlvladGTWSVTVPVADLANLTDGSWSVSASVSDVAGNPASTSHGMLV 1469
Cdd:COG3210 721 ALANANGDTVTFGN-LGTGATLTLNAGVTITSG-----NAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEI 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1470 DTTAPVVTINTFAGDNIVNRSEHAQAQVLSGKATGAAVGDSVKITVNGVEYSTVLDASGNWSLGLPAEVISGLADGKYTA 1549
Cdd:COG3210 795 SIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATA 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1550 TVVVTDKAGNVGGSSLAFDVATGLPQITINAIAQDDVINAAEKSAEVTVSGTSNQPDGTQITVNLNGVDYAAVVNGNAWS 1629
Cdd:COG3210 875 ASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1630 VKIPAPDVAKLGEASYTVSASVTDASGNANSASHSVLVDSSLPIITINAVAGDNIINLAEVNAGQVLTGSVINAAAGDEV 1709
Cdd:COG3210 955 SAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGT 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1710 TVILGGKSYTVIVQSDLSWNLPLSKEMLTALGDGDLTVHASVTNGRGNTGSTDHDITIDAQLPGLRLDTISGDDIINLAE 1789
Cdd:COG3210 1035 GTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTG 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1790 HNQDLVVSGTCSGLNAGSVVTVTLNGKDYLATVNADGSwsaavpaadvstwpdGVLTVTAKAQDGAQNPIGIDGIVDVDL 1869
Cdd:COG3210 1115 GVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVS---------------AVAGGASSASAGDTTAVAAATTTTTGS 1179
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1870 APVSISVNSVTADNVLNAAEKGVDLVLSGLTTNVEPGQTVTITFAGHRYTTSVNNDGSWSYTVPAADMARLKDGDAQVTV 1949
Cdd:COG3210 1180 AINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTG 1259
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1950 SVSNANGNPATSTQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLIVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSV 2029
Cdd:COG3210 1260 ATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAG 1339
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2030 SVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLSIDPVAGDDIINASEHSQAHTVGGTSTGAAAGDVVT 2109
Cdd:COG3210 1340 GGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSG 1419
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2110 VVVTNGQGTSFTFTTtlDGNGNWNVGIPASVINGLADGSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVI 2189
Cdd:COG3210 1420 TTVAGTTGSSATTGT--GGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGA 1497
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2190 NATEKGQDLVLSGTSNQPAGTLITVTLNGI--NYQAVAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHN 2267
Cdd:COG3210 1498 TASNGGTSTGAGGTAGGTTAEVAKASLEGGegTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGD 1577
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2268 VQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGE 2347
Cdd:COG3210 1578 TGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTL 1657
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|.
gi 701771264 2348 LTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDVI 2388
Cdd:COG3210 1658 SGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDTAP 1698
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6275-6482 |
2.55e-24 |
|
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: 104.09 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6275 AAFYYDEEEKVND--LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqldtadlrrDMTLLS 6352
Cdd:cd03250 6 ASFTWDSGEQETSftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6353 QQARLFFGSIRDNLTMGRPLASD--EEIHRALALSGALgfvQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQIL 6430
Cdd:cd03250 73 QEPWIQNGTIRENILFGKPFDEEryEKVIKACALEPDL---EILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6431 LLDEPTAWLDEISEQQLVAN--LASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6293-6482 |
3.63e-24 |
|
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: 104.11 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARLFFG-SIRDNLTMGRP 6371
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6372 -----LASDEE-IHRALALSGALGFvQKQKNGlnyliteggaGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISE- 6444
Cdd:cd03298 97 pglklTAEDRQaIEVALARVGLAGL-EKRLPG----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRa 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 701771264 6445 --QQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03298 166 emLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6278-6482 |
5.68e-24 |
|
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: 103.11 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQldtADLRRDMTLLSQQAR- 6356
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVDy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 -LFFGSIRDNLTMGRPLASD-----EEIHRALALSGAlgfvqKQKNGLNyliteggagLSGGQRQALLLARTLILQPQIL 6430
Cdd:cd03226 83 qLFTDSVREELLLGLKELDAgneqaETVLKDLDLYAL-----KERHPLS---------LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6431 LLDEPTAWLDEISeQQLVANLASWLGN--RTLVVATHRIPILQLV-DRIIVLDNG 6482
Cdd:cd03226 149 IFDEPTSGLDYKN-MERVGELIRELAAqgKAVIVITHDYEFLAKVcDRVLLLANG 202
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
584-2262 |
7.29e-24 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 112.55 E-value: 7.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 584 VTDNKGDSQGLLSSNAVTDDSTPTFSGSGQPGATIQVKDANGNTIASTMVDSNGNWKVLLSEQPDGTHTYSVVQIDGNKI 663
Cdd:COG3210 9 TGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 664 TSAGEITLNVVTAQASLTAATTAGDNTLNAAEQANDFVISGSATELASGTALTVTLNGKTYATTVGSDGSW---SVTVPA 740
Cdd:COG3210 89 AGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGnntNTNNSS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 741 ADAKSLADGSWTVTVSGKDAAGNNISASETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVTLKLNG 820
Cdd:COG3210 169 SGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 821 KTYTATVGADGGWSMEVP---AADVQAMADNSYTLNLSVSDKAGNTTTTNASLLVDTTPPEASVNTVAGDDILSVSEQGQ 897
Cdd:COG3210 249 SSLSVAAGAGTGGAGGTGnagNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 898 AQIISGTSQGAAPGDKVTVSIGSETYQTTVQADGSWSVGVPKEVISSLPEGPNTITVAITDVAGNTGTTTHDITVSSTPP 977
Cdd:COG3210 329 NGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 978 NVAFNAISQDNVLNAIEATQPLILSGTSNLPDGSHVTVTLNNVNYTAQVQGGVWQVQVPVSDVVKLGDTTYTLSVSGTDT 1057
Cdd:COG3210 409 NTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1058 TGNTGTATATLQVDTALPTVIVSTFAGDNRVNNSEIANDQMLSGRVTGAHQGDTVTINIGGKNYTATVQSDLTWSTTVPA 1137
Cdd:COG3210 489 GIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLG 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1138 ADLRALGDGDVSIVASVTNAHGNTGSGSRDININAQLPGLRINTVSGDDVINAIEQHQDLTVTGTSTHLSAGTIITVRIN 1217
Cdd:COG3210 569 VLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGS 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1218 GVDYQAAVSATGSWQIGIPAADVAGWPNGKLEMVASSADESGNPVAATRPVDVDLNAVAISINSVTSDGVLNAVEKAADL 1297
Cdd:COG3210 649 GTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANGD 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1298 TL------SGKTLGVEAGQTVVI----KFAGHTYTTTVNQSGDWTFTV---PAADMRDMIDGRADVSVSVTNVSGNGASG 1364
Cdd:COG3210 729 TVtfgnlgTGATLTLNAGVTITSgnagTLSIGLTANTTASGTTLTLANangNTSAGATLDNAGAEISIDITADGTITAAG 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1365 AREVLVDTQPPSITLNSITADNILNhaeaaqelVITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVADLANLTD 1444
Cdd:COG3210 809 TTAINVTGSGGTITINTATTGLTGT--------GDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1445 GSWSVSASVSDVAGNPASTSHGMLVDTTAPVVTINTFAGDNIVNRSEHAQAQVLSGKATGAAVGDSVKITVNGVEYSTVL 1524
Cdd:COG3210 881 SGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASAS 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1525 DASGNWSLGLPAEVISGLADGKYTATVVVTDKAGNVGGSSLAFDVATGLPQITINAIAQDDVINAAEKSAEVTVSGTSNQ 1604
Cdd:COG3210 961 DGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATA 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1605 PDGTQITVNLNGVDYAAVVNGNAWSVKIPAPDVAKLGEASYTVSASVTDASGNANSASHSVLVDSSLPIITINAVAGDNI 1684
Cdd:COG3210 1041 GGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASK 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1685 INLAEVNAGQVLTGSVINAAAGDEVTVILGGKSYTVIVQSDLSWNLPLSKEMLTALGDGDLTVHASVTNGRGNTGSTDHD 1764
Cdd:COG3210 1121 VGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKG 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1765 ITIDAQLPGLRLDTISGDDIINLAEHNQDLVVSGTCSGLNAGSVVTVTLNGKDYLATVNADGSWSAAVPAADVSTWPDGV 1844
Cdd:COG3210 1201 GDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGAT 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1845 LTVTAKAQDGAQNPIGIDGIVDVDLAPVSISVNSVTADNVLNAAEKGVDLVLSGLTTNVEPGQTVTITFAGHRYTTSVNN 1924
Cdd:COG3210 1281 ATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATD 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1925 DGSWSYTVPAADMARLKDGDAQVTVSVSNANGNPATSTQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLIVSGSSSAEP 2004
Cdd:COG3210 1361 SAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNT 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2005 GQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLSIDPVAGDDII 2084
Cdd:COG3210 1441 TGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVA 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2085 NASEHSQAHTVGGTSTGAAAGDVVTVVVTNGQGTSFTFTTTLDGNGNWNVGIPASVINGLADGSYTITASVTDAAGNSGS 2164
Cdd:COG3210 1521 KASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLS 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2165 ADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTTVPASAVSKLG 2244
Cdd:COG3210 1601 LAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGL 1680
|
1690
....*....|....*...
gi 701771264 2245 EANYTVTAAVTDAHGNSS 2262
Cdd:COG3210 1681 GGATTAAAGNVATGDTAP 1698
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1464-1561 |
7.32e-24 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 98.90 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1464 SHGMLVDTTAPVVTINTFAGDNIVNRSEHAQAQVLSGKATGAAvGDSVKITVNGVEYSTVLDASGNWSLGLPAEVISGLA 1543
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEA-GQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1544 DGKYTATVVVTDKAGNVG 1561
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6293-6485 |
9.54e-24 |
|
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: 102.94 E-value: 9.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLgqldtADLRRDMTLLSQQARLF-FGSIRDN----LT 6367
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDRGYVFQQDALLpWLTVLDNvalgLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLASD--EEIHRALALSGALGFVQK---QknglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEI 6442
Cdd:cd03293 100 LQGVPKAEarERAEELLELVGLSGFENAyphQ--------------LSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6443 SE---QQLVANLasWLGNR-TLVVATHRI-PILQLVDRIIVLDNGPAR 6485
Cdd:cd03293 166 TReqlQEELLDI--WRETGkTVLLVTHDIdEAVFLADRVVVLSARPGR 211
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1763-1858 |
1.19e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 98.52 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1763 HDITIDAQLPGLRLDTISGDDIINLAEHNQDLVVSGTcSGLNAGSVVTVTLNGKDYLATVNADGSWSAAVPAADVSTWPD 1842
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGT-TTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*.
gi 701771264 1843 GVLTVTAKAQDGAQNP 1858
Cdd:NF033510 81 GTYTVTVTVTDAAGNT 96
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
950-2591 |
2.08e-23 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 111.01 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 950 NTITVAITDVAGNTGTTTHDITVSSTPPNVAFNAISQDNVLNAIEATQPLILSGTSNLPDGSHVTVTLNNVNYTAQVQGG 1029
Cdd:COG3210 56 GTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1030 VWQVQVPVSDVVKLGDTTYTLSVSGTDTTGNTGTATATLQVDTALPTVIVSTFAGDNRVNNSEIANDQMLSGRVTGAHQG 1109
Cdd:COG3210 136 STNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1110 DTVTINIGGKNYTATVQSDLTWSTTVPAADLRALGDGDVSIVASVTNAHGNTGSGSRDININAQLPGLRINTVSGDDVIN 1189
Cdd:COG3210 216 TAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1190 AIEQHQDLTVTGTSTHLSAGTIITVRINGVDYQAAVSATGSWQIGIPAADVAGWPNGKLEMVASSADESGNPVAATRPVD 1269
Cdd:COG3210 296 TTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1270 VDLNAVAISINSVTSDGVLNAVEKAADLTLSGKTLGVEAGQTVVIKFAGHTYTTTVNQSGDWTFTVPAADmrdmidGRAD 1349
Cdd:COG3210 376 GAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGT------IGGL 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1350 VSVSVTNVSGNGASGAREVLVDTQPPSITLNSITADNILNHAEAAQELVITGTSTAQPGQTVTVSLNNQSYTGLVLADGT 1429
Cdd:COG3210 450 TGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATS 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1430 WSVTVPVADLANLTDGSWSVSASVSDVAGNPASTSHGMLVDTTAPVVTINTFAGDNIVNRsehAQAQVLSGKATGAAVGD 1509
Cdd:COG3210 530 GGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSAT---GGTGTNSGGTVLSIGTG 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1510 SVKITVNGVEYSTVLDASGNWSLGLPAEVISGLADGKYTATVVVTDKAGNVGGSSLAFDVATGLPQITINAIAQDDVINA 1589
Cdd:COG3210 607 SAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGT 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1590 AEKSAEVTVSGTSNQpDGTQITVNLNGVDYAAVVNGNAWSVKIPAPDVAKLGEASYTVSASVTDASGNANSASHSVLVDS 1669
Cdd:COG3210 687 TGTTLNAATGGTLNN-AGNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANT 765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1670 SL--PIITINAVAGDNIINLAEVNAGQVLTGSVINA----AAGDEVTVILGGKSYTVIVQSDLSWNLPLSKEMLTALGDG 1743
Cdd:COG3210 766 TAsgTTLTLANANGNTSAGATLDNAGAEISIDITADgtitAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNT 845
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1744 DLTVHASVTNGRGNTGSTDHDITIDAQLPGLRLDTISGDDIINLAEHNQDLVVSGTCSGLNAGSVVTVTLNGKDYLATVN 1823
Cdd:COG3210 846 TDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGG 925
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1824 ADGSWSAAVPAADVSTWPDGVLTVTAKAQDGAQNPIGIDGIVDVDLAPVSISVNSVTADNVLNAAEKGVDLVLSGLTTNV 1903
Cdd:COG3210 926 LTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTT 1005
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1904 EPGQTVTITFAGHRYTTSVNNDGSWSYTVPAADMARLKDGDAQVTVSVSNANGNPATSTQEYSVDASAPTLIIDPLSGDN 1983
Cdd:COG3210 1006 ASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQA 1085
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1984 LLNAAEAKQPLIVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKDGTLTVSASVADKAGNPANADRG 2063
Cdd:COG3210 1086 SGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGD 1165
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2064 MRVDITEPKLSIDPVAGDDIINASEHSQAHTVGGTSTGAAAGDVVTVVVTNGQGTSFTFTTTLDGNGNWNVGIPASVING 2143
Cdd:COG3210 1166 TTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFV 1245
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2144 LADGSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQA 2223
Cdd:COG3210 1246 AAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATG 1325
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2224 VAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTV 2303
Cdd:COG3210 1326 TAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVT 1405
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2304 TGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVA 2383
Cdd:COG3210 1406 TSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGT 1485
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2384 GDDVINAIEHTQNLIINGTSSGLGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWAEG--AVTIEVKGSSGAGND 2461
Cdd:COG3210 1486 TTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAvsGAGSEGGAAGGVTGS 1565
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2462 VAIQHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELSGMTQNVEPGQTVNITFAGHTYTATVQADGSWKYTVPAADMV 2541
Cdd:COG3210 1566 VGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLAL 1645
|
1610 1620 1630 1640 1650
....*....|....*....|....*....|....*....|....*....|
gi 701771264 2542 NLKEGDTAVQVSVTNKNGNSTDAAQNVSVDTLAPALTVDPVSQDNLLNAA 2591
Cdd:COG3210 1646 VAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGD 1695
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6293-6488 |
3.13e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFG-SIRDNLTMGR- 6370
Cdd:PRK13548 23 LTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPfTVEEVVAMGRa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 PLAS-----DEEIHRALALSGALGFVQKQknglnYLiteggaGLSGGQRQALLLARTLILQPQILLL------DEPTAWL 6439
Cdd:PRK13548 103 PHGLsraedDALVAAALAQVDLAHLAGRD-----YP------QLSGGEQQRVQLARVLAQLWEPDGPprwlllDEPTSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6440 DeISEQQLVANLASWL---GNRTLVVATHRipiLQLV----DRIIVLDNGPARDDG 6488
Cdd:PRK13548 172 D-LAHQHHVLRLARQLaheRGLAVIVVLHD---LNLAaryaDRIVLLHQGRLVADG 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6279-6482 |
3.20e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.83 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILldgisLGQLDTADLRRDMTLLSQQARLF 6358
Cdd:PRK11247 22 YGERTVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 -FGSIRDNLTMG-----RPLAsdeeiHRALAlsgALGFVQKQknglnyliTEGGAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:PRK11247 94 pWKKVIDNVGLGlkgqwRDAA-----LQALA---AVGLADRA--------NEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6433 DEPTAWLD---EISEQQLVANLasWLGNR-TLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:PRK11247 158 DEPLGALDaltRIEMQDLIESL--WQQHGfTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
6196-6482 |
5.79e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 107.49 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6196 GCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARKGLDDLMQRP--LDDPEEgkkvHKAHLQGNYQLN 6273
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEApvVKDGSE----PVPEGRGELDVN 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6274 YAAFYYDEEEKvNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQ 6353
Cdd:PRK10789 318 IRQFTYPQTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 QARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLD 6433
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 701771264 6434 EPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
868-964 |
5.80e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 96.59 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 868 ASLLVDTTPPEASVNTVAGDDILSVSEQGQAQIISGTSQgAAPGDKVTVSIGSETYQTTVQADGSWSVGVPKEVISSLPE 947
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 948 GPNTITVAITDVAGNTG 964
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2465-2562 |
5.86e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 96.59 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2465 QHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELSGmTQNVEPGQTVNITFAGHTYTATVQADGSWKYTVPAADMVNLK 2544
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2545 EGDTAVQVSVTNKNGNST 2562
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3862-3957 |
6.33e-23 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 96.21 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3862 SQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTgAAAGNKIIITLDGVQYVTQVDAKGNWSVGVPASAVSALK 3941
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*.
gi 701771264 3942 NGTATITATLTDSAGN 3957
Cdd:NF033510 80 DGTYTVTVTVTDAAGN 95
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6293-6489 |
8.39e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.60 E-value: 8.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARLFFG-SIRDNLTMG-R 6370
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLFPHlTVAQNIGLGlR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 P---LASDE--EIHRALAlsgalgfvqkqKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQ 6445
Cdd:COG3840 98 PglkLTAEQraQVEQALE-----------RVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6446 ---QLVANLASWLGNrTLVVATHRIP-ILQLVDRIIVLDNGPARDDGK 6489
Cdd:COG3840 167 emlDLVDELCRERGL-TVLMVTHDPEdAARIADRVLLVADGRIAADGP 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6285-6482 |
9.03e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.91 E-value: 9.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQARLF-FGSIR 6363
Cdd:COG1131 16 LDGVS---LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYpDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTM-----GRPLASDEE-IHRALALSGaLGFVQKQKNGlnyliteggaGLSGGQRQALLLARTlilqpqilllDEPTA 6437
Cdd:COG1131 92 ENLRFfarlyGLPRKEARErIDELLELFG-LTDAADRKVG----------TLSGGMKQRLGLALAllhdpellilDEPTS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 701771264 6438 WLDEISEQQ---LVANLASwlGNRTLVVATHRIPIL-QLVDRIIVLDNG 6482
Cdd:COG1131 161 GLDPEARRElweLLRELAA--EGKTVLLSTHYLEEAeRLCDRVAIIDKG 207
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
3781-5468 |
1.06e-22 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 108.70 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3781 ATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQYVIKVDVSDAAGNKTT 3860
Cdd:COG3210 1 GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3861 GSQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTGAAAGNKIIITLDGVQYVTQVDAKGNWSVGVPASAVSAL 3940
Cdd:COG3210 81 IGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3941 KNGTATITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTLNGIQYTT 4020
Cdd:COG3210 161 NTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4021 TIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGT 4100
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4101 SSAEAGQKVTVKLGSESYEATVQADGSWSITVAAEDLAKLADGEFSVHAAVNDKAGNPGSADRTLTVDTTAPTITFDKVA 4180
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4181 GDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPTIS 4260
Cdd:COG3210 401 GSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4261 INTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSNSI 4340
Cdd:COG3210 481 SATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4341 GNSAGVDRTITVDTTPPQMTITIDSLQNDTGLSASDFITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTGTSW 4420
Cdd:COG3210 561 SNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4421 AYADGPLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDTGLDA----HDFITSDNTLTLSGKLG 4496
Cdd:COG3210 641 AALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLnnagNTLTISTGSITVTGQIG 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4497 APLAAgehaqisiDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLRVVDDAGNIGSTASQLVTVD-TVAPDASKTVTID 4575
Cdd:COG3210 721 ALANA--------NGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANgNTSAGATLDNAGA 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4576 SISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYFNDGRTLSDGTYQYLVRVVDDAG 4655
Cdd:COG3210 793 EISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAA 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4656 NVGQSASKNVTVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLNGSLGAPLGSNEFVQISIDGGASWFYATSVNG 4735
Cdd:COG3210 873 TAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNA 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4736 TRWSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGISDDTGQSASDFITMDTTLTLNGTLGHA 4815
Cdd:COG3210 953 GLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASAT 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4816 LASDERVQISLDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNVGSTANQVVTVDTVAPDTVGSIVSYTDN 4895
Cdd:COG3210 1033 GTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTS 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4896 NGERTGNFDSSYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTFADSGLLDGSYHYVLRVTDKAGNY 4975
Cdd:COG3210 1113 TGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEG 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4976 TESNDFGLTVDTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVVTVNGKTYTSDRGGAVVVDPASNTWYLQIPDA 5055
Cdd:COG3210 1193 TAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATST 1272
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5056 DVLSLKSYDVTAQVKSSAGNGNSVDVTHGTVVVGAEASMTPAWAFTSATNAIAASFMLDANGMWTFASNQQFATANDRNS 5135
Cdd:COG3210 1273 VAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGL 1352
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5136 YSVSGNFSMTGSYTTGAYADINRDGHADMLVESTNYSyITQLMNNGDGTYTSTSPGSSATVGALLWYGAVVSIDFQGDGY 5215
Cdd:COG3210 1353 NGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGN-NTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSAT 1431
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5216 VDFVMGDAGGPDSSTFVNNNAGKLTGTSGGGTYTNFVSGSKVGNYNSVIETSGVDLNNDGMVDIAQHTTNGGNIYALSTM 5295
Cdd:COG3210 1432 TGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGT 1511
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5296 FNKGDGTFTWSQNFINTMYSATGSAAANNAVSMTWADFDGDGYMDLYMGMSRAGTGGLLMMNDGKGNLLTGTAVGSEKYN 5375
Cdd:COG3210 1512 AGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTA 1591
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5376 GTVSVAVDWNMDGRMDIIKLANTGQSYMYTNDGLKGVASFTSSKFGSATTSQVSGAALVDYDWDGAQDLLIFRQNGSVTL 5455
Cdd:COG3210 1592 GNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVD 1671
|
1690
....*....|...
gi 701771264 5456 ERNTNAVAPGTAI 5468
Cdd:COG3210 1672 LTDATLAGLGGAT 1684
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6279-6482 |
1.16e-22 |
|
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: 98.41 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLD--TADLRRDMTLLSQQAR 6356
Cdd:cd03229 10 YGQKTVLNDVS---LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFG-SIRDNLTMgrplasdeeihralalsgalgfvqkqknglnyliteggaGLSGGQRQALLLARTLILQPQILLLDEP 6435
Cdd:cd03229 87 LFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6436 TAWLDEISE---QQLVANLASWLGnRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03229 128 TSALDPITRrevRALLKSLQAQLG-ITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4250-4344 |
1.17e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 95.44 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4250 VTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDa 4329
Cdd:NF033510 4 VTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADGT- 82
|
90
....*....|....*
gi 701771264 4330 YVIHASVSNSIGNSA 4344
Cdd:NF033510 83 YTVTVTVTDAAGNTS 97
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6295-6482 |
1.86e-22 |
|
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: 100.37 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPlAS 6374
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6375 DEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASW 6454
Cdd:cd03288 123 DDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA 202
|
170 180
....*....|....*....|....*...
gi 701771264 6455 LGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03288 203 FADRTVVTIAHRVSTILDADLVLVLSRG 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6288-6482 |
2.05e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.13 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQ----ARLffg 6360
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRIGMIFQQfnlvPRL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 SIRDNLTMGR-----------PLASDEEIHRALALSGALGFVQK--QKnglnyliteggAG-LSGGQRQALLLARTLILQ 6426
Cdd:COG3638 96 SVLTNVLAGRlgrtstwrsllGLFPPEDRERALEALERVGLADKayQR-----------ADqLSGGQQQRVAIARALVQE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6427 PQILLLDEPTAWLD-EISEQ--QLVANLASWLGnRTLVVATHRIPI-LQLVDRIIVLDNG 6482
Cdd:COG3638 165 PKLILADEPVASLDpKTARQvmDLLRRIAREDG-ITVVVNLHQVDLaRRYADRIIGLRDG 223
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1865-1959 |
2.70e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 94.67 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1865 VDVDLAPVSISVNSVTADNVLNAAEKGVDLVLSGlTTNVEPGQTVTITFAGHRYTTSVNNDGSWSYTVPAADMARLKDGD 1944
Cdd:NF033510 4 VTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADGT 82
|
90
....*....|....*
gi 701771264 1945 AQVTVSVSNANGNPA 1959
Cdd:NF033510 83 YTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3564-3659 |
2.86e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 94.67 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3564 REFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGmSEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAA 3643
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*.
gi 701771264 3644 GNLTVTAAGSSSAGNP 3659
Cdd:NF033510 81 GTYTVTVTVTDAAGNT 96
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6286-6482 |
3.59e-22 |
|
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: 99.28 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6286 NDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQARLfFGS- 6361
Cdd:COG1127 22 DGVS---LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRRIGMLFQGGAL-FDSl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 -IRDN----LTMGRPLaSDEEIhRALALSgALGFVqkqknGLnyliteGGAG------LSGGQR-------------QAL 6417
Cdd:COG1127 98 tVFENvafpLREHTDL-SEAEI-RELVLE-KLELV-----GL------PGAAdkmpseLSGGMRkrvalaralaldpEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6418 LLartlilqpqilllDEPTAWLDEISEQ---QLVANLASWLGNrTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG1127 164 LY-------------DEPTAGLDPITSAvidELIRELRDELGL-TSVVVTHDLDsAFAIADRVAVLADG 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6285-6485 |
7.05e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.01 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLgqldtADLRRDMTLLSQQARLF-FGSIR 6363
Cdd:COG1116 27 LDDVS---LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDRGVVFQEPALLpWLTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTMGRPLA------SDEEIHRALALSGALGFVQK---QknglnyliteggagLSGGQRQ----A---------LLLar 6421
Cdd:COG1116 99 DNVALGLELRgvpkaeRRERARELLELVGLAGFEDAyphQ--------------LSGGMRQrvaiAralandpevLLM-- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6422 tlilqpqilllDEPTAWLDEISE---QQLVANLasWLGNR-TLVVATHRIP--ILqLVDRIIVLDNGPAR 6485
Cdd:COG1116 163 -----------DEPFGALDALTRerlQDELLRL--WQETGkTVLFVTHDVDeaVF-LADRVVVLSARPGR 218
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3363-3460 |
8.41e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 93.13 E-value: 8.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3363 SHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSaNLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLG 3442
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTT-TAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3443 EANYTLTATATSSIGNSA 3460
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2066-2163 |
9.26e-22 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 93.13 E-value: 9.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2066 VDITEPKLSIDPVAGDDIINASEHSQAHTVGGTSTgAAAGDVVTVVVtNGQgtsfTFTTTLDGNGNWNVGIPASVINGLA 2145
Cdd:NF033510 6 VDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTL-NGK----TYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2146 DGSYTITASVTDAAGNSG 2163
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
670-763 |
1.05e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 92.74 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 670 TLNVVTAQASLTAATTAGDNTLNAAEQANDFVISGSATeLASGTALTVTLNGKTYATTVGSDGSWSVTVPAADAKSLADG 749
Cdd:NF033510 3 PVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADG 81
|
90
....*....|....
gi 701771264 750 SWTVTVSGKDAAGN 763
Cdd:NF033510 82 TYTVTVTVTDAAGN 95
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
3992-5678 |
1.43e-21 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 105.23 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3992 QDLTIGGSSTELAVGTQVTVTLNGIQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNISVDTV 4071
Cdd:COG3210 2 SGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4072 APIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGQKVTVKLGSESYEATVQADGSWSITVAAEDLAKLADGEFSVHAAV 4151
Cdd:COG3210 82 GAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4152 NDKAGNPGSADRTLTVDTTAPTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAVDFLGAADGSYq 4231
Cdd:COG3210 162 TNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4232 isASVSDKAGNSSSADKQVTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGT 4311
Cdd:COG3210 241 --ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4312 WSYTLGSSAVSALADGDAYVIHAS--VSNSIGNSAGVDRTITVDTTPPQMTITIDSLQNDTGLSASDFITADNKVVVKGS 4389
Cdd:COG3210 319 GITTTNTVGGNGDGNNTTANSGAGlvSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4390 LSGALGNNEKAQISLDGGKTWTDLVVTGTSWAYADGPLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVE 4469
Cdd:COG3210 399 VLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4470 AISRDTGLDAHDFITSDNTLTLSGKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLRVVDDAG 4549
Cdd:COG3210 479 TTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4550 NIGSTASQLVTVDTVAPDASKTVTIDSISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGS 4629
Cdd:COG3210 559 SGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4630 TWYFNDGRTLSDGTYQYLVRVVDDAGNVGQSASKNVTVDTTPPDASVTVTVDSITTDSGFSN---SDFITNDNTLTLNGS 4706
Cdd:COG3210 639 VGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNnagNTLTISTGSITVTGQ 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4707 LGAPLGSNEFVQISIDGGASWFYATSVNGTRWSYTDGRQLADGDHTWQ-----VRVVDLAGNvgATTSQTVTVDTVAPAY 4781
Cdd:COG3210 719 IGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTasgttLTLANANGN--TSAGATLDNAGAEISI 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4782 GITIDGISDDTGQSASDFITMDTTLTLNG-TLGHALASDERVQISLDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVR 4860
Cdd:COG3210 797 DITADGTITAAGTTAINVTGSGGTITINTaTTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAAS 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4861 IIDQAGNVGSTANQVVTVDTVAPDTVGSIVSYTDNNGERTGNFDSSYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVG 4940
Cdd:COG3210 877 ITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4941 NVTITGGTRWTFADSGLLDGSYHYVLRVTDKAGNY--TESNDFGLTVDTSVPTTKALVNGLNTTDTTPIITGSVDANLVH 5018
Cdd:COG3210 957 ASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIaaTGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGT 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5019 GEFVVVTVNGKTYTSDRGGAVVVDPASNTWYLQIPDADVLSLKSYDVTAQVKSSAGNGNSVDVTHGTVVVGAEASMTPAW 5098
Cdd:COG3210 1037 AATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGV 1116
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5099 AFTSATNAIAASFMLDANGMWTFASNQQFATANDRNSYSVSGNFSMTGSYTTGAYADINRDGHADMLVESTNYSYITQLM 5178
Cdd:COG3210 1117 TASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGT 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5179 NNGDGTYTSTSPGSSATVGALLWYGAVVSIDFQGDGYVDFVMGDAGGPDSSTFVNNNAGKLTGTSGGGTYTNFVSGSKVG 5258
Cdd:COG3210 1197 DLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGN 1276
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5259 NYNSVIETSGVDLNNDGMVDIAQHTTNGGNIYALSTMFNKGDGTFTWSQNFINTMYSATGSAAANNAVSMTWADFDGDGY 5338
Cdd:COG3210 1277 AGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGN 1356
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5339 MDLYMGMSRAGTGGLLMMNDGKGNLLTGTAVGSE--KYNGTVSVAVDWNMDGRMDIIKLANTGQSYMYTNDGLKGVASFT 5416
Cdd:COG3210 1357 GATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNtgAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGG 1436
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5417 SSKFGSATTSQVSGAALVDYDWDGAQDLLIFRQNGSVTLERNTNAVAPGTAIHLKIVDSQGINVFFGNTVKLYNAAGELV 5496
Cdd:COG3210 1437 TGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTT 1516
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5497 ASQVINAQSGIGINDASALVSFYGLNPNETYHAELVRAINGVSSNTTWNGLTAGDGRESYALTADAATGVHAGTLTGTGY 5576
Cdd:COG3210 1517 AEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTAT 1596
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5577 NDTFIAEQGTYVYNGGGGWETSSDHQTWSATGGMDVVDFRNSTVGVTVDLGKTGAQNTGFNTATFSNIEGIVGSSHDDVI 5656
Cdd:COG3210 1597 LTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDAT 1676
|
1690 1700
....*....|....*....|..
gi 701771264 5657 TGNSGNNTFEGGGGNDTFNIGS 5678
Cdd:COG3210 1677 LAGLGGATTAAAGNVATGDTAP 1698
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3664-3760 |
2.78e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 91.58 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3664 RSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGkTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKD 3743
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 3744 GDASVKVSVTNVNGNGA 3760
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3065-3161 |
3.03e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 91.58 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3065 HTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGmTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKD 3144
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALAD 80
|
90
....*....|....*..
gi 701771264 3145 GDTSVEVSVVNVTGNGA 3161
Cdd:NF033510 81 GTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1068-1162 |
4.02e-21 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 91.20 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1068 LQVDTALPTVIVSTFAGDNRVNNSEIANDQMLSGRVTGAhQGDTVTINIGGKNYTATVQSDLTWSTTVPAADLRALGDGD 1147
Cdd:NF033510 4 VTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAE-AGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALADGT 82
|
90
....*....|....*
gi 701771264 1148 VSIVASVTNAHGNTG 1162
Cdd:NF033510 83 YTVTVTVTDAAGNTS 97
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6293-6482 |
5.79e-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: 96.03 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARlffGSIRDNLTMGR-- 6370
Cdd:COG1124 26 LEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPY---ASLHPRHTVDRil 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 --PLAS------DEEIHRALA---LSGALgfvqkqkngLNYLITEggagLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:COG1124 103 aePLRIhglpdrEERIAELLEqvgLPPSF---------LDRYPHQ----LSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6440 DeISEQQLVANLaswLG------NRTLVVATHRIPILQ-LVDRIIVLDNG 6482
Cdd:COG1124 170 D-VSVQAEILNL---LKdlreerGLTYLFVSHDLAVVAhLCDRVAVMQNG 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6295-6482 |
9.99e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.16 E-value: 9.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTmgrPL-- 6372
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD---PFle 1409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 ASDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQI-LLLDEPTAWLDEISEQQLVANL 6451
Cdd:PTZ00243 1410 ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGfILMDEATANIDPALDRQIQATV 1489
|
170 180 190
....*....|....*....|....*....|.
gi 701771264 6452 ASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PTZ00243 1490 MSAFSAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6277-6482 |
1.27e-20 |
|
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: 94.77 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQ-ILLDGISLGQLDTADLRRDMTLLSQ-- 6353
Cdd:COG1119 11 VRRGGKTILDDIS---WTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGLVSPal 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 QARL-------------FFGSIrdnltmGRPLA-SDEEIHRALALSGALGfvqkqkngLNYLITEGGAGLSGGQRQALLL 6419
Cdd:COG1119 88 QLRFprdetvldvvlsgFFDSI------GLYREpTDEQRERARELLELLG--------LAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6420 ARTLILQPQILLLDEPTAWLDEISEQQLVANLASW--LGNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVeEIPPGITHVLLLKDG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6293-6482 |
1.80e-20 |
|
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: 94.17 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQ----ARLffgSIRDN 6365
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIGMIFQQfnliERL---SVLEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6366 LTMGR-----------PLASDEEIHRALAlsgALgfvqkQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:cd03256 99 VLSGRlgrrstwrslfGLFPKEEKQRALA---AL-----ERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6435 PTAWLDEISEQQ---LVANLASWLGnRTLVVATHRIPI-LQLVDRIIVLDNG 6482
Cdd:cd03256 171 PVASLDPASSRQvmdLLKRINREEG-ITVIVSLHQVDLaREYADRIVGLKDG 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6278-6482 |
2.89e-20 |
|
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: 92.98 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQ--LDTADLRRDMTLLSQQA 6355
Cdd:cd03262 9 SFGDFHVLKGID---LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLF-FGSIRDNLTMG----RPLASDEEIHRALALSGALGFVQKQknglNYLITEggagLSGGQRQALLLARTLILQPQIL 6430
Cdd:cd03262 86 NLFpHLTVLENITLApikvKGMSKAEAEERALELLEKVGLADKA----DAYPAQ----LSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6431 LLDEPTAWLDE--ISE-QQLVANLASwlGNRTLVVATHRIPILQLV-DRIIVLDNG 6482
Cdd:cd03262 158 LFDEPTSALDPelVGEvLDVMKDLAE--EGMTMVVVTHEMGFAREVaDRVIFMDDG 211
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1265-1362 |
3.01e-20 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 88.89 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1265 TRPVDVDLNAVAISINSVTSDGVLNAVEKAADLTLSGkTLGVEAGQTVVIKFAGHTYTTTVNQSGDWTFTVPAADMRDMI 1344
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSG-TTTAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1345 DGRADVSVSVTNVSGNGA 1362
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
6293-6482 |
4.09e-20 |
|
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: 92.23 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISlgQLDTADLRRDMTLLSQQARLFFG-SIRDNLTMGrp 6371
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6372 lasdeeIHRALALSGalgfVQKQK-------NGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISE 6444
Cdd:TIGR01277 95 ------LHPGLKLNA----EQQEKvvdaaqqVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701771264 6445 QQ---LVANLASWlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:TIGR01277 165 EEmlaLVKQLCSE-RQRTLLMVTHHLSdARAIASQIAVVSQG 205
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4163-4244 |
9.39e-20 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 87.35 E-value: 9.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4163 RTLTVDTTAPTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAV--------------DFLGAADG 4228
Cdd:NF033510 2 HPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATvdadgswsvtvpaaDLAALADG 81
|
90
....*....|....*.
gi 701771264 4229 SYQISASVSDKAGNSS 4244
Cdd:NF033510 82 TYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2365-2460 |
9.96e-20 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 87.35 E-value: 9.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2365 SRDIVIDANLPGLRVDTVAGDDVINAIEHTQNLIINGTSSGlGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWA 2444
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*.
gi 701771264 2445 EGAVTIEVKGSSGAGN 2460
Cdd:NF033510 80 DGTYTVTVTVTDAAGN 95
|
|
| tolC |
PRK09465 |
outer membrane channel protein; Reviewed |
43-338 |
1.04e-19 |
|
outer membrane channel protein; Reviewed
Pssm-ID: 236529 [Multi-domain] Cd Length: 446 Bit Score: 96.16 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 43 ALDRDPSVSQQAAQFGIGQAQIDQARSAWMPQISLNGSTGHSR-TTDSSGSLKNSAAYGLSLTQLVYDFGKTNS-NISQQ 120
Cdd:PRK09465 32 ARLSNPELLKAAADRDAAFEKINEARSPLLPQLGLGAGYTYSNgYRDANGIDSNGTSASLQLTQTIFDMSKWRAlTLAEK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 121 QSQRESYRYQlmATLTGVAEKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQ--------T 192
Cdd:PRK09465 112 AAGIADVTYQ--TAQQTLILRTATAYFNVLRAIDNLSFTEAEKRAIYRQLDQTTQRFNVGLVAITDVQNAQaqydtvlaN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 193 RIAGmRSTLEQ-YRAARQ---SAKARLAVLTGVSAANYQAMPVRLALEQEPLDNIDysLIPSVLAAEAMRESsgyaVDKA 268
Cdd:PRK09465 190 EVLA-RNNLDNaYEALRQitgNYYPELAVLNTERFSTPKPQSVNALLKEAEKRNLS--LLSARLSQDLAREQ----IRLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 269 KSGHWPTLSL----------RGGRTRYQSNNSAYWDDQIQLNVDAPIYQGGAVSAQVEQAQGARRIAASQVEQAKFDVLQ 338
Cdd:PRK09465 263 QAGHMPTLDLtasygisdtsYSGANGTQYDDSDMGQNKVGLNLSLPLYSGGAVNSQVKQAQYNFVGASEQLESAHRSVVQ 342
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1165-1262 |
1.11e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.96 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1165 SRDININAQLPGLRINTVSGDDVINAIEQHQDLTVTGTSThLSAGTIITVRINGVDYQAAVSATGSWQIGIPAADVAGWP 1244
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1245 NGKLEMVASSADESGNPV 1262
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
5958-6211 |
1.23e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 93.29 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFsMQ-VYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARA 6036
Cdd:cd18567 7 ILLLSLALELFALASPLY-LQlVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6037 LRIKNS---ARpkSTGSFISQIRELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLVQR 6113
Cdd:cd18567 86 LRLPLSyfeKR--HLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6114 PLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVL 6193
Cdd:cd18567 164 PLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVI 243
|
250
....*....|....*...
