|
Name |
Accession |
Description |
Interval |
E-value |
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
71-337 |
7.08e-116 |
|
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
:
Pssm-ID: 238363 [Multi-domain] Cd Length: 275 Bit Score: 348.46 E-value: 7.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 71 VNFYLYTLQNPSTGQQIKAT-QDSIDGSFFNPQNPTRITIHGWNSNYKDGVNTRVADAWFQYGDYNMIAVDWLRGRSLEY 149
Cdd:cd00707 3 VRFLLYTRENPNCPQLLFADdPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLSRGDYNVIVVDWGRGANPNY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 150 ASSVAGAPGAGKKVAALVDFLVEGYGMSLDTLEIVGFSLGAHVAGHTAKQVNsGKVGKVVGLDPASPLISYSNTEKRLSS 229
Cdd:cd00707 83 PQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLN-GKLGRITGLDPAGPLFSGADPEDRLDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 230 DDALYVESIQTNGAILGFGQPIGKASFYMNGGRSQPGCGIDI----TGSCSHTKAVLYYVEALL-WNNFPSIKCESSVDA 304
Cdd:cd00707 162 SDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDIlssdFVACSHQRAVHYFAESILsPCGFVAYPCSSYDEF 241
|
250 260 270
....*....|....*....|....*....|....
gi 24650473 305 NKNNCGNTYSS-VFMGASINFFVAEGIFYVPVNK 337
Cdd:cd00707 242 LAGKCFPCGSGcVRMGYHADRFRREGKFYLKTNA 275
|
|
| MSCRAMM_ClfA super family |
cl41352 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
334-621 |
5.76e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
The actual alignment was detected with superfamily member NF033609:
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 46.44 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 334 PVNKESPYGLGELNSGGEATTGTPEITSTTVDGEDESTTEVSTSTTTDKPEESTTEEPEEDSTTNGKPEESSTTTEQPED 413
Cdd:NF033609 542 PVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASD 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 414 STTTTEEPIDSTTEAPEDeSTTSSPTDGGEQSTTEEPETTTEKPEETSTSPIDTE-DSTTKEPEDVSTTPKESEESTTSS 492
Cdd:NF033609 622 SDSASDSDSASDSDSASD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDS 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 493 PEDDDTTSAPGEDDDTTAAPGGDEEETTTEDPEETTTSPSDAD---DSTTEEPEEDTTTTKKPVEPSTTTEEPEDSTTEV 569
Cdd:NF033609 701 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 780
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24650473 570 PEESTTEEPDKETSTTNAEPEVTTTVEPDVDSTVDPEGDQSTREDLEDVSTT 621
Cdd:NF033609 781 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 832
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
71-337 |
7.08e-116 |
|
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238363 [Multi-domain] Cd Length: 275 Bit Score: 348.46 E-value: 7.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 71 VNFYLYTLQNPSTGQQIKAT-QDSIDGSFFNPQNPTRITIHGWNSNYKDGVNTRVADAWFQYGDYNMIAVDWLRGRSLEY 149
Cdd:cd00707 3 VRFLLYTRENPNCPQLLFADdPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLSRGDYNVIVVDWGRGANPNY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 150 ASSVAGAPGAGKKVAALVDFLVEGYGMSLDTLEIVGFSLGAHVAGHTAKQVNsGKVGKVVGLDPASPLISYSNTEKRLSS 229
Cdd:cd00707 83 PQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLN-GKLGRITGLDPAGPLFSGADPEDRLDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 230 DDALYVESIQTNGAILGFGQPIGKASFYMNGGRSQPGCGIDI----TGSCSHTKAVLYYVEALL-WNNFPSIKCESSVDA 304
Cdd:cd00707 162 SDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDIlssdFVACSHQRAVHYFAESILsPCGFVAYPCSSYDEF 241
|
250 260 270
....*....|....*....|....*....|....
