|
Name |
Accession |
Description |
Interval |
E-value |
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
74-256 |
1.33e-08 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 53.81 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 74 SLKEMVDAVESILNDLKELGKDVKE-VEDAINKAKE-MVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFG 151
Cdd:pfam01442 5 SLDELSTYAEELQEQLGPVAQELVDrLEKETEALRErLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 152 KLKEKVDGISDKLKEKVEDIFKSVKEKVENalneikspeealnkVKEVVEEALNKVKEVVEEALNKVKQMIEELVDKLKE 231
Cdd:pfam01442 85 RLNADAEELQEKLAPYGEELRERLEQNVDA--------------LRARLAPYAEELRQKLAERLEELKESLAPYAEEVQA 150
|
170 180
....*....|....*....|....*
gi 1309078200 232 IVEEALNKVKQIVEDALNKLKEMIE 256
Cdd:pfam01442 151 QLSQRLQELREKLEPQAEDLREKLD 175
|
|
| COG5412 |
COG5412 |
Phage-related protein [Mobilome: prophages, transposons]; |
27-317 |
3.29e-08 |
|
Phage-related protein [Mobilome: prophages, transposons];
Pssm-ID: 444167 [Multi-domain] Cd Length: 704 Bit Score: 55.09 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 27 ILGNLKDTVTEIITKLKEvvegaLNKLKEMVELSFSKLKEMVATAFNSLKEMVDA-VESILNDLKELGKDVKEVEDAINK 105
Cdd:COG5412 401 ALWKNSETFRNLVQGVWE-----LNAIKTAIEGVVSAIVTFISALWEAIKALLTAiGGALPQLIAAVWNGIVQFISAIIT 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 106 AKEMVkeVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKVDGIsdkLKEKVEDIFKSVKEKVENALNE 185
Cdd:COG5412 476 NLPLI--LQAALQLIKALIKGLWTAIKGVIQGAIEIITGIIQFITALLTGDWSGI---IWEGIKQLVSGIVEIIPNIVAA 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 186 IKSpeealnkvkEVVEEALNKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQIVEDALNKLKEMIEKLLTKL--- 262
Cdd:COG5412 551 VPQ---------GGIAALWDAIKGFFPGLIEAIVQLVSNIINAIISIISSILNAAGSIISSIWNAIKSAVSSIISAKsig 621
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 263 KEMIEELLK-----LRKMIEKALKLKQMIENMIKDLEDLKNKAlGELAKLENNLVEGLKG 317
Cdd:COG5412 622 KNIVNGLWNgiksaAGAVTDKVKDIVGGIVDGIKGALGIHSPS-RKFLEIGKMIVAGLAK 680
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
105-269 |
1.71e-07 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 50.73 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 105 KAKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEKVEDifksVKEKVENALN 184
Cdd:pfam01442 5 SLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEE----LRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 185 EIKSpeealnKVKEVVEEALNKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQIVEDALNKLKEMIEKLLTKLKE 264
Cdd:pfam01442 81 ELRK------RLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQ 154
|
....*
gi 1309078200 265 MIEEL 269
Cdd:pfam01442 155 RLQEL 159
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
4-279 |
4.85e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.47 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 4 LVLKDVKEISTELLSKLKEM-VEEILGNLKDTVTEIITKLKEVVEGALNKLKEMVELSFSKLKEMVATAFNSLKEMVDAV 82
Cdd:PRK05771 12 VTLKSYKDEVLEALHELGVVhIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 83 ESILNDLKElgkDVKEVEDAINKAKEMVKEVEDSLNKVK---------------ETVEEVLDKVKEKVEDVANKLKEK-I 146
Cdd:PRK05771 92 EEELEKIEK---EIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVeN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 147 EEVFGKLKEKVDGISDKLKEKVEDIFKSVKEK--VENALNEIKSPEEALNKVKEVVEEaLNKVKEVVEEALNKVKQMIEE 224
Cdd:PRK05771 169 VEYISTDKGYVYVVVVVLKELSDEVEEELKKLgfERLELEEEGTPSELIREIKEELEE-IEKERESLLEELKELAKKYLE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309078200 225 LVDKLKEIVEEALNKvkqivEDALNKLKE----------MIEKLLTKLKEMIEELLKLRKMIEKA 279
Cdd:PRK05771 248 ELLALYEYLEIELER-----AEALSKFLKtdktfaiegwVPEDRVKKLKELIDKATGGSAYVEFV 307
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-299 |
2.61e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 75 LKEMVDAVESILNDLKELGKDVKEVEDAINKAKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLK 154
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 155 EKVDGISDKLKEkvediFKSVKEKVENALNEIKSPEEALNKVKEVVEEaLNKVKEVVEEALNKVKQMIEELVDKLKEIVE 234
Cdd:TIGR02169 305 SLERSIAEKERE-----LEDAEERLAKLEAEIDKLLAEIEELEREIEE-ERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309078200 235 EAlnkvkQIVEDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKALKLKQMIENMIKDLEDLKNK 299
Cdd:TIGR02169 379 EF-----AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
74-299 |
5.81e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 74 SLKEMVDAVESILNDLKELGKDVKEVEDAINKAKEMVK---EVEDSLNKvKETVEEVLDKVKEKVEDVANKLKEKIEEVf 150
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEaedRIERLEER-REDLEELIAERRETIEEKRERAEELRERA- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 151 GKLKEKVDG---ISDKLKEKVEDIFKSVKEkVENALNEIKSPEEALNKVKEVVEEALNKVKEVveEALNKVKQMIEELVD 227
Cdd:PRK02224 547 AELEAEAEEkreAAAEAEEEAEEAREEVAE-LNSKLAELKERIESLERIRTLLAAIADAEDEI--ERLREKREALAELND 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309078200 228 KLKEIVEEALNKVKQIV----EDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKALKLKQMIENMIKDLEDLKNK 299
Cdd:PRK02224 624 ERRERLAEKRERKRELEaefdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
115-332 |
2.57e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 115 DSLNKVKETVEEVLDKVKEKVEDV---ANKLKEKIEEVFGKLKEKVDGIS------DKLKEKVEDIFKSVKEK-----VE 180
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELneeYNELQAELEALQAEIDKLQAEIAeaeaeiEERREELGERARALYRSggsvsYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 181 NALNEIKSPEEALNKVkevveEALNKVKEVVEEALNKVKQMIEELVDKlkeivEEALNKVKQIVEDALNKLKEMIEKLLT 260
Cdd:COG3883 106 DVLLGSESFSDFLDRL-----SALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309078200 261 KLKEMIEELLKLRKMIEKALKLKQMIENMIKDLEDLKNKALGELAKLENNLVEGLKGFEEGVSKGAENYKSS 332
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
17-171 |
4.55e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 43.41 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 17 LSKLKEMVEEILGNLKDTVTEIITKLKEVVEGALNKLKEMVELSFSKLKEMVATafnSLKEMVDAVESILNDLKE-LGKD 95
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQ---NVEELRQRLEPYTEELRKrLNAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 96 VKEVEDAIN-KAKEMVKEVEDSLNKVKET----VEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEKVED 170
Cdd:pfam01442 90 AEELQEKLApYGEELRERLEQNVDALRARlapyAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQAED 169
|
.
