|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
11-773 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1554.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 11 EEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDCKTCKALLNAFARVDFAAMNWVCPFC 90
Cdd:PLN00162 2 DFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPFC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 91 YHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFVFVLDTCMIEEELGYAKSALKQAIGLLPENALVG 170
Cdd:PLN00162 82 FQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 171 FVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAPTSGFSkGAQNGFQSSGVDRFLLPASECEYTL 250
Cdd:PLN00162 162 LITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIA-GARDGLSSSGVNRFLLPASECEFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 251 DLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDKDA 330
Cdd:PLN00162 241 NSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 331 APYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSLGL 409
Cdd:PLN00162 321 APYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFErDGEGSLGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 410 CFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQLYL 489
Cdd:PLN00162 401 SFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPPGQQFFL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 490 QFITRYQNSEGKSLARVTTLTRQWVDTAVSTEvnLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKFG 569
Cdd:PLN00162 481 QFLTRYQHSNGQTRLRVTTVTRRWVEGSSSEE--LVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 570 EYRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAALLD 649
Cdd:PLN00162 559 DYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 650 VASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQARFL 729
Cdd:PLN00162 639 VASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFL 718
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 145361384 730 LAKLNPSATYNNANEMSaGSDIIFTDDVSLQVFIEHLQKLAVQS 773
Cdd:PLN00162 719 LAKLNPSATYNSANAMG-GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
10-771 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 804.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 10 VEEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDC-KTCKALLNAFARVDFAAMNWVCP 88
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 89 FCYHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFvfvLDTCMIEEELGYAKSALKQAIGLLPENAL 168
Cdd:COG5047 81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFV---VDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 169 VGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKdQILDQLGLGSSSRRaptSGFSKGAQNGFQSSGVDRFLLPASECEY 248
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK-ENLQELLALSKPTK---SGGFESKISGIGQFASSRFLLPTQQCEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 249 TLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDK 328
Cdd:COG5047 234 KLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 329 DAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSL 407
Cdd:COG5047 314 DSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNrDSEGYL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 408 GLCFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQL 487
Cdd:COG5047 394 KMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 488 YLQFITRYQNSEGKSLARVTTLTRQWVDtavSTEVNLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSK 567
Cdd:COG5047 474 YIQFITTYQHSSGTYRIRVTTVARMFTD---GGLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 568 FGEYRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAAL 647
Cdd:COG5047 551 FADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVL 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 648 LDVASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQAR 727
Cdd:COG5047 631 LDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQAR 710
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 145361384 728 FLLAKLNPSATYNNANEmsAGSDIIFTDDVSLQVFIEHLQKLAV 771
Cdd:COG5047 711 FLLSKINPSDITNKMSG--GGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
140-398 |
2.29e-157 |
|
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: 457.60 E-value: 2.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 140 LDTCMIEEELGYAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAP 219
Cdd:cd01478 10 VDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 220 TSGFsKGAQNGFQSSGVDRFLLPASECEYTLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVAL 299
Cdd:cd01478 90 ASQH-PGAGNPLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 300 VGGPCTEGPGTIISKDLSDPVRSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGG 379
Cdd:cd01478 169 AGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGG 248
|
250
....*....|....*....
gi 145361384 380 LVVLSESFGHSVFKDSFKR 398
Cdd:cd01478 249 HVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
140-400 |
1.91e-79 |
|
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: 254.87 E-value: 1.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 140 LDTCMI---EEELGYAKSALKQAIGLLP--ENALVGFVSFGTQAHVHELGFSEmskvfvfKGNKEVTKDQILDQLglgss 214
Cdd:pfam04811 10 IDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 215 srraptsgfskgaqngfqSSGVDRFLLPASECEYTLDLLLDELQSdQWPVQpgHRPQRCTGVALSVAAGLLGAClpGTGA 294
Cdd:pfam04811 78 ------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAA--FTGG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 295 RIVALVGGPCTEGPGTIISKDLSDpvrSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAV 374
Cdd:pfam04811 135 KIMVFQGGLPTVGPGGKLKSRLDE---SHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLS 211
|
250 260 270
....*....|....*....|....*....|
gi 145361384 375 ESTGGLVVLSESFG----HSVFKDSFKRMF 400
Cdd:pfam04811 212 RLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
11-773 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1554.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 11 EEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDCKTCKALLNAFARVDFAAMNWVCPFC 90
Cdd:PLN00162 2 DFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPFC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 91 YHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFVFVLDTCMIEEELGYAKSALKQAIGLLPENALVG 170