gi 701771264 6194 LVGCYLVINGDMTTGALV 6211
Cdd:cd18567 244 YLGALLVLDGEFTVGMLF 261
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1564-1658 |
1.31e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.96 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1564 SLAFDVATGLPQITINAIAQDDVINAAEKSAEVTVSGTSNQPDGTQITVNLNGVDYAAVVNGN-AWSVKIPAPDVAKLGE 1642
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDADgSWSVTVPAADLAALAD 80
|
90
....*....|....*.
gi 701771264 1643 ASYTVSASVTDASGNA 1658
Cdd:NF033510 81 GTYTVTVTVTDAAGNT 96
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6293-6471 |
1.53e-19 |
|
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: 98.44 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQhGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTmgrPL 6372
Cdd:TIGR01271 1240 FSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD---PY 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 A--SDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVAN 6450
Cdd:TIGR01271 1316 EqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKT 1395
|
170 180
....*....|....*....|..
gi 701771264 6451 LASWLGNRTLVVATHRI-PILQ 6471
Cdd:TIGR01271 1396 LKQSFSNCTVILSEHRVeALLE 1417
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2265-2362 |
1.89e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.58 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2265 SHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVkGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALG 2344
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEA-GQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2345 NGELTITASVTNGHGNTG 2362
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6288-6489 |
2.04e-19 |
|
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: 94.02 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIArLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL----GQLDTADLRRDMTLLSQQARLF-FGSI 6362
Cdd:TIGR02142 14 LDAD-FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6363 RDNLTMGR-------PLASDEEIHRALalsgalgfvqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEP 6435
Cdd:TIGR02142 93 RGNLRYGMkrarpseRRISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6436 TAWLDEISEQQLVA---NLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:TIGR02142 159 LAALDDPRKYEILPyleRLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6294-6485 |
2.05e-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: 92.22 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQhGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTmgrPLA 6373
Cdd:cd03289 26 SISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLD---PYG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6374 --SDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANL 6451
Cdd:cd03289 102 kwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL 181
|
170 180 190
....*....|....*....|....*....|....
gi 701771264 6452 ASWLGNRTLVVATHRIPILQLVDRIIVLDNGPAR 6485
Cdd:cd03289 182 KQAFADCTVILSEHRIEAMLECQRFLVIEENKVR 215
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
1662-1759 |
2.11e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.19 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1662 SHSVLVDSSLPIITINAVAGDNIINLAEVNAGQVLTGSViNAAAGDEVTVILGGKSYTVIVQSDLSWNLPLSKEMLTALG 1741
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTT-TAEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 1742 DGDLTVHASVTNGRGNTG 1759
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3962-4060 |
2.25e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.19 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3962 SHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTeLAVGTQVTVTLNGIQYTTTIQPGGGWSVTVPANQVQNLA 4041
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTT-AEAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*....
gi 701771264 4042 HGSgYTVMASATDSANNAT 4060
Cdd:NF033510 80 DGT-YTVTVTVTDAAGNTS 97
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2964-3061 |
2.28e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 86.19 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2964 SRDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSSGlSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQ 3043
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3044 AGDITVSAGGTSSSGNPV 3061
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6285-6482 |
2.34e-19 |
|
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: 88.99 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQARLFfgsirD 6364
Cdd:cd03230 16 LDDIS---LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLY-----E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6365 NLTmgrplasdeeihralalsgalgfvqkqknGLNYLIteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISE 6444
Cdd:cd03230 87 NLT-----------------------------VRENLK------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701771264 6445 Q---QLVANLASwlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03230 132 RefwELLRELKK--EGKTILLSSHILEeAERLCDRVAILNNG 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6287-6482 |
3.27e-19 |
|
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: 89.66 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6287 DLDIArlTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL----GQLDTADLRRDMTLLSQQARLF-FGS 6361
Cdd:cd03297 14 TLKID--FDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 IRDNLTMGRPLASDEEIH-RALALSGALGfvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:cd03297 92 VRENLAFGLKRKRNREDRiSVDELLDLLG--------LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701771264 6441 EISEQQL---VANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03297 164 RALRLQLlpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
3263-3360 |
3.29e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 85.81 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3263 SHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAgDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLA 3342
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAG-QTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 3343 DGKVTINASLTDSAGNTG 3360
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6278-6482 |
3.54e-19 |
|
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: 90.33 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQ 6354
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 ARLFFG-SIRDNLTMgrPL----ASDEEIH-RALALsgaLGFVqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQ 6428
Cdd:cd03258 91 FNLLSSrTVFENVAL--PLeiagVPKAEIEeRVLEL---LELV-----GLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6429 ILLLDEPTAWLDEISEQQLVANLASWlgNR----TLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEvVKRICDRVAVMEKG 217
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
2864-2961 |
4.04e-19 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 85.42 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2864 SSTLEVASTLPGVIINAVAIDDIINAAELATGQTISGRVTGvQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALG 2943
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTA-EAGQTVTVTLNGKTYTATVDADGSWSVTVPAADLAALA 79
|
90
....*....|....*...
gi 701771264 2944 DGSLKINASVTDGAGNTG 2961
Cdd:NF033510 80 DGTYTVTVTVTDAAGNTS 97
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6278-6482 |
5.94e-19 |
|
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: 89.42 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD-LRRDMTLLSQQAR 6356
Cdd:cd03224 9 GYGKSQILFGVS---LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFG-SIRDNLTMG----RPLASDEEIHRALALSGALGFVQKQKNGLnyliteggagLSGGQRQALLLARTLILQPQILL 6431
Cdd:cd03224 86 IFPElTVEENLLLGayarRRAKRKARLERVYELFPRLKERRKQLAGT----------LSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6432 LDEPTAWL-----DEISEqqLVANLASwLGnRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03224 156 LDEPSEGLapkivEEIFE--AIRELRD-EG-VTILLVEQNARfALEIADRAYVLERG 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6279-6482 |
8.03e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLF 6358
Cdd:PRK11231 12 YGTKRILNDLS---LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG-SIRDNLTMGRP--------LASDEEIHRALALsgalgfvqkQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQI 6429
Cdd:PRK11231 89 EGiTVRELVAYGRSpwlslwgrLSAEDNARVNQAM---------EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6430 LLLDEPTAWLDeISEQQLVANLASWLGN--RTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK11231 160 VLLDEPTTYLD-INHQVELMRLMRELNTqgKTVVTVLHDLnQASRYCDHLVVLANG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6285-6482 |
1.30e-18 |
|
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: 93.43 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQL---DTADLRRDMTLLSQ--QARLF- 6358
Cdd:COG1123 281 VDDVS---LTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQdpYSSLNp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FGSIRDNLTMG---RPLASDEEIHRALAlsGALGFVQKQKNGLNYLITEggagLSGGQRQ------------ALLLArtl 6423
Cdd:COG1123 358 RMTVGDIIAEPlrlHGLLSRAERRERVA--ELLERVGLPPDLADRYPHE----LSGGQRQrvaiaralalepKLLIL--- 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6424 ilqpqilllDEPTAWLDeISEQ----QLVANLASWLGnRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG1123 429 ---------DEPTSALD-VSVQaqilNLLRDLQRELG-LTYLFISHDLAvVRYIADRVAVMYDG 481
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6276-6488 |
1.60e-18 |
|
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: 93.04 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6276 AFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQ---HGQILLDGISLGQLDTADLRRDMTLLS 6352
Cdd:COG1123 13 RYPGGDVPAVDGVS---LTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6353 Q--QARLFFGSIRDNLTMG---RPLASDEEIHRALALsgaLGFVqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQP 6427
Cdd:COG1123 90 QdpMTQLNPVTVGDQIAEAlenLGLSRAEARARVLEL---LEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6428 QILLLDEPTAWLDEISEQQ---LVANLASWLGnRTLVVATHRIP-ILQLVDRIIVLDNGPARDDG 6488
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEildLLRELQRERG-TTVLLITHDLGvVAEIADRVVVMDDGRIVEDG 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6278-6482 |
2.15e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.80 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD---LRRDMTLLSQQ 6354
Cdd:COG2884 11 YPGGREALSDVS---LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 ARLFFG-SIRDNLTMgrPL----ASDEEIHR----ALALSGALGFvqkqkngLNYLITEggagLSGGQRQ---------- 6415
Cdd:COG2884 88 FRLLPDrTVYENVAL--PLrvtgKSRKEIRRrvreVLDLVGLSDK-------AKALPHE----LSGGEQQrvaiaralvn 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6416 --ALLLArtlilqpqilllDEPTAWLD-EISEQ--QLVANLaswlgNR---TLVVATHRIPILQLVD-RIIVLDNG 6482
Cdd:COG2884 155 rpELLLA------------DEPTGNLDpETSWEimELLEEI-----NRrgtTVLIATHDLELVDRMPkRVLELEDG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6288-6489 |
2.43e-18 |
|
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: 88.12 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQ----ARLffg 6360
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRRIGMIFQHynliERL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 SIRDNLTMGRpLA------------SDEEIHRALALSGALGFVQKQKNGLNYLiteggaglSGGQRQALLLARTLILQPQ 6428
Cdd:TIGR02315 95 TVLENVLHGR-LGykptwrsllgrfSEEDKERALSALERVGLADKAYQRADQL--------SGGQQQRVAIARALAQQPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6429 ILLLDEPTAWLDEISEQQ---LVANLASWLGnRTLVVATHRIPI-LQLVDRIIVLDNGPARDDGK 6489
Cdd:TIGR02315 166 LILADEPIASLDPKTSKQvmdYLKRINKEDG-ITVIINLHQVDLaKKYADRIVGLKAGEIVFDGA 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6285-6482 |
2.58e-18 |
|
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: 87.56 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQArlfFGS 6361
Cdd:cd03257 21 LDDVS---FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQDP---MSS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 ----------IRDNLTMGRPLASDEEIHRALALSGALgfVQKQKNGLNYLITEggagLSGGQRQALLLARTLILQPQILL 6431
Cdd:cd03257 95 lnprmtigeqIAEPLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNRYPHE----LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6432 LDEPTAWLDEISEQQ---LVANLASWLGNrTLVVATHRIPILQ-LVDRIIVLDNG 6482
Cdd:cd03257 169 ADEPTSALDVSVQAQildLLKKLQEELGL-TLLFITHDLGVVAkIADRVAVMYAG 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6277-6482 |
2.79e-18 |
|
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: 87.74 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR 6356
Cdd:cd03295 9 RYGGGKKAVNNLN---LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LF-FGSIRDNLTMGRPLA--SDEEIH-RALALSGALGfvqkqknglnyLITEGGAG-----LSGGQRQALLLARTLILQP 6427
Cdd:cd03295 86 LFpHMTVEENIALVPKLLkwPKEKIReRADELLALVG-----------LDPAEFADrypheLSGGQQQRVGVARALAADP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6428 QILLLDEPTAWLDEISE---QQLVANLASWLGnRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:cd03295 155 PLLLMDEPFGALDPITRdqlQEEFKRLQQELG-KTIVFVTHDIdEAFRLADRIAIMKNG 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6294-6482 |
3.59e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 94.03 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTmgrPLA 6373
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD---PFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6374 --SDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANL 6451
Cdd:PLN03130 1338 ehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTI 1417
|
170 180 190
....*....|....*....|....*....|.
gi 701771264 6452 ASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PLN03130 1418 REEFKSCTMLIIAHRLNTIIDCDRILVLDAG 1448
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
6293-6489 |
4.90e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISlgQLDTADLRRDMTLLSQQARLFFG-SIRDNLTMGrp 6371
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLG-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6372 lasdeeIHRALALSGAlgfvQK-------QKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISE 6444
Cdd:PRK10771 96 ------LNPGLKLNAA----QReklhaiaRQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6445 QQLVANLASWLGNR--TLVVATHRIP-ILQLVDRIIVLDNGPARDDGK 6489
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGP 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6293-6480 |
5.15e-18 |
|
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: 86.01 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQ----ARLffgSIRDNLTM 6368
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLGHApgikTTL---SVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6369 GRPLASDEEIHRALALSGAlgfvqkqkNGLNYLITeggAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLV 6448
Cdd:cd03231 97 WHADHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180 190
....*....|....*....|....*....|..
gi 701771264 6449 ANLASWLGNRTLVVATHRIPILQLVDRIIVLD 6480
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6295-6482 |
6.73e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 92.73 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTmgrPLA- 6373
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID---PFSe 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6374 -SDEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLA 6452
Cdd:PLN03232 1336 hNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR 1415
|
170 180 190
....*....|....*....|....*....|
gi 701771264 6453 SWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PLN03232 1416 EEFKSCTMLVIAHRLNTIIDCDKILVLSSG 1445
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6288-6482 |
1.00e-17 |
|
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: 86.24 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARLF-FGSIRDNL 6366
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6367 TMG---RPLAS----DEEIHRALALsgaLGFVQkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:cd03296 96 AFGlrvKPRSErppeAEIRAKVHEL---LKLVQ-----LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6440 DeiseQQLVANLASWLG------NRTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:cd03296 168 D----AKVRKELRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKG 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6015-6488 |
1.36e-17 |
|
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: 91.93 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6015 HIADVVGKRADLRISDRVFARALRIKNSARPKSTGSFISQIRELESVRELITSTTIGTVSDIPF-FLLFVFILWLIGGPL 6093
Cdd:TIGR00957 380 HICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLqVILALYFLWLNLGPS 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6094 VFVVLLAIPLLLIPGLLVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWL 6173
Cdd:TIGR00957 460 VLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYL 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6174 TSL-LMTWTQE---VQSIVYAVVLLVGCYLVINGDMTTGALVGTSILAsrtiAPLAQISGVLSRWQQAKVARKGLDDLMQ 6249
Cdd:TIGR00957 540 HAVgTFTWVCTpflVALITFAVYVTVDENNILDAEKAFVSLALFNILR----FPLNILPMVISSIVQASVSLKRLRIFLS 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6250 RPLDDPEEGKKVHKAHLQGN-YQLNYAAFYY--DEEEKVNDLDIarlTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQH 6326
Cdd:TIGR00957 616 HEELEPDSIERRTIKPGEGNsITVHNATFTWarDLPPTLNGITF---SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6327 GQILLDGislgqldtadlrrDMTLLSQQARLFFGSIRDNLTMGRPLasDEEIHRALALSGAL-GFVQKQKNGLNYLITEG 6405
Cdd:TIGR00957 693 GHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKAL--NEKYYQQVLEACALlPDLEILPSGDRTEIGEK 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6406 GAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLG---NRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlkNKTRILVTHGISYLPQVDVIIVMSGG 837
|
....*.
gi 701771264 6483 PARDDG 6488
Cdd:TIGR00957 838 KISEMG 843
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6293-6482 |
1.46e-17 |
|
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: 86.74 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQ---LDTADLRRDMTLLSQQA--RLFFGSIRDNLT 6367
Cdd:TIGR04521 26 LTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDLRKKVGLVFQFPehQLFEETVYKDIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGrPL---ASDEEIHR----ALALSGaLGFVQKQKNGLNyliteggagLSGGQR-------------QALLLartlilqp 6427
Cdd:TIGR04521 106 FG-PKnlgLSEEEAEErvkeALELVG-LDEEYLERSPFE---------LSGGQMrrvaiagvlamepEVLIL-------- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6428 qilllDEPTAWLDEISEQQLVANLASW--LGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:TIGR04521 167 -----DEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMEdVAEYADRVIVMHKG 219
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
967-1053 |
2.08e-17 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 80.80 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 967 THDITVSSTPPNVAFNAISQDNVLNAIEATQPLILSGTSNLPDGSHVTVTLNNVNYTAQVQG-GVWQVQVPVSDVVKLGD 1045
Cdd:NF033510 1 THPVTVDTTAPALTINPVAGDDVLNAAEQGQGLTLSGTTTAEAGQTVTVTLNGKTYTATVDAdGSWSVTVPAADLAALAD 80
|
....*...
gi 701771264 1046 TTYTLSVS 1053
Cdd:NF033510 81 GTYTVTVT 88
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6293-6482 |
2.24e-17 |
|
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: 84.79 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDT---ADLRRD--------------MTLLsqqa 6355
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarARLRARhvgfvfqsfqllptLTAL---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 rlffgsirDNLTMGRPLASDEEIH-RALALsgaLGFVqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:COG4181 109 --------ENVMLPLELAGRRDARaRARAL---LERV-----GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6435 PTAWLDEISEQQlVANLASWLgNR----TLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:COG4181 173 PTGNLDAATGEQ-IIDLLFEL-NRergtTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6288-6482 |
2.50e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD---LRRDMTLLSQQArlfFGSIRD 6364
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDS---ISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6365 NLTMGRPLA----------SDEEIHRALALSGALGFVQKQKNGLNyliteggAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:PRK10419 105 RKTVREIIReplrhllsldKAERLARASEMLRAVDLDDSVLDKRP-------PQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6435 PTAWLD---EISEQQLVANLASWLGNRTLVVaTHRipiLQLVD----RIIVLDNG 6482
Cdd:PRK10419 178 AVSNLDlvlQAGVIRLLKKLQQQFGTACLFI-THD---LRLVErfcqRVMVMDNG 228
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
5958-6224 |
2.52e-17 |
|
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: 85.77 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLW--VLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFAR 6035
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAlnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6036 ALRIKNSARPK-STGSFISQI-RELESVRELITSTtIGTVSDIPFFLLFVFILWLIGGP-LVFVVLLAIPLLLIPGLLVQ 6112
Cdd:pfam00664 84 ILRQPMSFFDTnSVGELLSRLtNDTSKIRDGLGEK-LGLLFQSLATIVGGIIVMFYYGWkLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6113 RPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVV 6192
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 701771264 6193 LLVGCYLVINGDMTTGALVGTSILASRTIAPL 6224
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4677-4776 |
4.39e-17 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 80.00 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4677 TVTVDSIT----TDSGFSNSDFITNDNTLTLNGSLGAplGSNEFVQISIDGGASWFYATSVNGTRWSYTDGRQLADGDHT 4752
Cdd:pfam19077 1 TLSIPTIDlaagSDTGVSDSDNITNDTTPTFTGTNED--GDVVTVTVSIDGNGVTGTATAGADGNWSFTPPAALADGTYT 78
|
90 100
....*....|....*....|....
gi 701771264 4753 WQVRVVDLAGNVGATTSQTVTVDT 4776
Cdd:pfam19077 79 LTVTVTDIAGNTATSSPLSFTIDT 102
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6293-6482 |
5.43e-17 |
|
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: 83.40 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGeKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQarlfFGsIRDNLTMGRPL 6372
Cdd:cd03264 21 LTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE----FG-VYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 A------------SDEEIHRALALSGaLGFVQKQKNGlnyliteggaGLSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:cd03264 94 DyiawlkgipskeVKARVDEVLELVN-LGDRAKKKIG----------SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 701771264 6441 eISEQQLVANLASWLG-NRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03264 163 -PEERIRFRNLLSELGeDRIVILSTHIVEdVESLCNQVAVLNKG 205
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
4249-5771 |
6.89e-17 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 89.83 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4249 QVTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGD 4328
Cdd:COG3210 2 SGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4329 AYVIHASVSNSIGNSAGVDRTITVDTTPPQMTITIDSLQNDTGLSASDFITADNKVVVKGSLSGALGNNEKAQISLDGGK 4408
Cdd:COG3210 82 GAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4409 TWTDLVVTGTSWAYADGpLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDTGLDAHDFITSDNT 4488
Cdd:COG3210 162 TNTNNSSSGTNIGNSIP-TTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4489 LTLSGKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSwsyvDGRQLADGDHLYQLRVVDDAGNIGSTASQLVTVDTVAPDA 4568
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTT----VTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4569 SKTVTIDSISTDTGLSNTDFVTSDTSLTVhGSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYFNDGRTLSDGTYQYLV 4648
Cdd:COG3210 317 AAGITTTNTVGGNGDGNNTTANSGAGLVS-GGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNAS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4649 RVVDDAGNVGQSASKNVTVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLNGSLGAPLGSNEFVQISIDGGASWF 4728
Cdd:COG3210 396 STTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4729 YATSVNGTRWSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGISDDTGQSASDFITMDTTLTL 4808
Cdd:COG3210 476 AGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4809 NGTLGHALASDERVQISLDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNVGSTANQVVTVDTVAPDTVGS 4888
Cdd:COG3210 556 TAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLT 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4889 IVSYTDNNGERTGNFDSSYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTFADSGLLDGSYHYVLRV 4968
Cdd:COG3210 636 GSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITV 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4969 TDKAGNYTESNDFGLTVDTSVPTTKALVNGLNTTDT----TPIITGSVDANLVHGEFVVVTVNGKTYTSDrggavVVDPA 5044
Cdd:COG3210 716 TGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSgnagTLSIGLTANTTASGTTLTLANANGNTSAGA-----TLDNA 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5045 SNTWYLQIPDADVLslksydVTAQVKSSAGNGNSVDVTHGTV---VVGAEASMTPAWAFTSATNAIAASFMLDANGMWTF 5121
Cdd:COG3210 791 GAEISIDITADGTI------TAAGTTAINVTGSGGTITINTAttgLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAG 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5122 ASNQQFATANDRNSYSVSGNFSMTGSYTTGAYADINRDGHADMLVESTNYSYITQLMNNGDGTYTSTSPGSSATVGALLW 5201
Cdd:COG3210 865 ANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTA 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5202 YGAVVSIDFQGDGYVDFVMGDAGGPDSSTFVNNNAGKLTGTSGGGTYTNFVSGSKVGNYNSVIETSGVDLNNDGMVDIAQ 5281
Cdd:COG3210 945 LSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTG 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5282 HTTNGGNIYALSTMFNKGDGTFTWSQNFINTMYSATGSAAANNAVSMTWADFDGDGYMDLYMGMSRAGTGGLLMMNDGKG 5361
Cdd:COG3210 1025 TTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATG 1104
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5362 NLLTGTAVGSEKYNGTVSVAVDWNMDGRMDIIKLANTGQSYMYTNDGLKGVASFTSSKFGSATTSQVSGAALVDYDWDGA 5441
Cdd:COG3210 1105 TSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGG 1184
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5442 QDLLIFRQNGSVTLERNTNAVAPGTAIHLKIVDSQGINVFFGNTVKLYNAAGELVASQVINAQSGIGINDASALVSFYGL 5521
Cdd:COG3210 1185 ADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGA 1264
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5522 NPNETYHAELVRAINGVSSNTTWNGLTAGDGRESYALTADAATGVHAGTLTGTGYNDTFIAEQGTYVYNGGGGWETSSDH 5601
Cdd:COG3210 1265 VSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTIN 1344
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5602 QTWSATGGMDVVDFrNSTVGVTVDLGKTGAQNTGFNTATFSNIEGIVGSSHDDVITGNSGNNTFEGGGGNDTFNIGSGGH 5681
Cdd:COG3210 1345 TTAANTGLNGGNGA-TDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVA 1423
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5682 DTLLYKLLNGSDATGGNGHDVVNGFSVGTWEGTADSDRIDLRELLQGSGYAGDASAHYVNGVAQLGAGAGNIGDYIKVVQ 5761
Cdd:COG3210 1424 GTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGG 1503
|
1530
....*....|
gi 701771264 5762 NGSSTEIQID 5771
Cdd:COG3210 1504 TSTGAGGTAG 1513
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
249-415 |
8.53e-17 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 81.80 E-value: 8.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 249 PSVLAAEAMRESSGYAVDKAKSGHWPTLSLRGGRTRYQSNNSAYWDD----QIQLNVDAPIYQGGAVSAQVEQAQGARRI 324
Cdd:pfam02321 8 PDLKAAEAEIEAAEANIKLAKSEFLPDLSLSGGYGYNSNNSESGGDDpgtgEVGLGLSQPLFDGGKRRARVKAAKAQVEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 325 AASQVEQAKFDVLQKASVAMADWNGARGRETAGALQLENARRAREVYKNEYKLSKRSLNDLLSIEQDVFQAAYAQINA-- 402
Cdd:pfam02321 88 AEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARLELLNAea 167
|
170
....*....|...
gi 701771264 403 DFDGWQAAILEVI 415
Cdd:pfam02321 168 DLELALAQLEQLL 180
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6288-6488 |
9.54e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL--GQLDTADLRRDMTLLSQQARLF------- 6358
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFphltale 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 ---FGSIRdnlTMGrplASDEEIHR-ALALSGALGFVQKqkngLNYLITEggagLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:PRK09493 97 nvmFGPLR---VRG---ASKEEAEKqARELLAKVGLAER----AHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6435 PTAWLD-EISEQQL--VANLASwlGNRTLVVATHRIPILQLV-DRIIVLDNGPARDDG 6488
Cdd:PRK09493 163 PTSALDpELRHEVLkvMQDLAE--EGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDG 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6284-6482 |
1.28e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.35 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 KVNDLDIA-RL-----TITAGEKIAVLGRNGSGKSTLLQLLAGMqTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR- 6356
Cdd:COG4138 2 QLNDVAVAgRLgpisaQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFGSIRDNLTMGRP-LASDEEIHRALA-LSGALGFVQKqkngLNYLITEggagLSGGQRQALLLAR-------TLILQP 6427
Cdd:COG4138 81 PFAMPVFQYLALHQPaGASSEAVEQLLAqLAEALGLEDK----LSRPLTQ----LSGGEWQRVRLAAvllqvwpTINPEG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6428 QILLLDEPTAWLDeISEQ----QLVANLASwLGnRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG4138 153 QLLLLDEPMNSLD-VAQQaaldRLLRELCQ-QG-ITVVMSSHDLNhTLRHADRVWLLKQG 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6285-6482 |
1.33e-16 |
|
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: 82.87 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL-RRDMTLLSQQARLFFG-SI 6362
Cdd:cd03219 16 LDDVS---FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6363 RDNLTMGRPLASDEEIHRALALSG----------ALGFVqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:cd03219 93 LENVMVAAQARTGSGLLLARARREereareraeeLLERV-----GLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6433 DEPTAWL-----DEISEqqLVANLASwlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03219 168 DEPAAGLnpeetEELAE--LIRELRE--RGITVLLVEHDMDvVMSLADRVTVLDQG 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6288-6482 |
1.83e-16 |
|
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: 81.69 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLD---TADLRRDMTLLSQQARLFFG-SIR 6363
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDFRLLPDrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTMgrPLASDEEIHRALA--LSGALGFVqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDE 6441
Cdd:cd03292 97 ENVAF--ALEVTGVPPREIRkrVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6442 ISEQQlVANLASWLGNR--TLVVATHRipiLQLVD----RIIVLDNG 6482
Cdd:cd03292 170 DTTWE-IMNLLKKINKAgtTVVVATHA---KELVDttrhRVIALERG 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6059-6484 |
1.86e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6059 ESVRELITST---TIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIP---------------GLLVQRPLAHLSN 6120
Cdd:COG4178 132 EDIRLFTETTlslSLGLLSSVVTLISFIGILWSLSGSLTFTLGGYSITIPGYmvwaaliyaiigtllTHLIGRPLIRLNF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6121 EG-MRESAIRnATLVEAVQSIEDIKLLRAE--------QRFQNQWNNTNDVAAgvgmKQRWLTSllmtWTQEVQSIVYAV 6191
Cdd:COG4178 212 EQqRREADFR-FALVRVRENAESIALYRGEaaerrrlrRRFDAVIANWRRLIR----RQRNLTF----FTTGYGQLAVIF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6192 VLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQIS---GVLSRWQqAKVAR-KGLDDLMQRpLDDPEEGKKVHKAHLQ 6267
Cdd:COG4178 283 PILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVdnyQSLAEWR-ATVDRlAGFEEALEA-ADALPEAASRIETSED 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6268 GNYQLNYAAFY-YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILL-DGislgqldtadlr 6345
Cdd:COG4178 361 GALALEDLTLRtPDGRPLLEDLS---LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAG------------ 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6346 RDMTLLSQQARLFFGSIRDNLTmgRPLA----SDEEIHRALalsgalgfvqkQKNGLNYLI----TEG--GAGLSGGQRQ 6415
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALL--YPATaeafSDAELREAL-----------EAVGLGHLAerldEEAdwDQVLSLGEQQ 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6416 ALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPA 6484
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGS 561
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6279-6482 |
2.36e-16 |
|
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: 81.90 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAdlRRDMTLLSQQARLF 6358
Cdd:cd03300 10 YGGFVALDGVS---LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 -----FGSIRDNLTM-GRPLAS-DEEIHRALALSGALGFVQKQKnglnyliteggAGLSGGQRQALLLARTLILQPQILL 6431
Cdd:cd03300 85 phltvFENIAFGLRLkKLPKAEiKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6432 LDEPTAWLDEISEQQL---VANLASWLGNrTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:cd03300 154 LDEPLGALDLKLRKDMqleLKRLQKELGI-TFVFVTHdQEEALTMSDRIAVMNKG 207
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
6278-6467 |
2.48e-16 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 80.93 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIArltITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL--GQLDTADLRRDMTLLSQQA 6355
Cdd:TIGR01166 1 YPGGPEVLKGLNFA---AERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 --RLFFGSIRDNLTMGrPL---ASDEEIHR----ALALSGALGFVQKQKNGLnyliteggaglSGGQRQALLLARTLILQ 6426
Cdd:TIGR01166 78 ddQLFAADVDQDVAFG-PLnlgLSEAEVERrvreALTAVGASGLRERPTHCL-----------SGGEKKRVAIAGAVAMR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701771264 6427 PQILLLDEPTAWLDEISEQQLVANLASWL-GNRTLVVATHRI 6467
Cdd:TIGR01166 146 PDVLLLDEPTAGLDPAGREQMLAILRRLRaEGMTVVISTHDV 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6271-6484 |
2.58e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAafYYDEEEKVNDLDIarlTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG--ISLGQLDTADLRRDM 6348
Cdd:PRK13636 10 ELNYN--YSDGTHALKGINI---NIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6349 TLLSQQA--RLFFGSIRDN-----LTMGRPlasDEEIHRalALSGALgfvqkQKNGLNYLITEGGAGLSGGQRQALLLAR 6421
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDvsfgaVNLKLP---EDEVRK--RVDNAL-----KRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6422 TLILQPQILLLDEPTAWLDE--ISE-QQLVANLASWLGnRTLVVATHRIPILQL-VDRIIVLDNGPA 6484
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPmgVSEiMKLLVEMQKELG-LTIIIATHDIDIVPLyCDNVFVMKEGRV 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6279-6486 |
3.69e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILL-DGISLGQLD--TADLRRDMTLLsqqa 6355
Cdd:COG0488 325 YGDKTLLDDLS---LRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDqhQEELDPDKTVL---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 rlffgsirDNLTMGRPLASDEEIHRALalsGALGF----VQKQknglnyliteggAG-LSGGQRQALLLARTLILQPQIL 6430
Cdd:COG0488 398 --------DELRDGAPGGTEQEVRGYL---GRFLFsgddAFKP------------VGvLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6431 LLDEPTAWLDEISEQQLVANLASWLGnrTLVVATH-RIPILQLVDRIIVLDNGPARD 6486
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDFPG--TVLLVSHdRYFLDRVATRILEFEDGGVRE 509
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
6266-6482 |
5.42e-16 |
|
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: 83.61 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6266 LQGNYQLNYAAFyydeeekvnDLDiARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLgqLDTA--- 6342
Cdd:COG4148 3 LEVDFRLRRGGF---------TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSArgi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6343 DL---RRDMTLLSQQARLF-FGSIRDNLTMGRPLASDEEihRALALSGALGFVqkqknGLNYLITEGGAGLSGGQRQ--- 6415
Cdd:COG4148 71 FLpphRRRIGYVFQEARLFpHLSVRGNLLYGRKRAPRAE--RRISFDEVVELL-----GIGHLLDRRPATLSGGERQrva 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6416 ---------ALLLArtlilqpqilllDEPTAWLDEISEQQL---VANLASWLGNRTLVVaTHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG4148 144 igrallsspRLLLM------------DEPLAALDLARKAEIlpyLERLRDELDIPILYV-SHSLDeVARLADHVVLLEQG 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6293-6482 |
6.88e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.89 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLG-QLDTADlrRDMTLLSQQARLF-FGSIRDN----L 6366
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE--RRVGFVFQHYALFpHMTVAENiafgL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6367 TMGRPlaSDEEIH-RALALsgaLGFVQkqkngLnylitEGGAG-----LSGGQRQ-------------ALLLartlilqp 6427
Cdd:COG1118 101 RVRPP--SKAEIRaRVEEL---LELVQ-----L-----EGLADrypsqLSGGQRQrvalaralavepeVLLL-------- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6428 qilllDEPTAWLDEiseqQLVANLASWLG------NRTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:COG1118 158 -----DEPFGALDA----KVRKELRRWLRrlhdelGGTTVFVTHdQEEALELADRVVVMNQG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6279-6482 |
7.18e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQldTADLRRDMTLLSQQARLF 6358
Cdd:PRK11607 29 FDGQHAVDDVS---LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 ----------FGSIRDNLTMGRPLASDEEIhraLALSGALGFVQKQKNglnyliteggaGLSGGQRQALLLARTLILQPQ 6428
Cdd:PRK11607 104 phmtveqniaFGLKQDKLPKAEIASRVNEM---LGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6429 ILLLDEPTAWLDEI--SEQQL-VANLASWLGnRTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:PRK11607 170 LLLLDEPMGALDKKlrDRMQLeVVDILERVG-VTCVMVTHdQEEAMTMAGRIAIMNRG 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6293-6489 |
7.52e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDT-ADLRRDMTLLSQQARL-FFG-SIRDNLTMG 6369
Cdd:PRK13644 23 LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETqFVGrTVEEDLAFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 ------RPLASDEEIHRALAlsgalgfvqkqKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEIS 6443
Cdd:PRK13644 103 penlclPPIEIRKRVDRALA-----------EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6444 EQQLVANLASW-LGNRTLVVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:PRK13644 172 GIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
6293-6479 |
9.32e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQIlldgislgqldTADLRRDMTLLSQQARL---FFGSIRDNLTMG 6369
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVpdsLPLTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 ---------RPLASDE-EIHRALALSGALGFVQKQKnglnyliteggAGLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:NF040873 82 rwarrglwrRLTRDDRaAVDDALERVGLADLAGRQL-----------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 701771264 6440 DEISEQQLVANLASWLG-NRTLVVATHRIPILQLVDRIIVL 6479
Cdd:NF040873 151 DAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| biofilm_BapA_N |
NF033677 |
BapA prefix-like domain; Two largely unrelated repetitive proteins, both named ... |
414-476 |
1.57e-15 |
|
BapA prefix-like domain; Two largely unrelated repetitive proteins, both named biofilm-associated protein BapA (from Salmonella enterica and from Paracoccus denitrificans) share homology domains at the two ends. Both lack a typical signal peptide for translocation by Sec, and instead depend on type I secretion for export and for contribution to biofilm formation. The conserved prefix (i.e. N-terminal) domain is shared by a number of other large, repetitive proteins of Proteobacteria thought to be associated with adhesion or biofilm formation.