gi 1309078200 171 I 171
Cdd:pfam01442 170 L 170
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
55-269 |
5.77e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 44.20 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 55 EMVELSFSKLKEMVATAFNSLKEMVDAVESILNDLKELGKDVKEVEDAINKAKEMVKEVEDSLNKVKETVEEVLDKVKEk 134
Cdd:smart00283 7 EEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 135 vedvankLKEKIEEVfGKLKEKVDGISD-------------------------------KLKEKVEDIFKSVKEKVENAL 183
Cdd:smart00283 86 -------LEESSDEI-GEIVSVIDDIADqtnllalnaaieaarageagrgfavvadevrKLAERSAESAKEIESLIKEIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 184 NEIKSPEEALNKVKEVVEEALNKVKEVVeEALNKVKQMIEELVDKLKEI-------------VEEALNKVKQIVEDALNK 250
Cdd:smart00283 158 EETNEAVAAMEESSSEVEEGVELVEETG-DALEEIVDSVEEIADLVQEIaaatdeqaagseeVNAAIDEIAQVTQETAAM 236
|
250 260
....*....|....*....|....*
gi 1309078200 251 LKEM------IEKLLTKLKEMIEEL 269
Cdd:smart00283 237 SEEIsaaaeeLSGLAEELDELVERF 261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
134-336 |
7.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 134 KVEDVANKLKEKIEEVfGKLKEKVDGISDKLKEKVEDIfKSVKEKVENALNEIKSPEEALNKVKEVVEEALNKVKEVVEE 213
Cdd:COG3883 17 QIQAKQKELSELQAEL-EAAQAELDALQAELEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 214 AlnkvkQMIEELVDKLKEIVE-----EALNKVkqiveDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKAL----KLKQ 284
Cdd:COG3883 95 L-----YRSGGSVSYLDVLLGsesfsDFLDRL-----SALSKIADADADLLEELKADKAELEAKKAELEAKLaeleALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1309078200 285 MIENMIKDLEDLKNKALGELAKLENNLVEGLKGFEEGVSKGAENYKSSIEKE 336
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| COG5412 |
COG5412 |
Phage-related protein [Mobilome: prophages, transposons]; |
1-225 |
1.05e-04 |
|
Phage-related protein [Mobilome: prophages, transposons];
Pssm-ID: 444167 [Multi-domain] Cd Length: 704 Bit Score: 44.30 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 1 MVELVLKDVKEISTELLSKLKEMVEEILGNLKDTVTEIITKLKEVVEGALNKLKEMVELSFSK----------------L 64
Cdd:COG5412 465 GIVQFISAIITNLPLILQAALQLIKALIKGLWTAIKGVIQGAIEIITGIIQFITALLTGDWSGiiwegikqlvsgiveiI 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 65 KEMVATAFNS-LKEMVDAVESILNDLKELGKDVkeVEDAINKAKEMVKEVedsLNKVKETVEEVLDKVKEKVEDVANKlK 143
Cdd:COG5412 545 PNIVAAVPQGgIAALWDAIKGFFPGLIEAIVQL--VSNIINAIISIISSI---LNAAGSIISSIWNAIKSAVSSIISA-K 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 144 EKIEEVFGKLKEKVDGISDKLKEKVEDIFKSVKEKVENALNeIKSPEEALNKVKEVVEEALNKVKEVVEEALNKVKQMIE 223
Cdd:COG5412 619 SIGKNIVNGLWNGIKSAAGAVTDKVKDIVGGIVDGIKGALG-IHSPSRKFLEIGKMIVAGLAKGIEDAFSVNSAVSKLAD 697
|
..
gi 1309078200 224 EL 225
Cdd:COG5412 698 GL 699
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
80-291 |
1.57e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 80 DAVESILNDLKELGKDVKEVEDAINKAKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKekieevfgklKEKVDG 159
Cdd:cd22656 114 EAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIA----------RKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 160 ISDKLKEKVEDIFKSVKEKVENALNEIKSPEEALNKVKEVVEealnkvkevveeALNKVKQMIEELVDKLKEIVEeALNK 239
Cdd:cd22656 184 LQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIA------------DLTAADTDLDNLLALIGPAIP-ALEK 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1309078200 240 VK---QIVEDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKALKLKQMIENMIK 291
Cdd:cd22656 251 LQgawQAIATDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
103-268 |
1.83e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 103 INKAKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEkieevfgklkekvdgiSDKLKEKVEDIFKSVKEKVENA 182
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKE----------------AEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 183 LneikspEEALNKVKEVVEEAlnkvKEVVEEALNKVKQMIEELVDKLKEiveealnkvkQIVEDALNKLKEMIEKLLTKL 262
Cdd:PRK00409 568 L------EEAEKEAQQAIKEA----KKEADEIIKELRQLQKGGYASVKA----------HELIEARKRLNKANEKKEKKK 627
|
....*.
