|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
11-772 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1557.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 11 EEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDCKTCKALLNAFARVDFAAMNWVCPFC 90
Cdd:PLN00162 2 DFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPFC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 91 YHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFVFVLDTCMIEEELGYAKSALKQAIGLLPENALVG 170
Cdd:PLN00162 82 FQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 171 FVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAPTSGFSkGAQNGFQSSGVDRFLLPASECEYTL 250
Cdd:PLN00162 162 LITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIA-GARDGLSSSGVNRFLLPASECEFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 251 DLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDKDA 330
Cdd:PLN00162 241 NSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 331 APYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSLGL 409
Cdd:PLN00162 321 APYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFErDGEGSLGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 410 CFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQLYL 489
Cdd:PLN00162 401 SFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPPGQQFFL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 490 QFITRYQNSEGKSLARVTTLTRQWVDTAvSTENLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKFGE 569
Cdd:PLN00162 481 QFLTRYQHSNGQTRLRVTTVTRRWVEGS-SSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 570 YRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAALLDV 649
Cdd:PLN00162 560 YRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 650 ASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQARFLL 729
Cdd:PLN00162 640 ASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLL 719
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1789578152 730 AKLNPSATYNNANEMSaGSDIIFTDDVSLQVFIEHLQKLAVQS 772
Cdd:PLN00162 720 AKLNPSATYNSANAMG-GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
10-770 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 804.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 10 VEEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDC-KTCKALLNAFARVDFAAMNWVCP 88
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 89 FCYHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFvfvLDTCMIEEELGYAKSALKQAIGLLPENAL 168
Cdd:COG5047 81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFV---VDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 169 VGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKdQILDQLGLGSSSRRaptSGFSKGAQNGFQSSGVDRFLLPASECEY 248
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK-ENLQELLALSKPTK---SGGFESKISGIGQFASSRFLLPTQQCEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 249 TLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDK 328
Cdd:COG5047 234 KLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 329 DAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSL 407
Cdd:COG5047 314 DSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNrDSEGYL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 408 GLCFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQL 487
Cdd:COG5047 394 KMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 488 YLQFITRYQNSEGKSLARVTTLTRQWVDTavSTENLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKF 567
Cdd:COG5047 474 YIQFITTYQHSSGTYRIRVTTVARMFTDG--GLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 568 GEYRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAALL 647
Cdd:COG5047 552 ADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 648 DVASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQARF 727
Cdd:COG5047 632 DSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARF 711
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1789578152 728 LLAKLNPSATYNNANEmsAGSDIIFTDDVSLQVFIEHLQKLAV 770
Cdd:COG5047 712 LLSKINPSDITNKMSG--GGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
140-398 |
2.28e-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: 2.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 140 LDTCMIEEELGYAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAP 219
Cdd:cd01478 10 VDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 220 TSGFsKGAQNGFQSSGVDRFLLPASECEYTLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVAL 299
Cdd:cd01478 90 ASQH-PGAGNPLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 300 VGGPCTEGPGTIISKDLSDPVRSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGG 379
Cdd:cd01478 169 AGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGG 248
|
250
....*....|....*....
gi 1789578152 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 |
1.74e-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: 1.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 140 LDTCMI---EEELGYAKSALKQAIGLLP--ENALVGFVSFGTQAHVHELGFSEmskvfvfKGNKEVTKDQILDQLglgss 214
Cdd:pfam04811 10 IDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 215 srraptsgfskgaqngfqSSGVDRFLLPASECEYTLDLLLDELQSdQWPVQpgHRPQRCTGVALSVAAGLLGAClpGTGA 294
Cdd:pfam04811 78 ------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAA--FTGG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 295 RIVALVGGPCTEGPGTIISKDLSDpvrSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAV 374
Cdd:pfam04811 135 KIMVFQGGLPTVGPGGKLKSRLDE---SHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLS 211
|
250 260 270
....*....|....*....|....*....|
gi 1789578152 375 ESTGGLVVLSESFG----HSVFKDSFKRMF 400
Cdd:pfam04811 212 RLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
11-772 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1557.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 11 EEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDCKTCKALLNAFARVDFAAMNWVCPFC 90
Cdd:PLN00162 2 DFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPFC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 91 YHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFVFVLDTCMIEEELGYAKSALKQAIGLLPENALVG 170