Pssm-ID: 411274 [Multi-domain] Cd Length: 64 Bit Score: 74.13 E-value: 1.57e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 414 VISRKDAEKTLVTGDGNlsVALSSPSVIQIHGSAKDVAHYVRQGNDLLVYMKDGSVIRCNGYF 476
Cdd:NF033677 3 VISKETGVVLTQTQGEV--VLLNEPSVVKIKVSREDVASYTRQGNDLVITLKDGETIVIENFF 63
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
6288-6484 |
1.57e-15 |
|
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: 79.43 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislGQLDTADLRRdMTLLSQQARLFFGSIRDNLT 6367
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEPGPDR-MVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MG----RPLASDEE----IHRALALSGaLGFVQKQKNGlnyliteggaGLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:TIGR01184 77 LAvdrvLPDLSKSErraiVEEHIALVG-LTEAADKRPG----------QLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6440 DEISEQQLVANLAS-WLGNR-TLVVATHRI-PILQLVDRIIVLDNGPA 6484
Cdd:TIGR01184 146 DALTRGNLQEELMQiWEEHRvTVLMVTHDVdEALLLSDRVVMLTNGPA 193
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6277-6489 |
1.71e-15 |
|
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: 80.17 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEK--VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGIslgqlDTAD------LRRDM 6348
Cdd:TIGR04520 8 FSYPESEKpaLKNVS---LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL-----DTLDeenlweIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6349 TLLSQ----QarlFFGSI-RD-------NLTMGRplasdEEIHR----ALALSGALGFVQKQKnglnyliteggAGLSGG 6412
Cdd:TIGR04520 80 GMVFQnpdnQ---FVGATvEDdvafgleNLGVPR-----EEMRKrvdeALKLVGMEDFRDREP-----------HLLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6413 QRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASwL---GNRTLVVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRK-LnkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6285-6482 |
1.77e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 80.08 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRR--------------DMT- 6349
Cdd:COG0411 20 VDDVS---LEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARlgiartfqnprlfpELTv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6350 ----LLSQQARLFFGSIRDNLTMGRPLASDEEIH-RALALsgaLGFVqkqknGLNYLITEGGAGLSGGQRQALLLARTli 6424
Cdd:COG0411 97 lenvLVAAHARLGRGLLAALLRLPRARREEREAReRAEEL---LERV-----GLADRADEPAGNLSYGQQRRLEIARAla 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6425 lqpqilllDEPTAWL--DEISE-QQLVANLASWLGnRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG0411 169 tepkllllDEPAAGLnpEETEElAELIRRLRDERG-ITILLIEHDMDlVMGLADRIVVLDFG 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6278-6482 |
2.29e-15 |
|
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: 79.26 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL-RRDMTLLSQQAR 6356
Cdd:COG0410 12 GYGGIHVLHGVS---LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFG-SIRDNLTMGRPLASDEE-----IHRALALSGALGFVQKQKnglnyliteggAG-LSGGQRQALLLARtlilqpqi 6429
Cdd:COG0410 89 IFPSlTVEENLLLGAYARRDRAevradLERVYELFPRLKERRRQR-----------AGtLSGGEQQMLAIGR-------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6430 llldeptAW--------LDEISE---QQLVANLASWLG--NRT----LVV---ATHripILQLVDRIIVLDNG 6482
Cdd:COG0410 150 -------ALmsrpklllLDEPSLglaPLIVEEIFEIIRrlNREgvtiLLVeqnARF---ALEIADRAYVLERG 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6279-6488 |
2.80e-15 |
|
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: 78.03 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAdLRRDMTLLSQQArlF 6358
Cdd:cd03268 10 YGKKRVLDDIS---LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-LRRIGALIEAPG--F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG--SIRDNLTMGRPLA--SDEEIHRALALSGaLGFVQKQKNGlnyliteggaGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:cd03268 84 YPnlTARENLRLLARLLgiRKKRIDEVLDVVG-LKDSAKKKVK----------GFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6435 PTAWLDE--ISE-QQLVANLASWlgNRTLVVATHRI-PILQLVDRIIVLDNGPARDDG 6488
Cdd:cd03268 153 PTNGLDPdgIKElRELILSLRDQ--GITVLISSHLLsEIQKVADRIGIINKGKLIEEG 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6293-6469 |
5.02e-15 |
|
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: 77.01 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLdTADLRRDMTLLSQQ----ARLffgSIRDNLTM 6368
Cdd:TIGR01189 21 FTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLGHLpglkPEL---SALENLHF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6369 GRPLASDEE--IHRALALSGALGFVQKQknglnylitegGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQ 6446
Cdd:TIGR01189 97 WAAIHGGAQrtIEDALAAVGLTGFEDLP-----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|...
gi 701771264 6447 LVANLASWLGNRTLVVATHRIPI 6469
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTHQDL 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6327-6485 |
6.52e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6327 GQILLDGISLGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLITEGG 6406
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6407 AGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASW--LGNRTLVVATHRIPILQLVDRIIVLDNgPA 6484
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNN-PD 1435
|
.
gi 701771264 6485 R 6485
Cdd:PTZ00265 1436 R 1436
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6293-6459 |
6.63e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFG-SIRDNLTMGR- 6370
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVARGRy 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 ---PLASDEEIHRALALSGALgfvqkQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDeISEQQL 6447
Cdd:PRK10253 108 phqPLFTRWRKEDEEAVTKAM-----QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD-ISHQID 181
|
170
....*....|..
gi 701771264 6448 VANLASWLgNRT 6459
Cdd:PRK10253 182 LLELLSEL-NRE 192
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6279-6482 |
9.47e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 79.76 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGIslgqlDTADL---RRDMTLLSQQA 6355
Cdd:COG3842 15 YGDVTALDDVS---LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-----DVTGLppeKRNVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLF-FGSIRDN----LTMGRplASDEEIHR----ALALSGALGFVQKqknglnyLITEggagLSGGQRQ----------- 6415
Cdd:COG3842 87 ALFpHLTVAENvafgLRMRG--VPKAEIRArvaeLLELVGLEGLADR-------YPHQ----LSGGQQQrvalaralape 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6416 --ALLLartlilqpqilllDEPTAWLDeiseQQLVANLASWLGNR------TLVVATHRipilQ-----LVDRIIVLDNG 6482
Cdd:COG3842 154 prVLLL-------------DEPLSALD----AKLREEMREELRRLqrelgiTFIYVTHD----QeealaLADRIAVMNDG 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6288-6482 |
1.50e-14 |
|
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: 77.54 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD---LRRDMTLLSQQArlfFGSIRD 6364
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDS---PSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6365 NLT----MGRPL------ASDEEIHRALALSGALGFVQKQKNGLNyliteggAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:TIGR02769 104 RMTvrqiIGEPLrhltslDESEQKARIAELLDMVGLRSEDADKLP-------RQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6435 PTAWLD---EISEQQLVANLASWLGNRTLVVaTHRIPILQ-LVDRIIVLDNG 6482
Cdd:TIGR02769 177 AVSNLDmvlQAVILELLRKLQQAFGTAYLFI-THDLRLVQsFCQRVAVMDKG 227
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
581-1717 |
1.54e-14 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 81.74 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 581 TFMVTDNKGDSQGLLSSNAVTDDSTPTFSGSGQPGATIQVKDANGNTIASTMVDSNGNWKVLLSEQPDGTHTYSVVQIDG 660
Cdd:COG3210 497 ATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGT 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 661 NKITSAGEITLNVVTAQASLTAATTAGDNTLNAAEQANDFVISGSATELASGTALTVTLNGKTYATTVGSDGSWSVTVPA 740
Cdd:COG3210 577 SNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASA 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 741 ADAKSLADGSWTVTVSGKDAAGNNISASETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVTLKLNG 820
Cdd:COG3210 657 NGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANGDTVTFGNLG 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 821 KTYTATVGADGGWSMEVPAADVQAMADNSYT--LNLSVSDKAGNTTT----TNASLLVDTTPPEASVNTVAGDDILSVSE 894
Cdd:COG3210 737 TGATLTLNAGVTITSGNAGTLSIGLTANTTAsgTTLTLANANGNTSAgatlDNAGAEISIDITADGTITAAGTTAINVTG 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 895 QGQAQIISGTSQGAAPGDKVTVSIGSETYQTTVQADGSWSVGVPKEVISSLPEGPNTITVAITDVAGNTGTTTHDITVSS 974
Cdd:COG3210 817 SGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTL 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 975 TPPNVAFNAISQDNVLNAIEATQPLILSGTSNLPDGSHVTVTLNNVNYTAQVQGGVWQVQVPVSDVVKLGDTTYTLSVSG 1054
Cdd:COG3210 897 TNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSA 976
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1055 TDTTGNTGTATATLQVDTALPTVIVSTFAGDNRVNNSEIANDQMLSGRVTGAHQGDTVTINIGGKNYTATVQSDLTWSTT 1134
Cdd:COG3210 977 VGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGG 1056
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1135 VPAADLRALGDGDVSIVASVTNAHGNTGSGSRDININAQLPGLRINTVSGDDVINAIEQHQDLTVTGTSTHLSAGTIITV 1214
Cdd:COG3210 1057 NAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTAS 1136
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1215 RINGVDYQAAVSATGSWQIGIPAADVAGWPNGKLEMVASSADESGNPVAATRPVDVDLNAVAISINSVTSDGVLNAVEKA 1294
Cdd:COG3210 1137 TEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNV 1216
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1295 ------ADLTLSGKTLGVEAGQTVVIKFAGHTYTTTVNQSGDWTFTVPAADMRDMIDGRADVSVSVTNVSGNGASGAREV 1368
Cdd:COG3210 1217 tttttlTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSA 1296
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1369 LVDTQPPSITLNSITADNILNHAEAAQELVITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVADLANLTDGSWS 1448
Cdd:COG3210 1297 GGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAA 1376
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1449 VSASVSDVAGNPASTSHGMLVDTTAPVVTINTFAGDNIVNRSEHAQAQVLSGKATGAAVGDSVKITVNGVEYSTVLDASG 1528
Cdd:COG3210 1377 TAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADAS 1456
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1529 NWSLGLPAEVISGLADGKYTATVVVTDKAGNVGGSSLAFDVATGLPQITINAIAQDDVINAAEKSAEVTVSGTSNQPDGT 1608
Cdd:COG3210 1457 AINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSV 1536
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1609 QITVNLNGVDYAAVVNGNAWSVKIPAPDVAKLGEASYTVSASVTDASGNANSASHSVLVDSSLPIITINAVAGDNIINLA 1688
Cdd:COG3210 1537 AEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVT 1616
|
1130 1140
....*....|....*....|....*....
gi 701771264 1689 EVNAGQVLTGSVINAAAGDEVTVILGGKS 1717
Cdd:COG3210 1617 SGTAGNAGATGANSNTVVTTNGGEGVLAL 1645
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6278-6482 |
1.84e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 76.57 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLG--QLDTADLRRDMTLLSQQA 6355
Cdd:COG1126 10 SFGDLEVLKGIS---LDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLF-FGSIRDNLTMG----RPLASDEEIHRALALSGALGFVQKQKNglnYlitegGAGLSGGQRQ------AL-----LL 6419
Cdd:COG1126 87 NLFpHLTVLENVTLApikvKKMSKAEAEERAMELLERVGLADKADA---Y-----PAQLSGGQQQrvaiarALamepkVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6420 artlilqpqilLLDEPTAWLD-E-ISE-QQLVANLASwlGNRTLVVATH-----RipilQLVDRIIVLDNG 6482
Cdd:COG1126 159 -----------LFDEPTSALDpElVGEvLDVMRDLAK--EGMTMVVVTHemgfaR----EVADRVVFMDGG 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6293-6485 |
2.56e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.82 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGIslgQLDTADLRR-----DMTLLSQQarlffgSIRDNLT 6367
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADRgvvfqKDALLPWL------NVLDNVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 M-----GRPLASDEEI-HRALALSGALGFVQKQknglnylITEggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDE 6441
Cdd:COG4525 99 FglrlrGVPKAERRARaEELLALVGLADFARRR-------IWQ----LSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 701771264 6442 ISE---QQLVANLasW-LGNRTLVVATHRI-PILQLVDRIIVLDNGPAR 6485
Cdd:COG4525 168 LTReqmQELLLDV--WqRTGKGVFLITHSVeEALFLATRLVVMSPGPGR 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6293-6482 |
2.57e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqldtaDLRrdMTLLSQQARLF-FGSIRDNLTMG-- 6369
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQEPPLDdDLTVLDTVLDGda 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 --------------RPLASDEEIHRALALSG-------------------ALGFVQKQkngLNYLITEggagLSGGQR-- 6414
Cdd:COG0488 88 elraleaeleeleaKLAEPDEDLERLAELQEefealggweaearaeeilsGLGFPEED---LDRPVSE----LSGGWRrr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6415 ----QAL-------LLartlilqpqilllDEPTAWLDEISeqqlVANLASWLGNR--TLVVATH-RIPILQLVDRIIVLD 6480
Cdd:COG0488 161 valaRALlsepdllLL-------------DEPTNHLDLES----IEWLEEFLKNYpgTVLVVSHdRYFLDRVATRILELD 223
|
..
gi 701771264 6481 NG 6482
Cdd:COG0488 224 RG 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6288-6482 |
3.06e-14 |
|
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: 74.00 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqldtadlrrdmtllsQQARlfFGSIRDNLT 6367
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------------------KEVS--FASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGrplasdeeihralalsgaLGFV-QkqknglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQ 6446
Cdd:cd03216 75 AG------------------IAMVyQ----------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 701771264 6447 L---VANLASwlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03216 121 LfkvIRRLRA--QGVAVIFISHRLDeVFEIADRVTVLRDG 158
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6276-6482 |
3.10e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.57 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6276 AFYYDEEEKvNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQ-- 6353
Cdd:PRK13632 14 SFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQnp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 --QarlFFGS-IRDNLTMG--RPLASDEEIHRALAlsgalgFVQKQKNGLNYLITEgGAGLSGGQRQALLLARTLILQPQ 6428
Cdd:PRK13632 93 dnQ---FIGAtVEDDIAFGleNKKVPPKKMKDIID------DLAKKVGMEDYLDKE-PQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6429 ILLLDEPTAWLD-----EIseQQLVANLASwLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK13632 163 IIIFDESTSMLDpkgkrEI--KKIMVDLRK-TRKKTLISITHDMDEAILADKVIVFSEG 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6295-6476 |
3.16e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.62 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDT---ADLR-RDMTLLSQQARLF--FGSIrDNLTM 6368
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRnQKLGFIYQFHHLLpdFTAL-ENVAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6369 grPL-----ASDEEIHRALALSGALGFVQKQKNglnyliteGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEIS 6443
Cdd:PRK11629 111 --PLligkkKPAEINSRALEMLAAVGLEHRANH--------RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 701771264 6444 EQ---QLVANLASWLGNRTLVVaTHRipiLQLVDRI 6476
Cdd:PRK11629 181 ADsifQLLGELNRLQGTAFLVV-THD---LQLAKRM 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6278-6488 |
3.30e-14 |
|
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: 75.48 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQARL 6357
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 F-FGSIRDNLT-MGR--PLASDEEIHRALALSGALGFvqkqknglNYLITEGGAGLSGGQRQALLLARTLILQPQILLLD 6433
Cdd:cd03266 90 YdRLTARENLEyFAGlyGLKGDELTARLEELADRLGM--------EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6434 EPTAWLDEISEQQL---VANLASwlGNRTLVVATHRI-PILQLVDRIIVLDNGPARDDG 6488
Cdd:cd03266 162 EPTTGLDVMATRALrefIRQLRA--LGKCILFSTHIMqEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6277-6488 |
3.74e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.59 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEK--VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQ 6354
Cdd:PRK13635 13 FRYPDAATyaLKDVS---FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 A-RLFFGS-IRDNLTMG---RPLASDEEIHR---ALALSGALGFVQKQKnglnyliteggAGLSGGQRQALLLARTLILQ 6426
Cdd:PRK13635 90 PdNQFVGAtVQDDVAFGlenIGVPREEMVERvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6427 PQILLLDEPTAWLDEISEQQLVANLASWL--GNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
755-844 |
4.15e-14 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 71.75 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 755 VSGKDAAGNNISASE--TLVVDTQAP-SLTLDILAGDNIINAAE-HNAAVTVSGKT--DAEAGQVVTLKLNGKTYTATVG 828
Cdd:NF012196 1 VTSHDAAGNTATATAhhTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVggDVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|
gi 701771264 829 ADG----GWSMEVPAADVQA 844
Cdd:NF012196 81 DLGngqlGYSVDVDTSDLLN 100
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6279-6482 |
4.20e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.81 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARLF 6358
Cdd:COG3839 13 YGGVEALKDID---LDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 -FGSIRDNltMGRPL----ASDEEIHRA-------LALSGALGfvQKQKNglnyliteggagLSGGQRQ----------- 6415
Cdd:COG3839 88 pHMTVYEN--IAFPLklrkVPKAEIDRRvreaaelLGLEDLLD--RKPKQ------------LSGGQRQrvalgralvre 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6416 --ALLLartlilqpqilllDEPTAWLD---------EISE--QQLvanlaswlgNRTLVVATH-RIPILQLVDRIIVLDN 6481
Cdd:COG3839 152 pkVFLL-------------DEPLSNLDaklrvemraEIKRlhRRL---------GTTTIYVTHdQVEAMTLADRIAVMND 209
|
.
gi 701771264 6482 G 6482
Cdd:COG3839 210 G 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6277-6482 |
4.98e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.31 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVndLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQA- 6355
Cdd:PRK13647 12 FRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 -RLFFGSIRDNLTMG------RPLASDEEIHRALALSGALGFVQKQKNGLNYliteggaglsgGQRQALLLARTLILQPQ 6428
Cdd:PRK13647 90 dQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYHLSY-----------GQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6429 ILLLDEPTAWLDEISEQQLVANLASwLGNR--TLVVATHRIPI-LQLVDRIIVLDNG 6482
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDR-LHNQgkTVIVATHDVDLaAEWADQVIVLKEG 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5993-6488 |
5.12e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5993 WVLFGGVMLAILFE--FTMRMLRVhiadvvGKRADLRISDRVFARALRIKNSARPK-STGSFISQIRELESVRELITSTT 6069
Cdd:PLN03232 345 FLIFFGVTFGVLCEsqYFQNVGRV------GFRLRSTLVAAIFHKSLRLTHEARKNfASGKVTNMITTDANALQQIAEQL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6070 IGTVSdIPFFLLFVFILWL--IGGPLVFVVLLAIPLLLIPGLLVQRpLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLR 6147
Cdd:PLN03232 419 HGLWS-APFRIIVSMVLLYqqLGVASLFGSLILFLLIPLQTLIVRK-MRKLTKEGLQWTDKRVGIINEILASMDTVKCYA 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6148 AEQRFQNQWNNT-NDvaagvgmKQRWLTS--LLMTWTQEVQSIVYAVVLLV--GCYLVINGDMTTGALVGTSILASRTIA 6222
Cdd:PLN03232 497 WEKSFESRIQGIrNE-------ELSWFRKaqLLSAFNSFILNSIPVVVTLVsfGVFVLLGGDLTPARAFTSLSLFAVLRS 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6223 PLAQISGVLSRWQQAKVARKGLDDLM---QRPL-DDPEEGKKVHKAHLQGNYqlnyaaFYYDEEEKVNDLDIARLTITAG 6298
Cdd:PLN03232 570 PLNMLPNLLSQVVNANVSLQRIEELLlseERILaQNPPLQPGAPAISIKNGY------FSWDSKTSKPTLSDINLEIPVG 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6299 EKIAVLGRNGSGKSTLLQLLAGMQTPqhgqilldgislGQLDTADLRRDMTLLSQQARLFFGSIRDNLTMGRPLASdEEI 6378
Cdd:PLN03232 644 SLVAIVGGTGEGKTSLISAMLGELSH------------AETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFES-ERY 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6379 HRALALSgALgfvqkqKNGLNYL-------ITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD-EISEQQLVAN 6450
Cdd:PLN03232 711 WRAIDVT-AL------QHDLDLLpgrdlteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDaHVAHQVFDSC 783
|
490 500 510
....*....|....*....|....*....|....*...
gi 701771264 6451 LASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:PLN03232 784 MKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG 821
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6288-6482 |
5.13e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.24 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLG--QLDTADLRRDMTLLSQ--QARLFFGSIR 6363
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTMG-RPLA-SDEEIH----RALALSGALGFVQKQKNGLNyliteggagLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:PRK13637 103 KDIAFGpINLGlSEEEIEnrvkRAMNIVGLDYEDYKDKSPFE---------LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6438 WLD-----EISEQqlVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK13637 174 GLDpkgrdEILNK--IKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
428-963 |
5.59e-14 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 79.31 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 428 DGNL-SVALSSPSVIQIHGSAKDVAHYVRQGNDLLVYMKDGSVIRCNGYFmeEEGRPGHHSeLVF--DDGK-ALTHitFD 503
Cdd:NF040520 17 DGQLkKVVLNQPSIIQIGVNQKDIKSIEKQGNDLVITLKNGEKIVLENFF--NEANTTEHS-LAFptEDGKfVEAQ--FD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 504 EAGAAVGTQG---------TELTAIAVPIESIE---PFMDGSLLgdmpwgwvagavagGVGIGALLAHG---------GD 562
Cdd:NF040520 92 DSGKFIRYTGlthltqlayTETPTQAATMAAVDddpGISKSQLL--------------KAGLAALAAEGlylwavkddDK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 563 KSHTEVIDNTKPvesARPTfmvtdnkgdsqgllssnAVTDDSTPTFSGSGQPGATIQVKDANGNTIASTMVDSNGNWKVL 642
Cdd:NF040520 158 DDSNGPVDITPP---ATPT-----------------ATLADDTQTITGKAEANAKIYIKDATGKVIATGQADASGNYTIK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 643 LSEQPDGTHTYSVVQID-GNKITSAGEITLNVVT-AQASLTAATTAGDNTLNAAEQANDFVisgsATELASGTAL-TVTL 719
Cdd:NF040520 218 LDQPLVNGNKVNVTAIDaAGNASKATVVTGTKDTiAPDAPQAQLNADGTIVTGKTEANAKV----SVYDADGKLLgTVTA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 720 NgktyattvgSDGSWSV------------TVPAADA---KS-----------LADGSWTVTVSG---------------- 757
Cdd:NF040520 294 N---------KEGLYSIkvsppltsdkggTVIAEDAagnKSepskiiagkdtIAPDQPLVEVNKegtsiegraeanakvq 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 758 -KDAAGNNISaseTLVVDTQ-------APSLT-------------------LDILAGDNIIN----AAEHNAA-VTVSGK 805
Cdd:NF040520 365 iKDADGKVIG---TGTADAQgkfqitlSPALKtsqkgtiivedaagnqskpLEITAGKDTIApdkpTAQINAAgTSVTGT 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 806 tdAEAGQVVTLK-LNGKT-YTATVGADGGWSMEVPAadvqAMADNSYTlNLSVSDKAGN-TTTTNASLLVDTTPPEASVN 882
Cdd:NF040520 442 --AEANAKIEIKdSAGKViGTGTADADGKFTITISP----ALTDKNIG-KVYAIDAAGNrSDATDVTGTKDTIAPNKPVL 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 883 TVAGDDILSVSEQGQAqiiSGTSQGAAPgdKVTVSIGSETYQT-----------TVQADGSWSVGVPKEvissLPEGPNT 951
Cdd:NF040520 515 QKVTDDVGAVKGAIAA---GGETDDAKP--KLSGSGEAKATLTiydngqaigtvTVGDNGKWSFTLDKD----LALGKHK 585
|
650
....*....|..
gi 701771264 952 ITVAITDVAGNT 963
Cdd:NF040520 586 ITLTQTDAAGNT 597
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6285-6482 |
5.83e-14 |
|
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: 75.76 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL----RRDMTLLSQQARLF-F 6359
Cdd:cd03294 40 VNDVS---LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6360 GSIRDNLTMGRPLA--SDEEIHR----ALALSGALGFVQKqknglnyLITEggagLSGGQRQALLLARTLILQPQILLLD 6433
Cdd:cd03294 117 RTVLENVAFGLEVQgvPRAEREEraaeALELVGLEGWEHK-------YPDE----LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6434 EPTAWLD-----EISEQ--QLVANLaswlgNRTLVVATHR-IPILQLVDRIIVLDNG 6482
Cdd:cd03294 186 EAFSALDplirrEMQDEllRLQAEL-----QKTIVFITHDlDEALRLGDRIAIMKDG 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6288-6482 |
7.82e-14 |
|
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: 72.10 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDgislgqldtadlrrdmtllsqqarlffgsirDNLT 6367
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------------------STVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRplasdeeihralalsgalgFVQkqknglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQL 6447
Cdd:cd03221 65 IGY-------------------FEQ----------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*.
gi 701771264 6448 VANLASWlgNRTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:cd03221 110 EEALKEY--PGTVILVSHdRYFLDQVATKIIELEDG 143
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6294-6465 |
7.87e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.75 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislGQLDTADLRRDMTLLSQQ----ARLffgSIRDNLTMG 6369
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHRnamkPAL---TVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 RPL--ASDEEIHRALAlsgalgFVqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDeISEQQL 6447
Cdd:PRK13539 98 AAFlgGEELDIAAALE------AV-----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVAL 165
|
170 180
....*....|....*....|
gi 701771264 6448 VANL-ASWL-GNRTLVVATH 6465
Cdd:PRK13539 166 FAELiRAHLaQGGIVIAATH 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6279-6482 |
7.94e-14 |
|
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: 74.21 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARLF 6358
Cdd:cd03301 10 FGNVTALDDLN---LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 -FGSIRDNLTMG------RPLASDEEIHRA---LALSGALGFVQKQknglnyliteggagLSGGQRQALLLARTLILQPQ 6428
Cdd:cd03301 85 pHMTVYDNIAFGlklrkvPKDEIDERVREVaelLQIEHLLDRKPKQ--------------LSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6429 ILLLDEPTAWLDEISEQQLVANLASW---LGnRTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLqqrLG-TTTIYVTHdQVEAMTMADRIAVMNDG 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
6298-6482 |
1.31e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTP---QHGQILLDGISLGqldtadlRRDMTLLS---QQARLFFGSI--RDNLT-- 6367
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID-------AKEMRAISayvQQDDLFIPTLtvREHLMfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 ----MGRPLASDEEIHRALALSGALGFVQKQknglNYLITEGGA--GLSGGQRQALLLARTLILQPQILLLDEPTAWLDE 6441
Cdd:TIGR00955 124 ahlrMPRRVTKKEKRERVDEVLQALGLRKCA----NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 701771264 6442 ISEQQLVANLASWLGNRTLVVATHRIP---ILQLVDRIIVLDNG 6482
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPsseLFELFDKIILMAEG 243
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
6303-6488 |
1.32e-13 |
|
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: 75.99 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6303 VLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLdtADLRRDMTLLSQQARLF-FGSIRDNLTMG---RPLASDEEI 6378
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV--PPHLRHINMVFQSYALFpHMTVEENVAFGlkmRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6379 HRALAlsgALGFVQKQKNGLNYLITeggagLSGGQRQALLLARTLILQPQILLLDEPTAWLD----EISEQQLVAnLASW 6454
Cdd:TIGR01187 79 PRVLE---ALRLVQLEEFADRKPHQ-----LSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKT-IQEQ 149
|
170 180 190
....*....|....*....|....*....|....*
gi 701771264 6455 LGnRTLVVATH-RIPILQLVDRIIVLDNGPARDDG 6488
Cdd:TIGR01187 150 LG-ITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIG 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6293-6445 |
1.34e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFG-SIRDNLTMGR- 6370
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGmTVRELVAIGRy 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 P---------LASDEEIHRALALSGALGFVQKqknglnyLITEggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDe 6441
Cdd:PRK10575 112 PwhgalgrfgAADREKVEEAISLVGLKPLAHR-------LVDS----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD- 179
|
....
gi 701771264 6442 ISEQ 6445
Cdd:PRK10575 180 IAHQ 183
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6282-6482 |
1.58e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.35 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6282 EEKV--NDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqldtadlrRDMTLLSQQ----- 6354
Cdd:COG1101 17 NEKRalDGLN---LTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG------------KDVTKLPEYkraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 -ARLF----FG-----SIRDNLTM------GRPLAS------DEEIHRALALsgaLGfvqkqkNGL-NYLITEGGAgLSG 6411
Cdd:COG1101 82 iGRVFqdpmMGtapsmTIEENLALayrrgkRRGLRRgltkkrRELFRELLAT---LG------LGLeNRLDTKVGL-LSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6412 GQRQA-------------LLLartlilqpqilllDEPTAWLD--------EISEqQLVA--NLAswlgnrTLVVaTHRIP 6468
Cdd:COG1101 152 GQRQAlsllmatltkpklLLL-------------DEHTAALDpktaalvlELTE-KIVEenNLT------TLMV-THNME 210
|
250
....*....|....*
gi 701771264 6469 -ILQLVDRIIVLDNG 6482
Cdd:COG1101 211 qALDYGNRLIMMHEG 225
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
6293-6482 |
1.75e-13 |
|
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: 74.51 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqldtadlrrDMTLLSQQARLFFGSIRDNLTMGrpL 6372
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENIIFG--V 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 ASDEEIHRALALSGAL-----GFVQKQknglNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQL 6447
Cdd:cd03291 123 SYDEYRYKSVVKACQLeeditKFPEKD----NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 701771264 6448 VAN-LASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03291 199 FEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6277-6465 |
2.01e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.92 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVND--LDIARLTITAgekiaVLGRNGSGKSTLLQLLAGMQ--TPQ---HGQILLDG--ISLGQLDTADLRRD 6347
Cdd:COG1117 19 VYYGDKQALKDinLDIPENKVTA-----LIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGedIYDPDVDVVELRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6348 MTLLSQQARLFFGSIRDNLTMGRPLAS-------DEEIHRALalsgalgfvqKQ-------KNGLNylitEGGAGLSGGQ 6413
Cdd:COG1117 94 VGMVFQKPNPFPKSIYDNVAYGLRLHGikskselDEIVEESL----------RKaalwdevKDRLK----KSALGLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6414 RQALLLARTlilqpqilllDEPTAWLDEISEQQ---LVANLASwlgNRTLVVATH 6465
Cdd:COG1117 160 QQRLCIARAlavepevllmDEPTSALDPISTAKieeLILELKK---DYTIVIVTH 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6285-6482 |
2.36e-13 |
|
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: 72.92 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQARLFFG-SIR 6363
Cdd:cd03263 18 VDDLS---LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTM-----GRPLasDEEIHRALALSGALGFVQKQknglNYLITEggagLSGGQRQALLLARTLILQPQILLLDEPTAW 6438
Cdd:cd03263 94 EHLRFyarlkGLPK--SEIKEEVELLLRVLGLTDKA----NKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701771264 6439 LDEISEQQLVANLASWLGNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:cd03263 164 LDPASRRAIWDLILEVRKGRSIILTTHSMdEAEALCDRIAIMSDG 208
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6278-6482 |
2.46e-13 |
|
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: 72.94 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL-RRDMTLLSQqAR 6356
Cdd:TIGR03410 9 YYGQSHILRGVS---LEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQ-GR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFG--SIRDNLTMG---RPLASDEEIHRALALSGALGFVQKQKNGLnyliteggagLSGGQRQALLLARTLILQPQILL 6431
Cdd:TIGR03410 85 EIFPrlTVEENLLTGlaaLPRRSRKIPDEIYELFPVLKEMLGRRGGD----------LSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6432 LDEPT-----AWLDEIseQQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:TIGR03410 155 LDEPTegiqpSIIKDI--GRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6288-6488 |
2.95e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFG-SIRDNL 6366
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEfDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6367 TMGR--------PLASDEE--IHRALALSGALGFVQKQknglnylITEggagLSGGQRQALLLARTLILQPQILLLDEPT 6436
Cdd:PRK09536 99 EMGRtphrsrfdTWTETDRaaVERAMERTGVAQFADRP-------VTS----LSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6437 AWLD---EISEQQLVANLASwlGNRTLVVATHRIPI-LQLVDRIIVLDNGPARDDG 6488
Cdd:PRK09536 168 ASLDinhQVRTLELVRRLVD--DGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
5958-6240 |
3.68e-13 |
|
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: 74.00 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQ-VYDRVVPSQSVPTLWVLFGGVMLAILF--------EFTMRMLRVHIAdvvgkrADLRi 6028
Cdd:cd18552 3 LAILGMILVAATTAALAWLLKpLLDDIFVEKDLEALLLVPLAIIGLFLLrglasylqTYLMAYVGQRVV------RDLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6029 sDRVFARALRIKNS--ARpKSTGSFISQIR-ELESVRELITSTTIGTVSDiPFFLLFVFIL-----W------LIGGPlv 6094
Cdd:cd18552 76 -NDLFDKLLRLPLSffDR-NSSGDLISRITnDVNQVQNALTSALTVLVRD-PLTVIGLLGVlfyldWkltliaLVVLP-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6095 fvvllaipLLLIPGLLVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLT 6174
Cdd:cd18552 151 --------LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARAR 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6175 SLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18552 223 ALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAA 288
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5952-6420 |
3.88e-13 |
|
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: 76.38 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5952 WKRYGDIMLVAMAANVLALAGMIFSMQVYDRVV---PSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIA-DVVgkrADLR 6027
Cdd:COG4615 8 LRESRWLLLLALLLGLLSGLANAGLIALINQALnatGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGqHAV---ARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6028 IsdRVFARALRiknsarpkstgsfiSQIRELESVR--ELITSTT--IGTVSD----IPFFL--------LFVFILWLIGG 6091
Cdd:COG4615 85 L--RLSRRILA--------------APLERLERIGaaRLLAALTedVRTISQafvrLPELLqsvalvlgCLAYLAWLSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6092 PLVFVVLLAIPLLLIPGLLVQRPLAHLSN----------------EGMRE--------SAIRNATLVEAVQSIEDIKLlR 6147
Cdd:COG4615 149 LFLLTLVLLGLGVAGYRLLVRRARRHLRRareaedrlfkhfrallEGFKElklnrrrrRAFFDEDLQPTAERYRDLRI-R 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6148 AEQRFqnqwnntndvaagvgmkqrwltSLLMTWTQEVQSIVYAVVLLVgcyLVINGDMTTGALVGTSILASRTIAPLAQI 6227
Cdd:COG4615 228 ADTIF----------------------ALANNWGNLLFFALIGLILFL---LPALGWADPAVLSGFVLVLLFLRGPLSQL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6228 SGVLSRWQQAKVARKGLDDLMQR----PLDDPEEGKKVHKAHLQGnYQLNYAAFYYDEEE-----KVNDLDiarLTITAG 6298
Cdd:COG4615 283 VGALPTLSRANVALRKIEELELAlaaaEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDgdegfTLGPID---LTIRRG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6299 EKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFfgsirDNLTMGRPLASDEEI 6378
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARA 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6379 H---RALALSGALGFvqkqknglnylitEGGA----GLSGGQRQ--ALLLA 6420
Cdd:COG4615 434 RellERLELDHKVSV-------------EDGRfsttDLSQGQRKrlALLVA 471
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2752-2838 |
4.04e-13 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 68.67 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2752 SITDKAGNTGD--TSHTVTVDTVAP-TLSIDTIAGDNILNADE-KTGDVVISGTSTGLA-AGTSVTVNLNGKNYAATVGA 2826
Cdd:NF012196 2 TSHDAAGNTATatAHHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVGGDVkVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 2827 DGK----WTTTVPAGD 2838
Cdd:NF012196 82 LGNgqlgYSVDVDTSD 97
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6259-6482 |
4.30e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.21 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6259 KKVHKAHLQGNYQLNYAAFYydeeekvndldiarltITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQ 6338
Cdd:PRK10908 5 EHVSKAYLGGRQALQGVTFH----------------MRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6339 LDTAD---LRRDMTLLSQQARLFFG-SIRDNLTMgrPL----ASDEEIHRALalSGAL---GFVQKQKNglnYLITegga 6407
Cdd:PRK10908 69 LKNREvpfLRRQIGMIFQDHHLLMDrTVYDNVAI--PLiiagASGDDIRRRV--SAALdkvGLLDKAKN---FPIQ---- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6408 gLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWlgNR---TLVVATHRIPILQLVD-RIIVLDNG 6482
Cdd:PRK10908 138 -LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6279-6415 |
5.37e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.42 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQ----Q 6354
Cdd:COG4604 11 YGGKVVLDDVS---LTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQenhiN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 ARLffgSIRDnLTM--------GRPLASDEE-IHRALALSGALGFVQKqknglnYLITeggagLSGGQRQ 6415
Cdd:COG4604 88 SRL---TVRE-LVAfgrfpyskGRLTAEDREiIDEAIAYLDLEDLADR------YLDE-----LSGGQRQ 142
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6288-6447 |
6.28e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGIslgQLDTADLRRDMtLLSQQARLFFGSIRDNLT 6367
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAERGV-VFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLAS---DEEIHRA---LALSGALGFVQKqknglnyLITEggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDE 6441
Cdd:PRK11248 93 FGLQLAGvekMQRLEIAhqmLKKVGLEGAEKR-------YIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
....*.
gi 701771264 6442 ISEQQL 6447
Cdd:PRK11248 162 FTREQM 167
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6277-6482 |
8.14e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.46 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQA- 6355
Cdd:PRK13650 12 FKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLFFG-SIRDNLTMG---RPLASDEEIHR---ALALSGALGFVQKQKnglnyliteggAGLSGGQRQALLLARTLILQPQ 6428
Cdd:PRK13650 92 NQFVGaTVEDDVAFGlenKGIPHEEMKERvneALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6429 ILLLDEPTAWLDEISEQQLVANLASWLG--NRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6288-6482 |
9.50e-13 |
|
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: 71.60 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGIslgqlDTADL---RRDMTLLSQQARLF-FGSIR 6363
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK-----DITNLppeKRDISYVPQNYALFpHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTMG--RPLASDEEIHR-ALALSGALGfvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:cd03299 90 KNIAYGlkKRKVDKKEIERkVLEIAEMLG--------IDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701771264 6441 EISEQQLVANLASW--LGNRTLVVATHR-IPILQLVDRIIVLDNG 6482
Cdd:cd03299 162 VRTKEKLREELKKIrkEFGVTVLHVTHDfEEAWALADKVAIMLNG 206
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
6294-6482 |
9.63e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMqTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR-LFFGSIRDNLTMGRP- 6371
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYLTLHQPd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6372 LASDEEIHRALA-LSGALGFVQKqkngLNYLITEggagLSGGQRQALLLA-------RTLILQPQILLLDEPTAWLDeIS 6443
Cdd:PRK03695 97 KTRTEAVASALNeVAEALGLDDK----LGRSVNQ----LSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD-VA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 701771264 6444 EQ----QLVANLASwLGnRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:PRK03695 168 QQaaldRLLSELCQ-QG-IAVVMSSHDLNhTLRHADRVWLLKQG 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6293-6482 |
1.30e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 75.33 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqldtadlrrDMTLLSQQARLFFGSIRDNLTMGrpL 6372
Cdd:TIGR01271 447 FKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFG--L 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 ASDEEIHRALALSGALG-----FVQKQKNGLNylitEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQL 6447
Cdd:TIGR01271 512 SYDEYRYTSVIKACQLEedialFPEKDKTVLG----EGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*.
gi 701771264 6448 VAN-LASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:TIGR01271 588 FEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6288-6465 |
2.35e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.05 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQI-LLDGISLG-----QLDTadLRRDMTLLSQQARLffgs 6361
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGyfaqhQLEF--LRADESPLQHLARL---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 irdnltmgRPLASDEEIHRALalsGALGFvQKQKnglnylITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDE 6441
Cdd:PRK10636 402 --------APQELEQKLRDYL---GGFGF-QGDK------VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170 180
....*....|....*....|....
gi 701771264 6442 ISEQQLVANLASWLGnrTLVVATH 6465
Cdd:PRK10636 464 DMRQALTEALIDFEG--ALVVVSH 485
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6278-6482 |
2.50e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.43 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIArLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDgislgqldtadlrRDMTLLSQQARL 6357
Cdd:PTZ00243 667 FFELEPKVLLRDVS-VSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 FFGSIRDNLtmgrpLASDEE----IHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLD 6433
Cdd:PTZ00243 733 MNATVRGNI-----LFFDEEdaarLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6434 EPTAWLDEISEQQLVAN-LASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PTZ00243 808 DPLSALDAHVGERVVEEcFLGALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2254-2353 |
2.64e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 66.36 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2254 VTDAHGN--SSSDSHNVQVD-SALPTVIVNSVTSDNILNITEIAGGQTL-SGTVTGAVK-GDVVTINLGGKLYQATVQDD 2328
Cdd:NF012196 3 SHDAAGNtaTATAHHTVTIDtHADATITIDTVTGDNVLNAAESQQPTTTiTGTVGGDVKvGDPVTLTVNGHTYTGTVVDL 82
|
90 100
....*....|....*....|....*....
gi 701771264 2329 ----LSWSLPVSKeilTALGNGELTITAS 2353
Cdd:NF012196 83 gngqLGYSVDVDT---SDLLNNPNDVTAT 108
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6278-6488 |
2.70e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.29 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAdlRRDMTLLSQQARL 6357
Cdd:PRK09452 23 SFDGKEVISNLD---LTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 F-FGSIRDNLTMGRPLA--SDEEIHRALAlsGALGFVQkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:PRK09452 98 FpHMTVFENVAFGLRMQktPAAEITPRVM--EALRMVQ-----LEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6435 PTAWLDEISEQQL---VANLASWLGnRTLVVATH-RIPILQLVDRIIVLDNGPARDDG 6488
Cdd:PRK09452 171 SLSALDYKLRKQMqneLKALQRKLG-ITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3451-3549 |
3.33e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 66.36 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3451 TATSSIGNSAGASASLLV---DTAAPGITINPVTADNVLNAAEIAAGQTL-SGKVS-NAAAGDAVTINLGGKTYTATVQS 3525
Cdd:NF012196 2 TSHDAAGNTATATAHHTVtidTHADATITIDTVTGDNVLNAAESQQPTTTiTGTVGgDVKVGDPVTLTVNGHTYTGTVVD 81
|
90 100
....*....|....*....|....*...
gi 701771264 3526 D----LSWSLDLPADVLTAlGNGKLTVT 3549
Cdd:NF012196 82 LgngqLGYSVDVDTSDLLN-NPNDVTAT 108
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6204-6346 |
3.64e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6204 DMTTGALVGTSILASRTiaPLAQISGVLSRWQQAKVArkgLDDLMQRPLDDPEEGKKVHKAHlqGNYQ---LNYAAFYYD 6280
Cdd:PRK10522 261 DTNVAATYSLTLLFLRT--PLLSAVGALPTLLSAQVA---FNKLNKLALAPYKAEFPRPQAF--PDWQtleLRNVTFAYQ 333
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6281 EEE-KVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRR 6346
Cdd:PRK10522 334 DNGfSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3750-3837 |
4.25e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 65.97 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3750 VSVTNVNGN--GASAEREFSVDATAPG-LTINPIATDNVINAAEAGAGVT-VTGT--SNAQAGQTVTLTLDGKTYTGVVK 3823
Cdd:NF012196 1 VTSHDAAGNtaTATAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTvgGDVKVGDPVTLTVNGHTYTGTVV 80
|
90
....*....|....*...
gi 701771264 3824 ADG----TWSITLDSTAL 3837
Cdd:NF012196 81 DLGngqlGYSVDVDTSDL 98
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6298-6482 |
4.43e-12 |
|
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: 68.35 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTPQH--GQILLDGISLGQldtADLRRDMTLLSQQARLFfgsirDNLTmgrplasd 6375
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDK---RSFRKIIGYVPQDDILH-----PTLT-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6376 eeIHRALALSGALgfvqkqknglnyliteggAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVA---NLA 6452
Cdd:cd03213 99 --VRETLMFAAKL------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSllrRLA 158
|
170 180 190
....*....|....*....|....*....|..
gi 701771264 6453 SwlGNRTLVVATH--RIPILQLVDRIIVLDNG 6482
Cdd:cd03213 159 D--TGRTIICSIHqpSSEIFELFDKLLLLSQG 188
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4789-4880 |
4.50e-12 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 65.75 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4789 SDDTGQSASDFITMDTTLTLNGTlghALASDE-RVQISLDGGRNWVDAVVNGT-AWHYVDGRTLADGDYVYQVRIIDQAG 4866
Cdd:pfam19077 12 GSDTGVSDSDNITNDTTPTFTGT---NEDGDVvTVTVSIDGNGVTGTATAGADgNWSFTPPAALADGTYTLTVTVTDIAG 88
|
90
....*....|....