gi 1309078200 263 KEMIEE 268
Cdd:PRK00409 628 KKQKEK 633
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
76-283 |
1.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 76 KEMVDAVESI--LNDLKELGKDVKEVEDAINKAKEMVKEVEDslnKVKETVEEVLDKVKEKVEDVANKLKEKIEEvfgkL 153
Cdd:COG4913 242 EALEDAREQIelLEPIRELAERYAAARERLAELEYLRAALRL---WFAQRRLELLEAELEELRAELARLEAELER----L 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 154 KEKVDGISDKLKEKVEDIFKSVKEKVENALNEIKSPEEALNKVKEVVEEALNKVKEV------VEEALNKVKQMIEELVD 227
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpaSAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309078200 228 KLKEIVEEALNKVKQIvEDALNKLKEMIEKLLTKLKEM------I-EELLKLRKMIEKALKLK 283
Cdd:COG4913 395 ALEEELEALEEALAEA-EAALRDLRRELRELEAEIASLerrksnIpARLLALRDALAEALGLD 456
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-300 |
1.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 17 LSKLKEMVEEILGNLKDTVTEIITKLKEvvEGALNKLKEMVELSFSKLKEMVATAFNSLKEMVDAVESILNDLKELGKDV 96
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 97 KEVEDAINKAKEmvkevedsLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEKVEdiFKSVK 176
Cdd:PRK03918 542 KSLKKELEKLEE--------LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE--LKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 177 EKVENALNEIKSPEEALNKVKEVVEEALNKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQIVE--DALNKLKEM 254
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAelEELEKRREE 691
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1309078200 255 IEKLLTKLKEMIEELLKLRKMIEKALKLKQMIENMIKDLEDLKNKA 300
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
107-187 |
1.98e-04 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 40.34 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 107 KEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKVdgisDKLKEKVEDIFKSVKEKVENALNEI 186
Cdd:COG4980 30 KETRKKLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKI----EELKEEVEPKIEELKEEAEKLQKEV 105
|
.
gi 1309078200 187 K 187
Cdd:COG4980 106 E 106
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
71-293 |
2.72e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 71 AFNSLKEMVDAVESILNDLKELgkdVKEVEDAINKAKEMVKEVE------DSLNKVKETVEEvLDKVKEKVEDVAN--KL 142
Cdd:COG0497 149 AFAGLEELLEEYREAYRAWRAL---KKELEELRADEAERARELDllrfqlEELEAAALQPGE-EEELEEERRRLSNaeKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 143 KEKIEEVFGKLKEKVDGISDKLKEkvedifksvkekVENALNEIKSPEEALNKVKEVVEEALNKVKEV------------ 210
Cdd:COG0497 225 REALQEALEALSGGEGGALDLLGQ------------ALRALERLAEYDPSLAELAERLESALIELEEAaselrryldsle 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 211 --------VEEALNKVKQM-------IEELVDKLKEIVEEaLNKVKQIvEDALNKLKEMIEKLLTKLKEMIEELLKLRKm 275
Cdd:COG0497 293 fdperleeVEERLALLRRLarkygvtVEELLAYAEELRAE-LAELENS-DERLEELEAELAEAEAELLEAAEKLSAARK- 369
|
250
....*....|....*...
gi 1309078200 276 iEKALKLKQMIENMIKDL 293
Cdd:COG0497 370 -KAAKKLEKAVTAELADL 386
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
134-304 |
2.93e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.10 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 134 KVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEKVEDIFKSVKEKVENALNEI-KSPEEALNKVKEVVEEALNKVKEVVE 212
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLePYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 213 EALNKVKQMIEELVDKLKEIVEEALNKVKQIVEDALNKLKEMIEKLLTKLKEMIEELlkLRKMIEKALKLKQMIENMIKD 292
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEEL--KESLAPYAEEVQAQLSQRLQE 158
|
170
....*....|..
gi 1309078200 293 LEDLKNKALGEL 304
Cdd:pfam01442 159 LREKLEPQAEDL 170
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
17-287 |
3.01e-04 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 42.70 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 17 LSKLKEMVEEILGNLKDTVTEIITKLKEVVEGAlNKLKEMVElsfsKLKEMVATAFNSLKEMVDAVESILNDLKELGKDV 96
Cdd:COG0840 237 IGQLADAFNRMIENLRELVGQVRESAEQVASAS-EELAASAE----ELAAGAEEQAASLEETAAAMEELSATVQEVAENA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 97 KEVEDAINKAKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVaNKLKEKIEEVfGKLKEKVDGISD-------------- 162
Cdd:COG0840 312 QQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETI-EELGESSQEI-GEIVDVIDDIAEqtnllalnaaieaa 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 163 -----------------KLKEKVEDIFKSVKEKVENALNEIKSPEEALNKVKEVVEEALNKVKEVvEEALNKVKQMIEEL 225
Cdd:COG0840 390 rageagrgfavvadevrKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEA-GEALEEIVEAVEEV 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309078200 226 VDKLKEI---VEEALNKVKQIVEdALNKLKEMIEKLLTKLKEMIEELLKLRKMIEkalKLKQMIE 287
Cdd:COG0840 469 SDLIQEIaaaSEEQSAGTEEVNQ-AIEQIAAAAQENAASVEEVAAAAEELAELAE---ELQELVS 529
|
|
| PRK15362 |
PRK15362 |
type III secretion system translocon protein; |
116-306 |
3.88e-04 |
|
type III secretion system translocon protein;
Pssm-ID: 237952 Cd Length: 473 Bit Score: 42.11 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 116 SLNKVKETV------EEVLDKVKEKVEDVANKLKEKI-EEVFGKLKEKVDGisdKLKEKVEDIFKSVKEKVENALNEIKS 188
