|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
528-1279 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1198.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 528 EDRDGVRFSWNVWPSSRLEATRMVVPVASLFTPLKERPDLPPIQYEPVLCSraTCRAVLNPLCQVDYRAKLWACNFCYQR 607
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 608 NQFPPTYAGISEVNQPAELLPQFSTIEYVVQR---GPQMPLNFLYVVDTCMEDEDLQALKESLQMSLSLLPPTALVGLIT 684
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPgsgGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 685 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGL--SKQQVAQPGRGPQQ--PQAPPANRFLQPVQKIDMNLTDLL 760
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLggKKRRPAGGGIAGARdgLSSSGVNRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 761 GELQKDPWPVTQGKRPLRSLGVALSIAVGLLECTFPNTGARIMTFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKFM 840
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 841 KKATKHYEALANRAAANGHIIDIYACALDQTGLAEMKCCTNYTAGYMVMADSFNTSLFKQTFQRIFNKDVQGSFKMAFAG 920
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 921 TLEIKTSREIKISGAIGPCVSLNAKGPCVSENEIGTGGTCQWKICGLDPNTTLAVYFEVVNQHNA-PIPQGGRGAIQYVT 999
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1000 QYQHSSGQRRIRVTTVARNWADAqTQIQNISASFDQEASAILMARLAVYRAESEEGPDVLRWLDRQLIRLCQKFGDYHKD 1079
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1080 DPNSFRFSETFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFNGPPEPVLLDSSSIL 1159
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1160 PDRILLMDTFFQILIYHGETVAQWRKAGYQDMPEYENFRHLLQAPVDDAQEILQTRFPMPRYIDTEHGGSQARFLLSKVN 1239
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1832133605 1240 PSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLKKLAVSS 1279
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
525-1280 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 967.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 525 QQNEDRDGVRFSWNVWPSSRLEATRMVVPVASLFTPLKERPDLPPIQYEPVLCsRATCRAVLNPLCQVDYRAKLWACNFC 604
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 605 YQRNQFPPTYAGISEVNQPAELLPQFSTIEYVVQRGPQMPLNFLYVVDTCMEDEDLQALKESLQMSLSLLPPTALVGLIT 684
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 685 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKQ--QVAQPGRGPQQPQAPPaNRFLQPVQKIDMNLTDLLGE 762
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPtkSGGFESKISGIGQFAS-SRFLLPTQQCEFKLLNILEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 763 LQKDPWPVTQGKRPLRSLGVALSIAVGLLECTFPNTGARIMTFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKFMKK 842
Cdd:COG5047 242 LQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 843 ATKHYEALANRAAANGHIIDIYACALDQTGLAEMKCCTNYTAGYMVMADSFNTSLFKQTFQRIFNKDVQGSFKMAFAGTL 922
Cdd:COG5047 322 ATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 923 EIKTSREIKISGAIGPCVSLNAKGPCVSENEIGTGGTCQWKICGLDPNTTLAVYFEVVNQHNAPIPQGG-RGAIQYVTQY 1001
Cdd:COG5047 402 EVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1002 QHSSGQRRIRVTTVARNWADAQTQIqnISASFDQEASAILMARLAVYRAESEEGPDVLRWLDRQLIRLCQKFGDYHKDDP 1081
Cdd:COG5047 482 QHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1082 NSFRFSETFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFNGPPEPVLLDSSSILPD 1161
Cdd:COG5047 560 SSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPD 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1162 RILLMDTFFQILIYHGETVAQWRKAGYQDMPEYENFRHLLQAPVDDAQEILQTRFPMPRYIDTEHGGSQARFLLSKVNPS 1241
Cdd:COG5047 640 VILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPS 719
|
730 740 750
....*....|....*....|....*....|....*....
gi 1832133605 1242 QTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 1280
Cdd:COG5047 720 DITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
2-430 |
0e+00 |
|
signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.
Pssm-ID: 273615 [Multi-domain] Cd Length: 428 Bit Score: 801.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 2 VLADLGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFK 81
Cdd:TIGR01425 1 VLAQLGSSLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 82 ELVKLVDPGVKSWTPTKGKNNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYG 161
Cdd:TIGR01425 81 ELCNLVDPGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 162 SYTEMDPVIIAAEGVEKFKSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVD 241
Cdd:TIGR01425 161 SYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQAKAFKDSVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 242 VASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNE-ELID 320
Cdd:TIGR01425 241 VGSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKLLGMGDLKGLIDKVQDLALNDEEkTLIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 321 KLKHGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDNKDgaKLFSKQP 400
Cdd:TIGR01425 321 HLKEGTFTLRDWYEQFQNLLKMGPLGNIMSMIPGLSHPMMSKGNEEETSAKIKVFMTIMDSMTDRELDSTA--KTMLKDP 398
|
410 420 430
....*....|....*....|....*....|
gi 1832133605 401 NRVQRVARGAGVATRDVQELLTQYTKFAQM 430
Cdd:TIGR01425 399 SRIRRVARGSGRDIREVNELLEQYKLFAQM 428
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
6-464 |
2.14e-170 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 512.83 E-value: 2.14e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 6 LGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFKELVK 85
Cdd:PRK00771 1 LGESLRDALKKLAGKSRIDEKTVKEVVKDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGLTPREHVIKIVYEELVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 86 LV----DPGVKSWTPTKgknnmIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYG 161
Cdd:PRK00771 81 LLgeetEPLVLPLKPQT-----IMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 162 SYTEMDPVIIAAEGVEKFKSEnfEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVD 241
Cdd:PRK00771 156 DPDNKDAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQAKAFHEAVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 242 VASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNE-LKLDDNEELID 320
Cdd:PRK00771 234 IGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLLGMGDLESLLEKVEEaLDEEEEEKDVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 321 KLKHGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGTDfMSKGNEQESMARLKKLMTIMDSMNDQELDNKD--GAKlfsk 398
Cdd:PRK00771 314 KMMKGKFTLKDMYKQLEAMNKMGPLKQILQMLPGLGGK-LPDEALEVTEEKLKKYKAIMDSMTEEELENPEiiNAS---- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832133605 399 qpnRVQRVARGAGVATRDVQELLTQYtkfaQMVKKMggIKGlFKGGDMsknvnpsQMAKLNQQMAK 464
Cdd:PRK00771 389 ---RIRRIARGSGTTVEDVRELLKYY----KMMKKA--MKQ-LKKGKG-------KMGKLMKQFGF 437
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
642-904 |
1.59e-160 |
|
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238755 [Multi-domain] Cd Length: 267 Bit Score: 480.33 E-value: 1.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 642 QMPLNFLYVVDTCMEDEDLQALKESLQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLG 721
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 722 LSKQQVAQPGRGPQQPQAP----PANRFLQPVQKIDMNLTDLLGELQKDPWPVTQGKRPLRSLGVALSIAVGLLECTFPN 797
Cdd:cd01478 81 LGGPAMRPSASQHPGAGNPlpsaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 798 TGARIMTFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKFMKKATKHYEALANRAAANGHIIDIYACALDQTGLAEMK 877
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 1832133605 878 CCTNYTAGYMVMADSFNTSLFKQTFQR 904
Cdd:cd01478 241 VLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
6-430 |
3.07e-142 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 438.30 E-value: 3.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 6 LGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKA-AIDLEEMASgLNKRRMIQHAVFKELV 84
Cdd:COG0541 5 LSERLQGAFKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKErALGEEVLKS-LTPGQQVIKIVHDELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 85 KLVDPGVKSWTPTKGKNNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYT 164
Cdd:COG0541 84 ELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEED 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 165 EMDPVIIAAEGVEKFKSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVAS 244
Cdd:COG0541 164 GKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTGQDAVNVAKAFNEALGLTG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 245 VIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNE-LKLDDNEELIDKLK 323
Cdd:COG0541 244 VILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMASRILGMGDVLSLIEKAQEaIDEEEAEKLAKKLK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 324 HGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGtDFMSKGNEQESMARLKKLMTIMDSMNDQELDNKDGAKlfskqPNRV 403
Cdd:COG0541 324 KGKFDLEDFLEQLQQMKKMGPLKKLLGMLPGMG-KLKQLKDLDIDEKELKRIEAIINSMTPEERRNPDIIN-----GSRK 397
|
410 420
....*....|....*....|....*..