Cdd:PLN00162 82 FQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 171 FVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAPTSGFSkGAQNGFQSSGVDRFLLPASECEYTL 250
Cdd:PLN00162 162 LITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIA-GARDGLSSSGVNRFLLPASECEFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 251 DLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDKDA 330
Cdd:PLN00162 241 NSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 331 APYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSLGL 409
Cdd:PLN00162 321 APYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFErDGEGSLGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 410 CFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQLYL 489
Cdd:PLN00162 401 SFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPPGQQFFL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 490 QFITRYQNSEGKSLARVTTLTRQWVDTAvSTENLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKFGE 569
Cdd:PLN00162 481 QFLTRYQHSNGQTRLRVTTVTRRWVEGS-SSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 570 YRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAALLDV 649
Cdd:PLN00162 560 YRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 650 ASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQARFLL 729
Cdd:PLN00162 640 ASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLL 719
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1789578152 730 AKLNPSATYNNANEMSaGSDIIFTDDVSLQVFIEHLQKLAVQS 772
Cdd:PLN00162 720 AKLNPSATYNSANAMG-GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
10-770 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 804.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 10 VEEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDC-KTCKALLNAFARVDFAAMNWVCP 88
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 89 FCYHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFvfvLDTCMIEEELGYAKSALKQAIGLLPENAL 168
Cdd:COG5047 81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFV---VDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 169 VGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKdQILDQLGLGSSSRRaptSGFSKGAQNGFQSSGVDRFLLPASECEY 248
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK-ENLQELLALSKPTK---SGGFESKISGIGQFASSRFLLPTQQCEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 249 TLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPVRSHKDLDK 328
Cdd:COG5047 234 KLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 329 DAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFE-DGEHSL 407
Cdd:COG5047 314 DSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNrDSEGYL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 408 GLCFNGTLEINCSKDIKIQGVIGPCSSLEKKGPNVADTVIGEGNTSAWKLCGLDKSTCLTVFFDLSSTGSTAPGALNQQL 487
Cdd:COG5047 394 KMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 488 YLQFITRYQNSEGKSLARVTTLTRQWVDTavSTENLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKF 567
Cdd:COG5047 474 YIQFITTYQHSSGTYRIRVTTVARMFTDG--GLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 568 GEYRKDDPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLTSYSFNSGPQAALL 647
Cdd:COG5047 552 ADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 648 DVASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQEDSQMLVRERFPVPRLVVCDQHGSQARF 727
Cdd:COG5047 632 DSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARF 711
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1789578152 728 LLAKLNPSATYNNANEmsAGSDIIFTDDVSLQVFIEHLQKLAV 770
Cdd:COG5047 712 LLSKINPSDITNKMSG--GGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
140-398 |
2.28e-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: 2.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 140 LDTCMIEEELGYAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAP 219
Cdd:cd01478 10 VDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 220 TSGFsKGAQNGFQSSGVDRFLLPASECEYTLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVAL 299
Cdd:cd01478 90 ASQH-PGAGNPLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 300 VGGPCTEGPGTIISKDLSDPVRSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGG 379
Cdd:cd01478 169 AGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGG 248
|
250
....*....|....*....
gi 1789578152 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 |
1.74e-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: 1.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 140 LDTCMI---EEELGYAKSALKQAIGLLP--ENALVGFVSFGTQAHVHELGFSEmskvfvfKGNKEVTKDQILDQLglgss 214
Cdd:pfam04811 10 IDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 215 srraptsgfskgaqngfqSSGVDRFLLPASECEYTLDLLLDELQSdQWPVQpgHRPQRCTGVALSVAAGLLGAClpGTGA 294
Cdd:pfam04811 78 ------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAA--FTGG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 295 RIVALVGGPCTEGPGTIISKDLSDpvrSHKDLDKDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAV 374
Cdd:pfam04811 135 KIMVFQGGLPTVGPGGKLKSRLDE---SHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLS 211
|
250 260 270
....*....|....*....|....*....|
gi 1789578152 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 |
1.05e-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: 1.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 140 LDTCMI---EEELGYAKSALKQAIGLLP--ENALVGFVSFGTQAHVHELGFSEM-SKVFVFKGNKEVTkdqildqlglgs 213
Cdd:cd01468 10 IDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVF------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 214 ssrraptsgfskgaqngfqSSGVDRFLLPASECEYTLDLLLDELQSDQWPVqPGHRPQRCTGVALSVAAGLLGACLpgTG 293
Cdd:cd01468 78 -------------------LPLPDRFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGTF--AG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 294 ARIVALVGGPCTEGPGTIISKDLSDPVRSHkdldkDAAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVA 373
Cdd:cd01468 136 GRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQL 210
|
250 260
....*....|....*....|....*....