Cdd:PRK15362 251 GIAKAAEKVldsgagEELVERMVGGSEEAIEELAEEFgKQVSEQVSKQVAN---ELAEESAEFSRNVEKNMTRSLGKAFT 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 189 PEEALNKVKEVVEEALNK-VKEVVEEALNKV-KQMIEELVDK-LKEIVEEALNKVKQIVEDALNKLKEM----IEKLLTK 261
Cdd:PRK15362 328 KEAIEAMVTEAVEEALKKaVQEGVKFLLKEFtKQVVKEVFKKvIKALIRACSFKGLQAIRCTTEGANQIntgmINTEKAK 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1309078200 262 LKEMIEELLK----LRKMIEKALKLKQMIENMIKDLEDLKNKALGELAK 306
Cdd:PRK15362 408 LQKKIEQLILqqrfLDFIMEQYEKQKKIEQKRLEELYKGSGAALRDALD 456
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
165-309 |
4.62e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 165 KEKVEDIFKSVKEKVENALNEIKSPEEALNKVKevveealnKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQIV 244
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAE--------KLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA 586
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309078200 245 EDALNKLKEMIEKLLTKLKEmiEELLKLRKMIEKALKLKQMIENMIKdlEDLKNKALGELAKLEN 309
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKA--HELIEARKRLNKANEKKEKKKKKQK--EKQEELKVGDEVKYLS 647
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
130-205 |
5.09e-04 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 39.18 E-value: 5.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309078200 130 KVKEKVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEKVEDIFKSVKEKVENALNEIKSPEEALNKVKEVVEEALN 205
Cdd:COG4980 31 ETRKKLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEELKEEAEKLQKEVE 106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-321 |
5.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 76 KEMVDAVESILNDLKELGKDVKEVEDAINKAKEMVKEVEDSLNKVKETVEEvLDKVKEKVEDvankLKEKIEEVFGKLKE 155
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE-LETLEAEIED----LRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 156 KVDGISDkLKEKVEDIFKSVKEKVENALNEIKSPE------EALNKVKEVVEEALNKVKEVVEEALNKVKQMIEElVDKL 229
Cdd:PRK02224 277 LAEEVRD-LRERLEELEEERDDLLAEAGLDDADAEavearrEELEDRDEELRDRLEECRVAAQAHNEEAESLRED-ADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 230 KEIVEEALNKVKQIvEDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKALKLKQMIENMIKDLEDLKNKALGELAKLEN 309
Cdd:PRK02224 355 EERAEELREEAAEL-ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
250
....*....|..
gi 1309078200 310 NLVEGLKGFEEG 321
Cdd:PRK02224 434 TLRTARERVEEA 445
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
190-304 |
6.54e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 190 EEALNKVKEVVEEALNKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQiVEDALNKLKEMIEKLLTKLKEMIEEL 269
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110
....*....|....*....|....*....|....*
gi 1309078200 270 LKLRKMIEkalKLKQMIENMIKDLEDLKNKALGEL 304
Cdd:PRK12704 113 EKKEKELE---QKQQELEKKEEELEELIEEQLQEL 144
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
129-194 |
6.82e-04 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.80 E-value: 6.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309078200 129 DKVKEKVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEKVEDIFKSVKEKVENALNEIKSPEEALN 194
Cdd:COG4980 41 DDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEELKEEAEKLQKEVE 106
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
6-283 |
8.70e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.99 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 6 LKDVKEISTELLSKLKEMVEEIlgnlkdtvtEIITKLKEVVEGALNKLKEmvelsfsklKEMVATAFNSLKEmvdavesi 85
Cdd:pfam03148 52 IQDITFWKSELEKELEELDEEI---------ELLLEEKRRLEKALEALEE---------PLHIAQECLTLRE-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 86 lndlKELGKDV--KEVEDAINKAKEMVKEVEDSLNKVKETVEE---VLDKVKEKVE-DVANKLK-EKIEEVFGKLKEKVD 158
Cdd:pfam03148 106 ----KRQGIDLvhDEVEKELLKEVELIEGIQELLQRTLEQAWEqlrLLRAARHKLEkDLSDKKEaLEIDEKCLSLNNTSP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 159 GISdklkekvediFKSVKEKVEnalNEIKSPEEALNKVKEVVEEALN------KVKEVVEEALNKVKQMIEelvdKLKEI 232
Cdd:pfam03148 182 NIS----------YKPGPTRIP---PNSSTPEEWEKFTQDNIERAEKeraasaQLRELIDSILEQTANDLR----AQADA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1309078200 233 VEEALNKVKQIVEDALNKLkemiEKLLTKLKEMIEELLKLRKMIEKALKLK 283
Cdd:pfam03148 245 VNFALRKRIEETEDAKNKL----EWQLKKTLQEIAELEKNIEALEKAIRDK 291
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
122-295 |
1.32e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 122 ETVEEVLDKVKEKVEDvANKLKEKIEEVFGKLKEKVDGISDKLkEKVEDIFKSVKEKVENALNEIKSPEEALNKV----K 197
Cdd:pfam12128 600 EELRERLDKAEEALQS-AREKQAAAEEQLVQANGELEKASREE-TFARTALKNARLDLRRLFDEKQSEKDKKNKAlaerK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 198 EVVEEALNKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQIVED---ALNKLKEMIEKLLTKLK--------EMI 266
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGAldaQLALLKAAIAARRSGAKaelkaletWYK 757
|
170 180
....*....|....*....|....*....