gi 1832133605 404 QRVARGAGVATRDVQELLTQytkFAQM 430
Cdd:COG0541 398 RRIAKGSGTTVQDVNRLLKQ---FEQM 421
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
102-294 |
9.92e-141 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 425.07 E-value: 9.92e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKS 181
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 182 ENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALS 261
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAKGGGALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1832133605 262 AVAATKSPIIFIGTGEHIDDFEPFKTQPFISKL 294
Cdd:cd17875 161 AVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
102-294 |
2.91e-102 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 322.18 E-value: 2.91e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKS 181
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 182 ENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALS 261
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKGGAALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1832133605 262 AVAATKSPIIFIGTGEHIDDFEPFKTQPFISKL 294
Cdd:pfam00448 161 IVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
642-906 |
1.66e-89 |
|
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.
Pssm-ID: 398467 [Multi-domain] Cd Length: 241 Bit Score: 289.15 E-value: 1.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 642 QMPLNFLYVVDTCME---DEDLQALKESLQMSLSLLP--PTALVGLITFGRMVQVHELGCEGisksyvfRGTKDLSAKQL 716
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 717 QEMLGlskqqvaqpgrgpqqpqaPPANRFLQPVQKIDMNLTDLLGELQKdPWPVTqgKRPLRSLGVALSIAVGLLECTFp 796
Cdd:pfam04811 74 QDMFL------------------PLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 797 nTGARIMTFIGGPATQGPGMVVGDELKtpiRSWHDIEKDNAKFMKKATKHYEALANRAAANGHIIDIYACALDQTGLAEM 876
Cdd:pfam04811 132 -TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATL 207
|
250 260 270
....*....|....*....|....*....|....
gi 1832133605 877 KCCTNYTAGYMVMADSFN----TSLFKQTFQRIF 906
Cdd:pfam04811 208 GQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
102-296 |
3.91e-85 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 275.44 E-value: 3.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKT-CLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFK 180
Cdd:smart00962 2 GVILLVGPNGVGKTTTIAKLAARLKLKGGKKvLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 181 SENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGAL 260
Cdd:smart00962 82 ARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGTAKGGAAL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1832133605 261 SAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLG 296
Cdd:smart00962 162 SIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
528-1279 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1198.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 528 EDRDGVRFSWNVWPSSRLEATRMVVPVASLFTPLKERPDLPPIQYEPVLCSraTCRAVLNPLCQVDYRAKLWACNFCYQR 607
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 608 NQFPPTYAGISEVNQPAELLPQFSTIEYVVQR---GPQMPLNFLYVVDTCMEDEDLQALKESLQMSLSLLPPTALVGLIT 684
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPgsgGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 685 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGL--SKQQVAQPGRGPQQ--PQAPPANRFLQPVQKIDMNLTDLL 760
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLggKKRRPAGGGIAGARdgLSSSGVNRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 761 GELQKDPWPVTQGKRPLRSLGVALSIAVGLLECTFPNTGARIMTFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKFM 840
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 841 KKATKHYEALANRAAANGHIIDIYACALDQTGLAEMKCCTNYTAGYMVMADSFNTSLFKQTFQRIFNKDVQGSFKMAFAG 920
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 921 TLEIKTSREIKISGAIGPCVSLNAKGPCVSENEIGTGGTCQWKICGLDPNTTLAVYFEVVNQHNA-PIPQGGRGAIQYVT 999
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1000 QYQHSSGQRRIRVTTVARNWADAqTQIQNISASFDQEASAILMARLAVYRAESEEGPDVLRWLDRQLIRLCQKFGDYHKD 1079
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1080 DPNSFRFSETFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFNGPPEPVLLDSSSIL 1159
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1160 PDRILLMDTFFQILIYHGETVAQWRKAGYQDMPEYENFRHLLQAPVDDAQEILQTRFPMPRYIDTEHGGSQARFLLSKVN 1239
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1832133605 1240 PSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLKKLAVSS 1279
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
525-1280 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 967.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 525 QQNEDRDGVRFSWNVWPSSRLEATRMVVPVASLFTPLKERPDLPPIQYEPVLCsRATCRAVLNPLCQVDYRAKLWACNFC 604
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 605 YQRNQFPPTYAGISEVNQPAELLPQFSTIEYVVQRGPQMPLNFLYVVDTCMEDEDLQALKESLQMSLSLLPPTALVGLIT 684
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 685 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKQ--QVAQPGRGPQQPQAPPaNRFLQPVQKIDMNLTDLLGE 762
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPtkSGGFESKISGIGQFAS-SRFLLPTQQCEFKLLNILEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 763 LQKDPWPVTQGKRPLRSLGVALSIAVGLLECTFPNTGARIMTFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKFMKK 842
Cdd:COG5047 242 LQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 843 ATKHYEALANRAAANGHIIDIYACALDQTGLAEMKCCTNYTAGYMVMADSFNTSLFKQTFQRIFNKDVQGSFKMAFAGTL 922
Cdd:COG5047 322 ATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 923 EIKTSREIKISGAIGPCVSLNAKGPCVSENEIGTGGTCQWKICGLDPNTTLAVYFEVVNQHNAPIPQGG-RGAIQYVTQY 1001
Cdd:COG5047 402 EVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1002 QHSSGQRRIRVTTVARNWADAQTQIqnISASFDQEASAILMARLAVYRAESEEGPDVLRWLDRQLIRLCQKFGDYHKDDP 1081
Cdd:COG5047 482 QHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1082 NSFRFSETFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFNGPPEPVLLDSSSILPD 1161
Cdd:COG5047 560 SSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPD 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1162 RILLMDTFFQILIYHGETVAQWRKAGYQDMPEYENFRHLLQAPVDDAQEILQTRFPMPRYIDTEHGGSQARFLLSKVNPS 1241
Cdd:COG5047 640 VILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPS 719
|
730 740 750
....*....|....*....|....*....|....*....