gi 24650473 305 NKNNCGNTYSS-VFMGASINFFVAEGIFYVPVNK 337
Cdd:cd00707 242 LAGKCFPCGSGcVRMGYHADRFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
71-341 |
1.75e-50 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 178.79 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 71 VNFYLYTLQNPSTGQQIKATQDSIDGSFFNPQNPTRITIHGWN-SNYKDGVNTRVADAWFQYGDYNMIAVDWLRGRSLEY 149
Cdd:pfam00151 38 TRFLLYTNENPNNCQLITGDPETIRNSNFNTSRKTRFIIHGFIdKGYEESWLSDMCKALFQVEDVNVICVDWKSGSRTHY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 150 ASSVAGAPGAGKKVAALVDFLVEGYGMSLDTLEIVGFSLGAHVAGHTAKQVNsGKVGKVVGLDPASPLISYSNTEKRLSS 229
Cdd:pfam00151 118 TQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTN-GKLGRITGLDPAGPYFQGTPEEVRLDP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 230 DDALYVESIQTNGA---ILGFG--QPIGKASFYMNGGRSQPGC-------GIDITG--------SCSHTKAVLYYVEALL 289
Cdd:pfam00151 197 GDADFVDAIHTDTRpipGLGFGisQPVGHVDFFPNGGSEQPGCqknilsqIIDIDGiwegtqfvACNHLRSVHYYIDSLL 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24650473 290 -WNNFPSIKCES--SVDANK------NNCGNtyssvfMGASINFFVA-----EGIFYVPVNKESPY 341
Cdd:pfam00151 277 nPRGFPGYPCSSydAFSQNKclpcpkGGCPQ------MGHYADKFPGktsklEQTFYLNTGSSSPF 336
|
|
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
73-309 |
2.97e-33 |
|
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.
Pssm-ID: 132274 [Multi-domain] Cd Length: 442 Bit Score: 133.10 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 73 FYLYTLQNPS--TGQQIKATQDSIDGSFFNPQNPTRITIHGWNSN--YKDGVNTRVADAWFQYGDYNMIAVDWLRGRSLE 148
Cdd:TIGR03230 9 FSLRTPEEPDddTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTgmFESWVPKLVAALYEREPSANVIVVDWLSRAQQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 149 YASSVAGAPGAGKKVAALVDFLVEGYGMSLDTLEIVGFSLGAHVAGhTAKQVNSGKVGKVVGLDPASPLISYSNTEKRLS 228
Cdd:TIGR03230 89 YPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAG-IAGSLTKHKVNRITGLDPAGPTFEYADAPSTLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 229 SDDALYVESIQTN-----GAILGFGQPIGKASFYMNGGRSQPGC-------GIDITG--------SCSHTKAVLYYVEAL 288
Cdd:TIGR03230 168 PDDADFVDVLHTNtrgspDRSIGIQRPVGHIDIYPNGGTFQPGCdiqetllVIAEKGlgnmdqlvKCSHERSIHLFIDSL 247
|
250 260
....*....|....*....|...
gi 24650473 289 LWNNFPSI--KCESSVDANKNNC 309
Cdd:TIGR03230 248 LNEENPSMayRCSSKEAFNKGLC 270
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
334-621 |
5.76e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 46.44 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 334 PVNKESPYGLGELNSGGEATTGTPEITSTTVDGEDESTTEVSTSTTTDKPEESTTEEPEEDSTTNGKPEESSTTTEQPED 413
Cdd:NF033609 542 PVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASD 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 414 STTTTEEPIDSTTEAPEDeSTTSSPTDGGEQSTTEEPETTTEKPEETSTSPIDTE-DSTTKEPEDVSTTPKESEESTTSS 492
Cdd:NF033609 622 SDSASDSDSASDSDSASD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDS 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 493 PEDDDTTSAPGEDDDTTAAPGGDEEETTTEDPEETTTSPSDAD---DSTTEEPEEDTTTTKKPVEPSTTTEEPEDSTTEV 569
Cdd:NF033609 701 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 780
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24650473 570 PEESTTEEPDKETSTTNAEPEVTTTVEPDVDSTVDPEGDQSTREDLEDVSTT 621
Cdd:NF033609 781 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 832
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
468-611 |
2.14e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 44.20 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 468 EDSTTKEPEDVSTTPKESEESTT-------SSPEDDDTTSAPGEDDDTTAAPGGDEEETTTEDPEETTTSPSDADDSTTE 540
Cdd:PRK13108 293 DEALEREPAELAAAAVASAASAVgpvgpgePNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIE 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24650473 541 EPEEDTTTTKKPVEP-------STTTEEPEDSTTEVPEESTTEEPDKETSTTNA-EPEVTTTVEPDVDSTvDPEGDQST 611
Cdd:PRK13108 373 REQPGDLAGQAPAAHqvdaeaaSAAPEEPAALASEAHDETEPEVPEKAAPIPDPaKPDELAVAGPGDDPA-EPDGIRRQ 450
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
336-656 |