gi 1309078200 267 EELLKLRKMIEKALKLKQMIENMIKDLED 295
Cdd:pfam12128 758 RDLASLGVDPDVIAKLKREIRTLERKIER 786
|
|
| PRK03968 |
PRK03968 |
DNA primase large subunit PriL; |
2-157 |
1.76e-03 |
|
DNA primase large subunit PriL;
Pssm-ID: 235182 [Multi-domain] Cd Length: 399 Bit Score: 40.08 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 2 VELVLKDVKEISTELLSKLKEMVEEILGNLKDTVTEIITKLKEVVEGALNKLKEMVELSFSKLKEMVatafnSLKEMVDA 81
Cdd:PRK03968 86 AELVVESNGKIYEERLRRAKEIEETEIPVKVVNAIEIPEKDRKILERVRGRELPPEELEDLLPEYKI-----KWKDLLDL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 82 VESilNDLKEL----GKDVKEVEDAInkaKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKV 157
Cdd:PRK03968 161 IGS--GSLTDLyirnGRVYLRREEFL---KLWSKAFEKNLERAVNRLYEIRDELPEFYLELAEEIRETAEEEFSERGGAY 235
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
100-176 |
2.00e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 37.26 E-value: 2.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309078200 100 EDAINKAKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVANKLKEKIEEvfgkLKEKVDGISDKLKEKVEDIFKSVK 176
Cdd:COG4980 34 KKLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEE----LKEEVEPKIEELKEEAEKLQKEVE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-300 |
2.72e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 13 STELLSKLKEMVEEILGNLKDTVTEIITKLKEVVEGALNKLKEMVELSfSKLKEMVATAfNSLKEMVDAVESILND--LK 90
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE-ARIEELEEDL-HKLEEALNDLEARLSHsrIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 91 ELGKDVKEVEDAINKAKEMVKEVEDSLNKVKETVEEVLDKVKEKVEDVA------NKLKEKIEEVFGKlKEKVDGISDKL 164
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIdlkeqiKSIEKEIENLNGK-KEELEEELEEL 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 165 KEKVEDI---FKSVKEKVENALNEIKSPEEALNKVKEVVEEALNKVKEvVEEALNKVKQMIEELVDKLKEIVE------- 234
Cdd:TIGR02169 874 EAALRDLesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-LKAKLEALEEELSEIEDPKGEDEEipeeels 952
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309078200 235 -EALNKVKQIVEDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKALKLKQMIENMIKDLEDLKNKA 300
Cdd:TIGR02169 953 lEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
97-250 |
3.30e-03 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 37.69 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 97 KEVEDAINKAKEMVKEVEDSLNK---------VKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEK 167
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKqlglqnpeeVVNTLKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKLSET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 168 VEDIFKS--VKEKVENALNEIKSpeealnKVKEVVEEAlNKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQIVE 245
Cdd:cd13769 81 VPELRKSlpVEEKAQELQAKLQS------GLQTLVTES-QKLAKAISENSQKAQEELQKATKQAYDIAVEAAQNLQNQLQ 153
|
....*
gi 1309078200 246 DALNK 250
Cdd:cd13769 154 TATQK 158
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
62-236 |
3.82e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.89 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 62 SKLKEMVATAFNSLKEMVDAVESILNDLKELGKDVKEVEDAINKAKEMVKEVEDSLNK---------VKETVEEVLDKVK 132
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDlltdeggaiARKEIKDLQKELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 133 EKVEDVANKLKEKIEEvfgkLKEKVDGISDKLK--EKVEDIFKSVKEKVENALNEIKSPEEALNKVKEV---VEEALNKV 207
Cdd:cd22656 190 KLNEEYAAKLKAKIDE----LKALIADDEAKLAaaLRLIADLTAADTDLDNLLALIGPAIPALEKLQGAwqaIATDLDSL 265
|
170 180 190
....*....|....*....|....*....|....*
gi 1309078200 208 KEVVEEALNKVKQMI------EELVDKLKEIVEEA 236
Cdd:cd22656 266 KDLLEDDISKIPAAIlaklelEKAIEKWNELAEKA 300
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1-171 |
4.17e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.50 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 1 MVELVLKDVKEISTELLSKLKEMVEEILGNLKDTVTEIITKLKEVVEgALNKLKEMVELSFSKLKemvaTAFNSLKEMVD 80
Cdd:cd22656 96 ILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVD-KLTDFENQTEKDQTALE----TLEKALKDLLT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 81 AVESIL--NDLKELGKDVKEV-EDAINKAKEMVKEVEDSLNKVKETVE------EVLDKVKEKVEDVANKLK------EK 145
Cdd:cd22656 171 DEGGAIarKEIKDLQKELEKLnEEYAAKLKAKIDELKALIADDEAKLAaalrliADLTAADTDLDNLLALIGpaipalEK 250
|
170 180
....*....|....*....|....*.
gi 1309078200 146 IEEVFGKLKEKVDGISDKLKEKVEDI 171
Cdd:cd22656 251 LQGAWQAIATDLDSLKDLLEDDISKI 276
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
6-147 |
4.56e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 37.63 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 6 LKDVKEISTELLSKLKEMVEEILGNLKDTVTEIITKLKEVVEGALNKLKEMVELSFSKLKEMVATAFNSLKEmvdAVESI 85
Cdd:pfam01442 46 LEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRA---RLAPY 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309078200 86 LNDLKElgKDVKEVEDAINKAKEMVKEVEDSLNkvketveEVLDKVKEKVEDVANKLKEKIE 147
Cdd:pfam01442 123 AEELRQ--KLAERLEELKESLAPYAEEVQAQLS-------QRLQELREKLEPQAEDLREKLD 175
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
198-296 |
4.89e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 198 EVVEEAlnkvKEVVEEALNKVKQMIEELVDKLKEiVEEALNKVKQIVEDAlNKLKEMIEKLLTKLKEMIEELL-KLRKMI 276
Cdd:PRK00409 502 NIIEEA----KKLIGEDKEKLNELIASLEELERE-LEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLeEAEKEA 575
|
90 100
....*....|....*....|.