gi 1832133605 1242 QTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 1280
Cdd:COG5047 720 DITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
2-430 |
0e+00 |
|
signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.
Pssm-ID: 273615 [Multi-domain] Cd Length: 428 Bit Score: 801.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 2 VLADLGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFK 81
Cdd:TIGR01425 1 VLAQLGSSLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 82 ELVKLVDPGVKSWTPTKGKNNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYG 161
Cdd:TIGR01425 81 ELCNLVDPGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 162 SYTEMDPVIIAAEGVEKFKSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVD 241
Cdd:TIGR01425 161 SYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQAKAFKDSVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 242 VASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNE-ELID 320
Cdd:TIGR01425 241 VGSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKLLGMGDLKGLIDKVQDLALNDEEkTLIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 321 KLKHGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDNKDgaKLFSKQP 400
Cdd:TIGR01425 321 HLKEGTFTLRDWYEQFQNLLKMGPLGNIMSMIPGLSHPMMSKGNEEETSAKIKVFMTIMDSMTDRELDSTA--KTMLKDP 398
|
410 420 430
....*....|....*....|....*....|
gi 1832133605 401 NRVQRVARGAGVATRDVQELLTQYTKFAQM 430
Cdd:TIGR01425 399 SRIRRVARGSGRDIREVNELLEQYKLFAQM 428
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
6-464 |
2.14e-170 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 512.83 E-value: 2.14e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 6 LGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFKELVK 85
Cdd:PRK00771 1 LGESLRDALKKLAGKSRIDEKTVKEVVKDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGLTPREHVIKIVYEELVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 86 LV----DPGVKSWTPTKgknnmIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYG 161
Cdd:PRK00771 81 LLgeetEPLVLPLKPQT-----IMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 162 SYTEMDPVIIAAEGVEKFKSEnfEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVD 241
Cdd:PRK00771 156 DPDNKDAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQAKAFHEAVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 242 VASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNE-LKLDDNEELID 320
Cdd:PRK00771 234 IGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLLGMGDLESLLEKVEEaLDEEEEEKDVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 321 KLKHGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGTDfMSKGNEQESMARLKKLMTIMDSMNDQELDNKD--GAKlfsk 398
Cdd:PRK00771 314 KMMKGKFTLKDMYKQLEAMNKMGPLKQILQMLPGLGGK-LPDEALEVTEEKLKKYKAIMDSMTEEELENPEiiNAS---- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832133605 399 qpnRVQRVARGAGVATRDVQELLTQYtkfaQMVKKMggIKGlFKGGDMsknvnpsQMAKLNQQMAK 464
Cdd:PRK00771 389 ---RIRRIARGSGTTVEDVRELLKYY----KMMKKA--MKQ-LKKGKG-------KMGKLMKQFGF 437
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
642-904 |
1.59e-160 |
|
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238755 [Multi-domain] Cd Length: 267 Bit Score: 480.33 E-value: 1.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 642 QMPLNFLYVVDTCMEDEDLQALKESLQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLG 721
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 722 LSKQQVAQPGRGPQQPQAP----PANRFLQPVQKIDMNLTDLLGELQKDPWPVTQGKRPLRSLGVALSIAVGLLECTFPN 797
Cdd:cd01478 81 LGGPAMRPSASQHPGAGNPlpsaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 798 TGARIMTFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKFMKKATKHYEALANRAAANGHIIDIYACALDQTGLAEMK 877
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 1832133605 878 CCTNYTAGYMVMADSFNTSLFKQTFQR 904
Cdd:cd01478 241 VLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
6-430 |
3.07e-142 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 438.30 E-value: 3.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 6 LGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKA-AIDLEEMASgLNKRRMIQHAVFKELV 84
Cdd:COG0541 5 LSERLQGAFKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKErALGEEVLKS-LTPGQQVIKIVHDELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 85 KLVDPGVKSWTPTKGKNNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYT 164
Cdd:COG0541 84 ELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEED 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 165 EMDPVIIAAEGVEKFKSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVAS 244
Cdd:COG0541 164 GKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTGQDAVNVAKAFNEALGLTG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 245 VIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNE-LKLDDNEELIDKLK 323
Cdd:COG0541 244 VILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMASRILGMGDVLSLIEKAQEaIDEEEAEKLAKKLK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 324 HGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGtDFMSKGNEQESMARLKKLMTIMDSMNDQELDNKDGAKlfskqPNRV 403
Cdd:COG0541 324 KGKFDLEDFLEQLQQMKKMGPLKKLLGMLPGMG-KLKQLKDLDIDEKELKRIEAIINSMTPEERRNPDIIN-----GSRK 397
|
410 420
....*....|....*....|....*..