gi 701771264 4867 NVGSTANQVVTVDT 4880
Cdd:pfam19077 89 NTATSSPLSFTIDT 102
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6271-6476 |
5.50e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQ--TPQ---HGQILLDG--ISLGQLDTAD 6343
Cdd:PRK14239 7 QVSDLSVYYNKKKALNSVS---LDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGhnIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6344 LRRDMTLLSQQARLFFGSIRDNLTMGRPLAS-------DEEIHRALalSGAlGFVQKQKNGLNylitEGGAGLSGGQRQA 6416
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGLRLKGikdkqvlDEAVEKSL--KGA-SIWDEVKDRLH----DSALGLSGGQQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6417 LLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHRipiLQLVDRI 6476
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRS---MQQASRI 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6285-6482 |
6.63e-12 |
|
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: 69.11 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqLDTADL------RRDMTLLSQQARLF 6358
Cdd:cd03218 16 VNGVS---LSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-----QDITKLpmhkraRLGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG-SIRDNLTM---GRPLASDEEIHRALALSGALGF--VQKQKnglnylitegGAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:cd03218 88 RKlTVEENILAvleIRGLSKKEREEKLEELLEEFHIthLRKSK----------ASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6433 DEPTAWLDEISE---QQLVANLASW-LGnrtlVVAT-HRI-PILQLVDRIIVLDNG 6482
Cdd:cd03218 158 DEPFAGVDPIAVqdiQKIIKILKDRgIG----VLITdHNVrETLSITDRAYIIYEG 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6293-6482 |
7.03e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.88 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQARLfFGS--IRDNLT 6367
Cdd:COG1135 26 LTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaRRKIGMIFQHFNL-LSSrtVAENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MgrPL----ASDEEIH-RALALsgaLGFVqkqknGL-----NYLiteggAGLSGGQRQ------AL------LLArtlil 6425
Cdd:COG1135 105 L--PLeiagVPKAEIRkRVAEL---LELV-----GLsdkadAYP-----SQLSGGQKQrvgiarALannpkvLLC----- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6426 qpqilllDEPTAWLD-EISEQ--QLVANLaswlgNR----TLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG1135 165 -------DEATSALDpETTRSilDLLKDI-----NRelglTIVLITHEMDvVRRICDRVAVLENG 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6293-6465 |
7.10e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDtADLRRDMTLLSQQArlffgSIRDNLT----- 6367
Cdd:PRK13538 22 FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQP-----GIKTELTalenl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 -----MGRPlASDEEIHRALALSGALGFVQ---KQknglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:PRK13538 96 rfyqrLHGP-GDDEALWEALAQVGLAGFEDvpvRQ--------------LSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 701771264 6440 DEISEQQLVANLASWLGNRTLVV-ATH 6465
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVIlTTH 187
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
4151-4238 |
9.70e-12 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 64.81 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4151 VNDKAGNPGSA--DRTLTVDTTAP-TITFDKVAGDDIINSAE-QQAGQAISGTT--NAQPGQTITVTFNNHTYQA-VDFL 4223
Cdd:NF012196 3 SHDAAGNTATAtaHHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVggDVKVGDPVTLTVNGHTYTGtVVDL 82
|
90
....*....|....*
gi 701771264 4224 GAADGSYQISASVSD 4238
Cdd:NF012196 83 GNGQLGYSVDVDTSD 97
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6284-6482 |
1.02e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 KVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFG--S 6361
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSrmT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 IRDNLTMGRPLASDEE----IHRALALSGALGFVQKQKNGLnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:PRK11614 97 VEENLAMGGFFAERDQfqerIKWVYELFPRLHERRIQRAGT----------MSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6438 WLDEISEQQLVANLASWL--GNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLReqGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
6293-6482 |
1.30e-11 |
|
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: 68.07 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQtPQH----GQILLDGIslgQLDTADLRRDMTLLSQQARLFFG-SIRDNLT 6367
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGgttsGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGlTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLA----SDEEIHRALALSGALGFVQKQKNGLNYLiteggAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEIS 6443
Cdd:cd03234 104 YTAILRlprkSSDAIRKKRVEDVLLRDLALTRIGGNLV-----KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 701771264 6444 EQQLV---ANLASwlGNRTLVVATH--RIPILQLVDRIIVLDNG 6482
Cdd:cd03234 179 ALNLVstlSQLAR--RNRIVILTIHqpRSDLFRLFDRILLLSSG 220
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2655-2752 |
1.34e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 64.43 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2655 DQAGNPGSAS--RDVLVDVTVP-KVTIGTMATDDVINQTEHGQALV-ISGTSTG-AQAGDIVTVTLGNKQYTGVVDTNGN 2729
Cdd:NF012196 5 DAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTtITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLGN 84
|
90 100
....*....|....*....|....*..
gi 701771264 2730 ----WSVGVpraDVSALGDNTYTVTAS 2752
Cdd:NF012196 85 gqlgYSVDV---DTSDLLNNPNDVTAT 108
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6278-6482 |
2.13e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.34 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARL 6357
Cdd:PRK10851 11 SFGRTQVLNDIS---LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 F-FGSIRDNLTMG--------RPlaSDEEIHRALAlsGALGFVQkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQ 6428
Cdd:PRK10851 86 FrHMTVFDNIAFGltvlprreRP--NAAAIKAKVT--QLLEMVQ-----LAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6429 ILLLDEPTAWLDeiseQQLVANLASWLGNR------TLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:PRK10851 157 ILLLDEPFGALD----AQVRKELRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6271-6482 |
2.38e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD------L 6344
Cdd:COG4161 4 QLKNINCFYGSHQALFDIN---LECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekairlL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6345 RRDMTLLSQQARLF-FGSIRDNLTmgrplasdEEIHRALALSGALGfVQKQKNGLNYLITEGGAG-----LSGGQRQALL 6418
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLI--------EAPCKVLGLSKEQA-REKAMKLLARLRLTDKADrfplhLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6419 LARTLILQPQILLLDEPTAWLD-EISEQqlVANLASWLGNR--TLVVATHRIPILQLV-DRIIVLDNG 6482
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDpEITAQ--VVEIIRELSQTgiTQVIVTHEVEFARKVaSQVVYMEKG 217
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3849-3950 |
2.44e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 63.66 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3849 VDVSDAAGNKTTGS--QNMTLDTTAP-TVSFNAVAGDDIINLEE-HAQAQIISGSSTG-AAAGNKIIITLDGVQYVTQVD 3923
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100 110
....*....|....*....|....*....|.
gi 701771264 3924 AKGN----WSVGVPasaVSALKNGTATITAT 3950
Cdd:NF012196 81 DLGNgqlgYSVDVD---TSDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1949-2038 |
2.86e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 63.66 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1949 VSVSNANGNPATST--QEYSVDASAP-TLIIDPLSGDNLLNAAEAKQPLI-VSGSSS--AEPGQEVTVTLNNVNYTATVG 2022
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|
gi 701771264 2023 ADG----RWSVSVPASDLAA 2038
Cdd:NF012196 81 DLGngqlGYSVDVDTSDLLN 100
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6277-6482 |
4.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQAR 6356
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFF--GSIRDNLTMG---RPLASDEEIHR---ALALSGALGFVQKQKnglnyliteggAGLSGGQRQALLLARTLILQPQ 6428
Cdd:PRK13642 92 NQFvgATVEDDVAFGmenQGIPREEMIKRvdeALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6429 ILLLDEPTAWLDEISEQQLVANLASWLGNRTLVV--ATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVlsITHDLDEAASSDRILVMKAG 216
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
4650-5774 |
4.92e-11 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 70.18 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4650 VVDDAGNVGQSASKNVTVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLNGSLGAPLGSNEFVQISIDGGASWFY 4729
Cdd:COG3210 9 TGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4730 ATSVNGTRWSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGISDDTGQSASDFITMDTTLTLN 4809
Cdd:COG3210 89 AGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4810 GTLGHALASDERVQISLDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNVGSTAN-QVVTVDTVAPDTVGS 4888
Cdd:COG3210 169 SGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVaAGTGAGVISTGGTDI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4889 IVSYTDNNGERTGNFDSSYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTFADSGLLDGSYHYVLRV 4968
Cdd:COG3210 249 SSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4969 TDKAGNYTESNDFGLTVDTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVVTVNGKTYTSDRGGAVVVDPASNTW 5048
Cdd:COG3210 329 NGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5049 YLQIPDADVLSLKSYDVTAQVKSSAGNGNSVDVTHGTVVVGAEASMTPAWAFTSATNAIAASFMLDANGMWTFASNQQFA 5128
Cdd:COG3210 409 NTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5129 TANDRNSYSVSGNFSMTGSYTTGAYADINRDGHADMLVESTNYSYITQLMNNGDGTYTSTSPGSSATVGALLWYGAVVSI 5208
Cdd:COG3210 489 GIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLG 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5209 DFQGDGYVDFVMGDAGGPDSSTFVNNNAGKLTGTSGGGTYTNFVSGSKVGNYNSVIETSGVDLNNDGMVDIAQHTTNGGN 5288
Cdd:COG3210 569 VLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGS 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5289 IYALSTMFNKGDGTFTWSQNFINTMYSATGSAAANNAVSMTWADFDGDGYMDLyMGMSRAGTGGLLMMNDGKGNLLT--G 5366
Cdd:COG3210 649 GTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNN-AGNTLTISTGSITVTGQIGALANanG 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5367 TAVGSEKYNGTVSVAVDWNMDGRMDIIKLANTGQSYMYTNDGLKGVASFTSSKFGSATTSQVSGAALVDY-------DWD 5439
Cdd:COG3210 728 DTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDitadgtiTAA 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5440 GAQDLLIFRQNGSVTLERNTNAVAPGTAIHLKIVDSQGINVFFGNTVKLYNAAGELVASQVINAQSGIGINDASALVSFY 5519
Cdd:COG3210 808 GTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATS 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5520 GLNPNETYHAELVRAINGVSSNTTWNGLTAGDGRESYALTADAATGVHAGTLTGTGYNDTFIAEQGTYVYNGGGGWETSS 5599
Cdd:COG3210 888 TGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTG 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5600 DHQTWSATGGMDVVDFRNSTVGVTVDLGKTGAQNTGFNTATFSNIEGIVGSSHDDVITGNSGNNTFEGGGGNDTFNIGSG 5679
Cdd:COG3210 968 ASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVG 1047
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5680 GHDTLLYKLLNGSDATGGNGHDVVNGFSVGTWEGTADSDRIDLRELLQGSGYAGDASAHYVNGVAQLGAGAGNIGDYIKV 5759
Cdd:COG3210 1048 VNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTV 1127
|
1130
....*....|....*
gi 701771264 5760 VQNGSSTEIQIDRDD 5774
Cdd:COG3210 1128 GATGTSTASTEAAGA 1142
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1352-1441 |
4.97e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 62.89 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1352 VSVTNVSGNGASGA--REVLVDTQPP-SITLNSITADNILNHAEAAQELV-ITGTST--AQPGQTVTVSLNNQSYTGLVL 1425
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|
gi 701771264 1426 ADG----TWSVTVPVADLAN 1441
Cdd:NF012196 81 DLGngqlGYSVDVDTSDLLN 100
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6271-6482 |
5.31e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQIlldGISLGQLD---------T 6341
Cdd:PRK11124 4 QLNGINCFYGAHQALFDIT---LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL---NIAGNHFDfsktpsdkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6342 ADLRRDMTLLSQQARLF-FGSIRDNLTMG----RPLASDEEIHRALALsgalgfvqkqkngLNYLITEGGAG-----LSG 6411
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWpHLTVQQNLIEApcrvLGLSKDQALARAEKL-------------LERLRLKPYADrfplhLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6412 GQRQALLLARTLILQPQILLLDEPTAWLD-EISEQqlVANLASWLGNR--TLVVATHRIPILQLV-DRIIVLDNG 6482
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDpEITAQ--IVSIIRELAETgiTQVIVTHEVEVARKTaSRVVYMENG 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6293-6333 |
6.21e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.26 E-value: 6.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG 6333
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1452-1533 |
6.59e-11 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 62.50 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1452 SVSDVAGNP--ASTSHGMLVDTTAPV-VTINTFAGDNIVNRSE-HAQAQVLSGKATG-AAVGDSVKITVNGVEYSTVLDA 1526
Cdd:NF012196 2 TSHDAAGNTatATAHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
....*..
gi 701771264 1527 SGNWSLG 1533
Cdd:NF012196 82 LGNGQLG 88
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4571-4669 |
6.80e-11 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 62.28 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4571 TVTIDSIS----TDTGLSNTDFVTSDTSLTVHGSLGAPllAGEYVQISLDGGTVWQTVVTIGS-TWYFNDGRTLSDGTYQ 4645
Cdd:pfam19077 1 TLSIPTIDlaagSDTGVSDSDNITNDTTPTFTGTNEDG--DVVTVTVSIDGNGVTGTATAGADgNWSFTPPAALADGTYT 78
|
90 100
....*....|....*....|....
gi 701771264 4646 YLVRVVDDAGNVGQSASKNVTVDT 4669
Cdd:pfam19077 79 LTVTVTDIAGNTATSSPLSFTIDT 102
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6285-6484 |
8.74e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQ--------HGQILLDGISLGQLDTADLRRDMTLLSQQAR 6356
Cdd:PRK13547 17 LRDLS---LRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFG-SIRDNLTMGR-PLAS--------DEEI-HRALALSGALGFVQKQknglnylITEggagLSGGQRQALLLART--- 6422
Cdd:PRK13547 94 PAFAfSAREIVLLGRyPHARragalthrDGEIaWQALALAGATALVGRD-------VTT----LSGGELARVQFARVlaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6423 ------LILQPQILLLDEPTAWLDEISEQQLVANLAS----W-LGNRTLV-----VATHRIPILQLVDRIIVLDNGPA 6484
Cdd:PRK13547 163 lwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRlardWnLGVLAIVhdpnlAARHADRIAMLADGAIVAHGAPA 240
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6282-6487 |
8.99e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6282 EEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDT---ADLRrdmtllSQQARLF 6358
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLR------AKHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FGSI--------RDNLTMGRPLASDEEIH---RALALSGALGFVQKqkngLNYLitegGAGLSGGQRQALLLARTLILQP 6427
Cdd:PRK10584 94 FQSFmliptlnaLENVELPALLRGESSRQsrnGAKALLEQLGLGKR----LDHL----PAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6428 QILLLDEPTAWLDEISEQQLVANLASWlgNR----TLVVATHRIPILQLVDRIIVLDNGPARDD 6487
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSL--NRehgtTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6279-6486 |
1.06e-10 |
|
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: 65.51 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDIARLTITAG-----EKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLG---QLDTADlrRDMTL 6350
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpQYIKAD--YEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 lsqqaRLFFGSIRDNLTMGRPLASdeEIHRALALSGALgfvqkqknglNYLITEggagLSGGQRQALLLARTLILQPQIL 6430
Cdd:cd03237 79 -----RDLLSSITKDFYTHPYFKT--EIAKPLQIEQIL----------DREVPE----LSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6431 LLDEPTAWLDeiSEQQLVANLA----SWLGNRTLVVATHRIPILQLV-DRIIVLDNGPARD 6486
Cdd:cd03237 138 LLDEPSAYLD--VEQRLMASKVirrfAENNEKTAFVVEHDIIMIDYLaDRLIVFEGEPSVN 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6284-6481 |
1.18e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.81 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 KVNDLDIAR----------LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQ---HGQILLDGISLGQLDTadLRRDMTL 6350
Cdd:COG4136 3 SLENLTITLggrpllaplsLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQARLFfgsirDNLTMGRPLAsdeeihraLALSGALGFVQKQKN--------GLNYLITEGGAGLSGGQRQALLLART 6422
Cdd:COG4136 81 LFQDDLLF-----PHLSVGENLA--------FALPPTIGRAQRRARveqaleeaGLAGFADRDPATLSGGQRARVALLRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6423 LILQPQILLLDEPTAWLDeiseqqlvANLASWLgnRTLV---VATHRIPIL---------QLVDRIIVLDN 6481
Cdd:COG4136 148 LLAEPRALLLDEPFSKLD--------AALRAQF--REFVfeqIRQRGIPALlvthdeedaPAAGRVLDLGN 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6278-6465 |
1.31e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.57 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVND--LDIARLTITAgekiaVLGRNGSGKSTLLQ-------LLAGMQTpqHGQILLDGISL--GQLDTADLRR 6346
Cdd:PRK14243 19 YYGSFLAVKNvwLDIPKNQITA-----FIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyaPDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6347 DMTLLSQQARLFFGSIRDNLTMGRPLAS-----DEEIHRALAlSGALGFVQKQKnglnylITEGGAGLSGGQRQALLLAR 6421
Cdd:PRK14243 92 RIGMVFQKPNPFPKSIYDNIAYGARINGykgdmDELVERSLR-QAALWDEVKDK------LKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701771264 6422 TLILQPQILLLDEPTAWLDEISEQQlVANLASWLGNR-TLVVATH 6465
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLR-IEELMHELKEQyTIIIVTH 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6135-6481 |
1.53e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6135 EAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVI--------NGDMT 6206
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIIsdlsnqqpNNDFH 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6207 TGALVgtSILASRTIAP--LAQISGVLSRWQQAKVARKGLDDLMQR-PL-DDPEEGKKVHKAHlqgNYQLNYAAFYYDEE 6282
Cdd:PTZ00265 321 GGSVI--SILLGVLISMfmLTIILPNITEYMKSLEATNSLYEIINRkPLvENNDDGKKLKDIK---KIQFKNVRFHYDTR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6283 EKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILL-DGISLGQLDTADLRRDMTLLSQQARLFFGS 6361
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNS 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 IRDNLT-------------------------------------------MGRPLASDEEIH-----------RALALSGA 6387
Cdd:PTZ00265 476 IKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNELIEmrknyqtikdsEVVDVSKK 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6388 L---GFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISE---QQLVANLASwLGNRTLV 6461
Cdd:PTZ00265 556 VlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKG-NENRITI 634
|
410 420
....*....|....*....|
gi 701771264 6462 VATHRIPILQLVDRIIVLDN 6481
Cdd:PTZ00265 635 IIAHRLSTIRYANTIFVLSN 654
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6293-6482 |
1.53e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGI------SLGQLDTA--DLRRDMTLLSQQARLF-FGSIR 6363
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItidtarSLSQQKGLirQLRQHVGFVFQNFNLFpHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DNLTMG----RPLASDEEIHRALALSGALGFVQKQknglnyliTEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:PRK11264 104 ENIIEGpvivKGEPKEEATARARELLAKVGLAGKE--------TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6440 D-EISEQQL--VANLASwlGNRTLVVATHRIPILQLV-DRIIVLDNG 6482
Cdd:PRK11264 176 DpELVGEVLntIRQLAQ--EKRTMVIVTHEMSFARDVaDRAIFMDQG 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6291-6482 |
1.60e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.98 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6291 ARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL----RRDMTLLSQQARLF-FGSIRDN 6365
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6366 LTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYlitegGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQ 6445
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALRQVGLENYAHSY-----PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 701771264 6446 QLVANLASWLG--NRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK10070 202 EMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNG 241
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3551-3637 |
2.00e-10 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 60.96 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3551 SVTNGHGNSGTA--DREFTVDASLPG-IRINTVAGDDVVNAIE-HNQNLIISGSASG-MSEGSTVTVTINGKSYLATVSA 3625
Cdd:NF012196 2 TSHDAAGNTATAtaHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 3626 SG----TWSAAVPAGD 3637
Cdd:NF012196 82 LGngqlGYSVDVDTSD 97
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6279-6482 |
2.68e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARLF 6358
Cdd:PRK11000 13 YGDVVISKDIN---LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 -FGSIRDNLTMGRPLASDEEIHRALALSGALGFVQkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:PRK11000 88 pHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 701771264 6438 WLDEISEQQL---VANLASWLGnRTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:PRK11000 163 NLDAALRVQMrieISRLHKRLG-RTMIYVTHdQVEAMTLADKIVVLDAG 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6300-6482 |
2.78e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6300 KIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQA--RLFFGSIRDNLTMGrP--LASD 6375
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFG-PinLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6376 EEI--HRalaLSGALGFVqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVA--NL 6451
Cdd:PRK13652 111 EETvaHR---VSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDflND 182
|
170 180 190
....*....|....*....|....*....|..
gi 701771264 6452 ASWLGNRTLVVATHRIPIL-QLVDRIIVLDNG 6482
Cdd:PRK13652 183 LPETYGMTVIFSTHQLDLVpEMADYIYVMDKG 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6288-6488 |
2.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.03 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQ-----LDTADLRRDMTLLSQ--QARLFFG 6360
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 SIRDNLTMGrPL---ASDEEIHRalALSGALGFVQKQKNGLNYLITEggagLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:PRK13645 107 TIEKDIAFG-PVnlgENKQEAYK--KVPELLKLVQLPEDYVKRSPFE----LSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6438 WLDEISEQ---QLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:PRK13645 180 GLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6278-6482 |
4.82e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.67 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGIslgqlDTADLRRDMtlLSQQARL 6357
Cdd:PRK10535 14 YPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ-----DVATLDADA--LAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 FFGSI--RDNLTMGRPLASDEEI-------------HRALALSGALGFVQKqkngLNYLITEggagLSGGQRQALLLART 6422
Cdd:PRK10535 87 HFGFIfqRYHLLSHLTAAQNVEVpavyaglerkqrlLRAQELLQRLGLEDR----VEYQPSQ----LSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6423 LILQPQILLLDEPTAWLDEISEQQLVANLASwLGNR--TLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRghTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6293-6488 |
5.08e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG--ISL-----GQLDTAD------LRRDMTLLSQQARLF- 6358
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtINLvrdkdGQLKVADknqlrlLRTRLTMVFQHFNLWs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FGSIRDNLtMGRPLasdeeihRALALSGAlgfvQKQKNGLNYL----ITEGGAG-----LSGGQRQALLLARTLILQPQI 6429
Cdd:PRK10619 106 HMTVLENV-MEAPI-------QVLGLSKQ----EARERAVKYLakvgIDERAQGkypvhLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6430 LLLDEPTAWLDE--ISE-----QQLVANlaswlgNRTLVVATHRIPILQLV-DRIIVLDNGPARDDG 6488
Cdd:PRK10619 174 LLFDEPTSALDPelVGEvlrimQQLAEE------GKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEG 234
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
5959-6240 |
5.53e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) 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: 349990 [Multi-domain] Cd Length: 292 Bit Score: 64.43 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5959 MLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRA--DLRIsdRVFARA 6036
Cdd:cd18546 5 LLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLlyDLRL--RVFAHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6037 LRIKNSARPKST-GSFIS-QIRELESVRELITSTTIGTVSDIpffLLFVFI----LW---------LIGGPLVFVVLLai 6101
Cdd:cd18546 83 QRLSLDFHERETsGRIMTrMTSDIDALSELLQTGLVQLVVSL---LTLVGIavvlLVldprlalvaLAALPPLALATR-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6102 plllipgllVQRPLAHLSNEGMRE-SAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTW 6180
Cdd:cd18546 158 ---------WFRRRSSRAYRRARErIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6181 TQEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18546 229 VELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAA 288
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3161-3251 |
5.93e-10 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 59.81 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3161 ASAGREISVDT-AAPTLQINTIAGDDVLNAAEAGQPLV-ITGT--SNAEPGQTVTVTLNNETYTGIVQANG----TWSIT 3232
Cdd:NF012196 13 ATAHHTVTIDThADATITIDTVTGDNVLNAAESQQPTTtITGTvgGDVKVGDPVTLTVNGHTYTGTVVDLGngqlGYSVD 92
|
90
....*....|....*....
gi 701771264 3233 VPadkASALGDGVYTVDAS 3251
Cdd:NF012196 93 VD---TSDLLNNPNDVTAT 108
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6293-6333 |
7.14e-10 |
|
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: 62.94 E-value: 7.14e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG 6333
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6278-6482 |
7.15e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.56 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG--ISLGQLDTADLRRDMTLLSQQA 6355
Cdd:PRK13639 11 YPDGTEALKGIN---FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 --RLFFGSIRDNLTMGrPL---ASDEEIHR----ALALSGALGFVQKQKNglnyliteggaGLSGGQRQALLLARTLILQ 6426
Cdd:PRK13639 88 ddQLFAPTVEEDVAFG-PLnlgLSKEEVEKrvkeALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6427 PQILLLDEPTAWLDEISEQQLVaNLASWLGNR--TLVVATHRIPILQL-VDRIIVLDNG 6482
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIM-KLLYDLNKEgiTIIISTHDVDLVPVyADKVYVMSDG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6279-6482 |
7.24e-10 |
|
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: 62.77 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQARLF 6358
Cdd:cd03265 10 YGDFEAVRGVS---FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG-SIRDNLTM-----GRPLAS-DEEIHRALALSGALGFVQKQKNglNYliteggaglSGGQRQALLLARTLILQPQILL 6431
Cdd:cd03265 86 DElTGWENLYIharlyGVPGAErRERIDELLDFVGLLEAADRLVK--TY---------SGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6432 LDEPTAWLDEISEQQLvanlasWLGNRTLvVATHRIPIL----------QLVDRIIVLDNG 6482
Cdd:cd03265 155 LDEPTIGLDPQTRAHV------WEYIEKL-KEEFGMTILltthymeeaeQLCDRVAIIDHG 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6285-6482 |
7.42e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD--------LRRDMTL---LSQ 6353
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaaqlgigiIYQELSVideLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 QARLFFGSIRDNLTMGRPLASDEEIH-RALALSGALGFvqkqKNGLNYLIteggAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:PRK09700 98 LENLYIGRHLTKKVCGVNIIDWREMRvRAAMMLLRVGL----KVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6433 DEPTAWLDEISEQQLVANLASWLGN-RTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6256-6482 |
7.52e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6256 EEGKKVHKAHLQgnyqLNYAAFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQI-LLDGI 6334
Cdd:PRK15064 310 EQDKKLHRNALE----VENLTKGFDNGPLFKNLN---LLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6335 SLG---QLDTADLRRDMTLL---SQqarlfFGSIRDNLTM-----GRPLASDEEIHRalalsgalgfvqKQKNglnylit 6403
Cdd:PRK15064 383 NIGyyaQDHAYDFENDLTLFdwmSQ-----WRQEGDDEQAvrgtlGRLLFSQDDIKK------------SVKV------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6404 eggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLvaNLASWLGNRTLVVATH-RIPILQLVDRII-VLDN 6481
Cdd:PRK15064 439 -----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL--NMALEKYEGTLIFVSHdREFVSSLATRIIeITPD 511
|
.
gi 701771264 6482 G 6482
Cdd:PRK15064 512 G 512
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6285-6451 |
7.68e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.74 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLgqLDTADLRRDMTLLSQQARLF-FGSIR 6363
Cdd:PRK11432 22 IDNLN---LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV--THRSIQQRDICMVFQSYALFpHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DN----LTM-GRPLAS-DEEIHRALALSGALGFVQK---QknglnyliteggagLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:PRK11432 97 ENvgygLKMlGVPKEErKQRVKEALELVDLAGFEDRyvdQ--------------ISGGQQQRVALARALILKPKVLLFDE 162
|
170
....*....|....*..
gi 701771264 6435 PTAWLDeiseqqlvANL 6451
Cdd:PRK11432 163 PLSNLD--------ANL 171
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
5959-6240 |
8.29e-10 |
|
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: 63.66 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5959 MLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKR--ADLRIsdRVFARA 6036
Cdd:cd18543 5 LLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGveHDLRT--DLFAHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6037 LRIKNSARPK-STGSFISQ-IRELESVRELITSTTIGTVSDIPFFLLFVFILWL----------IGGPLVFVVLLAIPLL 6104
Cdd:cd18543 83 QRLDGAFHDRwQSGQLLSRaTSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLVLspplalvalaSLPPLVLVARRFRRRY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6105 LIPGLLVQRPLAHLsnegmresairnATLV-EAVQSIEDIKLLRAEQRFQNQWnntnDVAA----GVGMKQRWLTSLLMT 6179
Cdd:cd18543 163 FPASRRAQDQAGDL------------ATVVeESVTGIRVVKAFGRERRELDRF----EAAArrlrATRLRAARLRARFWP 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6180 WTQEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18543 227 LLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAA 287
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6287-6465 |
8.91e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.01 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6287 DLDIARLTITAgekiaVLGRNGSGKSTLLQLLAGM-----QTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLFFG- 6360
Cdd:PRK14247 23 NLEIPDNTITA-----LMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 SIRDNLTMG----RPLASDEEIHRAL--ALSGAlGFVQKQKNGLNylitEGGAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:PRK14247 98 SIFENVALGlklnRLVKSKKELQERVrwALEKA-QLWDEVKDRLD----APAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|.
gi 701771264 6435 PTAWLDEISEQQLVANLASWLGNRTLVVATH 6465
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6288-6482 |
1.04e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRR--------DMTLLSQqarLff 6359
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAagiaiihqELNLVPN---L-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6360 gSIRDNLTMGRPLAS------DEEIHRALALSGALGF-------VqkqknglnyliteggAGLSGGQRQALLLARTLILQ 6426
Cdd:COG1129 95 -SVAENIFLGREPRRgglidwRAMRRRARELLARLGLdidpdtpV---------------GDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6427 PQILLLDEPTAWLDEiSEQQ----LVANLASwlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG1129 159 ARVLILDEPTASLTE-REVErlfrIIRRLKA--QGVAIIYISHRLDeVFEIADRVTVLRDG 216
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4465-4563 |
1.50e-09 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 58.43 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4465 TITVEAISrDTGLDAHDFITSDNTLTLSGKLGAplAAGEHAQISIDGGKTWVDVSV-SGTSWSYVDGRQLADGDHLYQLR 4543
Cdd:pfam19077 6 TIDLAAGS-DTGVSDSDNITNDTTPTFTGTNED--GDVVTVTVSIDGNGVTGTATAgADGNWSFTPPAALADGTYTLTVT 82
|
90 100
....*....|....*....|
gi 701771264 4544 VVDDAGNIGSTASQLVTVDT 4563
Cdd:pfam19077 83 VTDIAGNTATSSPLSFTIDT 102
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6293-6488 |
1.54e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.72 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGM----QTPQ-HGQILLDGISlgqlDTADLRRDMtllsQQARLFFGSIRDNLT 6367
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGsHIELLGRTVQ----REGRLARDI----RKSRANTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 MGRPLASDEEIhralaLSGALG-----------FVQKQKN---------GLNYLITEGGAGLSGGQRQALLLARTLILQP 6427
Cdd:PRK09984 97 LVNRLSVLENV-----LIGALGstpfwrtcfswFTREQKQralqaltrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6428 QILLLDEPTAWLDEISEQQLVANLASWLGNR--TLVVATHRIP-ILQLVDRIIVLDNGPARDDG 6488
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2952-3028 |
1.58e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.65 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2952 SVTDGAGNTGTGS--RDVTIDA-ALPGIRVNTIAGDDVINAIE-HGLNLVINGTSSG-LSEGSTVTVTINGKDYAATVRA 3026
Cdd:NF012196 2 TSHDAAGNTATATahHTVTIDThADATITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
..
gi 701771264 3027 DG 3028
Cdd:NF012196 82 LG 83
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6288-6488 |
1.71e-09 |
|
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: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQT--PQHGQIL---------------------------------LD 6332
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6333 GISLGQLDTADLRRDMTLLSQQARLFFGSIR--DNLTMGRPLA---SDEEIHRALALsgaLGFVQkqkngLNYLITEGGA 6407
Cdd:TIGR03269 96 FWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvlDNVLEALEEIgyeGKEAVGRAVDL---IEMVQ-----LSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6408 GLSGGQRQALLLARTLILQPQILLLDEPTAWLD----EISEQQLVANLASWlgNRTLVVATHRIPILQ-LVDRIIVLDNG 6482
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtaKLVHNALEEAVKAS--GISMVLTSHWPEVIEdLSDKAIWLENG 245
|
....*.
gi 701771264 6483 PARDDG 6488
Cdd:TIGR03269 246 EIKEEG 251
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6284-6482 |
1.76e-09 |
|
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: 61.00 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 KVNDLDIAR---LTITAGEKIAVLGRNGSGKSTLLQLLAGMQ--TPQHGQILLDGISLGQLDTAD-LRRDMTLLSQqarl 6357
Cdd:cd03217 9 SVGGKEILKgvnLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEErARLGIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 ffgsirdnltmgRPlasdEEIhralalSGAlgfvqKQKNGLNYLitegGAGLSGGQR------QALLLARTlilqpqILL 6431
Cdd:cd03217 85 ------------YP----PEI------PGV-----KNADFLRYV----NEGFSGGEKkrneilQLLLLEPD------LAI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6432 LDEPTAWLDeISEQQLVANLASWL--GNRTLVVATHRIPILQLV--DRIIVLDNG 6482
Cdd:cd03217 128 LDEPDSGLD-IDALRLVAEVINKLreEGKSVLIITHYQRLLDYIkpDRVHVLYDG 181
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6276-6489 |
1.80e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6276 AFYYDEEEK--VNDLDIArltITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQ---HGQILLDGISLGQLDTADLRRDMTL 6350
Cdd:PRK13640 12 SFTYPDSKKpaLNDISFS---IPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQA-RLFFG-SIRDNLTMG---RPLASDEEI---HRALALSGALGFVQKQKnglnyliteggAGLSGGQRQALLLART 6422
Cdd:PRK13640 89 VFQNPdNQFVGaTVGDDVAFGlenRAVPRPEMIkivRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6423 LILQPQILLLDEPTAWLDEISEQQLVANLASWL--GNRTLVVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3950-4033 |
1.85e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.27 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3950 TLTDSAGNEG--ANSHTVEV-NAARIGLTIDTISHDDVINAAEARQDLT-IGGSSTELA-VGTQVTVTLNGIQYTTTIQP 4024
Cdd:NF012196 2 TSHDAAGNTAtaTAHHTVTIdTHADATITIDTVTGDNVLNAAESQQPTTtITGTVGGDVkVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|...
gi 701771264 4025 GG----GWSVTVP 4033
Cdd:NF012196 82 LGngqlGYSVDVD 94
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1756-1836 |
2.00e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.27 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1756 GNTG--STDHDITIDAQLPG-LRLDTISGDDIINLAE-HNQDLVVSGTCSG-LNAGSVVTVTLNGKDYLATVNADG---- 1826
Cdd:NF012196 8 GNTAtaTAHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLGngql 87
|
90
....*....|
gi 701771264 1827 SWSAAVPAAD 1836
Cdd:NF012196 88 GYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2452-2553 |
2.02e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 58.27 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2452 VKGSSGAGNDV--AIQHQVTVDLT-EVVISINAVTGDNVLNAAE-KGANLELSG-MTQNVEPGQTVNITFAGHTYTATVQ 2526
Cdd:NF012196 1 VTSHDAAGNTAtaTAHHTVTIDTHaDATITIDTVTGDNVLNAAEsQQPTTTITGtVGGDVKVGDPVTLTVNGHTYTGTVV 80
|
90 100
....*....|....*....|....*....
gi 701771264 2527 AD--GSWKYTVPaADMVNLKEGDTAVQVS 2553
Cdd:NF012196 81 DLgnGQLGYSVD-VDTSDLLNNPNDVTAT 108
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6277-6489 |
2.08e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEE--KVNDLDIARLTITAgekiaVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLgqlDTAdlRRDMTLLSQQ 6354
Cdd:PRK13638 9 FRYQDEPvlKGLNLDFSLSPVTG-----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYS--KRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6355 A---------RLFFGSIRDNLTMG-RPLA-SDEEIHR----ALALSGALGFVQKQKNGLnyliteggaglSGGQRQALLL 6419
Cdd:PRK13638 79 VatvfqdpeqQIFYTDIDSDIAFSlRNLGvPEAEITRrvdeALTLVDAQHFRHQPIQCL-----------SHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6420 ARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGN-RTLVVATHRIP-ILQLVDRIIVLDNGPARDDGK 6489
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDlIYEISDAVYVLRQGQILTHGA 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6293-6485 |
2.38e-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: 60.76 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD---------LRRDMTLLSQQarLFFGSIR 6363
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpeergLYPKMKVIDQL--VYLAQLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 DnltMGRplasdEEI-HRALALSGALGFVQKQKNGLNYliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEI 6442
Cdd:cd03269 99 G---LKK-----EEArRRIDEWLERLELSEYANKRVEE--------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 701771264 6443 SeQQLVANLASWL--GNRTLVVATHRIPILQ-LVDRIIVLDNGPAR 6485
Cdd:cd03269 163 N-VELLKDVIRELarAGKTVILSTHQMELVEeLCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6271-6489 |
2.40e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVNdLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTL 6350
Cdd:PRK13648 9 VFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQA-RLFFGSI-RDNLTMG--RPLASDEEIHRALALsgalgfVQKQKNGLNYLITEGGAgLSGGQRQALLLARTLILQ 6426
Cdd:PRK13648 88 VFQNPdNQFVGSIvKYDVAFGleNHAVPYDEMHRRVSE------ALKQVDMLERADYEPNA-LSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6427 PQILLLDEPTAWLDEISEQQLVaNLASWLG---NRTLVVATHRIPILQLVDRIIVLDNGPARDDGK 6489
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLL-DLVRKVKsehNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6298-6482 |
2.48e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---------RRDMTLLSQQArlffgsiRDNLTM 6368
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP-------RDGLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6369 --------GRPLASDEEIH----RALALSGaLGFVQKQKNGLNYLITEggagLSGGQRQALLLARTLILQPQILLLDEPT 6436
Cdd:PRK11701 105 qvsaggniGERLMAVGARHygdiRATAGDW-LERVEIDAARIDDLPTT----FSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6437 AWLDeISEQ----QLVANLASWLGNRTLVVaTHRIPILQLV-DRIIVLDNG 6482
Cdd:PRK11701 180 GGLD-VSVQarllDLLRGLVRELGLAVVIV-THDLAVARLLaHRLLVMKQG 228
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
854-954 |
3.69e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 57.50 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 854 LSVSDKAGNTTTTNAS--LLVDTTPPEA-SVNTVAGDDILSVSEQGQA-QIISGT-SQGAAPGDKVTVSIGSETYQTTVQ 928
Cdd:NF012196 1 VTSHDAAGNTATATAHhtVTIDTHADATiTIDTVTGDNVLNAAESQQPtTTITGTvGGDVKVGDPVTLTVNGHTYTGTVV 80
|
90 100 110
....*....|....*....|....*....|
gi 701771264 929 ADG----SWSVGVPkevISSLPEGPNTITV 954
Cdd:NF012196 81 DLGngqlGYSVDVD---TSDLLNNPNDVTA 107
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6278-6488 |
3.92e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.64 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVND--LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislgqLDTADLRRDMTLLSQQA 6355
Cdd:PRK13633 14 YESNEESTEKlaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-----LDTSDEENLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLF-----------------FGSirDNLTMgRPLASDEEIHRALALSGalgfVQKQKNGLNYLiteggagLSGGQRQALL 6418
Cdd:PRK13633 89 MVFqnpdnqivativeedvaFGP--ENLGI-PPEEIRERVDESLKKVG----MYEYRRHAPHL-------LSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6419 LARTLILQPQILLLDEPTAWLDEISEQQLVANLASWLGNR--TLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3053-3152 |
4.19e-09 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 57.50 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3053 GTSSSGNPVTI--DHTVNVDLSA-VAITIGQIAGDDVLNAAEKGADLLL-SG-MTQNVEAGQTISITFAGHTYTTQV--A 3125
Cdd:NF012196 3 SHDAAGNTATAtaHHTVTIDTHAdATITIDTVTGDNVLNAAESQQPTTTiTGtVGGDVKVGDPVTLTVNGHTYTGTVvdL 82
|
90 100
....*....|....*....|....*..