7.53e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.98 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 336 NKESPyGLGELNSGGEATTGTPEITSTTvdgedesttEVSTSTTTDKPEESTTEEPEEDSTTNGKPEESSTTTEQPEDST 415
Cdd:pfam05109 533 NATSP-TLGKTSPTSAVTTPTPNATSPT---------PAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 416 TTTEEPIDSTTEAP----EDESTTSSPTDG--GEQSTTEEPETTTEKPEETSTSPIDTEDSTTKEPEDVSTTPKESEEST 489
Cdd:pfam05109 603 NTTNHTLGGTSSTPvvtsPPKNATSAVTTGqhNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIT 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 490 TSSPEDDDT----TSAPGEDDDTTAAPGGDeeetttedpeetttspsdADDSTTEEPEEDTTTTKKPVEPSTTTEEPEDS 565
Cdd:pfam05109 683 QVTPASTSThhvsTSSPAPRPGTTSQASGP------------------GNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQ 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 566 TTEVPeeSTTEEPDKETSTTNAEPEVTTTVEPDVDSTVDPEGDQSTREDLEDVSTTAVPTK----LPSTTGVPPEVPITT 641
Cdd:pfam05109 745 KTAVP--TVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTssklRPRWTFTSPPVTTAQ 822
|
330
....*....|....*
gi 24650473 642 LAPEVPSTSPPQDGN 656
Cdd:pfam05109 823 ATVPVPPTSQPRFSN 837
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
93-222 |
3.77e-03 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 39.21 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 93 SIDGSFFNPQNPTRITI---HGWNSNYkdGVNTRVADAWFQYGdYNMIAVDWlR--GRSLEYASSVAGAPGAGKKVAALV 167
Cdd:COG2267 15 RLRGRRWRPAGSPRGTVvlvHGLGEHS--GRYAELAEALAAAG-YAVLAFDL-RghGRSDGPRGHVDSFDDYVDDLRAAL 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24650473 168 DFLVEGYGMSLDtleIVGFSLGAHVAGHTAKQvNSGKVGKVVGLDPA---SPLISYSN 222
Cdd:COG2267 91 DALRARPGLPVV---LLGHSMGGLIALLYAAR-YPDRVAGLVLLAPAyraDPLLGPSA 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
71-337 |
7.08e-116 |
|
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238363 [Multi-domain] Cd Length: 275 Bit Score: 348.46 E-value: 7.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 71 VNFYLYTLQNPSTGQQIKAT-QDSIDGSFFNPQNPTRITIHGWNSNYKDGVNTRVADAWFQYGDYNMIAVDWLRGRSLEY 149
Cdd:cd00707 3 VRFLLYTRENPNCPQLLFADdPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLSRGDYNVIVVDWGRGANPNY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 150 ASSVAGAPGAGKKVAALVDFLVEGYGMSLDTLEIVGFSLGAHVAGHTAKQVNsGKVGKVVGLDPASPLISYSNTEKRLSS 229
Cdd:cd00707 83 PQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLN-GKLGRITGLDPAGPLFSGADPEDRLDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 230 DDALYVESIQTNGAILGFGQPIGKASFYMNGGRSQPGCGIDI----TGSCSHTKAVLYYVEALL-WNNFPSIKCESSVDA 304
Cdd:cd00707 162 SDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDIlssdFVACSHQRAVHYFAESILsPCGFVAYPCSSYDEF 241
|
250 260 270
....*....|....*....|....*....|....
gi 24650473 305 NKNNCGNTYSS-VFMGASINFFVAEGIFYVPVNK 337
Cdd:cd00707 242 LAGKCFPCGSGcVRMGYHADRFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
71-341 |
1.75e-50 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 178.79 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 71 VNFYLYTLQNPSTGQQIKATQDSIDGSFFNPQNPTRITIHGWN-SNYKDGVNTRVADAWFQYGDYNMIAVDWLRGRSLEY 149
Cdd:pfam00151 38 TRFLLYTNENPNNCQLITGDPETIRNSNFNTSRKTRFIIHGFIdKGYEESWLSDMCKALFQVEDVNVICVDWKSGSRTHY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 150 ASSVAGAPGAGKKVAALVDFLVEGYGMSLDTLEIVGFSLGAHVAGHTAKQVNsGKVGKVVGLDPASPLISYSNTEKRLSS 229
Cdd:pfam00151 118 TQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTN-GKLGRITGLDPAGPYFQGTPEEVRLDP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 230 DDALYVESIQTNGA---ILGFG--QPIGKASFYMNGGRSQPGC-------GIDITG--------SCSHTKAVLYYVEALL 289
Cdd:pfam00151 197 GDADFVDAIHTDTRpipGLGFGisQPVGHVDFFPNGGSEQPGCqknilsqIIDIDGiwegtqfvACNHLRSVHYYIDSLL 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24650473 290 -WNNFPSIKCES--SVDANK------NNCGNtyssvfMGASINFFVA-----EGIFYVPVNKESPY 341
Cdd:pfam00151 277 nPRGFPGYPCSSydAFSQNKclpcpkGGCPQ------MGHYADKFPGktsklEQTFYLNTGSSSPF 336
|
|
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
73-309 |
2.97e-33 |
|
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.