gi 1832133605 404 QRVARGAGVATRDVQELLTQytkFAQM 430
Cdd:COG0541 398 RRIAKGSGTTVQDVNRLLKQ---FEQM 421
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
102-294 |
9.92e-141 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 425.07 E-value: 9.92e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKS 181
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 182 ENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALS 261
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAKGGGALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1832133605 262 AVAATKSPIIFIGTGEHIDDFEPFKTQPFISKL 294
Cdd:cd17875 161 AVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| ffh |
TIGR00959 |
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the ... |
6-433 |
4.70e-115 |
|
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the protein component that forms the bacterial (and organellar) signal recognition particle together with a 4.5S RNA. Ffh is a GTPase homologous to eukaryotic SRP54 and also to the GTPase FtsY (TIGR00064) that is the receptor for the signal recognition particle. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273364 [Multi-domain] Cd Length: 428 Bit Score: 366.23 E-value: 4.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 6 LGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFKELVK 85
Cdd:TIGR00959 4 LSERLQRIFKKLSGRGTITEKNIKEALREIRLALLEADVNLQVVKDFIKKVKEKALGQEVLKSLSPGQQFIKIVHEELVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 86 LVDPGVKSWTPTKGKNNMIMFVGLQGSGKTTTCTKLAYY-YQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYT 164
Cdd:TIGR00959 84 ILGGENAELNLAKKPPTVILMVGLQGSGKTTTCGKLAYYlKKKQGKKVLLVACDLYRPAAIEQLKVLGQQVGVPVFALGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 165 EMDPVIIAAEGVEKFKSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVAS 244
Cdd:TIGR00959 164 GQSPVEIARRALEYAKENGFDVVIVDTAGRLQIDEELMEELAAIKEILNPDEILLVVDAMTGQDAVNTAKTFNERLGLTG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 245 VIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNE-LKLDDNEELIDKLK 323
Cdd:TIGR00959 244 VVLTKLDGDARGGAALSVRSVTGKPIKFIGVGEKIDDLEPFHPERMASRILGMGDILSLVEKAQEvVDEEEAKKLAEKMK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 324 HGQFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDNKDGAKlfskqPNRV 403
Cdd:TIGR00959 324 KGQFDLEDFLEQLRQIKKMGPLSSLLKMIPGMGGVKPSLSDADLDEKQFKRIEAIISSMTPEERRNPKILN-----PSRR 398
|
410 420 430
....*....|....*....|....*....|
gi 1832133605 404 QRVARGAGVATRDVQELLTQYTKFAQMVKK 433
Cdd:TIGR00959 399 KRIAAGSGTTVQDVNKLIKRFEQMKKMMKK 428
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
102-294 |
2.91e-102 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 322.18 E-value: 2.91e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKS 181
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 182 ENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALS 261
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKGGAALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1832133605 262 AVAATKSPIIFIGTGEHIDDFEPFKTQPFISKL 294
Cdd:pfam00448 161 IVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
102-294 |
1.60e-100 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 317.78 E-value: 1.60e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKS 181
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 182 ENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALS 261
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAKGGAALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1832133605 262 AVAATKSPIIFIGTGEHIDDFEPFKTQPFISKL 294
Cdd:cd03115 161 IVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
642-906 |
1.66e-89 |
|
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.
Pssm-ID: 398467 [Multi-domain] Cd Length: 241 Bit Score: 289.15 E-value: 1.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 642 QMPLNFLYVVDTCME---DEDLQALKESLQMSLSLLP--PTALVGLITFGRMVQVHELGCEGisksyvfRGTKDLSAKQL 716
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 717 QEMLGlskqqvaqpgrgpqqpqaPPANRFLQPVQKIDMNLTDLLGELQKdPWPVTqgKRPLRSLGVALSIAVGLLECTFp 796
Cdd:pfam04811 74 QDMFL------------------PLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 797 nTGARIMTFIGGPATQGPGMVVGDELKtpiRSWHDIEKDNAKFMKKATKHYEALANRAAANGHIIDIYACALDQTGLAEM 876
Cdd:pfam04811 132 -TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATL 207
|
250 260 270
....*....|....*....|....*....|....
gi 1832133605 877 KCCTNYTAGYMVMADSFN----TSLFKQTFQRIF 906
Cdd:pfam04811 208 GQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
1126-1246 |
2.59e-85 |
|
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.
Pssm-ID: 200443 [Multi-domain] Cd Length: 121 Bit Score: 272.71 E-value: 2.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1126 QDLTQSLIMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFFQILIYHGETVAQWRKAGYQDMPEYENFRHLLQAPV 1205
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1832133605 1206 DDAQEILQTRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNN 1246
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
102-296 |
3.91e-85 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 275.44 E-value: 3.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKT-CLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFK 180
Cdd:smart00962 2 GVILLVGPNGVGKTTTIAKLAARLKLKGGKKvLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 181 SENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGAL 260
Cdd:smart00962 82 ARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGTAKGGAAL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1832133605 261 SAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLG 296
Cdd:smart00962 162 SIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
642-904 |
1.47e-83 |
|
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface. Some members of this family possess a partial MIDAS motif that is a characteristic feature of most vWA domain proteins.
Pssm-ID: 238745 [Multi-domain] Cd Length: 239 Bit Score: 272.58 E-value: 1.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 642 QMPLNFLYVVDTCME---DEDLQALKESLQMSLSLLP--PTALVGLITFGRMVQVHELGCEGI-SKSYVFRGTKDlsakq 715
Cdd:cd01468 1 PQPPVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 716 lqemlglskqqvaqpgrgpqqPQAPPANRFLQPVQKIDMNLTDLLGELQKDPWPVtQGKRPLRSLGVALSIAVGLLECTF 795
Cdd:cd01468 76 ---------------------VFLPLPDRFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 796 pnTGARIMTFIGGPATQGPGMVVGDELKTPIRSWhdiekDNAKFMKKATKHYEALANRAAANGHIIDIYACALDQTGLAE 875
Cdd:cd01468 134 --AGGRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVAT 206
|
250 260 270
....*....|....*....|....*....|...
gi 1832133605 876 MKCCTNYTAGYMVMADSFN----TSLFKQTFQR 904
Cdd:cd01468 207 LKQLAKSTGGQVYLYDSFQapndGSKFKQDLQR 239
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
9-296 |
4.07e-62 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 214.96 E-value: 4.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 9 KITSALRSLSNATIINEEVLNAmLKDvcaALLEADVNIKLVKQLRENVKAAIDLEEMASGlnkrRMIQHAVFKELVKLVD 88
Cdd:PRK10416 30 NFGEGINGLFAKKKIDEDLLEE-LEE---LLIEADVGVETTEEIIEELRERVKRKNLKDP----EELKELLKEELAEILE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 89 PGVKSWTPTKGKNNMIMFVGLQGSGKTTTCTKLAYYYQRKGwKTCLICA-DTFRAGAFDQLKQNATKARIPFYGSYTEMD 167
Cdd:PRK10416 102 PVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQG-KKVLLAAgDTFRAAAIEQLQVWGERVGVPVIAQKEGAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 168 PVIIAAEGVEKFKSENFEIIIVDTSGR-HKQEDsLFEEMLQVSNAVQ------PDNIVYVMDASIGQACEAQAKAFKDKV 240
Cdd:PRK10416 181 PASVAFDAIQAAKARGIDVLIIDTAGRlHNKTN-LMEELKKIKRVIKkadpdaPHEVLLVLDATTGQNALSQAKAFHEAV 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832133605 241 DVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLG 296
Cdd:PRK10416 260 GLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLG 315
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
8-296 |
8.42e-61 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 210.65 E-value: 8.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 8 RKITSALRSL-SNATIINEEVLNAmLKDVcaaLLEADVNI----KLVKQLRENVKAaidleemaSGLNKRRMIQHAVFKE 82
Cdd:COG0552 14 SGLGEKLKSLfSGKKKIDEDLLEE-LEEL---LIEADVGVetteEIIEELRERVKR--------KKLKDPEELKEALKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 83 LVKLVDPGVKSWTPTKGKNNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPF--- 159
Cdd:COG0552 82 LLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPViaq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 160 -YGSytemDPVIIAAEGVEKFKSENFEIIIVDTSGR-HKQEDsLFEEMLQVSNAVQ------PDNIVYVMDASIGQACEA 231
Cdd:COG0552 162 kEGA----DPAAVAFDAIQAAKARGADVVIIDTAGRlHNKKN-LMEELKKIKRVIKkldpdaPHEVLLVLDATTGQNALS 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832133605 232 QAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLG 296
Cdd:COG0552 237 QAKVFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFG 301
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
104-285 |
1.41e-60 |
|
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349786 Cd Length: 193 Bit Score: 205.91 E-value: 1.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 104 IMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKSEN 183
Cdd:cd18539 3 ILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 184 FEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAV 263
Cdd:cd18539 83 FDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARGGAALSIR 162
|
170 180
....*....|....*....|..