gi 701771264 3126 SDGSWKFTVPAnDMKGLKDGDTSVEVS 3152
Cdd:NF012196 83 GNGQLGYSVDV-DTSDLLNNPNDVTAT 108
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
6293-6488 |
4.70e-09 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 60.25 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLD------------TADLRRDM--TLLSQQARLF 6358
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWrhigyvpqrhefAWDFPISVahTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 fGSIRdnltmgRPLASDeeiHRALAlsGALGFVQkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAW 6438
Cdd:TIGR03771 81 -GWLR------RPCVAD---FAAVR--DALRRVG-----LTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6439 LDEISEQQLVANLASWLGN-RTLVVATHRIP-ILQLVDRIIVLdNGPARDDG 6488
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGAgTAILMTTHDLAqAMATCDRVVLL-NGRVIADG 194
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
5959-6242 |
5.90e-09 |
|
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: 61.30 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5959 MLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVML--AILFEFTMRMLRVhiadvVGKRADLRISDRVFARA 6036
Cdd:cd18551 5 LLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLlqAVLSALSSYLLGR-----TGERVVLDLRRRLWRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6037 LRIKNSA-RPKSTGSFISQI-RELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLLVQRP 6114
Cdd:cd18551 80 LRLPVSFfDRRRSGDLVSRVtNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6115 LAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLL 6194
Cdd:cd18551 160 IRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 701771264 6195 VGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVARK 6242
Cdd:cd18551 240 VGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALE 287
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6278-6482 |
6.04e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDM------ 6348
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRRQIgmifqh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6349 -TLLSqqARLFFgsirDNLTMGRPLA--SDEEIH-RALALSGALGFVQKQKnglNYlitegGAGLSGGQRQALLLARTLI 6424
Cdd:PRK11153 91 fNLLS--SRTVF----DNVALPLELAgtPKAEIKaRVTELLELVGLSDKAD---RY-----PAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6425 LQPQILLLDEPTAWLDEISEQQLVANLASWlgNR----TLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDvVKRICDRVAVIDAG 217
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
610-885 |
6.22e-09 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 63.13 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 610 GSGQPGATIQVKDANGNTIASTMVDSNGNWKVLLSEQPDGTHTYSVVQID--GNKIT----SAGEITLNVVTAQASLTAa 683
Cdd:NF040520 355 GRAEANAKVQIKDADGKVIGTGTADAQGKFQITLSPALKTSQKGTIIVEDaaGNQSKpleiTAGKDTIAPDKPTAQINA- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 684 ttAGDNTLNAAEQANDFVISGSAtelasgtaltvtlnGKTYAT-TVGSDGSWSVTV-PAADAKSLAdgswtvTVSGKDAA 761
Cdd:NF040520 434 --AGTSVTGTAEANAKIEIKDSA--------------GKVIGTgTADADGKFTITIsPALTDKNIG------KVYAIDAA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 762 GNNISASETL-VVDTQAP------SLTLDILAGDNIINAAEH--NAAVTVSGKtdAEAGQVVTLKLNGKTY-TATVGADG 831
Cdd:NF040520 492 GNRSDATDVTgTKDTIAPnkpvlqKVTDDVGAVKGAIAAGGEtdDAKPKLSGS--GEAKATLTIYDNGQAIgTVTVGDNG 569
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 832 GWSMEVpaadVQAMADNSYTLNLSVSDKAGNT--------------TTTNASLLVDTTPPEASVNTVA 885
Cdd:NF040520 570 KWSFTL----DKDLALGKHKITLTQTDAAGNTsevsdpftftvvapKTASASEQSEVDTSNTETASLA 633
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6279-6482 |
6.28e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.77 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL-GQLDTAdlRRDMTLLSQQARL 6357
Cdd:PRK13536 51 YGDKAVVNGLS---FTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 ---FfgSIRDNLTM-GRPLA-SDEEIHRalALSGALGFVQKQKNGlNYLITEggagLSGGQRQALLLARTLILQPQILLL 6432
Cdd:PRK13536 126 dleF--TVRENLLVfGRYFGmSTREIEA--VIPSLLEFARLESKA-DARVSD----LSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6433 DEPTAWLDEISEQQLVANLASWLG-NRTLVVATHRIPILQ-LVDRIIVLDNG 6482
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAErLCDRLCVLEAG 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6290-6482 |
6.60e-09 |
|
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: 63.49 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6290 IARLTITAGEK--IAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL-GQLDTadLRRDMTLLSQQARLFFG-SIRDN 6365
Cdd:TIGR01257 946 VDRLNITFYENqiTAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA--VRQSLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6366 LTMGRPLASDEEIHRALALSGALgfvqkQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQ 6445
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAML-----EDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190
....*....|....*....|....*....|....*...
gi 701771264 6446 QLVANLASWLGNRTLVVATHRIPILQLV-DRIIVLDNG 6482
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQG 1136
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6303-6482 |
6.98e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6303 VLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD----------------LRRDMTLLSQ--QARLFFGSIRD 6364
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6365 NLTMGrPLASDeeIHRALALSGALGFVQKQknGLNYLITEGGA-GLSGGQRQALLLARTLILQPQILLLDEPTAWLDEIS 6443
Cdd:PRK13631 137 DIMFG-PVALG--VKKSEAKKLAKFYLNKM--GLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 701771264 6444 EQQLVA-NLASWLGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:PRK13631 212 EHEMMQlILDAKANNKTVFVITHTMEhVLEVADEVIVMDKG 252
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
6143-6240 |
7.03e-09 |
|
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: 60.88 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6143 IKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTGALVgTSILASRTIA 6222
Cdd:cd18547 197 VKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQ-AFLQYSRQFS 275
|
90
....*....|....*....
gi 701771264 6223 -PLAQISGVLSRWQQAKVA 6240
Cdd:cd18547 276 qPINQISQQINSLQSALAG 294
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6271-6468 |
9.69e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVN--DLDIARLTITAgekiaVLGRNGSGKSTLLQLLAGMQTPQhGQILLDG--------ISLGQLD 6340
Cdd:PRK14258 9 KVNNLSFYYDTQKILEgvSMEIYQSKVTA-----IIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6341 TADLRRDMTLLSQQARLFFGSIRDNLTMGRPLASdeeIHRALALSGALGFVQKQK---NGLNYLITEGGAGLSGGQRQAL 6417
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVG---WRPKLEIDDIVESALKDAdlwDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6418 LLARTLILQPQILLLDEPTAWLDEISE---QQLVANLaSWLGNRTLVVATHRIP 6468
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSL-RLRSELTMVIVSHNLH 212
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
5958-6237 |
1.01e-08 |
|
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: 60.60 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPT----LWVLFGGVMLAILFEFTMRMLRVHIADVVGKR--ADLRisDR 6031
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGntslLLLLVLGLAGAYVLSALLGILRGRLLARLGERitADLR--RD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6032 VFARALRIKNS--ARpKSTGSFISQI-RELESVRELITSTTIGTVSDIpffLLFVFIL-------W------LIGGPLVF 6095
Cdd:cd18563 82 LYEHLQRLSLSffDK-RQTGSLMSRVtSDTDRLQDFLSDGLPDFLTNI---LMIIGIGvvlfslnWklallvLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6096 VVLLAiplllipgllVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMK--QRWL 6173
Cdd:cd18563 158 WGSYF----------FWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRaeKLWA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6174 T-----SLLMtwtqevqSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQA 6237
Cdd:cd18563 228 TffpllTFLT-------SLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRA 289
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2552-2652 |
1.13e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.96 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2552 VSVTNKNGNSTDAA--QNVSVDTLAPA-LTVDPVSQDNLLNAAEAKQDLV-ISGTST--AEAGQTVTVRLNGESYQATVK 2625
Cdd:NF012196 1 VTSHDAAGNTATATahHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVV 80
|
90 100 110
....*....|....*....|....*....|.
gi 701771264 2626 ADG----SWSLTVPAADvgkLTDGNITVTAS 2652
Cdd:NF012196 81 DLGngqlGYSVDVDTSD---LLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2353-2439 |
1.32e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.96 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2353 SVTNGHGNTG--SGSRDIVIDANLPG-LRVDTVAGDDVINAIE-HTQNLIINGTSSG-LGAGSAVTVTINGKDYAATVRA 2427
Cdd:NF012196 2 TSHDAAGNTAtaTAHHTVTIDTHADAtITIDTVTGDNVLNAAEsQQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 2428 DG----SWQAAVPGED 2439
Cdd:NF012196 82 LGngqlGYSVDVDTSD 97
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6279-6489 |
1.35e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.20 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLdtadlrrdmtllSQQARLF 6358
Cdd:PRK13537 17 YGDKLVVDGLS---FHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR------------ARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG------------SIRDNLTM-GRPLASDEEIHRALaLSGALGFVqKQKNGLNYLITEggagLSGGQRQALLLARTLIL 6425
Cdd:PRK13537 82 VGvvpqfdnldpdfTVRENLLVfGRYFGLSAAAARAL-VPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6426 QPQILLLDEPTAWLDEISEQQLVANLASWLGN-RTLVVATHRIPILQ-LVDRIIVLDNGPARDDGK 6489
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGA 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6118-6488 |
1.44e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6118 LSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVyaVVLLVGC 6197
Cdd:PLN03130 467 LTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLV--TVVSFGV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6198 YLVINGDMTTG-ALVGTSILASRTIaPLAQISGVLSRWQQAKVARKGLDDLM---QRPL-DDPEEGKKVHKAHLQGNYql 6272
Cdd:PLN03130 545 FTLLGGDLTPArAFTSLSLFAVLRF-PLFMLPNLITQAVNANVSLKRLEELLlaeERVLlPNPPLEPGLPAISIKNGY-- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6273 nyaaFYYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLdgislgqldtadLRRDMTLLS 6352
Cdd:PLN03130 622 ----FSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVP 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6353 QQARLFFGSIRDNLTMGRPLASdEEIHRALALSGALGFVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSPFDP-ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6433 DEPTAWLDEISEQQLVAN-LASWLGNRTLVVATHRIPILQLVDRIIVLDNGPARDDG 6488
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
4051-4138 |
1.47e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.96 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4051 SATDSANNATSAT--HNISVDTVAPI-VTIADISGDNAINAAEQQQPLT-IRGTSS--AEAGQKVTVKLGSESYEATVQA 4124
Cdd:NF012196 2 TSHDAAGNTATATahHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTVGgdVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*...
gi 701771264 4125 DG----SWSITVAAEDLA 4138
Cdd:NF012196 82 LGngqlGYSVDVDTSDLL 99
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6271-6441 |
1.59e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAAFYYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTL 6350
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNIS---FSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQARLFFGSIRDNLTMG---RPLASDEEIHRALALSGALGFVQKQKNglnylITEggagLSGGQRQALLLARTLILQP 6427
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDDLERFALPDTILTKN-----IAE----LSGGEKQRISLIRNLQFMP 156
|
170
....*....|....
gi 701771264 6428 QILLLDEPTAWLDE 6441
Cdd:PRK10247 157 KVLLLDEITSALDE 170
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6277-6482 |
1.65e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6277 FYYDEEEKVNDLDIarlTITAGEKIAVLGRNGSGKSTLLQLLAGM------QTPQHGQILLDGISLGQLDTADLRRDMTL 6350
Cdd:PRK14246 18 LYINDKAILKDITI---KIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQARLF-FGSIRDNLTMgrPLAS-----DEEIHRALALS-GALGFVQKQKNGLNYLITEggagLSGGQRQALLLARTL 6423
Cdd:PRK14246 95 VFQQPNPFpHLSIYDNIAY--PLKShgikeKREIKKIVEEClRKVGLWKEVYDRLNSPASQ----LSGGQQQRLTIARAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6424 ILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATHR-IPILQLVDRIIVLDNG 6482
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNG 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6295-6482 |
1.69e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.50 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLL-QLLAGMQTPQhGQILLDGISLGQLDTADL----RRDMTLLSQQARLFFGSIRDNLTMG 6369
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVEENITFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 RPLasDEEIHRALALSGALG-FVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD-EISEQQL 6447
Cdd:cd03290 103 SPF--NKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLM 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 701771264 6448 VANLASWLGN--RTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:cd03290 181 QEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6281-6482 |
1.80e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.79 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6281 EEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTAD-----LRRDMTLLSQ-- 6353
Cdd:PRK13646 19 EHQAIHDVN---TEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDkyirpVRKRIGMVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 QARLFFGSIRDNLTMGrP----LASDEEIHRALALSGALGFVQKqknglnyLITEGGAGLSGGQRQALLLARTLILQPQI 6429
Cdd:PRK13646 95 ESQLFEDTVEREIIFG-PknfkMNLDEVKNYAHRLLMDLGFSRD-------VMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6430 LLLDEPTAWLDEISEQQLVANLASWL--GNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMnEVARYADEVIVMKEG 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6288-6482 |
1.95e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.46 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL----GQLDTADLRRDMTLLSQ--QARLFFGS 6361
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 IRDNLTMGrPL---ASDEEihralALSGALGFVQKQknGLNY-LITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:PRK13641 103 VLKDVEFG-PKnfgFSEDE-----AKEKALKWLKKV--GLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6438 WLDEISEQQLVANLASW-LGNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYqKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6285-6451 |
2.31e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 59.75 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQArlfFGS 6361
Cdd:COG4608 34 VDGVS---FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP---YAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 IRDNLTMGRPLASDEEIHRALALSGALGFVQK--QKNGLNylitEGGAG-----LSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:COG4608 108 LNPRMTVGDIIAEPLRIHGLASKAERRERVAEllELVGLR----PEHADrypheFSGGQRQRIGIARALALNPKLIVCDE 183
|
170
....*....|....*..
gi 701771264 6435 PTAWLDeISEQQLVANL 6451
Cdd:COG4608 184 PVSALD-VSIQAQVLNL 199
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1256-1353 |
2.36e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.18 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1256 DESGNPVAAT--RPVDVDLNA-VAISINSVTSDGVLNAVEKAADLTL-SGKTLG-VEAGQTVVIKFAGHTYTTTV--NQS 1328
Cdd:NF012196 5 DAAGNTATATahHTVTIDTHAdATITIDTVTGDNVLNAAESQQPTTTiTGTVGGdVKVGDPVTLTVNGHTYTGTVvdLGN 84
|
90 100
....*....|....*....|....*
gi 701771264 1329 GDWTFTVPaADMRDMIDGRADVSVS 1353
Cdd:NF012196 85 GQLGYSVD-VDTSDLLNNPNDVTAT 108
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6288-6488 |
2.40e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.34 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTP-----QHGQILLDGISL-GQLDTADLRRDMTLLSQQARLFFGS 6361
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6362 IRDNLTMG---RPLASDEEIHR-ALALSGALGFVQKQKNGLnyliTEGGAGLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:PRK14271 117 IMDNVLAGvraHKLVPRKEFRGvAQARLTEVGLWDAVKDRL----SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6438 WLDEISEQQLVANLASWLGNRTLVVATHRIP-ILQLVDRIIVLDNGPARDDG 6488
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEG 244
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6284-6482 |
2.41e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 KVNDLDIAR---LTITAGEKIAVLGRNGSGKSTLLQLLAG--MQTPQHGQILLDGISLGQLDTaDLRrdmtllsqqAR-- 6356
Cdd:COG0396 9 SVEGKEILKgvnLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSP-DER---------ARag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6357 LFFG----------SIRD------NLTMGRPLASDEEIHRALALSGALG----FVQKqknGLNyliteggAGLSGGQR-- 6414
Cdd:COG0396 79 IFLAfqypveipgvSVSNflrtalNARRGEELSAREFLKLLKEKMKELGldedFLDR---YVN-------EGFSGGEKkr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6415 ----QALLLartlilqpqillldEPT-AWLDE------ISEQQLVANLASWL--GNRTLVVATHRIPILQLV--DRIIVL 6479
Cdd:COG0396 149 neilQMLLL--------------EPKlAILDEtdsgldIDALRIVAEGVNKLrsPDRGILIITHYQRILDYIkpDFVHVL 214
|
...
gi 701771264 6480 DNG 6482
Cdd:COG0396 215 VDG 217
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
6046-6238 |
2.59e-08 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain] Cd Length: 294 Bit Score: 59.38 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6046 KSTGSFISQIRELESVRELITSTTIGTV-S--------------DIPFFLLF-----VFILWLiggpLVFvvllaiplll 6105
Cdd:cd18571 96 KMTGDILQRINDHSRIESFLTSSSLSILfSllnlivfsivlayyNLTIFLIFligsvLYILWI----LLF---------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6106 ipgllvQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKqrwltslLMTWTQeVQ 6185
Cdd:cd18571 162 ------LKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIK-------SLKLDQ-YQ 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6186 SIVYA--------VVLLVGCYLVINGDMTTGALVGTS-ILASrTIAPLAQISGVLSRWQQAK 6238
Cdd:cd18571 228 QIGALfinqlkniLITFLAAKLVIDGEITLGMMLAIQyIIGQ-LNSPIEQLIGFIQSLQDAK 288
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3353-3439 |
2.61e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 55.18 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3353 TDSAGNTG--SGSHEVTVNTGLP-SVNFNAISGDNVLNAIE-KGEVLTLSGT-SANLAPGTAVIVTLNGKNYTATTDASG 3427
Cdd:NF012196 4 HDAAGNTAtaTAHHTVTIDTHADaTITIDTVTGDNVLNAAEsQQPTTTITGTvGGDVKVGDPVTLTVNGHTYTGTVVDLG 83
|
90
....*....|....*.
gi 701771264 3428 N----WRVDVQPGDLA 3439
Cdd:NF012196 84 NgqlgYSVDVDTSDLL 99
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3655-3751 |
3.49e-08 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 54.80 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3655 SAGNP--ISIDRSVNVDLS-PVAVSVENITADNVLNAAEKGADLVL-SGK-TQNVEAGQTVTITFGGRTYTAQVESD--G 3727
Cdd:NF012196 6 AAGNTatATAHHTVTIDTHaDATITIDTVTGDNVLNAAESQQPTTTiTGTvGGDVKVGDPVTLTVNGHTYTGTVVDLgnG 85
|
90 100
....*....|....*....|....
gi 701771264 3728 SWHYTVPAsDIAGLKDGDASVKVS 3751
Cdd:NF012196 86 QLGYSVDV-DTSDLLNNPNDVTAT 108
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
3786-3957 |
3.91e-08 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 60.44 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3786 INAAeagaGVTVTGTSNAQAGQTVTLTlDGKT-YTGVVKADGTWSITLDStalgALADNQyVIKVDVSDAAGNKTTGSQ- 3863
Cdd:NF040520 431 INAA----GTSVTGTAEANAKIEIKDS-AGKViGTGTADADGKFTITISP----ALTDKN-IGKVYAIDAAGNRSDATDv 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3864 NMTLDTTAPTVSFNAVAGDDIINLeehaQAQIISGSST--------GAAAGNKIIITLDGVQYV--TQVDAKGNWSVgvp 3933
Cdd:NF040520 501 TGTKDTIAPNKPVLQKVTDDVGAV----KGAIAAGGETddakpklsGSGEAKATLTIYDNGQAIgtVTVGDNGKWSF--- 573
|
170 180
....*....|....*....|....
gi 701771264 3934 aSAVSALKNGTATITATLTDSAGN 3957
Cdd:NF040520 574 -TLDKDLALGKHKITLTQTDAAGN 596
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
6287-6482 |
4.94e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6287 DLDIaRLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLD---------GISLgqldTADLRRdMTLLSQQARL 6357
Cdd:PRK11144 14 CLTV-NLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekGICL----PPEKRR-IGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 F-FGSIRDNLTMGRPLASDEEIHRALALSGalgfvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPT 6436
Cdd:PRK11144 88 FpHYKVRGNLRYGMAKSMVAQFDKIVALLG-----------IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6437 AWLDEISEQQLVA---NLASWLgNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK11144 157 ASLDLPRKRELLPyleRLAREI-NIPILYVSHSLdEILRLADRVVVLEQG 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6285-6489 |
6.33e-08 |
|
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: 59.43 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQI-------LLDGISLGQLDTADLRRDMTLLSQQARL 6357
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 F-FGSIRDNLT--MGRPLASDEEIHRALALSGALGFVQKQ-KNGLNYLITEggagLSGGQRQALLLARTLILQPQILLLD 6433
Cdd:TIGR03269 377 YpHRTVLDNLTeaIGLELPDELARMKAVITLKMVGFDEEKaEEILDKYPDE----LSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6434 EPTAWLDEISEQQLVANL--ASWLGNRTLVVATHRIP-ILQLVDRIIVLDNGPARDDGK 6489
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIGD 511
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6293-6443 |
7.34e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLD--GISLGQLDtADLRRDMTLLSQQARLFFG-SIRDN---- 6365
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLH-ARARRGIGYLPQEASIFRRlSVYDNlmav 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6366 LTMGRPLASDEEIHRALALsgalgfvqKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEIS 6443
Cdd:PRK10895 103 LQIRDDLSAEQREDRANEL--------MEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
|
| FG-GAP_3 |
pfam13517 |
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ... |
5270-5342 |
7.84e-08 |
|
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.
Pssm-ID: 433275 [Multi-domain] Cd Length: 61 Bit Score: 52.23 E-value: 7.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 5270 DLNNDGMVDIAQHTTNGGNIYalstmFNKGDGTFTWSQNFIntmysatgSAAANNAVSMTWADFDGDGYMDLY 5342
Cdd:pfam13517 1 DLDGDGKLDLVVANDGGLRLY-----LNNGDGTFTFITSVS--------LGGGGGGLSVAVGDLDGDGRLDLL 60
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
4859-5018 |
8.25e-08 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 59.28 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4859 VRIIDQAGNVGSTANQVVTVDTVAPDTvGSIVSYTDNNGERTGNFDSSYSTDDTSPVLNGTlnqaladGE---IAQIFRD 4935
Cdd:NF040520 485 VYAIDAAGNRSDATDVTGTKDTIAPNK-PVLQKVTDDVGAVKGAIAAGGETDDAKPKLSGS-------GEakaTLTIYDN 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4936 GVLVGNVTITGGTRWTFA-DSGLLDGSYHYVLRVTDKAGNYTE-SNDFGLTVDTSVPTTKALVNGLNTTDT-TPIITGSV 5012
Cdd:NF040520 557 GQAIGTVTVGDNGKWSFTlDKDLALGKHKITLTQTDAAGNTSEvSDPFTFTVVAPKTASASEQSEVDTSNTeTASLADSV 636
|
....*.
gi 701771264 5013 DANLVH 5018
Cdd:NF040520 637 GLNTLK 642
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6295-6482 |
8.75e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQH--GQILLDGislGQLDTADLRR------DMTL---LSQQARLFFGSIr 6363
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILKRtgfvtqDDILyphLTVRETLVFCSL- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6364 dnLTMGRPLASDEEIHRALALSGALGFVqKQKNGL--NYLITeggaGLSGGQRQALLLARTLILQPQILLLDEPTAWLDE 6441
Cdd:PLN03211 167 --LRLPKSLTKQEKILVAESVISELGLT-KCENTIigNSFIR----GISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701771264 6442 ISEQQLVANLASwLGN--RTLVVATHRIP--ILQLVDRIIVLDNG 6482
Cdd:PLN03211 240 TAAYRLVLTLGS-LAQkgKTIVTSMHQPSsrVYQMFDSVLVLSEG 283
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
2523-2960 |
9.29e-08 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 59.28 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2523 ATVQADGSWKYTVPAADmvNLKEGDTaVQVSVTNKNGNSTDAAQNV-SVDTLAPaltVDPVSQdnlLNAaeakQDLVISG 2601
Cdd:NF040520 204 ATGQADASGNYTIKLDQ--PLVNGNK-VNVTAIDAAGNASKATVVTgTKDTIAP---DAPQAQ---LNA----DGTIVTG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2602 TstAEAGQTVTVrlngesYQA------TVKA--DGSWSLTVPAAdvgkLTDGNI-TVTAsvEDQAGNPGSASRDVLVDVT 2672
Cdd:NF040520 271 K--TEANAKVSV------YDAdgkllgTVTAnkEGLYSIKVSPP----LTSDKGgTVIA--EDAAGNKSEPSKIIAGKDT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2673 V----PKVTIGTMATddVINQTEHGQALVISGTSTGAQAGdivtvtlgnkqyTGVVDTNGNWSVGVPradvSALGDNTyT 2748
Cdd:NF040520 337 IapdqPLVEVNKEGT--SIEGRAEANAKVQIKDADGKVIG------------TGTADAQGKFQITLS----PALKTSQ-K 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2749 VTASITDKAGNTgdtSHTVTVdtvapTLSIDTIAGDNI---LNADektGDVVisgtsTGLA-AGTSVTV-NLNGKN-YAA 2822
Cdd:NF040520 398 GTIIVEDAAGNQ---SKPLEI-----TAGKDTIAPDKPtaqINAA---GTSV-----TGTAeANAKIEIkDSAGKViGTG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2823 TVGADGKWTTTV-PAGDVGKLGeafyevSVSASNGVGNagsQSSTLEVASTLPGV-----IINAVaIDDI--INAAELAT 2894
Cdd:NF040520 462 TADADGKFTITIsPALTDKNIG------KVYAIDAAGN---RSDATDVTGTKDTIapnkpVLQKV-TDDVgaVKGAIAAG 531
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 2895 GQT------ISGRvtgVQAGADVTINIGGVNY-TAKVQSDLTWSLTLGQDvltaLGDGSLKINASVTDGAGNT 2960
Cdd:NF040520 532 GETddakpkLSGS---GEAKATLTIYDNGQAIgTVTVGDNGKWSFTLDKD----LALGKHKITLTQTDAAGNT 597
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6293-6482 |
9.89e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRR-DMTLLSQQARLFFG-SIRDNLTMGR 6370
Cdd:PRK15439 32 FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVKENILFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 PlASDEEIHRALALSGALGfVQkqknglnyLITEGGAG-LSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVA 6449
Cdd:PRK15439 112 P-KRQASMQKMKQLLAALG-CQ--------LDLDSSAGsLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFS 181
|
170 180 190
....*....|....*....|....*....|....*
gi 701771264 6450 NLASWLGNRT-LVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:PRK15439 182 RIRELLAQGVgIVFISHKLPeIRQLADRISVMRDG 216
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2679-2771 |
1.10e-07 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 53.04 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2679 GTMATDDVINQTehgqALVISGTstgAQAGDIVTVTL----GNKQYTGVVDTNGNWSVGVPradvSALGDNTYTVTASIT 2754
Cdd:pfam19077 16 GVSDSDNITNDT----TPTFTGT---NEDGDVVTVTVsidgNGVTGTATAGADGNWSFTPP----AALADGTYTLTVTVT 84
|
90
....*....|....*...
gi 701771264 2755 DKAGNTGDTSH-TVTVDT 2771
Cdd:pfam19077 85 DIAGNTATSSPlSFTIDT 102
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1650-1750 |
1.47e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.87 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1650 SVTDASGNA--NSASHSVLVDSSLPI-ITINAVAGDNIINLAEVNAGQVL-TGSVI-NAAAGDEVTVILGGKSYTVIVQS 1724
Cdd:NF012196 2 TSHDAAGNTatATAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTTiTGTVGgDVKVGDPVTLTVNGHTYTGTVVD 81
|
90 100 110
....*....|....*....|....*....|
gi 701771264 1725 D----LSWNLPLSKemlTALGDGDLTVHAS 1750
Cdd:NF012196 82 LgngqLGYSVDVDT---SDLLNNPNDVTAT 108
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1851-1950 |
1.59e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.87 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1851 AQDGAQNP--IGIDGIVDVDL-APVSISVNSVTADNVLNAAEKGVDLVL-SGLTT-NVEPGQTVTITFAGHRYTTSV--N 1923
Cdd:NF012196 3 SHDAAGNTatATAHHTVTIDThADATITIDTVTGDNVLNAAESQQPTTTiTGTVGgDVKVGDPVTLTVNGHTYTGTVvdL 82
|
90 100
....*....|....*....|....*..
gi 701771264 1924 NDGSWSYTVPaADMARLKDGDAQVTVS 1950
Cdd:NF012196 83 GNGQLGYSVD-VDTSDLLNNPNDVTAT 108
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6293-6474 |
1.80e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQQARLFFG-SIRDNLTM 6368
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTDmNVFDNVAY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6369 grPLASDEEIHRALALSGALgfVQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQ--- 6445
Cdd:PRK11831 108 --PLREHTQLPAPLLHSTVM--MKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGvlv 183
|
170 180 190
....*....|....*....|....*....|
gi 701771264 6446 QLVANLASWLGnRTLVVATHRIP-ILQLVD 6474
Cdd:PRK11831 184 KLISELNSALG-VTCVVVSHDVPeVLSIAD 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6294-6451 |
1.82e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTA---DLRRDMTLLSQQArlfFGSIRDNLTMGR 6370
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNP---YGSLNPRKKVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 PLASDEEIH----------RALALSGALGFVQKQKNGLNYLiteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:PRK11308 114 ILEEPLLINtslsaaerreKALAMMAKVGLRPEHYDRYPHM-------FSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170
....*....|.
gi 701771264 6441 eISEQQLVANL 6451
Cdd:PRK11308 187 -VSVQAQVLNL 196
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
566-696 |
1.85e-07 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 58.13 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 566 TEVIDNTKPVESARPTFM-VTDNKGDSQGLLSSNAVTDDSTPTFSGSGQPGATIQVKDaNGNTIASTMVDSNGNWKVLLS 644
Cdd:NF040520 498 TDVTGTKDTIAPNKPVLQkVTDDVGAVKGAIAAGGETDDAKPKLSGSGEAKATLTIYD-NGQAIGTVTVGDNGKWSFTLD 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 645 -EQPDGTHTYSVVQIDGNKITS--AGEITLNVVTAQASLTAATTAGDnTLNAAEQ 696
Cdd:NF040520 577 kDLALGKHKITLTQTDAAGNTSevSDPFTFTVVAPKTASASEQSEVD-TSNTETA 630
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
954-1039 |
1.91e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.49 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 954 VAITDVAGNTGT--TTHDITVSSTPPN-VAFNAISQDNVLNAIEATQPLIL-SGT--SNLPDGSHVTVTLNNVNYTAQVQ 1027
Cdd:NF012196 1 VTSHDAAGNTATatAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTTiTGTvgGDVKVGDPVTLTVNGHTYTGTVV 80
|
90
....*....|....*..
gi 701771264 1028 GG-----VWQVQVPVSD 1039
Cdd:NF012196 81 DLgngqlGYSVDVDTSD 97
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1076-1153 |
2.09e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 52.49 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1076 TVIVSTFAGDNRVNNSEIAND-QMLSGRVTG-AHQGDTVTINIGGKNYTATVQSD----LTWSTTVPAADLRalgDGDVS 1149
Cdd:NF012196 28 TITIDTVTGDNVLNAAESQQPtTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLgngqLGYSVDVDTSDLL---NNPND 104
|
....
gi 701771264 1150 IVAS 1153
Cdd:NF012196 105 VTAT 108
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
607-815 |
2.26e-07 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 57.74 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 607 TFSGSGQPGATIQVKDANGNTIASTMVDSNGNWKVLLSEQPDGTHTYSVVQID--GNKITSAGEITLNVVTAQASLTAAT 684
Cdd:NF040520 437 SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITISPALTDKNIGKVYAIDaaGNRSDATDVTGTKDTIAPNKPVLQK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 685 TAGDN-----TLNAAEQANDF--VISGSAtelASGTALTVTLNGKTYAT-TVGSDGSWSVTVpaadAKSLADGSWTVTVS 756
Cdd:NF040520 517 VTDDVgavkgAIAAGGETDDAkpKLSGSG---EAKATLTIYDNGQAIGTvTVGDNGKWSFTL----DKDLALGKHKITLT 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 757 GKDAAGNNISASETLVVDTQAPSLTLDILAGDNIINAAEHNAAVTVSGKTDAEAGQVVT 815
Cdd:NF040520 590 QTDAAGNTSEVSDPFTFTVVAPKTASASEQSEVDTSNTETASLADSVGLNTLKLAQETT 648
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6294-6482 |
3.19e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGislGQLDTADLRrdmtLLSQQARLFF-------------G 6360
Cdd:PRK15112 35 TLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGDYS----YRSQRIRMIFqdpstslnprqriS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 SIRD-NLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNYLiteggagLSGGQRQALLLARTLILQPQILLLDEPTAWL 6439
Cdd:PRK15112 108 QILDfPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-------LAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6440 DEISEQQLVaNLASWL----GNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK15112 181 DMSMRSQLI-NLMLELqekqGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2052-2154 |
3.43e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 51.72 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2052 DKAGNP--ANADRGMRVDIT-EPKLSIDPVAGDDIINASEHSQAHT-VGGTSTG-AAAGDVVTVVVtNGQgtsfTFTTTL 2126
Cdd:NF012196 5 DAAGNTatATAHHTVTIDTHaDATITIDTVTGDNVLNAAESQQPTTtITGTVGGdVKVGDPVTLTV-NGH----TYTGTV 79
|
90 100 110
....*....|....*....|....*....|..
gi 701771264 2127 DGNGN----WNVGIPASVingLADGSYTITAS 2154
Cdd:NF012196 80 VDLGNgqlgYSVDVDTSD---LLNNPNDVTAT 108
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4355-4457 |
3.58e-07 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 51.50 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4355 TPPQMTITIDsLQNDTGLSASDFITADNKVVVkgSLSGALGNNEKAQISLDGGKTWTDLVV-TGTSWAY-ADGPLPDGTV 4432
Cdd:pfam19077 1 TLSIPTIDLA-AGSDTGVSDSDNITNDTTPTF--TGTNEDGDVVTVTVSIDGNGVTGTATAgADGNWSFtPPAALADGTY 77
|
90 100
....*....|....*....|....*
gi 701771264 4433 TYHVRVVDNAGNVGSTATKNVTVDT 4457
Cdd:pfam19077 78 TLTVTVTDIAGNTATSSPLSFTIDT 102
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6284-6482 |
3.96e-07 |
|
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: 53.59 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 KVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL-----------RRDMTLLS 6352
Cdd:cd03215 15 AVRDVS---FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragiayvpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6353 QQarlffgSIRDNLTMGRplasdeeihralalsgalgfvqkqknglnyliteggaGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:cd03215 92 DL------SVAENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6433 DEPTAWLD-----EIseQQLVANLASwlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:cd03215 129 DEPTRGVDvgakaEI--YRLIRELAD--AGKAVLLISSELDeLLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6293-6482 |
3.97e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.41 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILL--DGISLG--QLDTADLRRDMTLLSQ--QARLFFGSIRDNL 6366
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgeRVITAGkkNKKLKPLRKKVGIVFQfpEHQLFEETVEKDI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6367 TMGrPL---ASDEEihrALAL-SGALGFVqkqknGLNY-LITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD- 6440
Cdd:PRK13634 108 CFG-PMnfgVSEED---AKQKaREMIELV-----GLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDp 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6441 ----EISEqqLVANLASwLGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:PRK13634 179 kgrkEMME--MFYKLHK-EKGLTTVLVTHSMEdAARYADQIVVMHKG 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6285-6348 |
4.24e-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: 56.62 E-value: 4.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQtPQHGQILLDGISLGQLDTAD---LRRDM 6348
Cdd:COG4172 302 VDGVS---LTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRM 364
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6295-6440 |
4.55e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISlgqLDTADLRRDMTLLSQQARLffgsirdnltmGRPLAS 6374
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT---ATRGDRSRFMAYLGHLPGL-----------KADLST 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6375 DEEIHRALALSGAlgfvQKQKNGLNYLITEGGAG--------LSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:PRK13543 100 LENLHFLCGLHGR----RAKQMPGSALAIVGLAGyedtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6285-6453 |
4.62e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.65 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGIslgqlDTADL------RRDMTLLSQQARLF 6358
Cdd:COG1137 19 VKDVS---LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE-----DITHLpmhkraRLGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG-SIRDNLTM---GRPLASDEEIHRALALSGALGF--VQKQKnglnylitegGAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:COG1137 91 RKlTVEDNILAvleLRKLSKKEREERLEELLEEFGIthLRKSK----------AYSLSGGERRRVEIARALATNPKFILL 160
|
170 180
....*....|....*....|....
gi 701771264 6433 DEPTAWLDEIS--E-QQLVANLAS 6453
Cdd:COG1137 161 DEPFAGVDPIAvaDiQKIIRHLKE 184
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
1504-1564 |
4.65e-07 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 51.50 E-value: 4.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 1504 GAAVGDSVKITVNGVEYSTVLDASGNWSLGLPAEvisgLADGKYTATVVVTDKAGNVGGSS 1564
Cdd:pfam19077 38 GDVVTVTVSIDGNGVTGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGNTATSS 94
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6276-6482 |
5.01e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6276 AFYYDEEEK--VNDLDiarLTITAGEKIAVLGRNGSGKS-TLLQLLAGMQTPQ----HGQILLDGISLGQLDTADLRR-- 6346
Cdd:PRK15134 14 AFRQQQTVRtvVNDVS---LQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6347 --DMTLLSQQARLffgSIRDNLTMGRPLASDEEIHRALALSGALG---------FVQKQKNGLNYLITEggagLSGGQRQ 6415
Cdd:PRK15134 91 gnKIAMIFQEPMV---SLNPLHTLEKQLYEVLSLHRGMRREAARGeilncldrvGIRQAAKRLTDYPHQ----LSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6416 ALLLARTLILQPQILLLDEPTAWLDeISEQ----QLVANLASWLgNRTLVVATHRIPIL-QLVDRIIVLDNG 6482
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALD-VSVQaqilQLLRELQQEL-NMGLLFITHNLSIVrKLADRVAVMQNG 233
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2604-2659 |
5.13e-07 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 51.11 E-value: 5.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2604 TAEAGQTVTVRL----NGESYQATVKADGSWSLTVPAAdvgkLTDGNITVTASVEDQAGN 2659
Cdd:pfam19077 34 TNEDGDVVTVTVsidgNGVTGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGN 89
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6280-6453 |
5.46e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6280 DEEEKVNDLdiaRLTITAGEKIAVLGRNGSGKST----LLQLLAgmqtpQHGQILLDGISLGQLDtadlRRDMTLLSQQA 6355
Cdd:PRK15134 297 DHNVVVKNI---SFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLN----RRQLLPVRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 RLFF----GSIRDNLTMGRPLASDEEIHRAlALSGAlgfvqKQKNGLNYLITEGG----------AGLSGGQRQALLLAR 6421
Cdd:PRK15134 365 QVVFqdpnSSLNPRLNVLQIIEEGLRVHQP-TLSAA-----QREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIAR 438
|
170 180 190
....*....|....*....|....*....|..
gi 701771264 6422 TLILQPQILLLDEPTAWLDEISEQQLVANLAS 6453
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
2875-2952 |
5.52e-07 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 51.33 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2875 GVIINAVAIDDIINAAEL-ATGQTISGRVTG-VQAGADVTINIGGVNYTAKVQSD----LTWSLtlgqDVLT-ALGDGSL 2947
Cdd:NF012196 28 TITIDTVTGDNVLNAAESqQPTTTITGTVGGdVKVGDPVTLTVNGHTYTGTVVDLgngqLGYSV----DVDTsDLLNNPN 103
|
....*
gi 701771264 2948 KINAS 2952
Cdd:NF012196 104 DVTAT 108
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
712-775 |
5.54e-07 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 51.11 E-value: 5.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 712 GTALTVTL----NGKTYATTVGSDGSWSVTVPAAdaksLADGSWTVTVSGKDAAGN-NISASETLVVDT 775
Cdd:pfam19077 38 GDVVTVTVsidgNGVTGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGNtATSSPLSFTIDT 102
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2400-3040 |
6.51e-07 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 56.32 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2400 NGTSSGLGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWAEGAVTIEVKGSSGAGNDVAIQHQVTVDLTEVVISI 2479
Cdd:COG5295 11 GTALTTVASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAASSVASGGASA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2480 NAVTGDNVLNAAEKGANLELSGMTQNVEPGQTVNITFAGhTYTATVQADGSWKYTVPAADMVNLKEGDTAVQVSVTNKNG 2559
Cdd:COG5295 91 ATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAA-AAAGSTAAAGGAAASTGGSSAAGGSNTATATGSSTANAAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2560 NSTDAAQNVSVDTLAPALTVDPVSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSLTVPAADV 2639
Cdd:COG5295 170 AAAGATSTSASGSSSGASGAAAASAATGASAGGTASAAASASSSATGTSASVGVNAGAATGSAASAGGSASAGAASGNAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2640 GKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTGAQAGDIVTVTLGNKQ 2719
Cdd:COG5295 250 TASASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2720 YTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGDTSHTVTVDTVAPTLSIDTIAGDNILNADEKTGDVVIS 2799
Cdd:COG5295 330 SGVGTASGASAAAATNDGTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGGSSTGASAGG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2800 GTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLGEAFYEVSVSASNGVGNAGSQSSTLEVASTLPGVIIN 2879
Cdd:COG5295 410 GASAAGGAAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAAATAAAATSSAAIAG 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2880 AVAIDDIINAAELATGQTISGRVTGVQ------AGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINASV 2953
Cdd:COG5295 490 ATATGAGAAAGGAGAGAAGGAGSAAAGgaanaaAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAVGNNTATGANSV 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2954 TDGAGNTGTGSRDVTIDAALPGIRVNTIAGDDVIN---AIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSW 3030
Cdd:COG5295 570 ALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNgggAVATGDNSVAVGNNAQASGANSVALGAGATATANNSVALGAG 649
|
650
....*....|
gi 701771264 3031 QTVVPGNEVS 3040
Cdd:COG5295 650 SVADRANTVS 659
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
4405-4964 |
6.87e-07 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 56.16 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4405 DGGKTWTDLVVTGTSWAYADGPLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDTGLDAHDFIT 4484
Cdd:COG3401 72 RAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4485 SDNTLTLSGKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLRVVDDAGNIGSTASQLVTVDTV 4564
Cdd:COG3401 152 GANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4565 APDASKTVTIDSistdtglsntdfvTSDTSLTVH-GSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYFNDGRTLsDGT 4643
Cdd:COG3401 232 PPSAPTGLTATA-------------DTPGSVTLSwDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTN-GTT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4644 YQYLVRVVDDAGNV-GQSASKNVTVDTTPPDASVTVTVDSITTDSgfsnsdfitndNTLTLNGSLGAPLGSNEFVQISID 4722
Cdd:COG3401 298 YYYRVTAVDAAGNEsAPSNVVSVTTDLTPPAAPSGLTATAVGSSS-----------ITLSWTASSDADVTGYNVYRSTSG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4723 GGASWFYATSVNGTrwSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGISDDTGQSASDFITM 4802
Cdd:COG3401 367 GGTYTKIAETVTTT--SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4803 DTTLTLNGTLGHALASDERVQISLDGGRNWVDAVVNGTAwhyVDGRTLADGDYVYQVRIIDQAGNVGSTANQVVTVDTVA 4882
Cdd:COG3401 445 ASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTD---TTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVG 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4883 PDTVGSIVSYTDNNGERTGNFDSSYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTFADSGLLDGSY 4962
Cdd:COG3401 522 GAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLL 601
|
..