gi 1309078200 277 EKALK-LKQMIENMIKDLEDL 296
Cdd:PRK00409 576 QQAIKeAKKEADEIIKELRQL 596
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
141-219 |
5.19e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 36.10 E-value: 5.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309078200 141 KLKEKIEEVFGKLKEKVDGISDKLKEKVEDIFKSVKEKVENALNEIKspeEALNKVKEVVEEALNKVKEVVEEALNKVK 219
Cdd:COG4980 31 ETRKKLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIK---EKIEELKEEVEPKIEELKEEAEKLQKEVE 106
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
73-292 |
5.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.46 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 73 NSLKEMVDAVESILNDLKELGKDvkEVEDAINKAKEMVKEVEDSLNKVKETVEEVLDKVKEkVEDVANKLKeKIEEVFGK 152
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGE--NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMD-IEDPSAALN-KLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 153 LKEKVDGISDKLK---------------EKVEDIFKSVKEKVENALNEIKSPEEALNKVKEVVEEALNKVKEVVE--EAL 215
Cdd:PHA02562 267 IKSKIEQFQKVIKmyekggvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElkNKI 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309078200 216 NKVKQMIEELVDKLKEIVEEalnkVKQIVEDALNKLKEmieklLTKLKEMIEELLKLRKMIEKALKLKQMIENMIKD 292
Cdd:PHA02562 347 STNKQSLITLVDKAKKVKAA----IEELQAEFVDNAEE-----LAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| Niban-like |
cd23949 |
Niban-like protein; Niban-like proteins contain an N-terminal Pleckstrin-Homology (PH) domain ... |
146-294 |
6.17e-03 |
|
Niban-like protein; Niban-like proteins contain an N-terminal Pleckstrin-Homology (PH) domain that may be involved in binding to specific ligands. Phosphatidylinositol (3)-phosphate (PI3P) was recognized as the innate ligand of the PH domain of MINERVA (melanoma invasion by ERK, also known as FAM129B) PH. Niban family proteins have been found to regulate phosphorylation of a number of proteins involved in the regularion of translation, such as EIF2A, EIF4EBP1 and RPS6KB1. They may also be involved in the endoplasmic reticulum stress response (FAM129A, Niban-like protein 1), suggested to play a role in apoptosis suppression in cancer cells, while Niban-like protein 2 (FAM129C) is a B-cell membrane protein that is overexpressed in chronic lymphocytic leukemia.
Pssm-ID: 469558 [Multi-domain] Cd Length: 550 Bit Score: 38.43 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 146 IEEVFGKLKEKVDGISDKLKEKVEDIFKSVKEKVENALNEIKSPEEAL-NKV-KEVVEEALNKVKEVVEEALnkvKQMIE 223
Cdd:cd23949 267 LEAVYTLVSEQVSEAWTALKQECEELRPELEAKIRSDMDQIIASKEHLaGKIrAMVSPPAKSFLAEHVQPHL---PSILE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 224 ELVDKLKEIVEEalnkVKQIVEDALNKLKEMIEKL--LTKLKEMIEELLKL----RKM---IEKALKLK-QMIENMIKDL 293
Cdd:cd23949 344 ELMGPVSAGFVE----VRRLFEKEVERLSENLENSgdDDKLREYLESLGNLpdapVKMqpcYEKVERLKlELQQQRFDFL 419
|
.
gi 1309078200 294 E 294
Cdd:cd23949 420 S 420
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
72-338 |
6.33e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 38.88 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 72 FNSLKEMVDAVESILNDLKELGKDVKeveDAINKAKEMVKEVEDSLNkvketVEEVLDKVKEKVEDvanklkEKIEEVFG 151
Cdd:TIGR01612 1357 LNKIKKIIDEVKEYTKEIEENNKNIK---DELDKSEKLIKKIKDDIN-----LEECKSKIESTLDD------KDIDECIK 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 152 KLKEKVDGISDKlKEKVEDIFKSVKEKVENALNEIKSPEEALNKVKEVVEEALNKVKEVVEEALNKVKqmieELVDKLKE 231
Cdd:TIGR01612 1423 KIKELKNHILSE-ESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELK----EHIDKSKG 1497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 232 IVEEALNKVKQIvedalNKLKEMIEKLLTKLKEMIEELLKLrKMIEKALKLKQMIENMIKDLEDLKNKALGELAKLENNL 311
Cdd:TIGR01612 1498 CKDEADKNAKAI-----EKNKELFEQYKKDVTELLNKYSAL-AIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKI 1571
|
250 260 270
....*....|....*....|....*....|
gi 1309078200 312 VEGLK---GFEEGVSKGAENYKSSIEKEMS 338
Cdd:TIGR01612 1572 KEIKKekfRIEDDAAKNDKSNKAAIDIQLS 1601
|
|
| PLN02745 |
PLN02745 |
Putative pectinesterase/pectinesterase inhibitor |
40-188 |
6.91e-03 |
|
Putative pectinesterase/pectinesterase inhibitor
Pssm-ID: 178346 [Multi-domain] Cd Length: 596 Bit Score: 38.30 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 40 TKLKEVVEGALNKLKEMvELSFSKLKEMVATAFNSLKemvDAVESILNDLKELGKDVKEVEDAINKAKEMVKEVEDSLNK 119
Cdd:PLN02745 89 TLYKQTCENTLKKGTEK-DPSLAQPKDLLKSAIKAVN---DDLDKVLKKVLSFKFENPDEKDAIEDCKLLVEDAKEELKA 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 120 VKETVEEVLDKVKEKVEDVANKLkekiEEVFGKLKEKVDGISD-KLKEKVEDIFKSVKEKVENALNEIKS 188
Cdd:PLN02745 165 SISRINDEVNKLAKNVPDLNNWL----SAVMSYQETCIDGFPEgKLKSEMEKTFKSSQELTSNSLAMVSS 230
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
34-307 |
6.96e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 38.14 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 34 TVTEIITKLKEVVEGALNKLKEMVELSFSklkemVATAFNSLKEMVDAVESILNDLKELGKD-VKEVEDAINKAKEMVKE 112