gi 1832133605 264 AATKSPIIFIGTGEHIDDFEPF 285
Cdd:cd18539 163 HVTGKPIKFIGVGEKIEDLEPF 184
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
23-295 |
2.92e-57 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 199.40 E-value: 2.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 23 INEEVLNamlkDVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFKELVKLVDPGVK-SWTPTKGKN 101
Cdd:TIGR00064 2 DDEDFFE----ELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKNTDlELIVEENKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPF----YGSytemDPVIIAAEGVE 177
Cdd:TIGR00064 78 NVILFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVikqkEGA----DPAAVAFDAIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 178 KFKSENFEIIIVDTSGR-HKQEDsLFEEMLQVSNAVQ------PDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKL 250
Cdd:TIGR00064 154 KAKARNIDVVLIDTAGRlQNKVN-LMDELKKIKRVIKkvdkdaPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1832133605 251 DGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLL 295
Cdd:TIGR00064 233 DGTAKGGIILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
19-296 |
3.20e-56 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 198.66 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 19 NATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEEMASGLNKRRMIQHAVFKELVKLVDPG-------- 90
Cdd:PRK14974 54 KITEIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVLSVGdlfdliee 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 91 VKSwtptKGKNNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPF----YGSytem 166
Cdd:PRK14974 134 IKS----KGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVikhkYGA---- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 167 DPVIIAAEGVEKFKSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVI 246
Cdd:PRK14974 206 DPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVGIDGVI 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1832133605 247 VTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLG 296
Cdd:PRK14974 286 LTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
102-294 |
1.62e-53 |
|
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.
Pssm-ID: 349783 Cd Length: 199 Bit Score: 185.85 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 102 NMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKS 181
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 182 ENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQ------PDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAK 255
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKkkdpeaPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1832133605 256 GGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKL 294
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
8-296 |
6.61e-37 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 143.47 E-value: 6.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 8 RKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEEmasglnkrrmIQHAVFKELVKLV 87
Cdd:COG1419 84 AELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELLEKLPEDLSAEE----------AWRALLEALARRL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 88 DPGVKSWTPTKGknnMIMFVGLQGSGKTTTCTKLAYYY-QRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEM 166
Cdd:COG1419 154 PVAEDPLLDEGG---VIALVGPTGVGKTTTIAKLAARFvLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 167 DpviiAAEGVEKFKseNFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASI-GQACEAQAKAFKDkVDVASV 245
Cdd:COG1419 231 E----LKEALERLR--DKDLVLIDTAGRSPRDPELIEELKALLDAGPPIEVYLVLSATTkYEDLKEIVEAFSS-LGLDGL 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1832133605 246 IVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHI-DDFEPFKTQPFISKLLG 296
Cdd:COG1419 304 ILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADPERLARLLLG 355
|
|
| SRP_SPB |
pfam02978 |
Signal peptide binding domain; |
326-429 |
7.64e-35 |
|
Signal peptide binding domain;
Pssm-ID: 460771 [Multi-domain] Cd Length: 95 Bit Score: 128.28 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 326 QFTLRDMYEQFQNIMKMGPFGQIMGMIPGFGtdfmSKGNEQESMARLKKLMTIMDSMNDQELDNKDgaklfSKQPNRVQR 405
Cdd:pfam02978 1 KFTLRDFLEQLQQIKKMGPLSKILSMIPGMG----KKDDDIDSEKKLKRIEAIIDSMTPKERDNPD-----IINASRKRR 71
|
90 100
....*....|....*....|....
gi 1832133605 406 VARGAGVATRDVQELLTQYTKFAQ 429
Cdd:pfam02978 72 IARGSGTSVQEVNRLLKQFKQMKK 95
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
1034-1133 |
1.01e-33 |
|
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is composed of five alpha helices.
Pssm-ID: 461441 [Multi-domain] Cd Length: 103 Bit Score: 125.31 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1034 DQEASAILMARLAVYRAESEEGPDVLRWLDRQLIRLCQKFGDYHKD--DPNSFRFSETFSLYPQFMFHLRRSPFLQVFNN 1111
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 1832133605 1112 SP-DESSYYRHHFMRQDLTQSLI 1133
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
917-1020 |
2.35e-31 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 118.02 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 917 AFAGTLEIKTSREIKISGAIGPCVSLNAkgpcvseneigtGGTcqWKICGLDPNTTLAVYFEvvnqHNAPIPQGGRGAIQ 996
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62
|
90 100
....*....|....*....|....
gi 1832133605 997 YVTQYQHSSGQRRIRVTTVARNWA 1020
Cdd:pfam08033 63 FALLYTHSSGERRIRVTTVALPVT 86
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
104-282 |
1.87e-30 |
|
C-terminal domain of signal recognition particle receptor alpha subunit; The signal-recognition particle (SRP) receptor (SR) alpha-subunit (SRalpha) of the eukaryotic SR interacts with the signal-recognition particle (SRP) and is essential for the co-translational membrane targeting of proteins.
Pssm-ID: 349785 Cd Length: 204 Bit Score: 119.64 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 104 IMFVGLQGSGKTTTCTKLAYYYQRKGWKtCLICA-DTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKFKSE 182
Cdd:cd17876 3 IVFCGVNGVGKSTNLAKIAYWLLSNGFR-VLIAAcDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARDQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 183 NFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVAS----------VIVTKLDG 252
Cdd:cd17876 82 GFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALADYSpsdnprlidgIVLTKFDT 161
|
170 180 190
....*....|....*....|....*....|.
gi 1832133605 253 -HAKGGGALSAVAATKSPIIFIGTGEHIDDF 282
Cdd:cd17876 162 iDDKVGAALSMVYATGQPIVFVGTGQTYTDL 192
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
104-294 |
1.55e-26 |
|
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).