Cdd:PLN00162 82 FQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 171 FVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAPTSGFSkGAQNGFQSSGVDRFLLPASECEYTL 250
Cdd:PLN00162 162 LITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIA-GARDGLSSSGVNRFLLPASECEFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 251 DLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDKDA 330
Cdd:PLN00162 241 NSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 331 APYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSLGL 409
Cdd:PLN00162 321 APYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFErDGEGSLGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 410 CFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQLYL 489
Cdd:PLN00162 401 SFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPPGQQFFL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 490 QFITRYQNSEGKSLARVTTLTRQWVDTAVSTEvnLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKFG 569
Cdd:PLN00162 481 QFLTRYQHSNGQTRLRVTTVTRRWVEGSSSEE--LVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 570 EYRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAALLD 649
Cdd:PLN00162 559 DYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 650 VASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQARFL 729
Cdd:PLN00162 639 VASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFL 718
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 145361384 730 LAKLNPSATYNNANEMSaGSDIIFTDDVSLQVFIEHLQKLAVQS 773
Cdd:PLN00162 719 LAKLNPSATYNSANAMG-GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
10-771 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 804.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 10 VEEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDC-KTCKALLNAFARVDFAAMNWVCP 88
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 89 FCYHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFvfvLDTCMIEEELGYAKSALKQAIGLLPENAL 168
Cdd:COG5047 81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFV---VDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 169 VGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKdQILDQLGLGSSSRRaptSGFSKGAQNGFQSSGVDRFLLPASECEY 248
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK-ENLQELLALSKPTK---SGGFESKISGIGQFASSRFLLPTQQCEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 249 TLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDK 328
Cdd:COG5047 234 KLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 329 DAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSL 407
Cdd:COG5047 314 DSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNrDSEGYL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 408 GLCFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQL 487
Cdd:COG5047 394 KMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 488 YLQFITRYQNSEGKSLARVTTLTRQWVDtavSTEVNLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSK 567
Cdd:COG5047 474 YIQFITTYQHSSGTYRIRVTTVARMFTD---GGLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 568 FGEYRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAAL 647
Cdd:COG5047 551 FADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVL 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 648 LDVASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQAR 727
Cdd:COG5047 631 LDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQAR 710
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 145361384 728 FLLAKLNPSATYNNANEmsAGSDIIFTDDVSLQVFIEHLQKLAV 771
Cdd:COG5047 711 FLLSKINPSDITNKMSG--GGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
140-398 |
2.29e-157 |
|
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: 457.60 E-value: 2.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 140 LDTCMIEEELGYAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAP 219
Cdd:cd01478 10 VDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 220 TSGFsKGAQNGFQSSGVDRFLLPASECEYTLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVAL 299
Cdd:cd01478 90 ASQH-PGAGNPLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 300 VGGPCTEGPGTIISKDLSDPVRSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGG 379
Cdd:cd01478 169 AGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGG 248
|
250
....*....|....*....
gi 145361384 380 LVVLSESFGHSVFKDSFKR 398
Cdd:cd01478 249 HVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
140-400 |
1.91e-79 |
|
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: 254.87 E-value: 1.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 140 LDTCMI---EEELGYAKSALKQAIGLLP--ENALVGFVSFGTQAHVHELGFSEmskvfvfKGNKEVTKDQILDQLglgss 214
Cdd:pfam04811 10 IDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 215 srraptsgfskgaqngfqSSGVDRFLLPASECEYTLDLLLDELQSdQWPVQpgHRPQRCTGVALSVAAGLLGAClpGTGA 294
Cdd:pfam04811 78 ------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAA--FTGG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 295 RIVALVGGPCTEGPGTIISKDLSDpvrSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAV 374
Cdd:pfam04811 135 KIMVFQGGLPTVGPGGKLKSRLDE---SHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLS 211
|
250 260 270
....*....|....*....|....*....|
gi 145361384 375 ESTGGLVVLSESFG----HSVFKDSFKRMF 400
Cdd:pfam04811 212 RLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
140-398 |
1.13e-73 |
|
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: 239.45 E-value: 1.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 140 LDTCMI---EEELGYAKSALKQAIGLLP--ENALVGFVSFGTQAHVHELGFSEM-SKVFVFKGNKEVTkdqildqlglgs 213
Cdd:cd01468 10 IDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVF------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 214 ssrraptsgfskgaqngfqSSGVDRFLLPASECEYTLDLLLDELQSDQWPVqPGHRPQRCTGVALSVAAGLLGACLpgTG 293
Cdd:cd01468 78 -------------------LPLPDRFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGTF--AG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 294 ARIVALVGGPCTEGPGTIISKDLSDPVRSHkdldkDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVA 373
Cdd:cd01468 136 GRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQL 210
|
250 260
....*....|....*....|....*....