Pssm-ID: 132274 [Multi-domain] Cd Length: 442 Bit Score: 133.10 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 73 FYLYTLQNPS--TGQQIKATQDSIDGSFFNPQNPTRITIHGWNSN--YKDGVNTRVADAWFQYGDYNMIAVDWLRGRSLE 148
Cdd:TIGR03230 9 FSLRTPEEPDddTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTgmFESWVPKLVAALYEREPSANVIVVDWLSRAQQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 149 YASSVAGAPGAGKKVAALVDFLVEGYGMSLDTLEIVGFSLGAHVAGhTAKQVNSGKVGKVVGLDPASPLISYSNTEKRLS 228
Cdd:TIGR03230 89 YPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAG-IAGSLTKHKVNRITGLDPAGPTFEYADAPSTLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 229 SDDALYVESIQTN-----GAILGFGQPIGKASFYMNGGRSQPGC-------GIDITG--------SCSHTKAVLYYVEAL 288
Cdd:TIGR03230 168 PDDADFVDVLHTNtrgspDRSIGIQRPVGHIDIYPNGGTFQPGCdiqetllVIAEKGlgnmdqlvKCSHERSIHLFIDSL 247
|
250 260
....*....|....*....|...
gi 24650473 289 LWNNFPSI--KCESSVDANKNNC 309
Cdd:TIGR03230 248 LNEENPSMayRCSSKEAFNKGLC 270
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
159-281 |
4.06e-19 |
|
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238382 [Multi-domain] Cd Length: 153 Bit Score: 84.47 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 159 AGKKVAALVDFLVE--GYGMSLDTLEIVGFSLGAHVAGHTAKQVNS---GKVGKVVGLDPASPLiSYSNTEKRLSSDDAL 233
Cdd:cd00741 6 AARSLANLVLPLLKsaLAQYPDYKIHVTGHSLGGALAGLAGLDLRGrglGRLVRVYTFGPPRVG-NAAFAEDRLDPSDAL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24650473 234 YVESIQTNGAILG------FGQPIGKASFYMNGGRSQPGC---------------GIDITGSCSHTKAV 281
Cdd:cd00741 85 FVDRIVNDNDIVPrlppggEGYPHGGAEFYINGGKSQPGCcknvleavdidfgniGLSGNGLCDHLRYF 153
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
334-621 |
5.76e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 46.44 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 334 PVNKESPYGLGELNSGGEATTGTPEITSTTVDGEDESTTEVSTSTTTDKPEESTTEEPEEDSTTNGKPEESSTTTEQPED 413
Cdd:NF033609 542 PVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASD 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 414 STTTTEEPIDSTTEAPEDeSTTSSPTDGGEQSTTEEPETTTEKPEETSTSPIDTE-DSTTKEPEDVSTTPKESEESTTSS 492
Cdd:NF033609 622 SDSASDSDSASDSDSASD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDS 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 493 PEDDDTTSAPGEDDDTTAAPGGDEEETTTEDPEETTTSPSDAD---DSTTEEPEEDTTTTKKPVEPSTTTEEPEDSTTEV 569
Cdd:NF033609 701 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 780
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24650473 570 PEESTTEEPDKETSTTNAEPEVTTTVEPDVDSTVDPEGDQSTREDLEDVSTT 621
Cdd:NF033609 781 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 832
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
468-611 |
2.14e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 44.20 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 468 EDSTTKEPEDVSTTPKESEESTT-------SSPEDDDTTSAPGEDDDTTAAPGGDEEETTTEDPEETTTSPSDADDSTTE 540
Cdd:PRK13108 293 DEALEREPAELAAAAVASAASAVgpvgpgePNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIE 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24650473 541 EPEEDTTTTKKPVEP-------STTTEEPEDSTTEVPEESTTEEPDKETSTTNA-EPEVTTTVEPDVDSTvDPEGDQST 611
Cdd:PRK13108 373 REQPGDLAGQAPAAHqvdaeaaSAAPEEPAALASEAHDETEPEVPEKAAPIPDPaKPDELAVAGPGDDPA-EPDGIRRQ 450
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
336-656 |