Pssm-ID: 349782 [Multi-domain] Cd Length: 189 Bit Score: 108.02 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 104 IMFVGLQGSGKTTTCTKLAYYYQ-RKGWKTCLICADTFRAGAFDQLKqnaTKARIpfygsyteMDPVIIAAEGVEKFK-- 180
Cdd:cd17873 3 IALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLK---TYAEI--------MGIPVEVAEDPEDLAda 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 181 ---SENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASiGQACEAQ--AKAFKDkVDVASVIVTKLDGHAK 255
Cdd:cd17873 72 lerLSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDIEVHLVLSAT-TKAKDLKeiIERFSP-LGYRGLILTKLDETTS 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1832133605 256 GGGALSAVAATKSPIIFIGTGEHI-DDFEPFKTQPFISKL 294
Cdd:cd17873 150 LGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
3-296 |
4.62e-24 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 106.52 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 3 LADLGRKITSaLRSL------SNATIINEEVLNAMLkdvCAALLEADVNIKLVKQLRENVkaaidLEEMAsglNKRRMIQ 76
Cdd:PRK05703 132 LDELRDELKE-LKNLledqlsGLRQVERIPPEFAEL---YKRLKRSGLSPEIAEKLLKLL-----LEHMP---PRERTAW 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 77 HAVFKELVKLVDPGVKSWTPTKGKnnmIMFVGLQGSGKTTTCTKLA----YYYQRKgwKTCLICADTFRAGAFDQLKQNA 152
Cdd:PRK05703 200 RYLLELLANMIPVRVEDILKQGGV---VALVGPTGVGKTTTLAKLAaryaLLYGKK--KVALITLDTYRIGAVEQLKTYA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 153 TKARIPFYGSYTEMDpviiAAEGVEKFKseNFEIIIVDTSGRHKQEDSLFEEmLQ--VSNAVQPDNIVYVMDASIG-QAC 229
Cdd:PRK05703 275 KIMGIPVEVVYDPKE----LAKALEQLR--DCDVILIDTAGRSQRDKRLIEE-LKalIEFSGEPIDVYLVLSATTKyEDL 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832133605 230 EAQAKAFKdKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHI-DDFEPFKTQPFISKLLG 296
Cdd:PRK05703 348 KDIYKHFS-RLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIKVANPEELVRLLLG 414
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
6-83 |
2.30e-19 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 83.29 E-value: 2.30e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832133605 6 LGRKITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVK-AAIDLEEmasgLNKRRMIQHAVFKEL 83
Cdd:pfam02881 1 LGEKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLReKAVGEKK----LKPPQEVKKILKEEL 75
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
449-1182 |
2.34e-17 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 87.92 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 449 NVNPSQMAKLNQQMAKMMDPrvlhhMGGMAGLQSMMRQFQQGAAGNMkgmmgFNNIEPTFSTSFLegamTTFPEFIQQ-- 526
Cdd:COG5028 73 NPAPSVMSPAFQSQQKFSSP-----YGGSMADGTAPKPTNPLVPVDL-----FEDQPPPISDLFL----PPPPIVPPLtt 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 527 --------NEDRDGVRFSWNVWP--SSRLEATRmvVPVASLFTPLKE-RPDLPPIQYE----PVLCSRatCRAVLNPLCQ 591
Cdd:COG5028 139 nfvgseqsNCSPKYVRSTMYAIPetNDLLKKSK--IPFGLVIRPFLElYPEEDPVPLVedgsIVRCRR--CRSYINPFVQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 592 VDYRAKLWACNFCYQRNQFP-----PTYAGI--SEVNQPAELLpqFSTIEYVVQ-----RGPQmPLNFLYVVDT---CME 656
Cdd:COG5028 215 FIEQGRKWRCNICRSKNDVPegfdnPSGPNDprSDRYSRPELK--SGVVDFLAPkeyslRQPP-PPVYVFLIDVsfeAIK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 657 DEDLQALKESLQMSLSLLP---PTALVGLITFGRMVqvhelgcegisksYVFRGTKDLSAKQLQEMLglskqqvaqpgrg 733
Cdd:COG5028 292 NGLVKAAIRAILENLDQIPnfdPRTKIAIICFDSSL-------------HFFKLSPDLDEQMLIVSD------------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 734 PQQPQAP-PANRFLQPVQKIDMNLTDLLGELQKDPwpvTQGKRPLRSLGVALSIAVGLLEctfpNTGARIMTFIGGPATQ 812
Cdd:COG5028 346 LDEPFLPfPSGLFVLPLKSCKQIIETLLDRVPRIF---QDNKSPKNALGPALKAAKSLIG----GTGGKIIVFLSTLPNM 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 813 GPGMVvgdELKTPIRSWHDIEKDnaKFMKKATKHYEALanraaanGHIIDIYACALDQTGLAEMKCCTNYTAGYMVMADS 892
Cdd:COG5028 419 GIGKL---QLREDKESSLLSCKD--SFYKEFAIECSKV-------GISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPN 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 893 FNTSLFKQTFQriFNKDV--QGSFKMAFAGTLEIKTSREIKISGAIGPCVSlNAKGPCvsenEIGTggtcqwkicgLDPN 970
Cdd:COG5028 487 FSATRPNDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFN-RSSDLC----AFST----------MPRD 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 971 TTLAVYFEVVNQHNAPipqggRGAIQYVTQYQHSSGQRRIRVTTVArnwADAQTQIQNISASFDQEASAILMARLAVYRA 1050
Cdd:COG5028 550 TSLLVEFSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKASTKA 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1051 ESEEGPDVLRWLDRQLIRLCQKfgdYHKDDPNS-----FRFSETFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFMR 1125
Cdd:COG5028 622 LNSSLKEARVLINKSMVDILKA---YKKELVKSntstqLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTS 698
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1126 QDLTQSLIMIQPILYAY---------SFNGP---PEPVLLDSSSILPDRILLMDTFFQILIY-HGETVAQ 1182
Cdd:COG5028 699 LPLKQLMRNIYPTLYALhdmpieaglPDEGLlvlPSPINATSSLLESGGLYLIDTGQKIFLWfGKDAVPS 768
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
574-612 |
5.64e-16 |
|
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is found to be zinc binding domain.