gi 701771264 4963 HY 4964
Cdd:COG3401 602 VL 603
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6293-6465 |
7.42e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.42 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG--ISL-----GQLDTADLRRDMTLLSQQARLFFG----- 6360
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeIRLkpdrdGELVPADRRQLQRIRTRLGMVFQSfnlws 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 --SIRDNLT------MGRPLAsdEEIHRALALSGALGFVQKQKNglnYlitegGAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:COG4598 109 hmTVLENVIeapvhvLGRPKA--EAIERAEALLAKVGLADKRDA---Y-----PAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 701771264 6433 DEPTAWLDEiseqQLVA-------NLASwlGNRTLVVATH 6465
Cdd:COG4598 179 DEPTSALDP----ELVGevlkvmrDLAE--EGRTMLVVTH 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6295-6443 |
8.92e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQlDTADLRRDMTLLSQQArlffgSIRDNLTMGRPLAS 6374
Cdd:PRK13540 24 LPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS-----GINPYLTLRENCLY 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6375 DeeIHRAlalSGALGFVQKQK-NGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEIS 6443
Cdd:PRK13540 98 D--IHFS---PGAVGITELCRlFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
6123-6238 |
1.13e-06 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 54.02 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6123 MRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQW--NNTNDVAAgvgmKQR--WLTSLLMTWTQEVQSIVYAVVLLVGCY 6198
Cdd:cd18569 173 LQDSGKLTGTTMSGLQMIETLKASGAESDFFSRWagYQAKVLNA----QQElgRTNQLLGALPTLLSALTNAAILGLGGL 248
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 701771264 6199 LVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAK 6238
Cdd:cd18569 249 LVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMR 288
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6285-6482 |
1.28e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD--------------LRRDMTl 6350
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagvaiiyqelhLVPEMT- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 lsqqarlffgsIRDNLTMGRPLASDEEIHRALALSGALGfvQKQKNGLNYLITEGGAGLSGGQRQALLLARTLILQPQIL 6430
Cdd:PRK11288 96 -----------VAENLYLGQLPHKGGIVNRRLLNYEARE--QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6431 LLDEPTAWLD--EIsEQ--QLVANLASwlGNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK11288 163 AFDEPTSSLSarEI-EQlfRVIRELRA--EGRVILYVSHRMeEIFALCDAITVFKDG 216
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
1995-2418 |
1.29e-06 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 55.34 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1995 IVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLS 2074
Cdd:COG3468 1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2075 IDPVAGDDIINASEHSQAHTVGGTSTGAAAGDVVTVVVTNGQGTSFTFTTTLDGNGNWNVGIPASVINGLADGSYTITAS 2154
Cdd:COG3468 81 SGGTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2155 VTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTT 2234
Cdd:COG3468 161 TGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2235 VPASAVSKLGEANYTVTAAVTDAHG---NSSSDSHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDV 2311
Cdd:COG3468 241 GGGSAGGTGGGGLTGGGAAGTGGGGggtGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2312 VTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDVINAI 2391
Cdd:COG3468 321 NAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGT 400
|
410 420
....*....|....*....|....*..
gi 701771264 2392 EHTQNLIINGTSSGLGAGSAVTVTING 2418
Cdd:COG3468 401 GNNGGGGVGGGGGGGLTLTGGTLTVNG 427
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6278-6465 |
1.29e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6278 YYDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQ----LLAGMQTPQ-HGQILLDGISL--GQLDTADLRRDMTL 6350
Cdd:PRK14267 13 YYGSNHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARvEGEVRLFGRNIysPDVDPIEVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6351 LSQQARLF-FGSIRDNLTMGRPL----ASDEEIHRAL--ALSGAlGFVQKQKNGLNylitEGGAGLSGGQRQALLLARTL 6423
Cdd:PRK14267 90 VFQYPNPFpHLTIYDNVAIGVKLnglvKSKKELDERVewALKKA-ALWDEVKDRLN----DYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701771264 6424 ILQPQILLLDEPTAWLDEISEQQLVANLASWLGNRTLVVATH 6465
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6294-6485 |
1.31e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLD-GISLG-QLDTADlrRDMTLlsqqaRLFFGSIRDNLTmgrp 6371
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYKpQYIKPD--YDGTV-----EDLLRSITDDLG---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6372 lAS--DEEIHRALalsgalgfvqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDeiSEQQLVA 6449
Cdd:PRK13409 430 -SSyyKSEIIKPL--------------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAV 492
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701771264 6450 -----NLASWLGNRTLVVaTHRIPILQLV-DRIIVLDNGPAR 6485
Cdd:PRK13409 493 akairRIAEEREATALVV-DHDIYMIDYIsDRLMVFEGEPGK 533
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6293-6333 |
1.38e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG 6333
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG 66
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
4235-4316 |
1.49e-06 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 50.18 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4235 SVSDKAGN--SSSADKQVTLSGEVP-TISINTFAGDDIVSAAEHGTPLVL-SGVT--NAPAGQTVTITLNGQKYTTTV-- 4306
Cdd:NF012196 2 TSHDAAGNtaTATAHHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTTTiTGTVggDVKVGDPVTLTVNGHTYTGTVvd 81
|
90
....*....|
gi 701771264 4307 NGDGTWSYTL 4316
Cdd:NF012196 82 LGNGQLGYSV 91
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
3204-3272 |
1.53e-06 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 49.96 E-value: 1.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 3204 AEPGQTVTVTL----NNETYTGIVQANGTWSITVPAdkasALGDGVYTVDASVSDAAGNGSSAShnlSVDVTV 3272
Cdd:pfam19077 35 NEDGDVVTVTVsidgNGVTGTATAGADGNWSFTPPA----ALADGTYTLTVTVTDIAGNTATSS---PLSFTI 100
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2101-2173 |
1.59e-06 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 49.96 E-value: 1.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 2101 GAAAGDVVTVVVTNGQGTSfTFTTTLDGNGNWNVGIPASvingLADGSYTITASVTDAAGNSGSADR-ALTVNT 2173
Cdd:pfam19077 34 TNEDGDVVTVTVSIDGNGV-TGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGNTATSSPlSFTIDT 102
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
784-874 |
1.70e-06 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 49.57 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 784 ILAGDNIINaaehNAAVTVSGKTDAEAGQVVTLKL--NGKTYTATVGADGGWSMEVPAadvqAMADNSYTLNLSVSDKAG 861
Cdd:pfam19077 17 VSDSDNITN----DTTPTFTGTNEDGDVVTVTVSIdgNGVTGTATAGADGNWSFTPPA----ALADGTYTLTVTVTDIAG 88
|
90
....*....|....
gi 701771264 862 NT-TTTNASLLVDT 874
Cdd:pfam19077 89 NTaTSSPLSFTIDT 102
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
580-666 |
1.93e-06 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 49.57 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 580 PTFMVTDNKGDSQGLLSSNAVTDDSTPTFSGSGQPGATIQV--KDANGNTIASTMVDSNGNWKV-LLSEQPDGTHTYSVV 656
Cdd:pfam19077 3 SIPTIDLAAGSDTGVSDSDNITNDTTPTFTGTNEDGDVVTVtvSIDGNGVTGTATAGADGNWSFtPPAALADGTYTLTVT 82
|
90
....*....|..
gi 701771264 657 QID--GNKITSA 666
Cdd:pfam19077 83 VTDiaGNTATSS 94
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6293-6482 |
2.00e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLG----QLDTADLRRDMTLLSQ--QARLFFGSIRDNL 6366
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQfpESQLFEETVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6367 TMG-RPLASDEEIHRALALSgALGFVQKQKNglnyLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQ 6445
Cdd:PRK13649 108 AFGpQNFGVSQEEAEALARE-KLALVGISES----LFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 701771264 6446 QLVANLASW-LGNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK13649 183 ELMTLFKKLhQSGMTIVLVTHLMdDVANYADFVYVLEKG 221
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
4481-5034 |
2.53e-06 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 54.24 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4481 DFITSDNTLTLSGKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLRVVDDAGNIGSTASQLVT 4560
Cdd:COG3401 39 YLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4561 VDTVAPDASKTVTIDSISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYFN---DGR 4637
Cdd:COG3401 119 SPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLvdgGGD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4638 TLSDGTYQYLVRVVDDAGNVGQSASKNVTVDTTPPDASVTVTVDSITTDSgfsnsdfitndNTLTLNGSLGAPLGSNEfV 4717
Cdd:COG3401 199 IEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGS-----------VTLSWDPVTESDATGYR-V 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4718 QISIDGGASWFYATSVNGTrwSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQ-TVTVDTVAPAYGITIDGISDDTGQsa 4796
Cdd:COG3401 267 YRSNSGDGPFTKVATVTTT--SYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvSVTTDLTPPAAPSGLTATAVGSSS-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4797 sdfitmdTTLTLNGTLGhALASDERVQISLDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNVGSTANQVV 4876
Cdd:COG3401 343 -------ITLSWTASSD-ADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4877 TVDTVAPDTVGSIVSYTDNNGERTGNFDSSYSTDDTsPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTFADSG 4956
Cdd:COG3401 415 ATTASAASGESLTASVDAVPLTDVAGATAAASAASN-PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTT 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 4957 LLDGSYHYVLRVTDKAGNYTESNDFGLTVDTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVVTVNGKTYTSD 5034
Cdd:COG3401 494 GSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNL 571
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6293-6484 |
4.17e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQ--TPQHGQILLDGISLGqldtadlrRDMTLLSQQARLffgsirdnltmGR 6370
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG--------REASLIDAIGRK-----------GD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6371 PLASDEEIHRAlALSGALGFVQKQKNglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVAN 6450
Cdd:COG2401 112 FKDAVELLNAV-GLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 701771264 6451 LASWL--GNRTLVVATHRIPILQLV--DRIIVLDNGPA 6484
Cdd:COG2401 179 LQKLArrAGITLVVATHHYDVIDDLqpDLLIFVGYGGV 216
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4067-4169 |
4.72e-06 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 48.42 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4067 SVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGQKVTVKL--GSESYEATVQADGSWSITVAAEdlakLADGE 4144
Cdd:pfam19077 1 TLSIPTIDLAAGSDTGVSDSDNITNDTTPTFTGTNEDGDVVTVTVSIdgNGVTGTATAGADGNWSFTPPAA----LADGT 76
|
90 100
....*....|....*....|....*.
gi 701771264 4145 FSVHAAVNDKAGNPGSADR-TLTVDT 4169
Cdd:pfam19077 77 YTLTVTVTDIAGNTATSSPlSFTIDT 102
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2711-2866 |
4.73e-06 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 50.75 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2711 VTVTLGNKQYTGVVDTnGNWSVGVPRADVSALGDNTYTVTAS-ITDKAGNTG--DTSHTVTVdtvAPTLSIDTIagdNIL 2787
Cdd:NF032891 33 ATATLGGVAVTSLTDT-ADKKVWTGEVVVPASSELTVGLVVSgYQDLSGNVGeeDTSHSLPI---TPTITITPI---GDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2788 NADEKTgDVVISGTSTGLAAGTSVTV-------NLNGKNYAATVGADGKWTTTvpAGDVGKLGEAFYEVSVSASNGVGNA 2860
Cdd:NF032891 106 DESEAA-TVVISGTSTRFEDGQTLTVevkaqgsETVEVTGTATVQSDGSWTTN--ELDLSSWPDGTITVTVTGTNNLGVA 182
|
....*.
gi 701771264 2861 GSQSST 2866
Cdd:NF032891 183 AEEAST 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6285-6346 |
4.76e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.15 E-value: 4.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKS----TLLQLLAGMQTPQHGQILLDGISLGQLDTADLRR 6346
Cdd:COG4172 26 VKGVS---FDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6291-6467 |
4.80e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6291 ARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLdgisLGQLDTADLRRDMTLLSQQAR----LFFGSIRDNL 6366
Cdd:PRK15056 26 ASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVAYVPQSEevdwSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6367 TMGR---------PLASDEEI-HRALALSGALGFVQKQknglnylITEggagLSGGQRQALLLARTLILQPQILLLDEPT 6436
Cdd:PRK15056 102 MMGRyghmgwlrrAKKRDRQIvTAALARVDMVEFRHRQ-------IGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|..
gi 701771264 6437 AWLDEISEQQLVANLASWLGN-RTLVVATHRI 6467
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEgKTMLVSTHNL 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6285-6479 |
5.72e-06 |
|
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: 52.36 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQH---GQILLDGISLGQLDTADLR----RDMTLLSQQArl 6357
Cdd:COG0444 21 VDGVS---FDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRkirgREIQMIFQDP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6358 fFGS------IRDnlTMGRPL-----ASDEEIH-RALALsgaLGFVqkqknGLNylitegGAG---------LSGGQRQ- 6415
Cdd:COG0444 96 -MTSlnpvmtVGD--QIAEPLrihggLSKAEAReRAIEL---LERV-----GLP------DPErrldrypheLSGGMRQr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6416 -----------ALLLArtlilqpqilllDEPTAWLDeISEQ----QLVANLASWLGNrTLVVATHRIPIL-QLVDRIIVL 6479
Cdd:COG0444 159 vmiaralalepKLLIA------------DEPTTALD-VTIQaqilNLLKDLQRELGL-AILFITHDLGVVaEIADRVAVM 224
|
|
| Big_6 |
pfam17936 |
Bacterial Ig domain; This domain is found in a wide variety of extracellular bacterial ... |
595-659 |
6.40e-06 |
|
Bacterial Ig domain; This domain is found in a wide variety of extracellular bacterial proteins often in multiple tandem copies.
Pssm-ID: 465576 [Multi-domain] Cd Length: 83 Bit Score: 47.62 E-value: 6.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 595 LSSNAVTDDSTpTFSGSGQPGATIQVKDANGNTIASTMVDSNGNWKVLLSEQPDGTHTYSVVQID 659
Cdd:pfam17936 5 PTNLAVSDDGT-TLTGTGEAGATVTVKDADGNVLGTGTVDADGTFSVTLDPAQANGETLSVTATD 68
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
3199-3616 |
8.25e-06 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 53.03 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3199 TGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGDG---VYTVDASVSDAAGNGSSASHNLSVDVTVPSI 3275
Cdd:COG3468 3 SGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGaggVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3276 SFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDS 3355
Cdd:COG3468 83 GTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3356 AGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQP 3435
Cdd:COG3468 163 SGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3436 GDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITI----NPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVT 3511
Cdd:COG3468 243 GSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGsgggGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3512 INLGGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEH 3591
Cdd:COG3468 323 GGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGN 402
|
410 420
....*....|....*....|....*
gi 701771264 3592 NQNLIISGSASGMSEGSTVTVTING 3616
Cdd:COG3468 403 NGGGGVGGGGGGGLTLTGGTLTVNG 427
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6298-6340 |
8.32e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 8.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQ-ILLDGISLG------QLD 6340
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKVGylpqepQLD 82
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
3045-3471 |
8.53e-06 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 52.64 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3045 GDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQTISITFAGHTYTTQV 3124
Cdd:COG3468 12 LGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3125 ASDGSWKFTVPANDMKG---LKDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGT 3201
Cdd:COG3468 92 GGGNSGTGGTGGGGGGGgsgNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3202 SNAEPGQTVTVTLNNETYTGIVQANGTWSITVPADKASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVA 3281
Cdd:COG3468 172 GGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3282 GDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGS 3361
Cdd:COG3468 252 GLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3362 GSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGL 3441
Cdd:COG3468 332 GGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGG 411
|
410 420 430
....*....|....*....|....*....|
gi 701771264 3442 GEANYTLTATATSSIGNSAGASASLLVDTA 3471
Cdd:COG3468 412 GGGGLTLTGGTLTVNGNYTGNNGTLVLNTV 441
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6288-6485 |
8.62e-06 |
|
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: 52.48 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLD-GISLG-QLDTADlrRDMT---LLSQQARLFFGSI 6362
Cdd:COG1245 356 LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlKISYKpQYISPD--YDGTveeFLRSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6363 RDNLTMGRPLAsdeeIHRALalsgalgfvqkQKNglnylITEggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDei 6442
Cdd:COG1245 434 YYKTEIIKPLG----LEKLL-----------DKN-----VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD-- 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 701771264 6443 SEQQLVAnlASWL------GNRTLVVATHRIPILQLV-DRIIVLDNGPAR 6485
Cdd:COG1245 488 VEQRLAV--AKAIrrfaenRGKTAMVVDHDIYLIDYIsDRLMVFEGEPGV 535
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6271-6488 |
8.78e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6271 QLNYAafYYDEEEKVNDLDIARLTITAGEKIAVLGRNGSGKS----TLLQLL--AGMQTpQHGQILL-----DGISLGQL 6339
Cdd:PRK10261 17 NLNIA--FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLV-QCDKMLLrrrsrQVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6340 DTADLRR----DMTLLSQQArlfFGSIRDNLTMGRPLASDEEIHRALALSGALGFVQKQKNGLNylITEGGA-------G 6408
Cdd:PRK10261 94 SAAQMRHvrgaDMAMIFQEP---MTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVR--IPEAQTilsryphQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6409 LSGGQRQALLLARTLILQPQILLLDEPTAWLD-EISEQ--QLVANLASWLgNRTLVVATHRIPIL-QLVDRIIVLDNGPA 6484
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQilQLIKVLQKEM-SMGVIFITHDMGVVaEIADRVLVMYQGEA 247
|
....
gi 701771264 6485 RDDG 6488
Cdd:PRK10261 248 VETG 251
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6285-6345 |
8.78e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 8.78e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6285 VNDLDIAR---LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQ--HGQILLDGISLGQLDtADLR 6345
Cdd:CHL00131 17 VNENEILKglnLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLE-PEER 81
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
5960-6237 |
9.62e-06 |
|
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: 51.33 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5960 LVAMAanVLALAGMIFSM---QVYDRVVPSQSVPTL----WVLFGGVMLAILFEFtmrmLRVHIADVVGKR--ADLRIsd 6030
Cdd:cd18576 2 LILLL--LSSAIGLVFPLlagQLIDAALGGGDTASLnqiaLLLLGLFLLQAVFSF----FRIYLFARVGERvvADLRK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6031 RVFARALRIK----NSARpksTGSFISQI-RELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLL 6105
Cdd:cd18576 74 DLYRHLQRLPlsffHERR---VGELTSRLsNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6106 IPGLLVQRPLAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQ 6185
Cdd:cd18576 151 LVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6186 SIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQA 6237
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKA 282
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6279-6482 |
1.01e-05 |
|
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: 50.41 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRRDMTLLSQQARLF 6358
Cdd:cd03267 31 YREVEALKGIS---FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG-SIRDNLTMGRPL--ASDEEIHRALA-LSGALGfvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDE 6434
Cdd:cd03267 108 WDlPVIDSFYLLAAIydLPPARFKKRLDeLSELLD--------LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6435 PTAWLDEISEQQLVANLASWLGNR--TLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMkDIEALARRVLVIDKG 230
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4909-4987 |
1.11e-05 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 47.26 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4909 TDDTSPVLNGTlNQALADGEIAQIFRDGVLVGNVTITGGTRWTF-ADSGLLDGSYHYVLRVTDKAGNYTESNDFGLTVDT 4987
Cdd:pfam19077 24 TNDTTPTFTGT-NEDGDVVTVTVSIDGNGVTGTATAGADGNWSFtPPAALADGTYTLTVTVTDIAGNTATSSPLSFTIDT 102
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
1374-1471 |
1.32e-05 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 47.26 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1374 PPSITLN------SITADNILNHAeaAQELVITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVAdlanLTDGSW 1447
Cdd:pfam19077 4 IPTIDLAagsdtgVSDSDNITNDT--TPTFTGTNEDGDVVTVTVSIDGNGVTGTATAGADGNWSFTPPAA----LADGTY 77
|
90 100
....*....|....*....|....*
gi 701771264 1448 SVSASVSDVAGNPASTSHGML-VDT 1471
Cdd:pfam19077 78 TLTVTVTDIAGNTATSSPLSFtIDT 102
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2743-3369 |
1.36e-05 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 52.08 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2743 GDNTYTVTASITDKAGNTGDTSHTVTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVTVNLNGKNYAA 2822
Cdd:COG5295 1 SASNAGAVAAGTALTTVASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2823 TVGADGkwTTTVPAGDVGKLGEAFYEVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAELATGQTISGRV 2902
Cdd:COG5295 81 SSVASG--GASAATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAAGSTAAAGGAAASTGGSSAAGGSNTAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2903 TGVQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINASVTDGAGNTGTGSRDVTIDAALPGIRVNTIA 2982
Cdd:COG5295 159 ATGSSTANAATAAAGATSTSASGSSSGASGAAAASAATGASAGGTASAAASASSSATGTSASVGVNAGAATGSAASAGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2983 GDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVT 3062
Cdd:COG5295 239 ASAGAASGNATTASASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3063 IDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQTISITFAghTYTTQVASDGSWKFTVPANDMKGL 3142
Cdd:COG5295 319 GAAALGSAGGSSGVGTASGASAAAATNDGTANGAGTSAAADATSGGGAGGGGAA--ATSSSGGSATAAGNAAGAAGAGSA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3143 KDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGI 3222
Cdd:COG5295 397 GSGGSSTGASAGGGASAAGGAAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3223 VQANGTWSITVPADKASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTvpSISFGVVAGDDVINLAEHGQAQIISGSSS 3302
Cdd:COG5295 477 TAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAAS--GATATAGSAGGGAAAAAGGGSTTAATGTN 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 3303 GAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVN 3369
Cdd:COG5295 555 SVAVGNNTATGANSVALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAVGNN 621
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
2522-2775 |
1.42e-05 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 51.96 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2522 TATVQADGSWKYTVPAAdmvnLKEGDTAvQVSVTNKNGNSTDAAQ-NVSVDTLAPAltvDPVSQdnlLNAAeakQDLVis 2600
Cdd:NF040520 375 TGTADAQGKFQITLSPA----LKTSQKG-TIIVEDAAGNQSKPLEiTAGKDTIAPD---KPTAQ---INAA---GTSV-- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2601 gTSTAEAGQTVTVRLNGES--YQATVKADGSWSLTVPAAdvgkLTDGNITvTASVEDQAGNPgSASRDVL--VDVTVPKV 2676
Cdd:NF040520 439 -TGTAEANAKIEIKDSAGKviGTGTADADGKFTITISPA----LTDKNIG-KVYAIDAAGNR-SDATDVTgtKDTIAPNK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2677 TIGTMATDDVinQTEHGQALVISGT-------STGAQAGDIVTVtLGNKQYTGVVD--TNGNWSVGVPRaDVsALGDNTY 2747
Cdd:NF040520 512 PVLQKVTDDV--GAVKGAIAAGGETddakpklSGSGEAKATLTI-YDNGQAIGTVTvgDNGKWSFTLDK-DL-ALGKHKI 586
|
250 260
....*....|....*....|....*...
gi 701771264 2748 TVTAsiTDKAGNTGDTSHTVTVDTVAPT 2775
Cdd:NF040520 587 TLTQ--TDAAGNTSEVSDPFTFTVVAPK 612
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
2683-3118 |
1.53e-05 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 51.87 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2683 TDDVINQTEHGQALVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGD 2762
Cdd:COG3468 1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2763 TSHTVTVDTVAPTLSIDTIAGDNILNadekTGDVVISGTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKL 2842
Cdd:COG3468 81 SGGTGGNSTGGGGGNSGTGGTGGGGG----GGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2843 GEAFYEVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAELATGQTISGRVTGVQAGADVTINIGGVNYTA 2922
Cdd:COG3468 157 AGGGTGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2923 KVQSDLTWSLTLGQDVLTALGDGSLKINASVTDGAGNTGTGSRDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTS 3002
Cdd:COG3468 237 GVGGGGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3003 SGLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIA 3082
Cdd:COG3468 317 GGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLT 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 701771264 3083 GDDVLNAAEKGADLLLSGMTQNVEAGQTISITFAGH 3118
Cdd:COG3468 397 TGGTGNNGGGGVGGGGGGGLTLTGGTLTVNGNYTGN 432
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6285-6489 |
1.60e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 50.49 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD---------LRRDMTLLSQQa 6355
Cdd:COG4152 17 VDDVS---FTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeergLYPKMKVGEQL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 rLFFGSIRDnltmgrpLASDEEIHRALALSGALGFVQKQKNGLNyliteggaGLSGGQRQ------ALL-------Lart 6422
Cdd:COG4152 93 -VYLARLKG-------LSKAEAKRRADEWLERLGLGDRANKKVE--------ELSKGNQQkvqliaALLhdpelliL--- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6423 lilqpqilllDEPTAWLDEISeQQLVAN----LASWlgNRTLVVATHRIPILQ-LVDRIIVLDNGPARDDGK 6489
Cdd:COG4152 154 ----------DEPFSGLDPVN-VELLKDvireLAAK--GTTVIFSSHQMELVEeLCDRIVIINKGRKVLSGS 212
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
3336-3836 |
1.61e-05 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 52.09 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3336 SVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLN 3415
Cdd:COG4625 1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3416 GKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQ 3495
Cdd:COG4625 81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3496 TLSGKVSNAAAGDAVTINLGGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGI 3575
Cdd:COG4625 161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3576 RINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSS 3655
Cdd:COG4625 241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3656 AGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPA 3735
Cdd:COG4625 321 GGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3736 SDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDG 3815
Cdd:COG4625 401 GGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTG 480
|
490 500
....*....|....*....|..
gi 701771264 3816 -KTYTGVVKADGTWSITLDSTA 3836
Cdd:COG4625 481 nNTYTGTTTVNGGGNYTQSAGS 502
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6288-6489 |
1.70e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.47 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQI------------------LLDGISLGQL------DTAD 6343
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTrfkkikKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6344 LRRDMTLLSQQA--RLFFGSIRDNLTMGrPLA---SDEEihralALSGALGFVQKQKNGLNYLiTEGGAGLSGGQRQALL 6418
Cdd:PRK13651 103 IRRRVGVVFQFAeyQLFEQTIEKDIIFG-PVSmgvSKEE-----AKKRAAKYIELVGLDESYL-QRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6419 LARTLILQPQILLLDEPTAWLD-----EISEqqLVANLasWLGNRTLVVATHRIP-ILQLVDRIIVLDNGPARDDGK 6489
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDpqgvkEILE--IFDNL--NKQGKTIILVTHDLDnVLEWTKRTIFFKDGKIIKDGD 248
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2006-2160 |
1.71e-05 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 49.21 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2006 QEVTVTL--NNVNYTATVGADGRW--SVSVPASDLAALkdgTLTVSaSVADKAGNPANADRGMRVDITePKLSIDPVaGD 2081
Cdd:NF032891 31 QEATATLggVAVTSLTDTADKKVWtgEVVVPASSELTV---GLVVS-GYQDLSGNVGEEDTSHSLPIT-PTITITPI-GD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2082 diINASEHSQAhTVGGTSTGAAAGDVVTVVVT--NGQGTSFTFTTTLDGNGNWNVgiPASVINGLADGSYTITASVTDAA 2159
Cdd:NF032891 105 --VDESEAATV-VISGTSTRFEDGQTLTVEVKaqGSETVEVTGTATVQSDGSWTT--NELDLSSWPDGTITVTVTGTNNL 179
|
.
gi 701771264 2160 G 2160
Cdd:NF032891 180 G 180
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
6135-6237 |
2.02e-05 |
|
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: 50.25 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6135 EAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTGALVgTS 6214
Cdd:cd18557 180 ESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELT-SF 258
|
90 100
....*....|....*....|....
gi 701771264 6215 ILASRTIA-PLAQISGVLSRWQQA 6237
Cdd:cd18557 259 ILYTIMVAsSVGGLSSLLADIMKA 282
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
660-756 |
2.09e-05 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 46.71 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 660 GNKITSAGEITLNVVT-AQASLTAATTAGDNTLNAAEQANDFV-ISGSATELA-SGTALTVTLNGKTYATTVGSDG---- 732
Cdd:NF012196 8 GNTATATAHHTVTIDThADATITIDTVTGDNVLNAAESQQPTTtITGTVGGDVkVGDPVTLTVNGHTYTGTVVDLGngql 87
|
90 100
....*....|....*....|....
gi 701771264 733 SWSVTVPAADaksLADGSWTVTVS 756
Cdd:NF012196 88 GYSVDVDTSD---LLNNPNDVTAT 108
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
2693-3223 |
2.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 51.70 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2693 GQALVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGDTSHTVTVDTV 2772
Cdd:COG4625 3 GGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2773 APTLSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLGEAFYEVSVS 2852
Cdd:COG4625 83 GGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2853 ASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAELATGQTISGRVTGVQAGADVTINIGGVNYTAKVQSDLTWSL 2932
Cdd:COG4625 163 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2933 TLGQDVLTALGDGSLKINASVTDGAGNTGTGSRDVTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSSGLSEGSTVT 3012
Cdd:COG4625 243 GGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3013 VTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEK 3092
Cdd:COG4625 323 GGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3093 GADLLLSGMTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKDGDTSVEVSVVNVTGNGASAGREISVDTA 3172
Cdd:COG4625 403 GGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNN 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 3173 APTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIV 3223
Cdd:COG4625 483 TYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLA 533
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2887-3506 |
2.69e-05 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 51.31 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2887 INAAELATGQTISGRVTGVQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINASVTDGAGNTGTGSRD 2966
Cdd:COG5295 1 SASNAGAVAAGTALTTVASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2967 VTIDAALPGIRVNTIAGDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSwQTVVPGNEVSQWQAGD 3046
Cdd:COG5295 81 SSVASGGASAATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAAGSTAAAGGAAA-STGGSSAAGGSNTATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3047 ITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQTISITFAGHTYTTQVAS 3126
Cdd:COG5295 160 TGSSTANAATAAAGATSTSASGSSSGASGAAAASAATGASAGGTASAAASASSSATGTSASVGVNAGAATGSAASAGGSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3127 DGSWKFTVPANDMKGLKDGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEP 3206
Cdd:COG5295 240 SAGAASGNATTASASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3207 GQTVTVTLNNETYTGIVQANGTWSITVpadkASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVI 3286
Cdd:COG5295 320 AAALGSAGGSSGVGTASGASAAAATND----GTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3287 NLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEV 3366
Cdd:COG5295 396 AGSGGSSTGASAGGGASAAGGAAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3367 TVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNwrvdvqpGDLAGLGEANY 3446
Cdd:COG5295 476 ATAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGG-------AAAAAGGGSTT 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3447 TLTATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAA 3506
Cdd:COG5295 549 AATGTNSVAVGNNTATGANSVALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGA 608
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
3144-3543 |
2.85e-05 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 51.10 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3144 DGDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIV 3223
Cdd:COG3468 13 GGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3224 QANGTWSITVPADKASALGDGVYTVDAS--VSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSS 3301
Cdd:COG3468 93 GGNSGTGGTGGGGGGGGSGNGGGGGGGGggGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3302 SGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPA----SVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNF 3377
Cdd:COG3468 173 GAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGgaagTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3378 NAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIG 3457
Cdd:COG3468 253 LTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3458 NSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKT----------YTATVQSDL 3527
Cdd:COG3468 333 GGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTglttggtgnnGGGGVGGGG 412
|
410
....*....|....*.
gi 701771264 3528 SWSLDLPADVLTALGN 3543
Cdd:COG3468 413 GGGLTLTGGTLTVNGN 428
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
6298-6482 |
2.93e-05 |
|
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: 47.75 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLdgislgqLDTADLRRDMTLLSQqarlffgsirdnltmgrplasdee 6377
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLL------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6378 ihralalsgalgfvqkqknglNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWL-- 6455
Cdd:smart00382 51 ---------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 701771264 6456 -----GNRTLVVATHRIPILQ------LVDRIIVLDNG 6482
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGpallrrRFDRRIVLLLI 147
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
5958-6228 |
3.19e-05 |
|
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: 49.77 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLA-LAGMIFSMQVYDRVVPSQSVPTLWVLfGGVMLA--ILFEFTMRMlRVHIADVVGKRADLRISDRVFA 6034
Cdd:cd18545 4 LALLLMLLSTAAsLAGPYLIKIAIDEYIPNGDLSGLLII-ALLFLAlnLVNWVASRL-RIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6035 RALRIKNS---ARPksTGSFISQ-IRELESVRELITSTTIGTVSDIpfFLLF---VFILW---------LIGGPLVFVVL 6098
Cdd:cd18545 82 HLQKLSFSffdSRP--VGKILSRvINDVNSLSDLLSNGLINLIPDL--LTLVgivIIMFSlnvrlalvtLAVLPLLVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6099 LaiplllipgllVQRPLAHLSNEGMRE-SAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLL 6177
Cdd:cd18545 158 F-----------LLRRRARKAWQRVRKkISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALF 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6178 MTWTQEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQIS 6228
Cdd:cd18545 227 WPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLS 277
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
3607-4171 |
3.27e-05 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 50.92 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3607 GSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVL 3686
Cdd:COG5295 53 GGSGSTSSLTAAAATAGAGSGGTSATAASSVASGGASAATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3687 NAAEKGADLVLSGKTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREF 3766
Cdd:COG5295 133 GSTAAAGGAAASTGGSSAAGGSNTATATGSSTANAATAAAGATSTSASGSSSGASGAAAASAATGASAGGTASAAASASS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3767 S--VDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQ 3844
Cdd:COG5295 213 SatGTSASVGVNAGAATGSAASAGGSASAGAASGNATTASASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3845 YVIKVDVSDAAGNKTTGSQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTGAAAGNKIIITLDGVQYVTQVDA 3924
Cdd:COG5295 293 AAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGTASGASAAAATNDGTANGAGTSAAADATSGGGAGGGGAA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3925 KGNWSVGVPASAVSALKNGTATITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELA 4004
Cdd:COG5295 373 ATSSSGGSATAAGNAAGAAGAGSAGSGGSSTGASAGGGASAAGGAAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4005 VGTQVTVTLNGiQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNISVDTVAPIVTIADISGDN 4084
Cdd:COG5295 453 GGGTAGAGGAA-NVGAATTAASAAATAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATA 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4085 AINAAEQQQPLTIRGTSSAEAGQKVTVKLGSESYEATVqADGSWSITVAAEDLAKLADGEFSVHAAVNDKAGNPGSADRT 4164
Cdd:COG5295 532 GSAGGGAAAAAGGGSTTAATGTNSVAVGNNTATGANSV-ALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVA 610
|
....*..
gi 701771264 4165 LTVDTTA 4171
Cdd:COG5295 611 TGDNSVA 617
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
4384-4812 |
3.27e-05 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 50.72 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4384 VVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTGTSWAYADGPLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAG 4463
Cdd:COG3468 1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4464 TTITVEAISRDTGLDAHDFITSDNTLTLSGKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLR 4543
Cdd:COG3468 81 SGGTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4544 VVDDAGNIGSTASQLVTVDTVAPDASKTVTIDSISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQT 4623
Cdd:COG3468 161 TGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4624 VVTIGSTWYFNDGRTLSDGTYQYLVRVVDDAGNVGQSASKNVTVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTL 4703
Cdd:COG3468 241 GGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4704 NGSLGAPLGSNEFVQISIDGGASWFYATSVNGTRWSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGI 4783
Cdd:COG3468 321 NAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGT 400
|
410 420
....*....|....*....|....*....
gi 701771264 4784 TIDGISDDTGQSASDFITMDTTLTLNGTL 4812
Cdd:COG3468 401 GNNGGGGVGGGGGGGLTLTGGTLTVNGNY 429
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
4230-4852 |
3.35e-05 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.77 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4230 YQISASVSDKAGNSSSADKQVTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQTVTITLNGQKYTTTVNGD 4309
Cdd:COG3401 1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4310 GTWSYTLGSSAVSALADGDAYVIHASVSNSIGNSAGVDRTITVDTTPPQMTITIDSLQNDTGLSASDFITADNKVVVKGS 4389
Cdd:COG3401 81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4390 LSGALGNNEKAQISLDGGKTWTDLVVTGTSWAYADGPL--PDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTIT 4467
Cdd:COG3401 161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiePGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4468 VEAisrdtgldahdfiTSDNTLTLS-GKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSwSYVDGRQLADGDHLYQLRVVD 4546
Cdd:COG3401 241 ATA-------------DTPGSVTLSwDPVTESDATGYRVYRSNSGDGPFTKVATVTTT-SYTDTGLTNGTTYYYRVTAVD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4547 DAGNIGSTASQL-VTVDTVAPDASktvtidsistdTGLSNTDFVTSDTSLTVHGSLGAPlLAGEYVQISLDGGTVWQTVV 4625
Cdd:COG3401 307 AAGNESAPSNVVsVTTDLTPPAAP-----------SGLTATAVGSSSITLSWTASSDAD-VTGYNVYRSTSGGGTYTKIA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4626 TIGSTWYFNDGRTLSDGTYQYLVRVVDDAGNVG-QSASKNVTVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLN 4704
Cdd:COG3401 375 ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESaPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4705 GSLGAPLGSNEFVQISIDGGASWFYATSVNGTRWSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGIT 4784
Cdd:COG3401 455 AAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGAS 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 4785 IDGISDDTGQSASDFITMDTTLTLNGTLGHALASDERVQISLDGGRNWVDAVVNGTAWHYVDGRTLAD 4852
Cdd:COG3401 535 PVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6288-6477 |
3.51e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAG---------------------MQTPQHGQILLDGISLG--------- 6337
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNeisadggsytfpgnwqlawvnQETPALPQPALEYVIDGdreyrqlea 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6338 QLDTADLRRD----MTLLSQQARLFFGSIRDnltmgrplasdeeihRALALSGALGFVQKQknglnylITEGGAGLSGGQ 6413
Cdd:PRK10636 97 QLHDANERNDghaiATIHGKLDAIDAWTIRS---------------RAASLLHGLGFSNEQ-------LERPVSDFSGGW 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6414 RQALLLARTLILQPQILLLDEPTAWLDeiseQQLVANLASWLGNR--TLVVATHRIPILQ-LVDRII 6477
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYqgTLILISHDRDFLDpIVDKII 217
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
3275-3760 |
3.53e-05 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 50.72 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3275 ISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTD 3354
Cdd:COG3468 1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3355 SAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQ 3434
Cdd:COG3468 81 SGGTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3435 PGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVTINL 3514
Cdd:COG3468 161 TGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3515 GGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQN 3594
Cdd:COG3468 241 GGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3595 LIISGSASGMSEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVA 3674
Cdd:COG3468 321 NAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3675 VSVENITADNVLNAAEKGADLVLSgkTQNVEAGQTVTITFGgrtytAQVESDGSwhytvpASD---IAGLKDGdaSVKVS 3751
Cdd:COG3468 401 GNNGGGGVGGGGGGGLTLTGGTLT--VNGNYTGNNGTLVLN-----TVLGDDNS------PTDrlvVNGNTSG--TTGVR 465
|
....*....