Cdd:pfam04108 4 SAQDLCRWANELLTDARSLLEELVVLLAK-----IAFLRRGLSVQLANLEKVREGLEKVLNElKKDFKQLLKDLDAALER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 113 VEDSLNKVKET-VEEVLDKVKEKV--------EDVANKLKEKIEEVFGKLKEKVDGISDKLKEKVEDIfksvkEKVENAL 183
Cdd:pfam04108 79 LEETLDKLRNTpVEPALPPGEEKQktlldfidEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDL-----RDLQKEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 184 NEIKSPEEALNKVKEVVEEaLNKVKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKQIVEDALNkLKEMIEKLLTKLK 263
Cdd:pfam04108 154 ESLSSPSESISLIPTLLKE-LESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDARE-LDDVVPELQDRLD 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309078200 264 EMIEELLKLRKMIEKALKLKQMIENMIKDLEDLKNKALGELAKL 307
Cdd:pfam04108 232 EMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAAL 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-297 |
7.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 10 KEISTELLSKLKEMVEEILGNLKDTVTEIITKLKEVVE--GALNKLKEMVE--LSFSKLKEMVATAFNSLKEMVDAVESI 85
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvKELKELKEKAEeyIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 86 LNDLKELGKDVKEVEDAINKAKEMVKEVEDSLNKVKETVEEvLDKVKEKVEDVANKLKEKIEEVFGKLKEKVDGISdKLK 165
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEELERLKKRLTGLTPEKLEKELEELE-KAK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 166 EKVEDIFKSVKEKVENALNEIKSPEEALNKVK-----------EVVEEALNKVKEVVEEALNKVKQMIEELVDKLKEIVE 234
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309078200 235 EALNKVKQIVED----ALNKLKEMIEKLLTKLKEMIEELLK-----LRKMIEKALKLKQMIENMIKDLEDLK 297
Cdd:PRK03918 481 ELRELEKVLKKEseliKLKELAEQLKELEEKLKKYNLEELEkkaeeYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
10-268 |
7.14e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 38.61 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 10 KEISTELLSKLKEMVEEILGNLKDTvteiitKLKEVVEGALNKLKEMVELSFSKLKEMVATAfNSLKEMVDAVESIL--- 86
Cdd:PTZ00341 827 KKILDLNHKDQKEIFEEIISYIVDI------SLSDIENTAKNAAEQILSDEGLDEKKLKKRA-ESLKKLANAIEKYAggg 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 87 -NDLKELGKDVKEVEDAINKA-----KEMVKEVEDSLNKVKETVEEVLDKVKEkvEDVANKLKEKIEEvfgKLKEKVD-G 159
Cdd:PTZ00341 900 kKDKKAKKKDAKDLSGNIAHEinlinKELKNQNENVPEHLKEHAEANIEEDAE--ENVEEDAEENVEE---NVEENVEeN 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 160 ISDKLKEKVED-IFKSVKEKVENALNEiKSPEEALNKVKEVVEEALNKV-KEVVEEALNKVKQMIEELVDKLKEIVEEal 237
Cdd:PTZ00341 975 VEENVEENVEEnVEENVEENVEENVEE-NIEENVEENVEENIEENVEEYdEENVEEVEENVEEYDEENVEEIEENAEE-- 1051
|
250 260 270
....*....|....*....|....*....|.
gi 1309078200 238 NKVKQIVEDALNKLKEMIEKLLTKLKEMIEE 268
Cdd:PTZ00341 1052 NVEENIEENIEEYDEENVEEIEENIEENIEE 1082
|
|
| Perilipin |
pfam03036 |
Perilipin family; The perilipin family includes lipid droplet-associated protein (perilipin), ... |
66-263 |
7.34e-03 |
|
Perilipin family; The perilipin family includes lipid droplet-associated protein (perilipin), adipose differentiation-related protein (adipophilin) and TIP47, also known as perilin-3, altogether form the PAT family of proteins. They predominantly localize to the surface of intracellular neutral lipid droplets. Perilipin is a modulator of adipocyte lipid metabolism and adipophilinis and are involved in the development and maintenance of adipose tissue. This family appears to share some similarity with pfam08618.
Pssm-ID: 460784 Cd Length: 400 Bit Score: 38.04 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 66 EMVATAFNSLKEMVDAVESILNDLKELGKDVKEVedAINKAKEMVKEVEDSLNKVKEtveevldkvkekvedVANKLKEK 145
Cdd:pfam03036 23 DMVSSAYSSTKESHPLLKSVCDAAEKGVKTLTSA--AATGAQPILDKLEPQIATANE---------------YACKGLDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 146 IEEVFGKLKEKVDGISDKLKEKVEDIFKSVKEKVENALNEIKSpeealnKVKEVVEEALNKVKEVVEEALN-----KVKQ 220
Cdd:pfam03036 86 LEEKLPILQQPAEKVVSDAKGAVSTTVSGAKDSVSVSVTGVVD------KTKGAVQGSVELTKSVVSGGVStvmgsRVGQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1309078200 221 MIEELVDklkeiveEALNKVKQIVEDALNKLKEMIEKLLTKLK 263
Cdd:pfam03036 160 LVSSGVD-------LALGKSEELVDHYLPMTEEELAALAAPVE 195
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
58-224 |
7.60e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 38.34 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 58 ELSFSKLKEMVATA-FNSLKEMVDAVESILNDLKELGKD-------VKEVEDAINKAKEMVKEVE----DSLNKVKETVE 125
Cdd:PLN02939 227 ELDVLKEENMLLKDdIQFLKAELIEVAETEERVFKLEKErslldasLRELESKFIVAQEDVSKLSplqyDCWWEKVENLQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 126 EVLDKVKEKVEDVANKLKEKIEevfgkLKEKVDGISDKLKEKVedIFKSVKEKVENALNEIKSPEEALNKVKEVVEEALN 205
Cdd:PLN02939 307 DLLDRATNQVEKAALVLDQNQD-----LRDKVDKLEASLKEAN--VSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQ 379
|
170
....*....|....*....