gi 1789578152 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 ... |
620-740 |
5.12e-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: 5.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 620 ENISNAIVMIQPSLTSYSFNSGPQAALLDVASIAADKILLLDAYFSVVVFHGMTISQWRNMGYHHQPEHEAFAQLLQAPQ 699
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1789578152 700 EDSQMLVRERFPVPRLVVCDQHGSQARFLLAKLNPSATYNN 740
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
528-627 |
3.15e-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: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 528 DQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSKFGEYRKD--DPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNN 605
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 1789578152 606 SP-DETAYFRMLLNRENISNAIV 627
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
410-514 |
1.38e-24 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 97.99 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 410 CFNGTLEINCSKDIKIQGVIGPCSSLekkgpNVADTvigegntsaWKLCGLDKSTCLTVFFDLSSTGSTapgalNQQLYL 489
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSR-----SSGDT---------WKLPSLDPDTSYAFEFDIDEPLPN-----GSNAYI 61
|
90 100
....*....|....*....|....*
gi 1789578152 490 QFITRYQNSEGKSLARVTTLTRQWV 514
Cdd:pfam08033 62 QFALLYTHSSGERRIRVTTVALPVT 86
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
21-647 |
3.42e-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: 86.38 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 21 VRMTWNLWPRTKVEASKCVIPLAASISPI-----RRHPLILDLPYAPLDCKTCKALLNAFARVDFAAMNWVCPFCYHRNH 95
Cdd:COG5028 153 VRSTMYAIPETNDLLKKSKIPFGLVIRPFlelypEEDPVPLVEDGSIVRCRRCRSYINPFVQFIEQGRKWRCNICRSKND 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 96 FPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFVFVLDTC-MIEEELGYAKSALKQAIGLLPENALVGFVSF 174
Cdd:COG5028 233 VPEGFDNPSGPNDPRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVfLIDVSFEAIKNGLVKAAIRAILENLDQIPNF 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 175 GTQAHVHELGFSemSKVFVFKGNKEVtKDQILDQLGLgsssrraptsgfskgaQNGFQSSGVDRFLLPASECEYTLDLLL 254
Cdd:COG5028 313 DPRTKIAIICFD--SSLHFFKLSPDL-DEQMLIVSDL----------------DEPFLPFPSGLFVLPLKSCKQIIETLL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 255 DELQSdqwPVQPGHRPQRCTGVALSVAAGLLGaclpGTGARIVALVGGPCTEGPGTIisKDLSDPVRSHKDLDKdaapyy 334
Cdd:COG5028 374 DRVPR---IFQDNKSPKNALGPALKAAKSLIG----GTGGKIIVFLSTLPNMGIGKL--QLREDKESSLLSCKD------ 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 335 kkavKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDSFKRMFEDGEH-SLGLCFNG 413
Cdd:COG5028 439 ----SFYKEFAIECSKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSATRPNDATKLANDLVSHlSMEIGYEA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 414 TLEINCSKDIKIQGVIGpcsslekkgpnvaDTVigegNTSAwKLCG---LDKSTCLTVFFDLSSTgSTAPGAlnqqlYLQ 490
Cdd:COG5028 515 VMRVRCSTGLRVSSFYG-------------NFF----NRSS-DLCAfstMPRDTSLLVEFSIDEK-LMTSDV-----YFQ 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 491 FITRYQNSEGKSLARVTTLTrqwVDTAVSTENLVQGFDQETAAVVMARLTSLKMETEEGFDATRWLDRTLIRLCSkfgEY 570
Cdd:COG5028 571 VALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKASTKALNSSLKEARVLINKSMVDILK---AY 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 571 RKD-----DPTSFTLKPYLTLFPQFMFNLRRSQFVQVFNNSPDETAYFRMLLNRENISNAIVMIQPSLtsYSFNSGPQAA 645
Cdd:COG5028 645 KKElvksnTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLKQLMRNIYPTL--YALHDMPIEA 722
|
..
gi 1789578152 646 LL 647
Cdd:COG5028 723 GL 724
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
62-99 |
2.01e-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: 2.01e-14
10 20 30
....*....|....*....|....*....|....*...
gi 1789578152 62 PLDCKTCKALLNAFARVDFAAMNWVCPFCYHRNHFPSH 99
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGGKKWTCNFCGTRNPVPPE 38
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
642-728 |
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 1789578152 642 PQAALLDVASIAADKILLLDAYFsvvvfhgmTISQWRnmGYHHQPEHEAFAQLLQApqedsQMLVRERFPVPRLVVCDQH 721
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAA-----QLDDDERFPLPEVIRVPQG 69
|
....*..
gi 1789578152 722 GSQARFL 728
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 |
7.53e-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: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 236 VDRFLLPASECEYTLDLLLDELQSdqwPVQPGHRPQRCTGVALSVAAGLLGaclpGTGARIVALVGGPCTEGPGTIISKD 315
Cdd:cd01479 82 PDGLLVNLKESRQVIEDLLDQIPE---MFQDTKETESALGPALQAAFLLLK----ETGGKIIVFQSSLPTLGAGKLKSRE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789578152 316 LSDPVRSHKDldkdaAPYYKKAVKFYDSIAKQLVAQGHVLDLFASALDQVGVAEMKVAVESTGGLVVLSESFGHSVFKDS 395
Cdd:cd01479 155 DPKLLSTDKE-----KQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPSFNFSAPNDV 229
|
..
gi 1789578152 396 FK 397
Cdd:cd01479 230 EK 231
|
|
| |