gi 701771264 3752 VTNVNGNGA 3760
Cdd:COG3468 466 VNNAGGLGA 474
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6282-6370 |
3.70e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6282 EEKVNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADLRR--------Dmtllsq 6353
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgvayipeD------ 341
|
90 100
....*....|....*....|..
gi 701771264 6354 qaRLFFG-----SIRDNLTMGR 6370
Cdd:COG3845 342 --RLGRGlvpdmSVAENLILGR 361
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2893-3062 |
4.32e-05 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 48.05 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2893 ATGQTISGRVTGVQAGADVTINIGGVNYTakvqsdlTWSLTLGQDVLTALGDGSLKINASVT-------DGAGNTGTGSR 2965
Cdd:NF032891 15 AIGQSVTVTLTFDKAVQEATATLGGVAVT-------SLTDTADKKVWTGEVVVPASSELTVGlvvsgyqDLSGNVGEEDT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2966 DVTIDAAlPGIRVNTIAGDDVINAIehglNLVINGTSSGLSEGSTVTVTINGKDYA-------ATVRADGSWQTvvPGNE 3038
Cdd:NF032891 88 SHSLPIT-PTITITPIGDVDESEAA----TVVISGTSTRFEDGQTLTVEVKAQGSEtvevtgtATVQSDGSWTT--NELD 160
|
170 180
....*....|....*....|....
gi 701771264 3039 VSQWQAGDITVSAGGTSSSGNPVT 3062
Cdd:NF032891 161 LSSWPDGTITVTVTGTNNLGVAAE 184
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
907-967 |
4.47e-05 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 45.72 E-value: 4.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 907 GAAPGDKVTVSI----GSETYQTTVQADGSWSVGVPkeviSSLPEGPNTITVAITDVAGNTGTTT 967
Cdd:pfam19077 34 TNEDGDVVTVTVsidgNGVTGTATAGADGNWSFTPP----AALADGTYTLTVTVTDIAGNTATSS 94
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6284-6482 |
4.47e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6284 KVNDLDIArltITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD-LRRDMTLLSQQARL--FFG 6360
Cdd:PRK09700 278 KVRDISFS---VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITESRRDngFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 --SIRDNLTMGRPLasdeeihRALALSGALGFV---------QKQKNGL-------NYLITEggagLSGGQRQALLLART 6422
Cdd:PRK09700 355 nfSIAQNMAISRSL-------KDGGYKGAMGLFhevdeqrtaENQRELLalkchsvNQNITE----LSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6423 LILQPQILLLDEPTAWLD-----EIseQQLVANLASwLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDvgakaEI--YKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
6130-6251 |
4.69e-05 |
|
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: 49.37 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6130 NATLVEAVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTG- 6208
Cdd:cd18578 193 SKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEq 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 701771264 6209 ------ALVGTSILASRTIAPLAQISgvlsrwqQAKVARKGLDDLMQRP 6251
Cdd:cd18578 273 ffivfmALIFGAQSAGQAFSFAPDIA-------KAKAAAARIFRLLDRK 314
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
801-954 |
6.11e-05 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 47.67 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 801 TVSGKTDAEAGQVVTLKLNG----KTYTATVGAD--GGWSMEVPA----ADVQAMADNSYTLNLSVS---DKAGNTTTTN 867
Cdd:NF032891 7 VTFNPTHQAIGQSVTVTLTFdkavQEATATLGGVavTSLTDTADKkvwtGEVVVPASSELTVGLVVSgyqDLSGNVGEED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 868 ASLLVDTTPpeasvnTVAGDDILSVSEQGQAQ-IISGTSQGAAPGDKVTVSI---GSETYQ----TTVQADGSWSvgVPK 939
Cdd:NF032891 87 TSHSLPITP------TITITPIGDVDESEAATvVISGTSTRFEDGQTLTVEVkaqGSETVEvtgtATVQSDGSWT--TNE 158
|
170
....*....|....*
gi 701771264 940 EVISSLPEGPNTITV 954
Cdd:NF032891 159 LDLSSWPDGTITVTV 173
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2001-2061 |
6.17e-05 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 45.33 E-value: 6.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 2001 SAEPGQEVTVTL----NNVNYTATVGADGRWSVSVPasdlAALKDGTLTVSASVADKAGNPANAD 2061
Cdd:pfam19077 34 TNEDGDVVTVTVsidgNGVTGTATAGADGNWSFTPP----AALADGTYTLTVTVTDIAGNTATSS 94
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
3311-3905 |
6.64e-05 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 49.77 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3311 TVTIGANSWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIE 3390
Cdd:COG5295 26 SGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAASSVASGGASAATAASTGTGNTAGTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3391 KGEVLTLSGTS---------ANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSAG 3461
Cdd:COG5295 106 ATVAGAASSGSatnagasagASAAAAAGSTAAAGGAAASTGGSSAAGGSNTATATGSSTANAATAAAGATSTSASGSSSG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3462 ASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKV--------SNAAAGDAVTINLGGKTYTATVQSDLSWSLDL 3533
Cdd:COG5295 186 ASGAAAASAATGASAGGTASAAASASSSATGTSASVGVNAgaatgsaaSAGGSASAGAASGNATTASASSVSGSAVAAGT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3534 PADVLTALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVT 3613
Cdd:COG5295 266 ASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGTASGASAAAATN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3614 INGKSYLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGA 3693
Cdd:COG5295 346 DGTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGGSSTGASAGGGASAAGGAAAGSAAAG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3694 DLVLSGKTQNVEAGQTVTI--TFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDAT 3771
Cdd:COG5295 426 TSSNTSAVGASNGASGTSSsaSSAGAAGGGTAGAGGAANVGAATTAASAAATAAAATSSAAIAGATATGAGAAAGGAGAG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3772 APGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQYVIKVDV 3851
Cdd:COG5295 506 AAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAVGNNTATGANSVALGAGSVASGANSVSV 585
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 3852 SDAAgnkTTGSQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTGAAA 3905
Cdd:COG5295 586 GAAG---AENVAAGATDTDAVNGGGAVATGDNSVAVGNNAQASGANSVALGAGA 636
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
3251-3351 |
6.98e-05 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 45.17 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3251 SVSDAAGN--GSSASHNLSVDVTVP-SISFGVVAGDDVINLAEHGQAQ--IISGSSSGAAAGDKITVTIGANSWTTTVDA 3325
Cdd:NF012196 2 TSHDAAGNtaTATAHHTVTIDTHADaTITIDTVTGDNVLNAAESQQPTttITGTVGGDVKVGDPVTLTVNGHTYTGTVVD 81
|
90 100 110
....*....|....*....|....*....|
gi 701771264 3326 AGN----WSIGVPASVvsqLADGKVTINAS 3351
Cdd:NF012196 82 LGNgqlgYSVDVDTSD---LLNNPNDVTAT 108
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6298-6339 |
7.32e-05 |
|
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: 49.55 E-value: 7.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILL-DGISLGQL 6339
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVGYL 73
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6285-6482 |
7.36e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQtPQ---HGQILLDGISLGQLDTADL-RRDMTLLSQQARLFFG 6360
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 -SIRDNLTMGRPL-------ASDEEIHRALALsgalgFVQKQKNGLNylITEGGAGLSGGQRQALLLARTLILQPQILLL 6432
Cdd:TIGR02633 93 lSVAENIFLGNEItlpggrmAYNAMYLRAKNL-----LRELQLDADN--VTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 701771264 6433 DEPTAWLDEiSEQQLVANLASWLGNRTL--VVATHRIPILQLV-DRIIVLDNG 6482
Cdd:TIGR02633 166 DEPSSSLTE-KETEILLDIIRDLKAHGVacVYISHKLNEVKAVcDTICVIRDG 217
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1153-1239 |
8.31e-05 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 45.17 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1153 SVTNAHGNTG--SGSRDININAQLPG-LRINTVSGDDVINAIEQHQDLT-VTGT-STHLSAGTIITVRINGVDYQAAVSA 1227
Cdd:NF012196 2 TSHDAAGNTAtaTAHHTVTIDTHADAtITIDTVTGDNVLNAAESQQPTTtITGTvGGDVKVGDPVTLTVNGHTYTGTVVD 81
|
90
....*....|....*.
gi 701771264 1228 TG----SWQIGIPAAD 1239
Cdd:NF012196 82 LGngqlGYSVDVDTSD 97
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6288-6329 |
8.68e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 8.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQI 6329
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI 60
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
3238-3795 |
8.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 49.39 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3238 ASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGAN 3317
Cdd:COG4625 3 GGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3318 SWTTTVDAAGNWSIGVPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTL 3397
Cdd:COG4625 83 GGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3398 SGTSANLAPGTAVIVTLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITI 3477
Cdd:COG4625 163 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3478 NPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLSWSLDLPADVLTALGNGKLTVTASVTNGHG 3557
Cdd:COG4625 243 GGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3558 NSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKSYLATVSASGTWSAAVPAGD 3637
Cdd:COG4625 323 GGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3638 VSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLSGKTQNVEAGQTVTITFGGR 3717
Cdd:COG4625 403 GGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNN 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 3718 TYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTINPIATDNVINAAEAGAGV 3795
Cdd:COG4625 483 TYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTILAVAAALDALAGNGDL 560
|
|
| FG-GAP_3 |
pfam13517 |
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ... |
5332-5393 |
9.03e-05 |
|
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.
Pssm-ID: 433275 [Multi-domain] Cd Length: 61 Bit Score: 43.37 E-value: 9.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 5332 DFDGDGYMDLYMGMSRAGTgglLMMNDGKGNLLTGTAVGSEKYNGTVSVAV-DWNMDGRMDII 5393
Cdd:pfam13517 1 DLDGDGKLDLVVANDGGLR---LYLNNGDGTFTFITSVSLGGGGGGLSVAVgDLDGDGRLDLL 60
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2894-2970 |
1.06e-04 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 44.56 E-value: 1.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 2894 TGQTISGRVTGVQagadVTINIGGVNYTAKVQSDLTWSLTLGqdvlTALGDGSLKINASVTDGAGNTGTGSR-DVTID 2970
Cdd:pfam19077 32 TGTNEDGDVVTVT----VSIDGNGVTGTATAGADGNWSFTPP----AALADGTYTLTVTVTDIAGNTATSSPlSFTID 101
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
3781-3869 |
1.08e-04 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 44.56 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3781 ATDNVINAAEAGagVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDStalgALADNQYVIKVDVSDAAGNKTT 3860
Cdd:pfam19077 19 DSDNITNDTTPT--FTGTNEDGDVVTVTVSIDGNGVTGTATAGADGNWSFTPPA----ALADGTYTLTVTVTDIAGNTAT 92
|
90
....*....|
gi 701771264 3861 GS-QNMTLDT 3869
Cdd:pfam19077 93 SSpLSFTIDT 102
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
3445-3883 |
1.13e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 49.17 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3445 NYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIAAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQ 3524
Cdd:COG3468 17 TGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGGGGNS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3525 SDLSWSLDLPADVLTALGNGKLTVTASVTNGhGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGM 3604
Cdd:COG3468 97 GTGGTGGGGGGGGSGNGGGGGGGGGGGGTGG-GGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3605 SEGSTVTVTINGKSYLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADN 3684
Cdd:COG3468 176 GGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3685 VLNAAeKGADLVLSGKTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAer 3764
Cdd:COG3468 256 GGAAG-TGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGG-- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3765 efSVDATAPGLTINPIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQ 3844
Cdd:COG3468 333 --GGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGG 410
|
410 420 430
....*....|....*....|....*....|....*....
gi 701771264 3845 yvikVDVSDAAGNKTTGSQNMTLDTTAPTVSFNAVAGDD 3883
Cdd:COG3468 411 ----GGGGGLTLTGGTLTVNGNYTGNNGTLVLNTVLGDD 445
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6287-6482 |
1.20e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.81 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6287 DLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISL----GQLDTADLRRDMTLLSQ--QARLFFG 6360
Cdd:PRK13643 24 DID---LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6361 SIRDNLTMGrPL---ASDEEIHRALALSGALGFVQKQknglnyLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTA 6437
Cdd:PRK13643 101 TVLKDVAFG-PQnfgIPKEKAEKIAAEKLEMVGLADE------FWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701771264 6438 WLDEISEQQLVANLAS-WLGNRTLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK13643 174 GLDPKARIEMMQLFESiHQSGQTVVLVTHLMdDVADYADYVYLLEKG 220
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
4550-5157 |
1.28e-04 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 48.85 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4550 NIGSTASQLVTVDTVAPDASKTVTIDSISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGS 4629
Cdd:COG3401 4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4630 TW-YFNDGRTLSDGTYQYLVRVVDDAGNVGQSASKNVTVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLNGSLG 4708
Cdd:COG3401 84 VAaAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4709 APLGSNEFVQISIdGGASWFYATSVNGTRWSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGI 4788
Cdd:COG3401 164 AGAGVVVSPDTSA-TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4789 SDDTGQsasdfitmdTTLTLNGTLGHALASdERVQISLDGGRNWVdAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNV 4868
Cdd:COG3401 243 ADTPGS---------VTLSWDPVTESDATG-YRVYRSNSGDGPFT-KVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4869 GSTANQV-VTVDTVAPDTVGSIVSYTDNNGERTGNFDSSYSTDDTSpvlngtlnqaladgeiAQIFRDGVLVGNVTITGG 4947
Cdd:COG3401 312 SAPSNVVsVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG----------------YNVYRSTSGGGTYTKIAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4948 TRWT--FADSGLLDG-SYHYVLRVTDKAGNYTESNDFGLTVDTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVV 5024
Cdd:COG3401 376 TVTTtsYTDTGLTPGtTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5025 TVNGKTYTSDRGGAVVVDPASNTWYlqipDADVLSLKSYDVTAQVKSSAGNGNSVDVTHGTVVVGAEASMTPAWAFTSAT 5104
Cdd:COG3401 456 AVLADGGDTGNAVPFTTTSSTVTAT----TTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVT 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 701771264 5105 NAIAASFMLDANGMWTFASNQQFATANDRNSYSVSGNFSMTGSYTTGAYADIN 5157
Cdd:COG3401 532 GASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTT 584
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6293-6482 |
1.35e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD-LRRDMTLLS---QQARLFF-GSIRDN-- 6365
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYLdAPLAWNvc 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6366 -LTMGRP---------LASDEEIHRALALSgalgFVQKQknglnylitEGGAGLSGGQRQALLLARTLILQPQILLLDEP 6435
Cdd:PRK15439 364 aLTHNRRgfwikpareNAVLERYRRALNIK----FNHAE---------QAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701771264 6436 TAWLDeISEQ----QLVANLASWlGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK15439 431 TRGVD-VSARndiyQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
4663-5219 |
1.36e-04 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 48.79 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4663 KNVTVDTtPPDASVTVTVDSITTDSGFSNSDFIT--NDNTLTLNGSLGAPLGSNEFVQISIDGGASWFY-ATSVNgtrws 4739
Cdd:COG4733 424 RVVTLDR-PVTMEAGDRYLRVRLPDGTSVARTVQsvAGRTLTVSTAYSETPEAGAVWAFGPDELETQLFrVVSIE----- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4740 ytdgrqlADGDHTWQVRVVDLAGNVGATTsQTVTVDTVAPAYgiTIDGISDDTGQSASDFITMDTTLTLNGTLGHAlASD 4819
Cdd:COG4733 498 -------ENEDGTYTITAVQHAPEKYAAI-DAGAFDDVPPQW--PPVNVTTSESLSVVAQGTAVTTLTVSWDAPAG-AVA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4820 ERVQISLDGGrNWVDAVVNGTAWHYVDGrtLADGDYVYQVRIIDQAGNVG---STANQVVTVDTVAPDTVGSIVsytdnn 4896
Cdd:COG4733 567 YEVEWRRDDG-NWVSVPRTSGTSFEVPG--IYAGDYEVRVRAINALGVSSawaASSETTVTGKTAPPPAPTGLT------ 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4897 gertgnfdssystddTSPVLNG-TLNQALADG------EIAQIFRDGVLVGNVTITGGTRWTFADSGLLDG-SYHYVLRV 4968
Cdd:COG4733 638 ---------------ATGGLGGiTLSWSFPVDadtlrtEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGqTYYYRARA 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4969 TDKAGNYTESNDFGLTVDTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVVTVNGKTYTSDRGGAVVVDPASNTW 5048
Cdd:COG4733 703 VDRSGNVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIG 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5049 YLQIPDADVLSLKSYDVTAQVKSSAGNGNSVDVTHGTVVVGAEASMTPAWAFTSATNAIAASFMLDANgmwTFASNQQFA 5128
Cdd:COG4733 783 AEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYGDA---IIESGNTGD 859
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5129 TANDRNSYSVSGNFSMTGSYTTGAYADINRDGHADMLVESTNYSYITQLMNNGDGTYTSTSPGSSATVGALLWYGAVVSI 5208
Cdd:COG4733 860 IVATGDIASAAAGAVATTVSGTTAADVSAVADSTAASLTAIVIAATTIIDAIGDGTTREPAGDIGASGGAQGFAVTIVGS 939
|
570
....*....|.
gi 701771264 5209 DFQGDGYVDFV 5219
Cdd:COG4733 940 FDGAGAVATVD 950
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6293-6482 |
1.49e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.48 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD-LRRDMTLLS---QQARLFFG-SIRDNLT 6367
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrKGEGLVLDlSIRENIT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6368 mgrpLASDEEIHRAlalsgalGFVQKQK----------------NGLNYLITEggagLSGGQRQALLLARTLILQPQILL 6431
Cdd:COG1129 353 ----LASLDRLSRG-------GLLDRRReralaeeyikrlriktPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 6432 LDEPTAWLD-----EIseQQLVANLASwlGNRTLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG1129 418 LDEPTRGIDvgakaEI--YRLIRELAA--EGKAVIVISSELPeLLGLSDRILVMREG 470
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
3745-4220 |
1.50e-04 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 48.50 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3745 DASVKVSVTNVNGN-----GASAEREFSVDATAP---GLTINPIATDNVINAAEAGAgvtVTGTSNAQA--GQTVTLTLD 3814
Cdd:NF040520 188 EANAKIYIKDATGKviatgQADASGNYTIKLDQPlvnGNKVNVTAIDAAGNASKATV---VTGTKDTIApdAPQAQLNAD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3815 GKTYTGVVKADGTWSI-TLDSTALG---ALADNQYVIK------------VDVSDAAGNKTTGSQNM----TLDTTAPTV 3874
Cdd:NF040520 265 GTIVTGKTEANAKVSVyDADGKLLGtvtANKEGLYSIKvsppltsdkggtVIAEDAAGNKSEPSKIIagkdTIAPDQPLV 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3875 SFNAvAGDDIINLEEhAQAQIISGSSTGaaagnKIIITldGVqyvtqVDAKGNWSVGVPasavSALKNG-TATItaTLTD 3953
Cdd:NF040520 345 EVNK-EGTSIEGRAE-ANAKVQIKDADG-----KVIGT--GT-----ADAQGKFQITLS----PALKTSqKGTI--IVED 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3954 SAGNEganSHTVEVNAARigltiDTISHDDV---INA--------AEARQDLTIGGSSTELaVGTQvTVTLNGiQYTTTI 4022
Cdd:NF040520 405 AAGNQ---SKPLEITAGK-----DTIAPDKPtaqINAagtsvtgtAEANAKIEIKDSAGKV-IGTG-TADADG-KFTITI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4023 QpgggwsvtvPANQVQNlaHGSGYtvmasATDSANNATSATHNISV-DTVAP----IVTIADISGD--NAINAAEQQQPL 4095
Cdd:NF040520 474 S---------PALTDKN--IGKVY-----AIDAAGNRSDATDVTGTkDTIAPnkpvLQKVTDDVGAvkGAIAAGGETDDA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4096 TIRGTSSAEAGQKVT-----VKLGSesyeATVQADGSWSITVAAEdlakLADGEFSVHAAVNDKAGNPGSADRTLTVDTT 4170
Cdd:NF040520 538 KPKLSGSGEAKATLTiydngQAIGT----VTVGDNGKWSFTLDKD----LALGKHKITLTQTDAAGNTSEVSDPFTFTVV 609
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 701771264 4171 APTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAV 4220
Cdd:NF040520 610 APKTASASEQSEVDTSNTETASLADSVGLNTLKLAQETTNETNSQQQESV 659
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
3492-3657 |
1.60e-04 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 46.13 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3492 AAGQTLSGKVSNAAAGDAVTINLGGKTYTATVQSDLS--W--SLDLPADVLTALGngkLTVTaSVTNGHGNSGTADREFT 3567
Cdd:NF032891 15 AIGQSVTVTLTFDKAVQEATATLGGVAVTSLTDTADKkvWtgEVVVPASSELTVG---LVVS-GYQDLSGNVGEEDTSHS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3568 VDASlPGIRINTVAGDDVVNAiehnQNLIISGSASGMSEGSTVTVTI---NGKSYL----ATVSASGTWSaaVPAGDVSL 3640
Cdd:NF032891 91 LPIT-PTITITPIGDVDESEA----ATVVISGTSTRFEDGQTLTVEVkaqGSETVEvtgtATVQSDGSWT--TNELDLSS 163
|
170
....*....|....*..
gi 701771264 3641 WAAGNLTVTAAGSSSAG 3657
Cdd:NF032891 164 WPDGTITVTVTGTNNLG 180
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
5981-6240 |
1.65e-04 |
|
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: 47.41 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5981 DRVVPSQSVPTLWVLFGGVMLAI-----LFEFTMRMLRVHIADVVGKraDLRisDRVFARALRI------KNSarpksTG 6049
Cdd:cd18541 27 DALTAGTLTASQLLRYALLILLLalligIFRFLWRYLIFGASRRIEY--DLR--NDLFAHLLTLspsfyqKNR-----TG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6050 SFISQIRE-LESVRELI-------------TSTTIGT----------VSDIPFFLLFVFILWLigGPLVFVVLLAiplll 6105
Cdd:cd18541 98 DLMARATNdLNAVRMALgpgilylvdalflGVLVLVMmftispkltlIALLPLPLLALLVYRL--GKKIHKRFRK----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6106 ipgllVQRPLAHLSNEgmresairnatlveaVQ-SIEDIKLLRA---EQRFQNQWNNTNDVAAGVGMKQRWLTSLLMTWT 6181
Cdd:cd18541 171 -----VQEAFSDLSDR---------------VQeSFSGIRVIKAfvqEEAEIERFDKLNEEYVEKNLRLARVDALFFPLI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6182 QEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18541 231 GLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAAS 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
6281-6484 |
1.86e-04 |
|
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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6281 EEEKVNDLDIARLTITA-----GEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGqldtadlrrdmtllsqqa 6355
Cdd:cd03222 3 YPDCVKRYGVFFLLVELgvvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6356 rlffgsirdnltmgrplasdeeihralalsgalgfVQKQKnglnyliteggAGLSGGQRQALLLARTLILQPQILLLDEP 6435
Cdd:cd03222 65 -----------------------------------YKPQY-----------IDLSGGELQRVAIAAALLRNATFYLFDEP 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701771264 6436 TAWLDeiSEQQLVANLA----SWLGNRTLVVATHRIPILQ-LVDRIIVLDNGPA 6484
Cdd:cd03222 99 SAYLD--IEQRLNAARAirrlSEEGKKTALVVEHDLAVLDyLSDRIHVFEGEPG 150
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
5282-5704 |
2.26e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 48.02 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5282 HTTNGGNIYALSTMFNKGDGTFTWSQNFINTMYSATGSAAANNAVSMTWADFDGDGYMDLYMGMSRAGTGGLLMMNDGKG 5361
Cdd:COG3468 17 TGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGGGGNS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5362 NLLTGTAVGSEKYNGTVSVAVDWNMDGRMDIIKLANTGQSYMYTNDGLKGVASF--TSSKFGSATTSQVSGAALVDYDWD 5439
Cdd:COG3468 97 GTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGgtGAAAAGGGTGSGGGGSGGGGGAGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5440 GAQDLLIFRQNGSVTLERNTNAVAPGTAIHLKIVDSQGINVFFGNTVKLYNAAGELVASQVINAQSGIGINDASALVSFY 5519
Cdd:COG3468 177 GGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5520 GLNPNETYHAELVRAINGVSSNTTWNGLTAGDGRESYALTADAATGVHAGTLTGTGYNDTFIAEQGTYVYNGGGGWETSS 5599
Cdd:COG3468 257 GAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5600 DHQTWSATGGMDVVDFRNSTVGVTVDLGKTGAQNTGFNTATFSNIEGIVGSSHDDVITGNSGNNTFEGGGGNDTFNIGSG 5679
Cdd:COG3468 337 GGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGL 416
|
410 420
....*....|....*....|....*
gi 701771264 5680 GHDTllYKLLNGSDATGGNGHDVVN 5704
Cdd:COG3468 417 TLTG--GTLTVNGNYTGNNGTLVLN 439
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
4554-5337 |
2.70e-04 |
|
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];
Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 47.83 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4554 TASQLVTVDTVAPDASKTVTIDSISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEYVQISLDGGTVWQTVVTIGSTWYF 4633
Cdd:COG3209 3 SLGLVGGTTGASSTLLAATNAGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4634 NDGRTLSDGTYQYLVRVVDDAGNVGQSASKNVTVDTTPPDASVTVTVDSITTDSGFSNSDFITNDNTLTLNGSLGAPLGS 4713
Cdd:COG3209 83 LGDASAAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4714 NEFVQISIDGGASWFYATSVNGTRWSYTDGRQLADGDHTWQVRVVDLAGNVGATTSQTVTVDTVAPAYGITIDGISDDTG 4793
Cdd:COG3209 163 GGGASAYGLTLGGAAAGPATGVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4794 QSASDFITMDTTLTLNGTLGHALASDERVQISLDGGRNWVDAVVNGTAWHYVDGRTLADGDYVYQVRIIDQAGNVGSTAN 4873
Cdd:COG3209 243 TGAAGAGAAVATAATTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4874 QVVTVDTVAPDTVGSIVSYTD-NNGERTGNFDSSYSTDDTSPVLNGTLNQALADGEIAQIFRDGVLVGNVTITGGTRWTF 4952
Cdd:COG3209 323 TAAVSGAADAGTTTTTGTGTGgTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4953 ADSGLLDGSYHYVLRVTDKAGNYTESNDFGLTVDTSVPTTKALVNGLNTTDTTPIITGSVDANLVHGEFVVVTVNGKTYT 5032
Cdd:COG3209 403 VGAGTTTTSTTGGDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTG 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5033 SDRGGAVVVDPAS-NTWYLQIPDADVLSLKSYDVTAQVKSSAGNGNSVDVTHGTVVVGAEASMTPAWAFTSATNAIAASF 5111
Cdd:COG3209 483 GGTLTSGSAGATTlGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGT 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5112 MLDANGMWTFASNQQFATANDRNSYSVSGNFSMTGSYTTGAYADINRDGHADMLVESTNYSYITQLMNNGDGTYTSTSPG 5191
Cdd:COG3209 563 GGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5192 SSATVGALLWYGAVVSIDFQGDGYVDFVMGDAGGPDSSTFVNNNAGKLTGTSGGGTYTNFVSGSKVGNYNSVIETSGVDL 5271
Cdd:COG3209 643 GTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTT 722
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5272 NNDGMVDIAQHTTNGGNIYALSTMFNKGDGTF----TWSQNFINTMYSATGSAAANNAVSMTWADFDGDG 5337
Cdd:COG3209 723 TTGGGGGTTTDGTGTGGTTGTLTTTSTTTTTTagalTYTYDALGRLTSETTPGGVTQGTYTTRYTYDALG 792
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
4179-4601 |
2.77e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 48.02 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4179 VAGDDIINSAEQQAGQAISGTTNAQPGQTITVTFNNHTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPT 4258
Cdd:COG3468 11 GLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4259 ISINTFAGDDIVSAAEHGTplvlSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSN 4338
Cdd:COG3468 91 GGGGNSGTGGTGGGGGGGG----SGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4339 SIGNSAGVDRTITVDTTPPQMTITIDSLQNDTGLSASDFITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTGT 4418
Cdd:COG3468 167 GSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4419 SWAYADGPLPDGTVTYHVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDTGLDAHDFITSDNTLTLSGKLGAP 4498
Cdd:COG3468 247 GTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4499 LAAGEHAQISIDGGKTWVDVSVSGTSWSYVDGRQLADGDHLYQLRVVDDAGNIGSTASQLVTVDTVAPDASKTVTIDSIS 4578
Cdd:COG3468 327 GGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGG 406
|
410 420
....*....|....*....|...
gi 701771264 4579 TDTGLSNTDFVTSDTSLTVHGSL 4601
Cdd:COG3468 407 GVGGGGGGGLTLTGGTLTVNGNY 429
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
5958-6240 |
2.85e-04 |
|
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: 46.66 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMA-ANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKRADLRISDRVFARA 6036
Cdd:cd18542 3 LAILALLlATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6037 LRIK----NSARpksTGSFISQIRE-LESVRELITSTTIGTVSDIpffLLFVFILWLIGG-------------PLVFVVL 6098
Cdd:cd18542 83 QRLSfsfhDKAR---TGDLMSRCTSdVDTIRRFLAFGLVELVRAV---LLFIGALIIMFSinwkltlislaiiPFIALFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6099 LAIPLLLipgllvqRPLAHLSNEgmRESAIrNATLVEavqSIEDIKLLRA-------EQRFQNQwnntNDVAAGVGMKQR 6171
Cdd:cd18542 157 YVFFKKV-------RPAFEEIRE--QEGEL-NTVLQE---NLTGVRVVKAfaredyeIEKFDKE----NEEYRDLNIKLA 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6172 WLTSLLMTWTQEVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18542 220 KLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASAS 288
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
1993-2407 |
3.09e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 47.63 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1993 PLIVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPK 2072
Cdd:COG3468 30 NAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGGGGNSGTGGTGGGGGGGG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2073 LSIDPVAGDDIINASEHSQAHTVGGTSTGAAAGDVVTVVVTNGQGTSFTFTTTLDGNGNWNVGIPASVINGLADGSYTIT 2152
Cdd:COG3468 110 SGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAGGGGGGGAGGSGGAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2153 ASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWS 2232
Cdd:COG3468 190 STGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGGGAAGTGGGGGGTG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2233 TTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDVV 2312
Cdd:COG3468 270 TGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2313 TINLGGKLyqATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDvinaie 2392
Cdd:COG3468 350 GGGTGAAL--AGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGLTLTGG------ 421
|
410
....*....|....*
gi 701771264 2393 htqNLIINGTSSGLG 2407
Cdd:COG3468 422 ---TLTVNGNYTGNN 433
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6293-6482 |
3.11e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADlrRDMTLLSQQARLF-FGSIRDNLTMG-- 6369
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNYALYpHMSVRENMAYGlk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6370 -RPLASDEEIHRALALSGALGfvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD-------- 6440
Cdd:PRK11650 103 iRGMPKAEIEERVAEAARILE--------LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqmr 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 701771264 6441 -EIseQQLVANLASwlgnrTLVVATH-RIPILQLVDRIIVLDNG 6482
Cdd:PRK11650 175 lEI--QRLHRRLKT-----TSLYVTHdQVEAMTLADRVVVMNGG 211
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
3013-3516 |
3.15e-04 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 47.85 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3013 VTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVTIDHTVNVDLSAVAITIGQIAGDDVLNAAEK 3092
Cdd:COG4625 1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3093 GADLLLSGMTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKDGDTSVEVSVVNVTGNGASAGREISVDTA 3172
Cdd:COG4625 81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3173 APTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWsitvpadkasALGDGVYTVDASV 3252
Cdd:COG4625 161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGG----------GGGGGGGGGGGGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3253 SDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGAAAGDKITVTIGANSWTTTVDAAGNWSIG 3332
Cdd:COG4625 231 GGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3333 VPASVVSQLADGKVTINASLTDSAGNTGSGSHEVTVNTGLPSVNFNAISGDNVLNAIEKGEVLTLSGTSANLAPGTAVIV 3412
Cdd:COG4625 311 GGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3413 TLNGKNYTATTDASGNWRVDVQPGDLAGLGEANYTLTATATSSIGNSAGASASLLVDTAAPGITINPVTADNVLNAAEIA 3492
Cdd:COG4625 391 GGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSG 470
|
490 500
....*....|....*....|....
gi 701771264 3493 AGQTLSGKVSNAAAGDAVTINLGG 3516
Cdd:COG4625 471 SGAGTLTLTGNNTYTGTTTVNGGG 494
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
1942-2060 |
3.77e-04 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 45.36 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1942 DGDAQVTVSVSN---ANGNPATSTQEYSVDASaPTLIIDPLSGDNLLNAAEakqpLIVSGSSSA-EPGQEVTVTLN---- 2013
Cdd:NF032891 63 SSELTVGLVVSGyqdLSGNVGEEDTSHSLPIT-PTITITPIGDVDESEAAT----VVISGTSTRfEDGQTLTVEVKaqgs 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 701771264 2014 ---NVNYTATVGADGRWSVSvpASDLAALKDGTLTVSASVADKAGNPANA 2060
Cdd:NF032891 138 etvEVTGTATVQSDGSWTTN--ELDLSSWPDGTITVTVTGTNNLGVAAEE 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6294-6440 |
4.54e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQilldgISLG-QLDTA-------DLRRDMTLLsqqarlffgsirDN 6365
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-----IHCGtKLEVAyfdqhraELDPEKTVM------------DN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6366 LTMGRplaSDEEI-----HralalsgALGFVQkqknglNYLITEGGA-----GLSGGQRQALLLARTLILQPQILLLDEP 6435
Cdd:PRK11147 404 LAEGK---QEVMVngrprH-------VLGYLQ------DFLFHPKRAmtpvkALSGGERNRLLLARLFLKPSNLLILDEP 467
|
....*
gi 701771264 6436 TAWLD 6440
Cdd:PRK11147 468 TNDLD 472
|
|
| FG-GAP_3 |
pfam13517 |
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ... |
5155-5219 |
5.19e-04 |
|
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.
Pssm-ID: 433275 [Multi-domain] Cd Length: 61 Bit Score: 41.44 E-value: 5.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 5155 DINRDGHADMLVesTNYSYITQLMNNGDGTYTSTSPGSSATVGallWYGAVVSIDFQGDGYVDFV 5219
Cdd:pfam13517 1 DLDGDGKLDLVV--ANDGGLRLYLNNGDGTFTFITSVSLGGGG---GGLSVAVGDLDGDGRLDLL 60
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
5813-5914 |
5.74e-04 |
|
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.
Pssm-ID: 239073 [Multi-domain] Cd Length: 122 Bit Score: 43.14 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5813 AVARHYRLDFSEEHVR--VVINQESQSPHHLVleDMARQLGLALRSVPADVSLIDPWRLPLVVELNDGQMAVLTHMDKHg 5890
Cdd:cd02259 14 MLLRYFGIPVRRDVLLnaQQRRQQGLSLADLV--SLANKLGLTAQGVKLPLAALSRLQLPALLLWKQGHFVILYGADKG- 90
|
90 100
....*....|....*....|....
gi 701771264 5891 QLSIQLSGDSGLETvVSREALSQR 5914
Cdd:cd02259 91 QVLIADPLEEGPVT-LSESELEER 113
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
5958-6239 |
5.85e-04 |
|
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: 45.94 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5958 IMLVAMAANVLALAGMIFSMQVYDRVVPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKR--ADLRisDRVFAR 6035
Cdd:cd18550 4 VLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGvmYDLR--VQLYAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6036 A----LRIKNSARpksTGSFISQI-RELESVRELITSTTIGTVSDIPFFLLFVFILWLIGGPLVFVVLLAIPLLLIPGLL 6110
Cdd:cd18550 82 LqrmsLAFFTRTR---TGEIQSRLnNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6111 VQRPLAHLSNEGMRESAIRNATLVE--AVQSIEDIKLLRAEQRFQNQWNNTNDVAAGVGMKQ----RWLTSLLMTWTqev 6184
Cdd:cd18550 159 VGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQalagRWFFAALGLFT--- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6185 qSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKV 6239
Cdd:cd18550 236 -AIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLA 289
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6288-6481 |
6.99e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6288 LDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQIlldgislgqldTADLRRdMTLLS--QQARLFFGSIRDN 6365
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-----------QSQFSH-ITRLSfeQLQKLVSDEWQRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6366 LT---------MGRPLAS---DEEIHRALALSGALGFvqkqknGLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLD 6433
Cdd:PRK10938 87 NTdmlspgeddTGRTTAEiiqDEVKDPARCEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701771264 6434 EPTAWLDEISEQQLVANLASWLGNR-TLVVATHR---IPilQLVDRIIVLDN 6481
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGiTLVLVLNRfdeIP--DFVQFAGVLAD 210
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
4378-4445 |
7.74e-04 |
|
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).
Pssm-ID: 239028 [Multi-domain] Cd Length: 317 Bit Score: 45.37 E-value: 7.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 4378 ITADNKVVVKGSLSGALGNNEKAQISLDGGKTWTDLVVTG-----TSWA--YADGPLPDGTVTYHVRVVDNAGNV 4445
Cdd:cd02110 219 LVSGGRVEIGGVAWSGGRGIRRVEVSLDGGRTWQEARLEGplagpRAWRqwELDWDLPPGEYELVARATDSTGNV 293
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6279-6482 |
7.79e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.46 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6279 YDEEEKVNDLDiarLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISlGQLDTADLRRDMTLLsqqarlf 6358
Cdd:COG4586 32 YREVEAVDDIS---FTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-PFKRRKEFARRIGVV------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6359 FG---------SIRDNLTMgrpLA-----SDEEIHRALA-LSGALG---FVQKQ--KnglnyliteggagLSGGQRQ--- 6415
Cdd:COG4586 101 FGqrsqlwwdlPAIDSFRL---LKaiyriPDAEYKKRLDeLVELLDlgeLLDTPvrQ-------------LSLGQRMrce 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6416 ---ALL-----LartlilqpqilLLDEPTAWLDEISEQQLVANLASWlgNR----TLVVATHRIP-ILQLVDRIIVLDNG 6482
Cdd:COG4586 165 laaALLhrpkiL-----------FLDEPTIGLDVVSKEAIREFLKEY--NRergtTILLTSHDMDdIEALCDRVIVIDHG 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6293-6482 |
8.21e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQL--------------DTADLRRDMT-----LLSQ 6353
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfQHVRLFREMTvienlLVAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6354 ----QARLFFGSIRdnlTMGRPLASDEEIHRA---LALSGALGFVQKQKNGLNYliteggaglsgGQRQALLLARTLILQ 6426
Cdd:PRK11300 106 hqqlKTGLFSGLLK---TPAFRRAESEALDRAatwLERVGLLEHANRQAGNLAY-----------GQQRRLEIARCMVTQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6427 PQILLLDEPTAWLD--EISE-QQLVANLASWLGNRTLVVATHRIPILQLVDRIIVLDNG 6482
Cdd:PRK11300 172 PEILMLDEPAAGLNpkETKElDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| FG-GAP_3 |
pfam13517 |
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ... |
5383-5446 |
9.00e-04 |
|
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.
Pssm-ID: 433275 [Multi-domain] Cd Length: 61 Bit Score: 40.67 E-value: 9.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701771264 5383 DWNMDGRMDIIkLANTGQSYMYTNDGlKGVASFtSSKFGSATTSQVSGAALVDYDWDGAQDLLI 5446
Cdd:pfam13517 1 DLDGDGKLDLV-VANDGGLRLYLNNG-DGTFTF-ITSVSLGGGGGGLSVAVGDLDGDGRLDLLV 61
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
6115-6227 |
9.06e-04 |
|
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: 45.10 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6115 LAHLSNEGMRESAIRNATLVEAVQSIEDIKLLRAEQRFQNQWNNTNdvaagvgmkQRWLTSLL--MTWTQEVQSIVYAV- 6191
Cdd:cd18554 170 LRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRN---------GHFLTRALkhTRWNAKTFSAVNTIt 240
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 701771264 6192 ------VLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQI 6227
Cdd:cd18554 241 dlapllVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRL 282
|
|
| Peptidase_M10_C |
pfam08548 |
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ... |
5604-5729 |
1.05e-03 |
|
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.