Pssm-ID: 461437 [Multi-domain] Cd Length: 38 Bit Score: 72.48 E-value: 5.64e-16
10 20 30
....*....|....*....|....*....|....*....
gi 1832133605 574 PVLCSRatCRAVLNPLCQVDYRAKLWACNFCYQRNQFPP 612
Cdd:pfam04810 1 PVRCRR--CRAYLNPFCQFDFGGKKWTCNFCGTRNPVPP 37
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
10-87 |
7.40e-16 |
|
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species.
Pssm-ID: 214941 [Multi-domain] Cd Length: 77 Bit Score: 73.35 E-value: 7.40e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832133605 10 ITSALRSLSNATIINEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIdLEEMASGLNKRRMIQHAVFKELVKLV 87
Cdd:smart00963 1 LSKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKA-KGEVLKGLTPKQEVKKILKEELVKIL 77
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
46-295 |
7.06e-15 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 78.47 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 46 IKLVKQL-RENVKAAIdLEEMASGLNKR-----RMIQHAVFKELVKL------VDPGVKSWTPtKGKNNMIMFVGLQGSG 113
Cdd:PRK12724 158 QRLGERLvREGMSQSY-VEEMASKLEERlspvdQGRNHNVTERAVTYleervsVDSDLFSGTG-KNQRKVVFFVGPTGSG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 114 KTTTCTKLAY-YYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYgsytemdpviiAAEGVEKFKS----ENFEIII 188
Cdd:PRK12724 236 KTTSIAKLAAkYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFY-----------PVKDIKKFKEtlarDGSELIL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 189 VDTSG-RHKQEDSL-----FEEMLQVSNAVQpdNIVYVMDASIGQACEAQAKAFkDKVDVASVIVTKLDGHAKGGGALSA 262
Cdd:PRK12724 305 IDTAGySHRNLEQLermqsFYSCFGEKDSVE--NLLVLSSTSSYHHTLTVLKAY-ESLNYRRILLTKLDEADFLGSFLEL 381
|
250 260 270
....*....|....*....|....*....|...
gi 1832133605 263 VAATKSPIIFIGTGEHIddfePFKTQPFISKLL 295
Cdd:PRK12724 382 ADTYSKSFTYLSVGQEV----PFDILNATKNLM 410
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
8-193 |
8.03e-15 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 76.22 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 8 RKITSALRSLSNATI--INEEVLNAMLKDVCAALLEADVNIKLVKQLRENVKAAIDLEE-MASGLNK-RRMIQHAVFKEl 83
Cdd:TIGR03499 110 RKELEALRELLERLLagLAWLQRPPERAKLYERLLEAGVSEELARELLEKLPEDADAEDaWRWLREAlEGMLPVKPEED- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 84 VKLVDPGVkswtptkgknnmIMFVGLQGSGKTTTCTKLA--YYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYG 161
Cdd:TIGR03499 189 PILEQGGV------------IALVGPTGVGKTTTLAKLAarFALEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKV 256
|
170 180 190
....*....|....*....|....*....|..
gi 1832133605 162 SYTEMDpviiAAEGVEKFKseNFEIIIVDTSG 193
Cdd:TIGR03499 257 ARDPKE----LREALDRLR--DKDLILIDTAG 282
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
1148-1234 |
5.00e-14 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 68.10 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1148 PEPVLLDSSSILPDRILLMDTFFQIliyhgetvAQWRkaGYQDMPEYENFRHLLQAPVDDaqeilQTRFPMPRYIDTEHG 1227
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGFTI--------FLWV--GKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69
|
....*..
gi 1832133605 1228 GSQARFL 1234
Cdd:pfam00626 70 KEPARFL 76
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
1136-1234 |
3.55e-13 |
|
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.
Pssm-ID: 200436 Cd Length: 88 Bit Score: 66.24 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 1136 QPILYAYSFNG--PPEPVLLDSSSILPDRILLMDTFFQILIYHGEtvaqwrkagyqdmpeyENFRHLLQAPVDDAQEILQ 1213
Cdd:cd11280 1 PPRLYRVRGSKaiEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|.
gi 1832133605 1214 TRFPMPRYIDTEHGGSQARFL 1234
Cdd:cd11280 65 ERKGKPEIVRIRQGQEPREFW 85
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
104-279 |
2.80e-11 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 67.40 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 104 IMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNatkarIPFYGSytEMDPVIIAA---EGVEKFK 180
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDY-----VKTIGF--EVIAVRDEAamtRALTYFK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 181 SE-NFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQ-AKAFKDkVDVASVIVTKLDGHAKGGG 258
Cdd:PRK11889 317 EEaRVDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSASMKSKDMIEiITNFKD-IHIDGIVFTKFDETASSGE 395
|
170 180
....*....|....*....|.
gi 1832133605 259 ALSAVAATKSPIIFIGTGEHI 279
Cdd:PRK11889 396 LLKIPAVSSAPIVLMTDGQDV 416
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
104-279 |
4.52e-11 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 65.15 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 104 IMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLkQNATKArIPFYGSYTEMDPVIIAAegVEKFKSE- 182
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQL-QDYVKT-IGFEVIAVRDEAAMTRA--LTYFKEEa 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 183 NFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQ-AKAFKDkVDVASVIVTKLDGHAKGGGALS 261
Cdd:PRK06731 154 RVDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSASMKSKDMIEiITNFKD-IHIDGIVFTKFDETASSGELLK 232
|
170
....*....|....*...
gi 1832133605 262 AVAATKSPIIFIGTGEHI 279
Cdd:PRK06731 233 IPAVSSAPIVLMTDGQDV 250
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
100-212 |
1.15e-10 |
|
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: 61.24 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 100 KNNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEgvekf 179
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR----- 75
|
90 100 110
....*....|....*....|....*....|...
gi 1832133605 180 kSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAV 212
Cdd:smart00382 76 -KLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
101-296 |
1.45e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 61.68 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 101 NNMIMFVGLQGSGKTTTCTKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDpviiAAEGVEKFK 180
Cdd:PRK12726 206 HRIISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIVATSPAE----LEEAVQYMT 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 181 SEN-FEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGA 259
Cdd:PRK12726 282 YVNcVDHILIDTVGRNYLAEESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTRIGDL 361
|
170 180 190
....*....|....*....|....*....|....*....