gi 145361384 374 VESTGGLVVLSESF----GHSVFKDSFKR 398
Cdd:cd01468 211 AKSTGGQVYLYDSFqapnDGSKFKQDLQR 239
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
621-741 |
5.09e-69 |
|
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: 222.63 E-value: 5.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 621 ENISNAIVMIQPSLTSYSFNSGPQAALLDVASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQ 700
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 145361384 701 EDSQMLVRERFPVPRLVVCDQHGSQARFLLAKLNPSATYNN 741
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
529-628 |
3.10e-26 |
|
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: 103.35 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 529 DQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKFGEYRKD--DPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNN 606
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 145361384 607 SP-DETAYFRMLLNRENISNAIV 628
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
410-514 |
1.46e-24 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 97.99 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 410 CFNGTLEINCSKDIKIQGVIGPCSSLekkgpNVADTvigegntsaWKLCGLDKSTCLTVFFDLSSTGSTapgalNQQLYL 489
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSR-----SSGDT---------WKLPSLDPDTSYAFEFDIDEPLPN-----GSNAYI 61
|
90 100
....*....|....*....|....*
gi 145361384 490 QFITRYQNSEGKSLARVTTLTRQWV 514
Cdd:pfam08033 62 QFALLYTHSSGERRIRVTTVALPVT 86
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
21-648 |
2.07e-16 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 83.69 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 21 VRMTWNLWPRTKVEASKCVIPLAASISPI-----RRHPLILDLPYAPLDCKTCKALLNAFARVDFAAMNWVCPFCYHRNH 95
Cdd:COG5028 153 VRSTMYAIPETNDLLKKSKIPFGLVIRPFlelypEEDPVPLVEDGSIVRCRRCRSYINPFVQFIEQGRKWRCNICRSKND 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 96 FPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFVFVLDTC-MIEEELGYAKSALKQAIGLLPENALVGFVSF 174
Cdd:COG5028 233 VPEGFDNPSGPNDPRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVfLIDVSFEAIKNGLVKAAIRAILENLDQIPNF 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 175 GTQAHVHELGFSemSKVFVFKGNKEVtKDQILDQLGLgsssrraptsgfskgaQNGFQSSGVDRFLLPASECEYTLDLLL 254
Cdd:COG5028 313 DPRTKIAIICFD--SSLHFFKLSPDL-DEQMLIVSDL----------------DEPFLPFPSGLFVLPLKSCKQIIETLL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 255 DELQSdqwPVQPGHRPQRCTGVALSVAAGLLGaclpGTGARIVALVGGPCTEGPGTIisKDLSDPVRSHKDLDKdaapyy 334
Cdd:COG5028 374 DRVPR---IFQDNKSPKNALGPALKAAKSLIG----GTGGKIIVFLSTLPNMGIGKL--QLREDKESSLLSCKD------ 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 335 kkavKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFEDGEH-SLGLCFNG 413
Cdd:COG5028 439 ----SFYKEFAIECSKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSATRPNDATKLANDLVSHlSMEIGYEA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 414 TLEINCSKDIKIQGVIGpcsslekkgpnvaDTVigegNTSAwKLCG---LDKSTCLTVFFDLSSTgSTAPGAlnqqlYLQ 490
Cdd:COG5028 515 VMRVRCSTGLRVSSFYG-------------NFF----NRSS-DLCAfstMPRDTSLLVEFSIDEK-LMTSDV-----YFQ 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 491 FITRYQNSEGKSLARVTTLTRQwvdtAVSTEVNLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSkfgE 570
Cdd:COG5028 571 VALLYTLNDGERRIRVVNLSLP----TSSSIREVYASADQLAIACILAKKASTKALNSSLKEARVLINKSMVDILK---A 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 571 YRKD-----DPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLtsYSFNSGPQA 645
Cdd:COG5028 644 YKKElvksnTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLKQLMRNIYPTL--YALHDMPIE 721
|
...
gi 145361384 646 ALL 648
Cdd:COG5028 722 AGL 724
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
62-99 |
2.02e-14 |
|
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: 67.47 E-value: 2.02e-14
10 20 30
....*....|....*....|....*....|....*...
gi 145361384 62 PLDCKTCKALLNAFARVDFAAMNWVCPFCYHRNHFPSH 99
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGGKKWTCNFCGTRNPVPPE 38
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
643-729 |
1.06e-12 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 63.87 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 643 PQAALLDVASIAADKILLLDAYFsvvvfhgmTISQWRnmGYHHQPEHEAFAQLLQApqedsQMLVRERFPVPRLVVCDQH 722
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAA-----QLDDDERFPLPEVIRVPQG 69
|
....*..
gi 145361384 723 GSQARFL 729
Cdd:pfam00626 70 KEPARFL 76
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
236-397 |
7.68e-05 |
|
Sec24-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 24 is very similar to Sec23. 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 carry a partial MIDAS motif and have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238756 [Multi-domain] Cd Length: 244 Bit Score: 44.96 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 236 VDRFLLPASECEYTLDLLLDELQSdqwPVQPGHRPQRCTGVALSVAAGLLGaclpGTGARIVALVGGPCTEGPGTIISKD 315
Cdd:cd01479 82 PDGLLVNLKESRQVIEDLLDQIPE---MFQDTKETESALGPALQAAFLLLK----ETGGKIIVFQSSLPTLGAGKLKSRE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361384 316 LSDPVRSHKDldkdaAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDS 395
Cdd:cd01479 155 DPKLLSTDKE-----KQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPSFNFSAPNDV 229
|
..
gi 145361384 396 FK 397
Cdd:cd01479 230 EK 231
|
|
| |