Pssm-ID: 430067 [Multi-domain] Cd Length: 222 Bit Score: 44.29 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5604 WSAtGGMDVVDFRnstvgvtvdlGKTGAQNTGFNTATFSN---------------IEGIVGSSHDDVITGNSGNNTFEGG 5668
Cdd:pfam08548 37 WDA-GGNDTFDFS----------GYSQNQRINLNEGSFSDvgglkgnvsiahgvtIENAIGGSGNDVLIGNDADNILKGG 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 5669 GGNDTFNIGSG--------GHDTLLYklLNGSDATgGNGHDVVNGFSVGTwegtadsDRIDLRELLQGS 5729
Cdd:pfam08548 106 AGNDILYGGGGadqlwggaGNDIFVY--ASAKDSL-TAAPDTIRDFVSGI-------DKIDLSALNNNS 164
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6285-6481 |
1.13e-03 |
|
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: 43.30 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDIarlTITAGEKIAVLGRNGSGKSTLLQLLAGMQtpQHGQilldgislGQLDTADlRRDMTLLSQQARLFFGSIRD 6364
Cdd:cd03223 17 LKDLSF---EIKPGDRLLITGPSGTGKSSLFRALAGLW--PWGS--------GRIGMPE-GEDLLFLPQRPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6365 NLTmgrpLASDEEihralalsgalgfvqkqknglnyliteggagLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISE 6444
Cdd:cd03223 83 QLI----YPWDDV-------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*..
gi 701771264 6445 QQLVANLASWLGnrTLVVATHRIPILQLVDRIIVLDN 6481
Cdd:cd03223 128 DRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2605-2758 |
1.13e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 43.82 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2605 AEAGQTVTVRLNGESYQATVKAdgswslTVPAADVGKLTD--------GNITVTASVE-----------DQAGNPGSASR 2665
Cdd:NF032891 14 QAIGQSVTVTLTFDKAVQEATA------TLGGVAVTSLTDtadkkvwtGEVVVPASSEltvglvvsgyqDLSGNVGEEDT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2666 DVLVDVTvPKVTIGTMATDDVINQTEhgqaLVISGTSTGAQAGDIVTVTL-------GNKQYTGVVDTNGNWSvgVPRAD 2738
Cdd:NF032891 88 SHSLPIT-PTITITPIGDVDESEAAT----VVISGTSTRFEDGQTLTVEVkaqgsetVEVTGTATVQSDGSWT--TNELD 160
|
170 180
....*....|....*....|
gi 701771264 2739 VSALGDNTYTVTASITDKAG 2758
Cdd:NF032891 161 LSSWPDGTITVTVTGTNNLG 180
|
|
| Big_3_3 |
pfam13750 |
Bacterial Ig-like domain (group 3); This family consists of bacterial domains with an Ig-like ... |
1428-1567 |
1.23e-03 |
|
Bacterial Ig-like domain (group 3); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
Pssm-ID: 404614 [Multi-domain] Cd Length: 157 Bit Score: 43.21 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1428 GTWSVTVpvaDLANLTDGSWSVSASVSDVAGNPASTSHG--MLVDTTAPVVTI---NTFAGDNIVNRSEHAQAQVLSgkA 1502
Cdd:pfam13750 1 GNYTYTF---DLNRLPEGKYNLVLVAMDTFHNPTTLSPLqtILVDNTPPTVSIfdgKPISDGAVVNGLENLRITLAD--D 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 1503 TGAAVGDSVKI----TVNGVEYSTVLDASGNWSLGLPAEVISGLADGKYTATVVVTDKAGNVGGSSLAF 1567
Cdd:pfam13750 76 ATKSSLTSITLsggpANDKVYLSWVSLGKGRYRLNYPRLFPSLEEGESYTLTVTAEDEQGNAKTKSVGF 144
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6285-6482 |
1.29e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6285 VNDLDIARLTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTAD-LRRDMTLLSQQARLFFG-SI 6362
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQrSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6363 RDNLTMGR-PLASdeeihralalsgalGFVQKQKN-----------GLNYLITEGGAGLSGGQRQALLLARTLILQPQIL 6430
Cdd:PRK10982 91 MDNMWLGRyPTKG--------------MFVDQDKMyrdtkaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 6431 LLDEPTAWLDEISEQQLVANLASwLGNR--TLVVATHRI-PILQLVDRIIVLDNG 6482
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRK-LKERgcGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
4279-4354 |
1.36e-03 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 41.48 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 4279 LVLSGVTNAPAGQTVTITLNGQKYTTTVNGDGTWSYTLGssavSALADGDaYVIHASVSNSIGNSAGVDR-TITVDT 4354
Cdd:pfam19077 31 FTGTNEDGDVVTVTVSIDGNGVTGTATAGADGNWSFTPP----AALADGT-YTLTVTVTDIAGNTATSSPlSFTIDT 102
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
1997-2475 |
1.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 45.54 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1997 SGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPASDLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLSID 2076
Cdd:COG4625 12 GGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2077 PVAGDDIINASEHSQAHTVGGTSTGAAAGDVVTVVVTNGQGTSFTFTTTLDGNGNWNVGIPASVINGLADGSYTITASVT 2156
Cdd:COG4625 92 GVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2157 DAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTTVP 2236
Cdd:COG4625 172 GGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2237 ASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSALPTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDVVTINL 2316
Cdd:COG4625 252 GGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2317 GGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSRDIVIDANLPGLRVDTVAGDDVINAIEHTQN 2396
Cdd:COG4625 332 GGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGG 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 2397 LIINGTSSGLGAGSAVTVTINGKDYAATVRADGSWQAAVPGEDVARWAEGAVTIEVKGSSGAGNDVAIQHQVTVDLTEV 2475
Cdd:COG4625 412 GAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTV 490
|
|
| HemolysinCabind |
pfam00353 |
RTX calcium-binding nonapeptide repeat (4 copies); |
5648-5684 |
1.49e-03 |
|
RTX calcium-binding nonapeptide repeat (4 copies);
Pssm-ID: 459777 [Multi-domain] Cd Length: 36 Bit Score: 39.34 E-value: 1.49e-03
10 20 30
....*....|....*....|....*....|....*..
gi 701771264 5648 VGSSHDDVITGNSGNNTFEGGGGNDTFNiGSGGHDTL 5684
Cdd:pfam00353 1 YGGDGNDTLVGGAGNDTIYGGAGNDTLD-GGAGNDTL 36
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6293-6440 |
1.49e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.33 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLD-GISLGQLdTADLRRDMTLlsqqarlffgsirdNLTMGRP 6371
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYV-PQKLYLDTTL--------------PLTVNRF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701771264 6372 LASDEEIHRALALSgALGFVQKQknglnYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:PRK09544 90 LRLRPGTKKEDILP-ALKRVQAG-----HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
1398-1567 |
1.51e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 45.41 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1398 VITGTSTAQPGQTVTVSLNNQSYTGLVLADGTWSVTVPVAdlanLTDGSwSVSASVSDVAGN-PASTSHGMLVDTTAPVV 1476
Cdd:NF040520 437 SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITISPA----LTDKN-IGKVYAIDAAGNrSDATDVTGTKDTIAPNK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1477 -TINTFAGDN------IVNRSEHAQAQ-VLSGKATGAAVgdsVKITVNGVEYSTV-LDASGNWSLGLPAEvisgLADGKY 1547
Cdd:NF040520 512 pVLQKVTDDVgavkgaIAAGGETDDAKpKLSGSGEAKAT---LTIYDNGQAIGTVtVGDNGKWSFTLDKD----LALGKH 584
|
170 180
....*....|....*....|
gi 701771264 1548 TATVVVTDKAGNVGGSSLAF 1567
Cdd:NF040520 585 KITLTQTDAAGNTSEVSDPF 604
|
|
| Ig_like_ice |
NF012196 |
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of ... |
1551-1623 |
1.59e-03 |
|
Ig-like domain; This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
Pssm-ID: 467952 [Multi-domain] Cd Length: 108 Bit Score: 41.32 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1551 VVVTDKAGNVGGSSLAFDV-----ATGlpQITINAIAQDDVINAAE-KSAEVTVSGT--SNQPDGTQITVNLNGVDYAAV 1622
Cdd:NF012196 1 VTSHDAAGNTATATAHHTVtidthADA--TITIDTVTGDNVLNAAEsQQPTTTITGTvgGDVKVGDPVTLTVNGHTYTGT 78
|
.
gi 701771264 1623 V 1623
Cdd:NF012196 79 V 79
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
2137-2921 |
1.62e-03 |
|
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];
Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 45.52 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2137 PASVINGLADGSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEKGQDLVLSGTSNQPAGTLITVTL 2216
Cdd:COG3209 2 TSLGLVGGTTGASSTLLAATNAGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2217 NGINYQAVAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSALPTVIVNSVTSDNILNITEIAGG 2296
Cdd:COG3209 82 ALGDASAAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2297 QTLSGTVTGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASVTNGHGNTGSGSRDIVIDANLPG 2376
Cdd:COG3209 162 AGGGASAYGLTLGGAAAGPATGVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2377 LRVDTVAGDDVINAIEHTQNLIINGTSSGLGAGSAVTVTINGKD-YAATVRADGSWQAAVPGEDVARWAEGAVTIEVKGS 2455
Cdd:COG3209 242 ATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDASTGTGGAGGsNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2456 SGAGNDVAIQHQVTVDLTEVVISINAVTGDNVLNAAEKGANLELSGMTQNVEPGQTVNITFAGHTYTATVQADGSWKYTV 2535
Cdd:COG3209 322 GTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2536 PAADMVNLKEGDTAVQVSVTNKNGNSTDAAQNVSVDTLAPALTVDPVSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRL 2615
Cdd:COG3209 402 GVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGT 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2616 NGESYQATVKADGSWSLTVPAADVGKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDVINQTEHGQA 2695
Cdd:COG3209 482 GGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2696 LVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVGVPRADVSALGDNTYTVTASITDKAGNTGDTSHTVTVDTVAPT 2775
Cdd:COG3209 562 TGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTT 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2776 LSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVTVNLNGKNYAATVGADGKWTTTVPAGDVGKLGEAFYEVSVSASN 2855
Cdd:COG3209 642 GGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGT 721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 2856 GVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAELATGQTISGRVTGVQAGADVTINIGGVNYT 2921
Cdd:COG3209 722 TTTGGGGGTTTDGTGTGGTTGTLTTTSTTTTTTAGALTYTYDALGRLTSETTPGGVTQGTYTTRYT 787
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2507-2572 |
1.62e-03 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 41.10 E-value: 1.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 2507 EPGQTVNITFA----GHTYTATVQADGSWKYTVPAAdmvnLKEGDTAVQVSVTNKNGN-STDAAQNVSVDT 2572
Cdd:pfam19077 36 EDGDVVTVTVSidgnGVTGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGNtATSSPLSFTIDT 102
|
|
| outer_NodT |
TIGR01845 |
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this ... |
62-215 |
1.63e-03 |
|
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins]
Pssm-ID: 273830 [Multi-domain] Cd Length: 460 Bit Score: 45.10 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 62 AQIDQARSAWMPQISLNGSTGHSRTTDSSGSLKNSAAYGL--SLTQLVYDFGKTNSNISQQQSQRESYRYQLMATLTGVA 139
Cdd:TIGR01845 298 AQIGVAKAAFFPSITLSASIGLSASQLSRLFDGGSRFWSIgpALALPIFDGGSLRAALDSAKATYDAAVAQYRQTVLTAF 377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 140 EKTAQAYVDLKRNEALVEATEESIAALQNVNAMAKLRADAGLNSSSDVLQTQTRIAGMRSTLEQYRAARQSAKARL 215
Cdd:TIGR01845 378 QEVADALVALQALARRLDAQRQAVEQAQEALSLAQTRYRAGLDSYLTVLEAQRSLLTAQRSLATLQARRLSDSVAL 453
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
1756-1850 |
1.92e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 43.05 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1756 GNTGSTDHDITIDAQlPGLRLDTISGDDIINLAehnqDLVVSGTCSGLNAGSVVTVTLN-------GKDYLATVNADGSW 1828
Cdd:NF032891 80 GNVGEEDTSHSLPIT-PTITITPIGDVDESEAA----TVVISGTSTRFEDGQTLTVEVKaqgsetvEVTGTATVQSDGSW 154
|
90 100
....*....|....*....|..
gi 701771264 1829 SaaVPAADVSTWPDGVLTVTAK 1850
Cdd:NF032891 155 T--TNELDLSSWPDGTITVTVT 174
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
3166-3359 |
1.96e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 45.03 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3166 EISV--DTAAP---TLQINTiAGDdvlnaaeagqplVITGTSNAEPGQTVTVTLNNETYTGIVQANGTWSITVpadkASA 3240
Cdd:NF040520 414 EITAgkDTIAPdkpTAQINA-AGT------------SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITI----SPA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3241 LGDG----VYtvdasVSDAAGNGSSASHNLSV-DVTVPSISFGVVAGDDVinLAEHGQaqiISGSSSGAAAGDKITVTIG 3315
Cdd:NF040520 477 LTDKnigkVY-----AIDAAGNRSDATDVTGTkDTIAPNKPVLQKVTDDV--GAVKGA---IAAGGETDDAKPKLSGSGE 546
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 3316 ANSWTT-----------TVDAAGNWSIgvpaSVVSQLADGKVTINASLTDSAGNT 3359
Cdd:NF040520 547 AKATLTiydngqaigtvTVGDNGKWSF----TLDKDLALGKHKITLTQTDAAGNT 597
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
1995-2194 |
2.25e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 44.64 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1995 IVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPAsdlaALKDGTLTvSASVADKAGNPANA-DRGMRVDITEPKL 2073
Cdd:NF040520 437 SVTGTAEANAKIEIKDSAGKVIGTGTADADGKFTITISP----ALTDKNIG-KVYAIDAAGNRSDAtDVTGTKDTIAPNK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2074 SIDPVAGDDIinaSEHSQAHTVGGTS-------TGAAAGDVVTVVVTNGQGTSftfTTTLDGNGNWNVgipaSVINGLAD 2146
Cdd:NF040520 512 PVLQKVTDDV---GAVKGAIAAGGETddakpklSGSGEAKATLTIYDNGQAIG---TVTVGDNGKWSF----TLDKDLAL 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 2147 GSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEK 2194
Cdd:NF040520 582 GKHKITLTQTDAAGNTSEVSDPFTFTVVAPKTASASEQSEVDTSNTET 629
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
2476-2692 |
2.45e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 44.64 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2476 VISINAvTGDNVLNAAEKGANLELSGMTQNVepgqtvnitfaghTYTATVQADGswKYTV---PAadmvnLKEGDTAvQV 2552
Cdd:NF040520 428 TAQINA-AGTSVTGTAEANAKIEIKDSAGKV-------------IGTGTADADG--KFTItisPA-----LTDKNIG-KV 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2553 SVTNKNGNSTDAAQNVSV-DTLAPALTVDPVSQDNL------LNAAEAKQDLVISGTSTAEAGQTVTVRLNGesyQA--- 2622
Cdd:NF040520 486 YAIDAAGNRSDATDVTGTkDTIAPNKPVLQKVTDDVgavkgaIAAGGETDDAKPKLSGSGEAKATLTIYDNG---QAigt 562
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 2623 -TVKADGSWSLTVpaadVGKLTDGNITVTASVEDQAGNPGSASRDVLVDVTVPKVTIGTMATDDVINQTEH 2692
Cdd:NF040520 563 vTVGDNGKWSFTL----DKDLALGKHKITLTQTDAAGNTSEVSDPFTFTVVAPKTASASEQSEVDTSNTET 629
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
5959-6240 |
2.63e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 43.68 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 5959 MLVAMAANVLALAGMIFSMQVYDRV-VPSQSVPTLWVLFGGVMLAILFEFTMRMLRVHIADVVGKR--ADLRisDRVFAR 6035
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKvvADLR--SDLYDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6036 ALRIknSAR---PKSTGSFISQI----RELE-----SVRELITST-TIGTVSDIPFFL-----LFVF--ILWLIGGPLVF 6095
Cdd:cd18778 83 LQRL--SLRyfdDRQTGDLMSRVindvANVErliadGIPQGITNVlTLVGVAIILFSInpklaLLTLipIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6096 VVllaiplllipgllVQRPLAHLSNEgmRESAIrNATLVEAVQSIEDIKLLRAEQRFQNQWNN-TNDVAAGV--GMKQRW 6172
Cdd:cd18778 161 SK-------------KVRPRYRKVRE--ALGEL-NALLQDNLSGIREIQAFGREEEEAKRFEAlSRRYRKAQlrAMKLWA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 6173 LTSLLMTWtqeVQSIVYAVVLLVGCYLVINGDMTTGALVGTSILASRTIAPLAQISGVLSRWQQAKVA 6240
Cdd:cd18778 225 IFHPLMEF---LTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAG 289
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
4820-4868 |
2.66e-03 |
|
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).
Pssm-ID: 239028 [Multi-domain] Cd Length: 317 Bit Score: 43.83 E-value: 2.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 701771264 4820 ERVQISLDGGRNWVDAVVNG--------TAWHYvDGRtLADGDYVYQVRIIDQAGNV 4868
Cdd:cd02110 239 RRVEVSLDGGRTWQEARLEGplagprawRQWEL-DWD-LPPGEYELVARATDSTGNV 293
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
3972-4396 |
2.68e-03 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 44.55 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3972 IGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTLNGIQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMAS 4051
Cdd:COG3468 11 GLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4052 ATDSANNATSATHNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGQKVTVKLGSESYEATVQADGSWSIT 4131
Cdd:COG3468 91 GGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4132 VAAEDLAKLADGEFSVHAAVNDKAGNPGSADRTLTVDTTAPTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITVT 4211
Cdd:COG3468 171 GGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4212 FNNHTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAGQ 4291
Cdd:COG3468 251 GGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4292 TVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSNSIGNSAGVDRTITVDTTPPQMTITIDSLQNDTG 4371
Cdd:COG3468 331 GGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGG 410
|
410 420
....*....|....*....|....*
gi 701771264 4372 LSASDFITADNKVVVKGSLSGALGN 4396
Cdd:COG3468 411 GGGGGLTLTGGTLTVNGNYTGNNGT 435
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6295-6482 |
2.69e-03 |
|
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: 42.62 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6295 ITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQH--GQILLDGISLGQldtaDLRRdMTLLSQQARLFFGsirdNLTmgrpl 6372
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTAGVitGEILINGRPLDK----NFQR-STGYVEQQDVHSP----NLT----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6373 asdeeIHRALALSGALgfvqkqknglnyliteggAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDEISEQ---QLVA 6449
Cdd:cd03232 96 -----VREALRFSALL------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYnivRFLK 152
|
170 180 190
....*....|....*....|....*....|....*
gi 701771264 6450 NLASwlGNRTLVVATHR--IPILQLVDRIIVLDNG 6482
Cdd:cd03232 153 KLAD--SGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
3308-3370 |
3.79e-03 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 40.33 E-value: 3.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701771264 3308 DKITVTI----GANSWTTTVDAAGNWSIGVPASvvsqLADGKVTINASLTDSAGNTGSGSH-EVTVNT 3370
Cdd:pfam19077 39 DVVTVTVsidgNGVTGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGNTATSSPlSFTIDT 102
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
689-769 |
3.84e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 42.28 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 689 NTLNAAEQANdFVISGSATELASGTALTVTLN-------GKTYATTVGSDGSWSVTvpAADAKSLADGSWTVTVSGKDAa 761
Cdd:NF032891 103 GDVDESEAAT-VVISGTSTRFEDGQTLTVEVKaqgsetvEVTGTATVQSDGSWTTN--ELDLSSWPDGTITVTVTGTNN- 178
|
....*...
gi 701771264 762 gNNISASE 769
Cdd:NF032891 179 -LGVAAEE 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6291-6465 |
4.25e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6291 ARLTITAGEKIAVLGRNGSGKSTLLQLLAgMQT----PQHGQILL-------DGISLGQ--LDTaDLRR------DMTLL 6351
Cdd:PLN03073 196 ASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAidgiPKNCQILHveqevvgDDTTALQcvLNT-DIERtqlleeEAQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6352 SQQARLFF------GSIRDNLTMGRPLASD--EEIHRALALSGALGFVQKQKN---GLNY---LITEGGAGLSGGQRQAL 6417
Cdd:PLN03073 274 AQQRELEFetetgkGKGANKDGVDKDAVSQrlEEIYKRLELIDAYTAEARAASilaGLSFtpeMQVKATKTFSGGWRMRI 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701771264 6418 LLARTLILQPQILLLDEPTAWLDEISEQQLVANLASWlgNRTLVVATH 6465
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
2494-3034 |
4.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 44.00 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2494 GANLELSGMTQNVEPGQTVNITFAGHTYTATVQADGSWKYTVPAADMVNLKEGDTAVQVSVTNKNGNSTDAAQNVSVDTL 2573
Cdd:COG4625 5 GGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2574 APALTVDPVSQDNLLNAAEAKQDLVISGTSTAEAGQTVTVRLNGESYQATVKADGSWSLTVPAADVGKLTDGNITVTASV 2653
Cdd:COG4625 85 GGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2654 EDQAGNPGSASRDVLVDVTVPKVTIGTMATDDVINQTEHGQALVISGTSTGAQAGDIVTVTLGNKQYTGVVDTNGNWSVG 2733
Cdd:COG4625 165 GGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2734 VPRADVSALGDNTYTVTASITDKAGNTGDTSHTVTVDTVAPTLSIDTIAGDNILNADEKTGDVVISGTSTGLAAGTSVTV 2813
Cdd:COG4625 245 GGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2814 NLNGKNYAATVGADGKWTTTVPAGDVGKLGEAFYEVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAELA 2893
Cdd:COG4625 325 GGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2894 TGQTISGRVTGVQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINASVTDGAGNTGTGSRDVTIDAAL 2973
Cdd:COG4625 405 AGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTY 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701771264 2974 PGIRVNTIAGDDVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQTVV 3034
Cdd:COG4625 485 TGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTIL 545
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
3539-4060 |
4.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 44.00 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3539 TALGNGKLTVTASVTNGHGNSGTADREFTVDASLPGIRINTVAGDDVVNAIEHNQNLIISGSASGMSEGSTVTVTINGKS 3618
Cdd:COG4625 2 GGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3619 YLATVSASGTWSAAVPAGDVSLWAAGNLTVTAAGSSSAGNPISIDRSVNVDLSPVAVSVENITADNVLNAAEKGADLVLS 3698
Cdd:COG4625 82 GGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3699 GKTQNVEAGQTVTITFGGRTYTAQVESDGSWHYTVPASDIAGLKDGDASVKVSVTNVNGNGASAEREFSVDATAPGLTIN 3778
Cdd:COG4625 162 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3779 PIATDNVINAAEAGAGVTVTGTSNAQAGQTVTLTLDGKTYTGVVKADGTWSITLDSTALGALADNQYVIKVDVSDAAGNK 3858
Cdd:COG4625 242 GGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3859 TTGSQNMTLDTTAPTVSFNAVAG-----DDIINLEEHAQAQIISGSSTGAAAGNKIIITLDGVQYVTQVDAKGNWSVGVP 3933
Cdd:COG4625 322 GGGGGGGGGGGGAGGGGGSGGAGaggggAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3934 ASAVSALKNGTATITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTL 4013
Cdd:COG4625 402 GGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGN 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 701771264 4014 NGIQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSANNAT 4060
Cdd:COG4625 482 NTYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGT 528
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
2825-3317 |
4.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 44.00 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2825 GADGKWTTTVPAGDVGKLGEAFYEVSVSASNGVGNAGSQSSTLEVASTLPGVIINAVAIDDIINAAELATGQTISGRVTG 2904
Cdd:COG4625 3 GGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2905 VQAGADVTINIGGVNYTAKVQSDLTWSLTLGQDVLTALGDGSLKINASVTDGAGNTGTGSRDVTIDAALPGIRVNTIAGD 2984
Cdd:COG4625 83 GGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2985 DVINAIEHGLNLVINGTSSGLSEGSTVTVTINGKDYAATVRADGSWQTVVPGNEVSQWQAGDITVSAGGTSSSGNPVTID 3064
Cdd:COG4625 163 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3065 HTVNVDLSAVAITIGQIAGDDVLNAAEKGADLLLSGMTQNVEAGQTISITFAGHTYTTQVASDGSWKFTVPANDMKGLKD 3144
Cdd:COG4625 243 GGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3145 GDTSVEVSVVNVTGNGASAGREISVDTAAPTLQINTIAGDDVLNAAEAGQPLVITGTSNAEPGQTVTVTLNNETYTGIVQ 3224
Cdd:COG4625 323 GGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3225 ANGTWSITVPADKASALGDGVYTVDASVSDAAGNGSSASHNLSVDVTVPSISFGVVAGDDVINLAEHGQAQIISGSSSGA 3304
Cdd:COG4625 403 GGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNN 482
|
490
....*....|...
gi 701771264 3305 AAGDKITVTIGAN 3317
Cdd:COG4625 483 TYTGTTTVNGGGN 495
|
|
| Big_13 |
pfam19077 |
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ... |
2198-2271 |
4.73e-03 |
|
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.
Pssm-ID: 465968 [Multi-domain] Cd Length: 102 Bit Score: 39.94 E-value: 4.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701771264 2198 LVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTTVPASavskLGEANYTVTAAVTDAHGNSS-SDSHNVQVD 2271
Cdd:pfam19077 31 FTGTNEDGDVVTVTVSIDGNGVTGTATAGADGNWSFTPPAA----LADGTYTLTVTVTDIAGNTAtSSPLSFTID 101
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
3891-4670 |
5.36e-03 |
|
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];
Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 43.59 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3891 AQAQIISGSSTGAAAGNKIIITLDGVQYVTQVDAKGNWSVGVPASAVSALKNGTATITATLTDSAGNEGANSHTVEVNAA 3970
Cdd:COG3209 17 LLAATNAGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGYVGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3971 RIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVTLNGIQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMA 4050
Cdd:COG3209 97 AAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4051 SATDSANNATSATHNISVDTVAPIVTIADISGDNAINAAEQQQPLTIRGTSSAEAGQKVTVKLGSESYEATVQADGSWSI 4130
Cdd:COG3209 177 AAGPATGVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVATAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4131 TVAAEDLAKLADGEFSVHAAVNDKAGNPGSADRTLTVDTTAPTITFDKVAGDDIINSAEQQAGQAISGTTNAQPGQTITV 4210
Cdd:COG3209 257 TTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4211 TFNNHTYQAVDFLGAADGSYQISASVSDKAGNSSSADKQVTLSGEVPTISINTFAGDDIVSAAEHGTPLVLSGVTNAPAG 4290
Cdd:COG3209 337 TTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4291 QTVTITLNGQKYTTTVNGDGTWSYTLGSSAVSALADGDAYVIHASVSNSIGNSAGVDRTITVDTTPPQMTITIDSLQNDT 4370
Cdd:COG3209 417 GGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTL 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4371 GLSASDFITADNKVVVKGSLSGALGNNekaqisldGGKTWTDLVVTGTSWAYADGPLPDGTVTYHVRVVDNAGNVGSTAT 4450
Cdd:COG3209 497 GTDTTLDDTLGGTTTTTAGARGLVVTT--------GTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTV 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4451 KNVTVDTVAPDAGTTITVEAISRDTGLdahdfiTSDNTLTLSGKLGAPLAAGEHAQISIDGGKTWVDVSVSGTSWSYVDG 4530
Cdd:COG3209 569 TTTGDGTGGASTTTGTTGGTATTTTVT------TTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4531 RQLADGDHLYQLRVVDDAGNIGSTASQLVTVDTVAPDASKTVTIDSISTDTGLSNTDFVTSDTSLTVHGSLGAPLLAGEY 4610
Cdd:COG3209 643 GTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTT 722
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4611 VQISlDGGTVWQTVVTIGSTWYFNDGRTLSDGTYQYLVRVVDDAGNVGQSASKNVTVDTT 4670
Cdd:COG3209 723 TTGG-GGGTTTDGTGTGGTTGTLTTTSTTTTTTAGALTYTYDALGRLTSETTPGGVTQGT 781
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6293-6479 |
5.52e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.77 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISLGQLDTADL---RRDMTLLSQ------QARLFFGSI- 6362
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQdplaslNPRMTIGEIi 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6363 RDNLTMGRPLASDEEI-HRALALSGALGFvqkqkngLNYLITEGGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLDe 6441
Cdd:PRK15079 122 AEPLRTYHPKLSRQEVkDRVKAMMLKVGL-------LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701771264 6442 ISEQQLVANLASWLGNR---TLVVATHRIPILQ-LVDRIIVL 6479
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmglSLIFIAHDLAVVKhISDRVLVM 235
|
|
| PRK08026 |
PRK08026 |
FliC/FljB family flagellin; |
648-881 |
5.67e-03 |
|
FliC/FljB family flagellin;
Pssm-ID: 236140 [Multi-domain] Cd Length: 529 Bit Score: 43.19 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 648 DGTHTYSVvqIDGNKITSAGEItLNVVTAQASLTAATTAGDNTLNAAeqANDFVISGSATELASGTALTVTLNGKTYatt 727
Cdd:PRK08026 199 DTTGLYDV--KTKNAALTTADA-LAKLGDGDKVTATATGGDYTYNAK--SGKYQAADLAATLTPDVGGTAGASYTIK--- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 728 vgsDGSWSVTVpAADAKSLADGSWTVTVSGKDAAGNNISAsetlvvdtqAPSLTLDILAGDNIINAAEHNAAVTVSGKTD 807
Cdd:PRK08026 271 ---DGTYEVNV-DSDGKITLGGSALYIDATGNLTTNNAGA---------ATKATLDALKKTASEGAATAKAALAAAGVTV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 808 AEAGQVVTLKLNGkTYTATVGADGGWSMEVPaADVQAMADN------SYTLNLSVSDKAGNTTTTNASLLVDTTPPEASV 881
Cdd:PRK08026 338 ADGVTAKTVKMSY-TDKNGKVIDGGYAVKTG-DDYYAADYDeitgaiSATTTYYTAKDGTTKTAANKLGGADGKTEVVTI 415
|
|
| Ca_tandemer |
NF033510 |
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the ... |
4556-4658 |
5.77e-03 |
|
Ca2+-stabilized adhesin repeat; This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
Pssm-ID: 411149 [Multi-domain] Cd Length: 97 Bit Score: 39.58 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4556 SQLVTVDTVAPdaskTVTIDSISTDTGLSNTDfvtSDTSLTVHGSLGAPllAGEYVQISLDGgTVWQTVVTIGSTWYFN- 4634
Cdd:NF033510 1 THPVTVDTTAP----ALTINPVAGDDVLNAAE---QGQGLTLSGTTTAE--AGQTVTVTLNG-KTYTATVDADGSWSVTv 70
|
90 100
....*....|....*....|....*..
gi 701771264 4635 ---DGRTLSDGTYQYLVRVVDDAGNVG 4658
Cdd:NF033510 71 paaDLAALADGTYTVTVTVTDAAGNTS 97
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
1875-2356 |
5.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 43.61 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1875 SVNSVTADNVLNAAEKGVDLVLSGLTTNVEPGQTVTITFAGHRYTTSVNNDGSWSYTVPAADMARLKDGDAQVTVSVSNA 1954
Cdd:COG4625 1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 1955 NGNPATSTQEYSVDASAPTLIIDPLSGDNLLNAAEAKQPLIVSGSSSAEPGQEVTVTLNNVNYTATVGADGRWSVSVPAS 2034
Cdd:COG4625 81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2035 DLAALKDGTLTVSASVADKAGNPANADRGMRVDITEPKLSIDPVAGDDIINASEHSQAHTVGGTSTGAAAGDVVTVVVTN 2114
Cdd:COG4625 161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2115 GQGTSFTFTTTLDGNGNWNVGIPASVINGLADGSYTITASVTDAAGNSGSADRALTVNTALPVISLATIAGDDVINATEK 2194
Cdd:COG4625 241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2195 GQDLVLSGTSNQPAGTLITVTLNGINYQAVAGTDGSWSTTVPASAVSKLGEANYTVTAAVTDAHGNSSSDSHNVQVDSAL 2274
Cdd:COG4625 321 GGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2275 PTVIVNSVTSDNILNITEIAGGQTLSGTVTGAVKGDVVTINLGGKLYQATVQDDLSWSLPVSKEILTALGNGELTITASV 2354
Cdd:COG4625 401 GGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTG 480
|
..
gi 701771264 2355 TN 2356
Cdd:COG4625 481 NN 482
|
|
| Ig_like_BLP2 |
NF040520 |
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ... |
4065-4579 |
6.47e-03 |
|
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.
Pssm-ID: 468522 [Multi-domain] Cd Length: 729 Bit Score: 43.10 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4065 NISVDTVAPIVTIADISGDNainaaeqqqpLTIRGTssAEAGQKVTVKLGSESYEATVQADGSWSITVAAEDlaKLADGE 4144
Cdd:NF040520 161 NGPVDITPPATPTATLADDT----------QTITGK--AEANAKIYIKDATGKVIATGQADASGNYTIKLDQ--PLVNGN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4145 fSVHAAVNDKAGNPGSADR-TLTVDTTAPtitfdkvagdDIINSAEQQAGQAISGttNAQPGQTITVtfnnhtYQAVD-F 4222
Cdd:NF040520 227 -KVNVTAIDAAGNASKATVvTGTKDTIAP----------DAPQAQLNADGTIVTG--KTEANAKVSV------YDADGkL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4223 LGAA----DGSYQISAS------------VSDKAGNSSSADKQV----TLSGEVPTISINTfAGDDIVSAAEHGTPLVLS 4282
Cdd:NF040520 288 LGTVtankEGLYSIKVSppltsdkggtviAEDAAGNKSEPSKIIagkdTIAPDQPLVEVNK-EGTSIEGRAEANAKVQIK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4283 GVTNAPAGqtvtitlngqkyTTTVNGDGTWSYTLGSsavsALADGD-AYVIhasVSNSIGNSagvdrtitvdTTPPQMTI 4361
Cdd:NF040520 367 DADGKVIG------------TGTADAQGKFQITLSP----ALKTSQkGTII---VEDAAGNQ----------SKPLEITA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4362 TIDSLQNDtglSASDFITADNKVVvkgslSGALGNNEKAQISLDGGKTwtdlVVTGTswAYADG--------PLPDGTVT 4433
Cdd:NF040520 418 GKDTIAPD---KPTAQINAAGTSV-----TGTAEANAKIEIKDSAGKV----IGTGT--ADADGkftitispALTDKNIG 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4434 YhVRVVDNAGNVGSTATKNVTVDTVAPDAGTTITVEAISRDT-GLDAHDFITSDNTLTLSGKlgaplaaGE-HAQISI-D 4510
Cdd:NF040520 484 K-VYAIDAAGNRSDATDVTGTKDTIAPNKPVLQKVTDDVGAVkGAIAAGGETDDAKPKLSGS-------GEaKATLTIyD 555
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4511 GGKTWVDVSV-SGTSWSYVDGRQLADGDHLYQLRVVDDAGNIgSTASQLVTVDTVAPDASKTVTIDSIST 4579
Cdd:NF040520 556 NGQAIGTVTVgDNGKWSFTLDKDLALGKHKITLTQTDAAGNT-SEVSDPFTFTVVAPKTASASEQSEVDT 624
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
2344-2459 |
6.82e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 41.51 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 2344 GNGELTITASVTN---GHGNTGSGSRDIVIDANlPGLRVDTVAGDDVINAiehtQNLIINGTSSGLGAGSAVTVTINGKD 2420
Cdd:NF032891 62 ASSELTVGLVVSGyqdLSGNVGEEDTSHSLPIT-PTITITPIGDVDESEA----ATVVISGTSTRFEDGQTLTVEVKAQG 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 701771264 2421 YA-------ATVRADGSWqaAVPGEDVARWAEGAVTIEVKGSSGAG 2459
Cdd:NF032891 137 SEtvevtgtATVQSDGSW--TTNELDLSSWPDGTITVTVTGTNNLG 180
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
3718-4107 |
7.13e-03 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 43.40 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3718 TYTAQVESD-GSWHY----TVPASDIAGLKDGDASVKVSVTNVNG----NGASAEREFSVDATAP----GLTINPIATDN 3784
Cdd:COG4733 566 AYEVEWRRDdGNWVSvprtSGTSFEVPGIYAGDYEVRVRAINALGvssaWAASSETTVTGKTAPPpaptGLTATGGLGGI 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3785 VIN-AAEAGAGVTVT----GTSNAQAGQTVTLTL-DGKTYTGV-VKADGT---WSITLDSTALGALADNQYVIKVDVSDA 3854
Cdd:COG4733 646 TLSwSFPVDADTLRTeirySTTGDWASATVAQALyPGNTYTLAgLKAGQTyyyRARAVDRSGNVSAWWVSGQASADAAGI 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3855 AGNKTTGSQNMTLDTTAPTVSFNAVAGDDIINLEEHAQAQIISGSSTGAAAGNKIIITLDGVQYVTQVDAKGNWSVGVpa 3934
Cdd:COG4733 726 LDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVAATVAESATAAAATGT-- 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 3935 SAVSALKNGTATITATLTDSAGNEGANSHTVEVNAARIGLTIDTISHDDVINAAEARQDLTIGGSSTELAVGTQVTVT-L 4013
Cdd:COG4733 804 AADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGTtA 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4014 NGIQYTTTIQPGGGWSVTVPANQVQNLAHGSGYTVMASATDSANNATSATHNI-SVDTVAPIVTIADISGDNAINAAEQQ 4092
Cdd:COG4733 884 ADVSAVADSTAASLTAIVIAATTIIDAIGDGTTREPAGDIGASGGAQGFAVTIvGSFDGAGAVATVDAGQSVVDGVGTAV 963
|
410
....*....|....*
gi 701771264 4093 QPLTIRGTSSAEAGQ 4107
Cdd:COG4733 964 EAANGTETAAGGGSQ 978
|
|
| tail_200_repeat |
NF032891 |
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 ... |
4007-4147 |
7.15e-03 |
|
tandem large repeat; This HMM describes a domain of nearly 200 amino acids, found in up to 14 tandem repeats in the C-terminal region of very large protein, in Vibrio parahaemolyticus and related species.
Pssm-ID: 467960 [Multi-domain] Cd Length: 192 Bit Score: 41.51 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 4007 TQVTVTLNGIQYTTTIQPGGG--W--SVTVPANQVqnlaHGSGYTVmASATDSANNATSATHNISVDtVAPIVTIADISG 4082
Cdd:NF032891 31 QEATATLGGVAVTSLTDTADKkvWtgEVVVPASSE----LTVGLVV-SGYQDLSGNVGEEDTSHSLP-ITPTITITPIGD 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701771264 4083 DNAINAAEqqqpLTIRGTSSA-EAGQKVTVKL---GSESYE----ATVQADGSWsiTVAAEDLAKLADGEFSV 4147
Cdd:NF032891 105 VDESEAAT----VVISGTSTRfEDGQTLTVEVkaqGSETVEvtgtATVQSDGSW--TTNELDLSSWPDGTITV 171
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
6294-6333 |
7.38e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 7.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 701771264 6294 TITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG 6333
Cdd:PRK13545 46 EVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6298-6440 |
8.02e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6298 GEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDG-----ISLGQLDTadLRRDMTLLSQQArlfFGSIRDNLTMGRPL 6372
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtLSPGKLQA--LRRDIQFIFQDP---YASLDPRQTVGDSI 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701771264 6373 ASDEEIHRALALSGALGFVQ--------KQKNGLNYlitegGAGLSGGQRQALLLARTLILQPQILLLDEPTAWLD 6440
Cdd:PRK10261 425 MEPLRVHGLLPGKAAAARVAwllervglLPEHAWRY-----PHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6293-6449 |
8.51e-03 |
|
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: 41.65 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6293 LTITAGEKIAVLGRNGSGKSTLLQLLAGMQTPQHGQILLDGISlGQLDTA--------DLRRDmTL--LSQqarlFFGSI 6362
Cdd:COG4778 32 FSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDLAqaspreilALRRR-TIgyVSQ----FLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701771264 6363 -----RDnLTMGRPLASDEEIHRALALSGALgfvqkqkngLNYL-ITEGGAGL-----SGGQRQALLLARTLILQPQILL 6431
Cdd:COG4778 106 prvsaLD-VVAEPLLERGVDREEARARAREL---------LARLnLPERLWDLppatfSGGEQQRVNIARGFIADPPLLL 175
|
170
....*....|....*...
gi 701771264 6432 LDEPTAWLDEISEQQLVA 6449
Cdd:COG4778 176 LDEPTASLDAANRAVVVE 193
|
|
| |