gi 1309078200 206 KVKEVVEEALNKVKQMIEE 224
Cdd:PLN02939 380 LYQESIKEFQDTLSKLKEE 398
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
98-294 |
7.62e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 37.91 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 98 EVEDAINKAKEMVKEVEDSLNKVKETVEE---VLDKVKEKVE-DVANKLK-EKIEEVFGKLKEKVDGISdklkekvediF 172
Cdd:pfam03148 116 EVEKELLKEVELIEGIQELLQRTLEQAWEqlrLLRAARHKLEkDLSDKKEaLEIDEKCLSLNNTSPNIS----------Y 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 173 KSVKEKVENalnEIKSPEEALNKVKEVVEEALN------KVKEVVEEALNKVKQMIEelvdKLKEIVEEALNKVKQIVED 246
Cdd:pfam03148 186 KPGPTRIPP---NSSTPEEWEKFTQDNIERAEKeraasaQLRELIDSILEQTANDLR----AQADAVNFALRKRIEETED 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1309078200 247 ALNKLKEmieklltklkemieELLKLRKMIEKALKLKQMIENMIKDLE 294
Cdd:pfam03148 259 AKNKLEW--------------QLKKTLQEIAELEKNIEALEKAIRDKE 292
|
|
| HCoV-NL63-229E-like_Spike_SD1-2_S1-S2_S2 |
cd22375 |
SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) ... |
162-265 |
7.87e-03 |
|
SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoproteins from HCoV-NL63, HCoV-229E, and related alphacoronavirus; This group contains the SD-1 and SD-2 subdomains of the S1 subunit C-terminal domain (C-domain), the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from alphacoronaviruses, including human coronaviruses (HCoVs), HCoV-NL63 and HCoV-229E. The CoV S protein is an envelope glycoprotein that plays a very important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains the coronavirus fusion machinery and is primarily alpha-helical. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-domain. The S1 C-domain also contains two subdomains (SD-1 and SD-2), which connect the S1 and S2 subunits. Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV and MERS-CoV use the C-domain to bind their receptors. The S2 subunit comprises the fusion peptide (FP), a second proteolytic site (S2'), followed by an internal fusion peptide (IFP) and two heptad-repeat domains (HR1 and HR2) preceding the transmembrane domain (TM). After binding of the S1 subunit RBD on the virion to its receptor on the target cell, the HR1 and HR2 domains interact with each other to form a six-helix bundle (6-HB) fusion core, bringing viral and cellular membranes into close proximity for fusion and infection. In order to catalyze the membrane fusion reaction, CoV S needs to be primed through cleavage at the S1/S2 and S2' sites. In the case of human-infecting coronaviruses such as SARS-CoV-2, HCoV-OC43, MERS-CoV, and HKU1, the spike protein contains an insertion of (R/K)-(2X)n-(R/K) (furin cleavage motif) at the S1/S2 site, which is absent in SARS-CoV and other SARS-related coronaviruses, as well as Rousettus bat coronavirus HKU9. The region modeled in this cd (SD-1 and SD-2, the S1/S2 cleavage region, and the S2 fusion subunit) plays an essential role in viral entry by initiating fusion of the viral and cellular membranes.
Pssm-ID: 411962 [Multi-domain] Cd Length: 677 Bit Score: 38.34 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 162 DKLKEKVEDIFKSVKEKVENALNEIKSPEEALNKVKEVVEE---ALNKVKEVVEEALNKVKQMIEELVDKLKEIveEALN 238
Cdd:cd22375 363 NKAMTNIVDAFTGVNDAITQTSQAIQTVATALNKIQDVVNQqgnALNHLTSQLRQNFQAISSSIQAIYDRLDTI--QADQ 440
|
90 100
....*....|....*....|....*..
gi 1309078200 239 KVKQIVEDALNKLKEMIEKLLTKLKEM 265
Cdd:cd22375 441 QVDRLITGRLAALNAFVSQTLTKYTEV 467
|
|
| DUF6674 |
pfam20379 |
Family of unknown function (DUF6674); This family of proteins is functionally uncharacterized. ... |
87-306 |
7.97e-03 |
|
Family of unknown function (DUF6674); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 259 and 297 amino acids in length. There are two conserved sequence motifs: AMKIP and SMN.
Pssm-ID: 466528 [Multi-domain] Cd Length: 251 Bit Score: 37.59 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 87 NDLKELGKDVKEVEDAINKAKEMVKEVEDSLNKVKETVEEVLDK-VKEKVEDVANKLKEKIEEvfgkLKEKVDGISDKLK 165
Cdd:pfam20379 15 NGMKPEAKEFFELVEYVDGMEKQLDAVVEELQAVRQQLNKMQDKsLKAALQKAVEALEGKVQE----MKEQLSELKDNII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 166 EKVEDIFKSVKEKVENALNEIKSP---EEALNKVKEVVEEALNKVKEVVE----------EALNKVKQMIEELVDklKEI 232
Cdd:pfam20379 91 EGAKNAVAAFKEKGKSALNKVVEFlgiKPALEKIREGVEESIKSMDKTIAkidafgtelhEAGQHLKNMGRALAG--KEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309078200 233 VEEALNKVKQIVEDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKALKLKQMIEnmiKDLEDLKNKALGELAK 306
Cdd:pfam20379 169 VEYSEAKEDGGLAAAVKKPFKAERSCLSSMEKSADKALDKLDRLEQAAELKPSVK---EALEEQKGAEAFEAAA 239
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
37-198 |
8.45e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 38.27 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 37 EIITKLKEVVEGALNKLKEMvelsfsklkemvatafnslkemvdaVESILNDLKELGKDVKEVEDAINKAKEMVKEVEDS 116
Cdd:PRK00409 502 NIIEEAKKLIGEDKEKLNEL-------------------------IASLEELERELEQKAEEAEALLKEAEKLKEELEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 117 LNKVKETVEEVLDKVKEKVEDVANKLKEKIEEVFGKLKEKVDGISDKLKEK-VEDIFKSVKEKVENALNEIKSPEEALNK 195
Cdd:PRK00409 557 KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHeLIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
...
gi 1309078200 196 VKE 198
Cdd:PRK00409 637 LKV 639
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
122-306 |
8.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 37.92 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 122 ETVEEVLDKVKEKVedvanklKEKIEEVFGKLKEKVDGISDKLKEKVEDifksvkekvenaLNEikspeealnKVKEVVE 201
Cdd:COG2433 376 LSIEEALEELIEKE-------LPEEEPEAEREKEHEERELTEEEEEIRR------------LEE---------QVERLEA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309078200 202 EalnkvKEVVEEALNKVKQMIEELVDKLKEIVEEALNKVKqiVEDALNKLKEMIEKLLTKLKEMIEELLKLRKMIEKALK 281
Cdd:COG2433 428 E-----VEELEAELEEKDERIERLERELSEARSEERREIR--KDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
170 180
....*....|....*....|....*....
gi 1309078200 282 LKQMIEN----MIKDLEDLKNKALGELAK 306
Cdd:COG2433 501 LWKLEHSgelvPVKVVEKFTKEAIRRLEE 529
|
|
| |