gi 1832133605 260 LSAVAATKSPIIFIGTGEHIDD--FEPfKTQPFISKLLG 296
Cdd:PRK12726 362 YTVMQETNLPVLYMTDGQNITEniFRP-KSRWLAERFVG 399
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
107-295 |
1.01e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 59.81 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 107 VGLQGSGKTTTCTKL-AYYYQRKGW-KTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKfksenf 184
Cdd:PRK14723 191 VGPTGVGKTTTTAKLaARCVAREGAdQLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAADLRFALAALGDK------ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 185 EIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMD-ASIGQACEAQAKAFKDKV--DVASVIVTKLDGHAKGGGALS 261
Cdd:PRK14723 265 HLVLIDTVGMSQRDRNVSEQIAMLCGVGRPVRRLLLLNaASHGDTLNEVVHAYRHGAgeDVDGCIITKLDEATHLGPALD 344
|
170 180 190
....*....|....*....|....*....|....*
gi 1832133605 262 AVAATKSPIIFIGTGEHI-DDFEPFKTQPFISKLL 295
Cdd:PRK14723 345 TVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
100-293 |
1.67e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 58.19 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 100 KNNMIMFVGLQGSGKTTTCTKLAYY-YQRKGW-KTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEgve 177
Cdd:PRK14722 136 RGGVFALMGPTGVGKTTTTAKLAARcVMRFGAsKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLALAE--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 178 kfkSENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQPDNIVYVMDA-SIGQACEAQAKAFKDKV--------DVASVIVT 248
Cdd:PRK14722 213 ---LRNKHMVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNAtSHGDTLNEVVQAYRSAAgqpkaalpDLAGCILT 289
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1832133605 249 KLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISK 293
Cdd:PRK14722 290 KLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPENLYVATKKFLLK 334
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
4-323 |
2.20e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 57.99 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 4 ADLGRKITSALRSLSNATIinEEVLNAmLKDVCAALLEADVNI------KLVKQLREN------VKAAIDL---EEMASG 68
Cdd:PRK12723 67 EDEKRKILQSIKKEENSSI--EDVLKE-VKSLKNELAHKKEEInhptilKIEDILRENdfsesyIKDINEFikkEFSLSD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 69 LNKRRMIQHAVF---KELVKLVDPgvksWTPTKGKNNMIMfVGLQGSGKTTTCTKLAYYY----QRKGWKTCLICADTFR 141
Cdd:PRK12723 144 LDDYDKVRDSVIiyiAKTIKCSGS----IIDNLKKRVFIL-VGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 142 AGAfdqlkqnatKARIPFYGsytemDPVIIAAEGVEKFK--------SENFEIIIVDTSGRHKQEDSLFEEMLQVSNAVQ 213
Cdd:PRK12723 219 IGA---------KKQIQTYG-----DIMGIPVKAIESFKdlkeeitqSKDFDLVLVDTIGKSPKDFMKLAEMKELLNACG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 214 PDNIVYVMDASIGQACE-----AQAKAFKDKvdvaSVIVTKLDGHAKGGGALSAVAATKSPIIFIGTG----EHIDDFEP 284
Cdd:PRK12723 285 RDAEFHLAVSSTTKTSDvkeifHQFSPFSYK----TVIFTKLDETTCVGNLISLIYEMRKEVSYVTDGqivpHNISIAEP 360
|
330 340 350
....*....|....*....|....*....|....*....
gi 1832133605 285 FKtqpfiskllgmgdiegLIDKVNELKLDDNEELIDKLK 323
Cdd:PRK12723 361 LT----------------FIKKINGYRISDDAEFIRKLK 383
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
103-281 |
2.82e-06 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 51.53 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 103 MIMFVGLQGSGKTTTCTKLAYYY--QRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYgsytEMDPVIIAAEGVEKFK 180
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAVH----EADSAESLLDLLERLR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 181 seNFEIIIVDTSGRhKQEDSLFEEMLQVSNAVQPDNIVYVM--DASIGQACEAqAKAFKdKVDVASVIVTKLDGHAKGGG 258
Cdd:PRK12727 428 --DYKLVLIDTAGM-GQRDRALAAQLNWLRAARQVTSLLVLpaNAHFSDLDEV-VRRFA-HAKPQGVVLTKLDETGRFGS 502
|
170 180
....*....|....*....|...
gi 1832133605 259 ALSAVAATKSPIIFIGTGEHIDD 281
Cdd:PRK12727 503 ALSVVVDHQMPITWVTDGQRVPD 525
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
111-255 |
3.25e-05 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 44.84 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 111 GSGKTTTCTKLAYYYQRKGWKTCLICADTfragafdQlkQNATKARipfygsytemdpviiaaegvekfksenFEIIIVD 190
Cdd:cd02042 11 GVGKTTLAVNLAAALALRGKRVLLIDLDP-------Q--GSLTSWL---------------------------YDYILID 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832133605 191 TSGRHkqeDSLFEEMLQVSNAV----QPDniVYVMDASIG--QACEAQAKAFKDKVDVASVIVTKLDGHAK 255
Cdd:cd02042 55 TPPSL---GLLTRNALAAADLVlipvQPS--PFDLDGLAKllDTLEELKKQLNPPLLILGILLTRVDPRTK 120
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
111-274 |
7.38e-05 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 45.80 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 111 GSGKTTTCTKLAYYYQRKGWKTCLICAD-----TFRAGA---FDQLKQNATKARIPfygsYTEMDPVIIA---------- 172
Cdd:pfam01656 9 GVGKTTLAANLARALARRGLRVLLIDLDpqsnnSSVEGLegdIAPALQALAEGLKG----RVNLDPILLKeksdeggldl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 173 ------AEGVEKFKS----------------ENFEIIIVDTSGrhkqedSLFEEML-------QVSNAVQPDnIVYVMDA 223
Cdd:pfam01656 85 ipgnidLEKFEKELLgprkeerlrealealkEDYDYVIIDGAP------GLGELLRnaliaadYVIIPLEPE-VILVEDA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1832133605 224 S-IGQACEAQAKAFKD-KVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIG 274
Cdd:pfam01656 158 KrLGGVIAALVGGYALlGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLG 210
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
106-279 |
1.82e-04 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 45.33 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 106 FVGLQGSGKTTTCTKLAYY-YQRKGW-KTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAAEGVEKfksen 183
Cdd:PRK14721 196 LIGPTGVGKTTTTAKLAARaVIRHGAdKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIADLQLMLHELRGK----- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832133605 184 fEIIIVDTSGRHKQEDSLFEEMLQVSNA-VQPDNIVYVMDASIGQACEAQAKAFKdKVDVASVIVTKLDGHAKGGGALSA 262
Cdd:PRK14721 271 -HMVLIDTVGMSQRDQMLAEQIAMLSQCgTQVKHLLLLNATSSGDTLDEVISAYQ-GHGIHGCIITKVDEAASLGIALDA 348
|
170
....*....|....*..
gi 1832133605 263 VAATKSPIIFIGTGEHI 279
Cdd:PRK14721 349 VIRRKLVLHYVTNGQKV 365
|
|
| |