7.53e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.98 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 336 NKESPyGLGELNSGGEATTGTPEITSTTvdgedesttEVSTSTTTDKPEESTTEEPEEDSTTNGKPEESSTTTEQPEDST 415
Cdd:pfam05109 533 NATSP-TLGKTSPTSAVTTPTPNATSPT---------PAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 416 TTTEEPIDSTTEAP----EDESTTSSPTDG--GEQSTTEEPETTTEKPEETSTSPIDTEDSTTKEPEDVSTTPKESEEST 489
Cdd:pfam05109 603 NTTNHTLGGTSSTPvvtsPPKNATSAVTTGqhNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIT 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 490 TSSPEDDDT----TSAPGEDDDTTAAPGGDeeetttedpeetttspsdADDSTTEEPEEDTTTTKKPVEPSTTTEEPEDS 565
Cdd:pfam05109 683 QVTPASTSThhvsTSSPAPRPGTTSQASGP------------------GNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQ 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 566 TTEVPeeSTTEEPDKETSTTNAEPEVTTTVEPDVDSTVDPEGDQSTREDLEDVSTTAVPTK----LPSTTGVPPEVPITT 641
Cdd:pfam05109 745 KTAVP--TVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTssklRPRWTFTSPPVTTAQ 822
|
330
....*....|....*
gi 24650473 642 LAPEVPSTSPPQDGN 656
Cdd:pfam05109 823 ATVPVPPTSQPRFSN 837
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
394-653 |
1.19e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 42.40 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 394 DSTTNGKPEESSTTTEQPEDSTTTTEEPIDSTTEAPE---DESTTSSPTDGGEQSTTEEPE------------------- 451
Cdd:PRK14949 479 DADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNsaaDNTVDDNYSAEDTLESNGLDEgdyaqdsapldayqddyva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 452 ------TTTEKPEETSTSPIDTEDSTTKEPEDVSTTPKESEESTTSSPEDDDTTSA---------PGEDDDTTAApggde 516
Cdd:PRK14949 559 fssesyNALSDDEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAAASLADDDILDAvlaardsllSDLDALSPKE----- 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 517 eetttedpeetttspSDADDSTTEEPEEDTTTTKKPVEPSTTTEEPEDSTTEVPEESTTEEP------DKETSTTNAEPE 590
Cdd:PRK14949 634 ---------------GDGKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFElathqsVPEAALASGSAP 698
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 591 VTTTVEPDVD-------STVDPEGDQSTREDLEDVSTTAVPTKLPSTTGVPPEVpitTLAPEVPSTSPPQ 653
Cdd:PRK14949 699 APPPVPDPYDrppweeaPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQA---THQPQVQAEAQSP 765
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
400-651 |
3.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 40.34 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 400 KPEESSTTTEQPEDSTTTTEEPIDSTTEAPEDESTTSSPTDGgeqstteepettTEKPEETSTSPIDTEDSTTKEPEDVS 479
Cdd:PHA03169 47 APPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERG------------QGGPSGSGSESVGSPTPSPSGSAEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 480 TTPKESEESTTSSPEDDDTTSAPGEdddttaaPGGDEEETTTEDPEETTTSPSDADDSTTEEpeedttttkkpvEPSTTT 559
Cdd:PHA03169 115 ASGLSPENTSGSSPESPASHSPPPS-------PPSHPGPHEPAPPESHNPSPNQQPSSFLQP------------SHEDSP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 560 EEPEDSTTEVPEESttEEPDKETSTTNAEPEVTTTVEPDVDSTVDPEGDQSTREDlEDVSTTAVPTKlPSTTGVPPEVPI 639
Cdd:PHA03169 176 EEPEPPTSEPEPDS--PGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQ-QAVEHEDEPTE-PEREGPPFPGHR 251
|
250
....*....|....*
gi 24650473 640 T---TLAPEVPSTSP 651
Cdd:PHA03169 252 ShsyTVVGWKPSTRP 266
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
93-222 |
3.77e-03 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 39.21 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 93 SIDGSFFNPQNPTRITI---HGWNSNYkdGVNTRVADAWFQYGdYNMIAVDWlR--GRSLEYASSVAGAPGAGKKVAALV 167
Cdd:COG2267 15 RLRGRRWRPAGSPRGTVvlvHGLGEHS--GRYAELAEALAAAG-YAVLAFDL-RghGRSDGPRGHVDSFDDYVDDLRAAL 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24650473 168 DFLVEGYGMSLDtleIVGFSLGAHVAGHTAKQvNSGKVGKVVGLDPA---SPLISYSN 222
Cdd:COG2267 91 DALRARPGLPVV---LLGHSMGGLIALLYAAR-YPDRVAGLVLLAPAyraDPLLGPSA 144
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
396-652 |
4.96e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 40.28 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 396 TTNGKPEESSTTTEQPeDSTTTTEEPIDSTTEAPEDESTTSSPTDGGEQSTTEEPETTTEKPEETSTSPIDTEDSTTKEP 475
Cdd:pfam05109 489 TPSPSPRDNGTESKAP-DMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTP 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 476 E-DVSTTPKESEESTTSSPEDDDTTSAPGED----DDTTAAPGGDEEETTTEDPEETTTSPSDADDSTTEEPEEDTTTTK 550
Cdd:pfam05109 568 NaTIPTLGKTSPTSAVTTPTPNATSPTVGETspqaNTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLR 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 551 KPVEPSTTTEEPEDSTTEVPEESTTEEPDKETSTTNAEPEVTTTVEPDVDSTVDPEGDQSTREDLEDVSTTAVPTKLPST 630
Cdd:pfam05109 648 PSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVT 727
|
250 260
....*....|....*....|..
gi 24650473 631 TGVPPEVPITTLAPEVPSTSPP 652
Cdd:pfam05109 728 KGTPPKNATSPQAPSGQKTAVP 749
|
|
| DUF4775 |
pfam16001 |
Domain of unknown function (DUF4775); This family of proteins is functionally uncharacterized. ... |
395-656 |
5.42e-03 |
|
Domain of unknown function (DUF4775); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 308 and 484 amino acids in length.
Pssm-ID: 406411 [Multi-domain] Cd Length: 456 Bit Score: 39.72 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 395 STTNGKPEESSTTTEQPEDSTTTTEEPIdstteapedeSTTSSPTDGGEQSTTEEPETTTEKPEETSTSPIDTEDSTTKE 474
Cdd:pfam16001 35 SSTRGTPTRSAETVTPPPSKKARTSPAT----------ATKSSGGKGRGARKLDVGAEEPVEQETKKKKKVQNEPEAKEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 475 PEDVSTTPKESEESTTSSPEDDDTTSAPGEDDDTTAAPGGDEEETTTEDPEETTTSPSDADDSTTEEPEEDTTTTKKP-- 552
Cdd:pfam16001 105 KEKVSEPVKGKPAAKKEKKEEKKQKKKEADEKEVVEEKEKEDKEEEKTETKETDAKTAESKDQPDGVGQLPAVAEEKQnh 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650473 553 -VEPSTTTEEPEDSTTEVPEESTTEEPDKetSTTNAEPEVTTTVEPDVDSTVDPEGDqstrEDLEDVSTTAVPTKLPSTT 631
Cdd:pfam16001 185 vDEDKPETEEPEEKEKTPEEVAKAEEPPK--TSENGAATDTPAAVPESESAMEVDEE----EKLQENTPQATADAPSDDK 258
|
250 260
....*....|....*....|....*
gi 24650473 632 GVPPEVPITTLAPEVPSTSPPQDGN 656
Cdd:pfam16001 259 AVPDIKVEEKVAAVSESSEEPKETS 283
|
|
| DUF3664 |
pfam12406 |
Surface protein; This family of proteins is found in eukaryotes. Proteins in this family are ... |
531-597 |
8.28e-03 |
|
Surface protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 131 and 312 amino acids in length.
Pssm-ID: 289191 [Multi-domain] Cd Length: 99 Bit Score: 36.39 E-value: 8.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24650473 531 PSDADDSTTEEPEEDTTTTKKPVEPSTTTE--------EPEDSTTEVPEESTTEEP---DKETSTTNAEPEVTTTVEP 597
Cdd:pfam12406 17 PLDPDQLIDQIEPSEQPAQQEPIEPQQPTQpstepeelQPETVTVEVPEPVTSEEPkesDQTEEQKHEEPEASPAPEP 94
|
|
| |
